EntryName stringlengths 5 11 | ProteinName stringlengths 16 246 | Function stringlengths 17 14.1k ⌀ | SubcellularLocation stringlengths 29 5.91k ⌀ | Similarity stringlengths 38 604 ⌀ | Sequence stringlengths 2 3k |
|---|---|---|---|---|---|
1433B_PONAB | PROTEIN NAME: 14-3-3 protein beta/alpha | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13. {ECO:0000250|UniProtKB:P31946}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31946}. Melanosome {ECO:0000250|UniProtKB:P31946}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN |
1433B_RAT | PROTEIN NAME: 14-3-3 protein beta/alpha | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13. {ECO:0000250|UniProtKB:P31946}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31946}. Melanosome {ECO:0000250|UniProtKB:P31946}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICSDVLELLDKYLILNATHAESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN |
1433B_SHEEP | PROTEIN NAME: 14-3-3 protein beta/alpha | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13. {ECO:0000250|UniProtKB:P31946}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31946}. Melanosome {ECO:0000250|UniProtKB:P31946}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAG |
1433B_SOYBN | PROTEIN NAME: 14-3-3-like protein B | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | AEGLNREQYVYLANVSEQAERYEEMVEFMQKVVVGSTPASELTVEERNLLSVAYKNVIGSLRAAWRIVSSIEQKEEGRKNDDHVSLVKHYRSKVENELTQVCATILSLLDSNLVPSASASESKVFYLKMKGDYHRYLAEFKVGDERKTATEDTMLSYKAAQDIASADLPPTHPIRLGLALNFSVFYYEILNQSDKACAMAKQAFEEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDVQDQLDEP |
1433B_TOBAC | PROTEIN NAME: 14-3-3-like protein B | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAREENVYMAKLAEQAERYEEMVSFMEKVSTSLGTSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVKCIQEYRSKIESELSNICDGILKLLDSCLIPSASAGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLSAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDGADEIKETKTDNEQQ |
1433B_VICFA | PROTEIN NAME: 14-3-3-like protein B | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MASTKDRENFVYIAKLAEQAERYEEMVDSMKNVANLDVELTIEERNLLSVGYKNVIGARRASWRILSSIEQKEESKGNDVNAKRIKEYRHKVETELSNICIDVMRVIDEHLIPSAAAGESTVFYYKMKGDYYRYLAEFKTGNEKKEAGDQSMKAYESATTAAEAELPPTHPIRLGLALNFSVFYYEILNSPERACHLAKQAFDEAISELDTLNEESYKDSTLIMQLLRDNLTLWTSDIPEDGEDSQKANGTAKFGGGDDAE |
1433B_XENTR | PROTEIN NAME: 14-3-3 protein beta/alpha | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKSELVQKAKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLGLLDKYLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVTCSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKSAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGEEADNAEADN |
1433C_SOYBN | PROTEIN NAME: 14-3-3-like protein C | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MASTKERENFVYVAKLAEQAERYEEMVEAMKNVANLNVELTVEERNLLSVGYKNVVGARRASWRILSSIEQKEEAKGNDVSVKRIKEYRLKVESELSNICSDIMTVIDEYLIPSSSSGEPSVFFYKMKGDYYRYLAEFKSGDERKEAADHSMKAYQLASTTAEAELASTHPIRLGLALNFSVFYYEILNSPERACHLAKQAFDEAISELDTLSEESYKDSTLIMQLLRDNLTLWTSDIPEDGEEQKVDSARADGGDDA |
1433C_TOBAC | PROTEIN NAME: 14-3-3-like protein C | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAVAPTAREENVYMAKLAEQAERYEEMVEFMEKVSNSLGSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEEHVNSIREYRSKIENELSKICDGILKLLDAKLIPSAASGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLTAYKAAQDIATTELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDGADEIKEDPKPDEAKN |
1433D_SOYBN | PROTEIN NAME: 14-3-3-like protein D | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MTASKDRENFVYIAKLAEQAERYEEMVESMKNVANLDVELTVEERNLLSVGYKNVIGARRASWRILSSIEQKEETKGNELNAKRIKEYRQKVELELSNICNDVMRVIDEHLIPSAAAGESTVFYYKMKGDYYRYLAEFKSGNEKKEAADQSMKAYESATAAAEADLPPTHPIRLGLALNFSVFYYEILNSPERACHLAKQAFDEAISELDTLNEESYKDSTLIMQLLRDNLTLWTSDIPEDGEDAQKVNGTAKLGGGEDAE |
1433D_TOBAC | PROTEIN NAME: 14-3-3-like protein D | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAVPENLTREQCLYLAKLAEQAERYEEMVKFMDRLVAVSASSELTVEERNLLSVAYKNVIGSLRAAWRIVSSIEQKEEGRKNEEHVVLVKDYRSKVESELSDVCAGILKILDQYLIPSAAAGESKVFYLKMKGDYYRYLAEFKVGNERKEAAEDTMLAYKAAQDIALAELAPTHPIRLGLALNYSVFYYEILNASEKACSMAKQAFEEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQEQMDEA |
1433E_BOVIN | PROTEIN NAME: 14-3-3 protein epsilon | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:7931346). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:7931346). Binding generally results in the modulation of the activity of the binding partner (PubMed:7931346). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:P62258, ECO:0000269|PubMed:7931346}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm {ECO:0000250|UniProtKB:P62258}. Melanosome {ECO:0000250|UniProtKB:P62258}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ |
1433E_CHICK | PROTEIN NAME: 14-3-3 protein epsilon | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. {ECO:0000250|UniProtKB:P62261}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm {ECO:0000250|UniProtKB:P62258}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000255}. | MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ |
1433E_DROME | PROTEIN NAME: 14-3-3 protein epsilon | FUNCTION: Positively regulates Ras-mediated pathways. Acts downstream or parallel to Raf, but upstream of nuclear factors in Ras signaling. Three mutants have been isolated, that suppress the rough eye phenotype caused by mutated Ras1 (sev-Ras1 v12). Inhibits yki activity by restricting its nuclear localization. Together with pav, has a role in the inhibition of microtubule sliding during neurite outgrowth (PubMed:32022690). {ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:32022690}. | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MTERENNVYKAKLAEQAERYDEMVEAMKKVASMDVELTVEERNLLSVAYKNVIGARRASWRIITSIEQKEENKGAEEKLEMIKTYRGQVEKELRDICSDILNVLEKHLIPCATSGESKVFYYKMKGDYHRYLAEFATGSDRKDAAENSLIAYKAASDIAMNDLPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQAEEVDPNAGDGEPKEQIQDVEDQDVS |
1433E_HUMAN | PROTEIN NAME: 14-3-3 protein epsilon | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (PubMed:12917326). {ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:12917326}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12917326}. Cytoplasm {ECO:0000269|PubMed:12917326}. Melanosome {ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:17081065}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ |
1433E_MOUSE | PROTEIN NAME: 14-3-3 protein epsilon | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm. {ECO:0000250|UniProtKB:P62258, ECO:0000250|UniProtKB:P62261}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm {ECO:0000250|UniProtKB:P62258}. Melanosome {ECO:0000250|UniProtKB:P62258}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ |
1433E_RAT | PROTEIN NAME: 14-3-3 protein epsilon | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm. {ECO:0000250|UniProtKB:P62258, ECO:0000250|UniProtKB:P62261}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm {ECO:0000250|UniProtKB:P62258}. Melanosome {ECO:0000250|UniProtKB:P62258}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ |
1433E_SHEEP | PROTEIN NAME: 14-3-3 protein epsilon | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ |
1433E_TOBAC | PROTEIN NAME: 14-3-3-like protein E | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAESTREENVYMAKLAEQAERYEEMVEFMEKVAKTVDVEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVSSIKEYRGKIEAELSKICDGILNLLESHLIPVASTAESKVFYLKMKGDYHRYLAEFKTGAERKEAAENTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSSDRACNLAKQAFDDAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDTTVSLSLSQKYTPTNADAPTNNTVHTSKSFLGSA |
1433F_BOVIN | PROTEIN NAME: 14-3-3 protein eta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:7931346}. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLALLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEHMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN |
1433F_HUMAN | PROTEIN NAME: 14-3-3 protein eta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. {ECO:0000269|PubMed:12177059}. | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLSLLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEQMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN |
1433F_MOUSE | PROTEIN NAME: 14-3-3 protein eta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLALLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEHMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN |
1433F_RAT | PROTEIN NAME: 14-3-3 protein eta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MGDREQLLQRARLAEQAERYDDMASAMKAVTELNEPLSNEDRNLLSVAYKNVVGARRSSWRVISSIEQKTMADGNEKKLEKVKAYREKIEKELETVCNDVLALLDKFLIKNCNDFQYESKVFYLKMKGDYYRYLAEVASGEKKNSVVEASEAAYKEAFEISKEHMQPTHPIRLGLALNFSVFYYEIQNAPEQACLLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDEEAGEGN |
1433F_TOBAC | PROTEIN NAME: 14-3-3-like protein F | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MSSSRDEFVYMAKLAEQAERYEEMVDFMEKVVTAADGGEELTIEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVTSIKTYRSKIESELTSICNGILKLLDSNLIRAASTGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAENTLSSYKSAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDEGTEEMKEVAKPDNEEH |
1433G_BOVIN | PROTEIN NAME: 14-3-3 protein gamma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. {ECO:0000269|PubMed:7931346}. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQIESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
1433G_CHICK | PROTEIN NAME: 14-3-3 protein gamma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELGAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
1433G_HUMAN | PROTEIN NAME: 14-3-3 protein gamma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. {ECO:0000269|PubMed:16511572}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
1433G_MOUSE | PROTEIN NAME: 14-3-3 protein gamma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
1433G_PONAB | PROTEIN NAME: 14-3-3 protein gamma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
1433G_RAT | PROTEIN NAME: 14-3-3 protein gamma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
1433G_SHEEP | PROTEIN NAME: 14-3-3 protein gamma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | AAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEITAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGG |
1433I_PLAF7 | PROTEIN NAME: 14-3-3 protein I {ECO:0000305} | FUNCTION: Adapter protein which binds to its partners, usually via a phosphoserine or phosphothreonine motif (PubMed:23308157, PubMed:32484216, PubMed:32817103). Binding generally results in the modulation of the activity and/or cellular localization of the binding partner (Probable). Via its interaction with CDPK1 and PKAr, involved in merozoite microneme secretion and thus in merozoite invasion of host erythrocytes (PubMed:32817103). {ECO:0000269|PubMed:23308157, ECO:0000269|PubMed:32484216, ECO:0000269|PubMed:32817103, ECO:0000305|PubMed:32817103}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32484216}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:32484216}. Cytoplasm {ECO:0000269|PubMed:23308157, ECO:0000269|PubMed:32484216}. Nucleus {ECO:0000269|PubMed:23308157}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000255|RuleBase:RU003466}. | MATSEELKQLRCDCTYRSKLAEQAERYDEMADAMRTLVEQCVNNDKDELTVEERNLLSVAYKNAVGARRASWRIISSVEQKEMSKANVHNKNVAATYRKKVEEELNNICQDILNLLTKKLIPNTSESESKVFYYKMKGDYYRYISEFSCDEGKKEASNCAQEAYQKATDIAENELPSTHPIRLGLALNYSVFFYEILNQPHQACEMAKRAFDDAITEFDNVSEDSYKDSTLIMQLLRDNLTLWTSDLQGDQTEEKSKDEGLE |
1433S_BOVIN | PROTEIN NAME: 14-3-3 protein sigma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEESSEEKGPEVQEYREKVETELRGVCDTVLGLLDTHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPEEPQS |
1433S_HUMAN | PROTEIN NAME: 14-3-3 protein sigma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53. {ECO:0000269|PubMed:18382127}. FUNCTION: p53-regulated inhibitor of G2/M progression. {ECO:0000269|PubMed:18382127}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Secreted. Note=May be secreted by a non-classical secretory pathway. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPQEPQS |
1433S_MOUSE | PROTEIN NAME: 14-3-3 protein sigma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53. {ECO:0000269|PubMed:16710422}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16710422}. Nucleus {ECO:0000269|PubMed:16710422}. Secreted {ECO:0000250}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVKEYREKVETELRGVCDTVLGLLDSHLIKGAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADSAGEEGGEAPEEPQS |
1433S_SHEEP | PROTEIN NAME: 14-3-3 protein sigma | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway. May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEESSEEKGPEVQEYREKVETELRGVCDTVLGLLDTHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADNAGEEGGEAPEEPQS |
1433T_BOVIN | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433T_CHICK | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKMQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433T_HUMAN | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. {ECO:0000269|PubMed:12177059}. | SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally transported to the nerve terminals. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433T_MOUSE | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433T_PONAB | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433T_RABIT | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433T_RAT | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433T_XENLA | PROTEIN NAME: 14-3-3 protein theta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
1433X_MAIZE | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | ILNSPDRACNLAKQAFDEAISELDSLGEESYKDSTLIMQLLXDNLTLWTSDTNEDGGDEIK |
1433Z_AEDAE | PROTEIN NAME: 14-3-3 protein zeta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MSTVDKEELVQKAKLAEQSERYDDMAQAMKSVTETGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTESSARKQQLAREYRERVEKELREICYEVLGLLDKFLIPKASNPESKVFYLKMKGDYYRYLAEVATGETRNTVVDDSQAAYQDAFEISKGKMQPTHPIRLGLALNFSVFYYEILNSPDKACQLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDTQGDGDEPQEGGDN |
1433Z_BOMMO | PROTEIN NAME: 14-3-3 protein zeta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MSVDKEELVQRAKLAEQAERYDDMAAAMKEVTETGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGSERKQQMAKEYRVKVEKELREICYDVLGLLDKHLIPKASNPESKVFYLKMKGDYYRYLAEVATGETRHSVVEDSQKAYQDAFEISKAKMQPTHPIRLGLALNFSVFYYEILNSPDKACQLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDTQGDGDEPAEGGDN |
1433Z_BOVIN | PROTEIN NAME: 14-3-3 protein zeta/delta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Activates the ADP- ribosyltransferase (exoS) activity of bacterial origin. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (By similarity). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity). {ECO:0000250|UniProtKB:O55043, ECO:0000250|UniProtKB:P63104, ECO:0000269|PubMed:7931346}. | SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to stage IV melanosomes. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN |
1433Z_CHICK | PROTEIN NAME: 14-3-3 protein zeta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMASCMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVEQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN |
1433Z_DROME | PROTEIN NAME: 14-3-3 protein zeta | FUNCTION: Required in Raf-dependent cell proliferation and photoreceptor differentiation during eye development (PubMed:9159395). Acts upstream of Raf and downstream of Ras, and is essential for viability (PubMed:9159395). Acts as a negative regulator of the slo calcium channel via its interaction with slo-binding protein slob (PubMed:10230800). Inhibits yki activity by restricting its nuclear localization (PubMed:19900439). Binds to and promotes the activity of phosphoinositide 3-kinase Pi3K68D which converts phosphatidylinositol to phosphatidylinositol-3-phosphate and promotes maturation of early endosomes (PubMed:27015288). {ECO:0000269|PubMed:10230800, ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:27015288, ECO:0000269|PubMed:9159395}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome {ECO:0000269|PubMed:27015288}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MSTVDKEELVQKAKLAEQSERYDDMAQAMKSVTETGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEASARKQQLAREYRERVEKELREICYEVLGLLDKYLIPKASNPESKVFYLKMKGDYYRYLAEVATGDARNTVVDDSQTAYQDAFDISKGKMQPTHPIRLGLALNFSVFYYEILNSPDKACQLAKQAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDTQGDEAEPQEGGDN |
1433Z_HUMAN | PROTEIN NAME: 14-3-3 protein zeta/delta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (PubMed:16959763). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity). {ECO:0000250|UniProtKB:O55043, ECO:0000269|PubMed:14578935, ECO:0000269|PubMed:15071501, ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:16376338, ECO:0000269|PubMed:16959763, ECO:0000269|PubMed:31024343, ECO:0000269|PubMed:9360956}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Located to stage I to stage IV melanosomes. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN |
1433Z_MOUSE | PROTEIN NAME: 14-3-3 protein zeta/delta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (By similarity). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity). {ECO:0000250|UniProtKB:O55043, ECO:0000250|UniProtKB:P63104}. | SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to stage IV melanosomes. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQPESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN |
1433Z_PONAB | PROTEIN NAME: 14-3-3 protein zeta/delta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (By similarity). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity). {ECO:0000250|UniProtKB:O55043, ECO:0000250|UniProtKB:P63104}. | SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to stage IV melanosomes. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN |
1433Z_RAT | PROTEIN NAME: 14-3-3 protein zeta/delta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (PubMed:16959763). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (PubMed:16959763). {ECO:0000269|PubMed:16959763}. | SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to stage IV melanosomes. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQPESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN |
1433Z_SHEEP | PROTEIN NAME: 14-3-3 protein zeta/delta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation (By similarity). In neurons, regulates spine maturation through the modulation of ARHGEF7 activity (By similarity). {ECO:0000250|UniProtKB:O55043, ECO:0000250|UniProtKB:P63104}. | SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to stage IV melanosomes. {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNRSQPESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN |
1433Z_XENLA | PROTEIN NAME: 14-3-3 protein zeta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKRVTEEGGELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQEMSREYREKIEAELREICNDVLNLLDKFLIANATQPESKVFYLKMKGDYYRYLAEVAAGNAKTEIVGQSQKAYQDAFDISKTEMQPTHPIRLGLALNFSVFYYEILNCPDKACALAKAAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEQGEGGEN |
1433Z_XENTR | PROTEIN NAME: 14-3-3 protein zeta | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | SUBCELLULAR LOCATION: Cytoplasm. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNELVQKAKLAEQAERYDDMAACMKRVTEEGGELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQEMSREYREKIEAELREICNDVLNLLDKFLIANASQPESKVFYLKMKGDYYRYLAEVASGDAKADIVAQSQKAYQDAFDISKTEMQPTHPIRLGLALNFSVFYYEILNCPEKACSLAKAAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEQGEGGEN |
1433_CANAL | PROTEIN NAME: 14-3-3 protein homolog | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MPASREDSVYLAKLAEQAERYEEMVENMKAVASSGQELSVEERNLLSVAYKNVIGARRASWRIVSSIEQKEEAKGNESQVALIRDYRAKIEAELSKICEDILSVLSDHLITSAQTGESKVFYYKMKGDYHRYLAEFAIAEKRKEAADLSLEAYKAASDVAVTELPPTHPIRLGLALNFSVFYYEILNSPDRACHLAKQAFDDAVADLETLSEDSYKDSTLIMQLLRDNLTLWTDLSEAPAATEEQQQSSQAPAAQPTEGKADQE |
1433_CHLRE | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAVDREECVYMAKLAEQAERYDEMVEEMKKVAKLVHDQELSVEERNLLSVAYKNVIGARRASWRIISSIEQKEEAKGNEEHVQRIRKYRTVVEEELSKICASILQLLDDHLIPTASTGESKVFYLKMKGDYHRYLAEFKTGADRKEAAEHTLLAYKAAQDIALVDLPPTHPIRLGLALNFSVFYYEILNSPERACHLAKQAFDEAIAELDSLGEESYKDSTLIMQLLRDNLTLWTSDMQDPAAGDDREGADMKVEDAEP |
1433_DICDI | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MTREENVYMAKLAEQAERYEEMVEAMKKVAELDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESKGNENHVKKIKEYKCKVEKELTDICNDILEVLESHLIVSSASGESKVFYYKMKGDYFRYLAEFATGNPRKTSAESSLIAYKAASDIAVTELPPTHPIRLGLALNFSVFYYEILNSPDRACNLAKTAFDDAIAELDTLSEDSYKDSTLIMQLLRDNLTLWTSDVHNMEKNQDGDDDQNEPGM |
1433_EIMTE | PROTEIN NAME: 14-3-3 protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MIEDIKTLREEHVYRAKLAEQAERYDEMAEAMKNLVENCLDQNNSPPGAKGDELTVEERNLLSVAYKNAVGARRASWRIISSVEQKEANRNHMANKALAASYRQKVENELNKICQEILTLLTDKLLPRTTDSESRVFYFKMKGDYYRYISEFSNEEGKKASAEQAEESYKRATDTAEAELPSTHPIRLGLALNYSVFYYEILNQPQKACEMAKLAFDDAITEFDSVSEDSYKDSTLIMQLLRDNLTLWTSDLQTQEQQQQPVGEGAEAPKVEATEQQ |
1433_ENCCU | PROTEIN NAME: 14-3-3 protein homolog | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MASKQYEEALQKANLSDMAERYDDMAKEMRLAVTLAHEDKHILNVMARNLFSVAYKNLVSSRRSSWRMLCSERQKLEGKDPSVVHVINEKIKVVEEELLRFCDEVLDIITTYILSLEEAQKNIEYNIFFLKMKGDYYRYKAEVVTGPEHSEVSKHAAESYKEATEKAKTLPPTNPIKLGLALNYSVFHYEILNDSEKACSIAKGAFDEAIKELDTLSEEHYRDSTLIMQLLRDNLTLWTSREEGNVMGDEGKGDPDEN |
1433_FUCVE | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MASRDDLVYMAKLAEQAERFDEMVDHMKAVAQQPKELSVEERNLLSVAYKNVIGSRRASWRVISSIEGKDTVSDQLPLIRDYKSKIETELTDICADILKIIEAELIPNSTSEEGKVFYYKMKGDYHRYLAEFQSADERKTSASDALDAYQLASDHANQDLPPTHPIRLGLALNFSVFYYEILNSPDRACGLAKAAFDDAIAELDTLSEESYKDSTLIIMQLLRDNLTLWTSDQGEAEEAPGNADGTVVEDL |
1433_GIAIC | PROTEIN NAME: 14-3-3 protein {ECO:0000303|PubMed:16368691, ECO:0000303|PubMed:24658679, ECO:0000303|PubMed:26551337, ECO:0000303|PubMed:28932813, ECO:0000312|EMBL:EDO79081.1} | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Binds with varying affinity to various synthetic phosphopeptides having a consensus binding motif RSX(pS/pT)XP, called mode-1, where X is any residue and pS/pT is a phosphorylated serine/threonine, and to synthetic phosphopeptides having a consensus binding motif Xp(S/T)X1-2-COOH, called mode-3, in which the phosphorylated residue occupies the penultimate C-terminal position in the target protein, but does not bind to their unphosphorylated counterparts (PubMed:19733174). Binds to synthetic human RAF1 phosphopeptides, but not to their unphosphorylated forms. Binds to difopein, a polypeptide containing a phosphorylation- independent binding motif (PubMed:16368691, PubMed:19733174). Involved in encystation (PubMed:19733174). Involved in cell proliferation. Required for actin and tubulin cytoskeletal organization. Regulates actin filament formation and nuclear size (PubMed:28932813). {ECO:0000250|UniProtKB:P62261, ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:28932813}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:19861170, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:24147113, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28932813}. Nucleus {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:21135098, ECO:0000269|PubMed:22452640}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:28932813}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:28932813}. Nucleus envelope {ECO:0000269|PubMed:28932813}. Endoplasmic reticulum {ECO:0000269|PubMed:28932813}. Note=In trophozoites and cysts, localizes intensely in the cytoplasm. Not detected in the central area of the cell corresponding to the median body nor in flagella. Detected in the nuclei of the encysting cells. Nuclear localization increases during the transition of cells from the early to the late encysting stage. Does not localize to the encystation-specific vesicles of the encysting cells (PubMed:16368691, PubMed:19733174). In interphase cells, detected throughout the cell with somewhat enriched at the cortex and perinuclear region. Associates with the intracytoplasmic axonemes of all flagella, but it is most apparent in the anterior flagella of interphase cells. Localizes also to the nuclear envelope/endoplasmic reticulum and to the microtubule bare area of the ventral disc during interphase. In mitotic cells, disassociates from the intracytoplasmic axonemes and localizes around the spindle. During cytokinesis, localizes with the ingressing furrow, which does not utilize a contractile ring (PubMed:28932813). Does no colocalize with F-actin (PubMed:24728194, PubMed:28932813). {ECO:0000269|PubMed:16368691, ECO:0000269|PubMed:19733174, ECO:0000269|PubMed:24728194, ECO:0000269|PubMed:28932813}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAEAFTREDYVFMAQLNENAERYDEMVETMRKISGMEGELSDKERNLLSVAYKNVIGPRRAAWRIVSSIEAKEKGRQKPNAKRIEQIRVYRQKIEKELSDICNDILKLLQEQFVPRSTNADAKVFYYKMQGDYYRYLAEYSSGEDKEKIAGSALNAYNSAFEISQQLPPTHPIRLGLALNFSVFYYEILASPDRACELARKAFDAAITDLDKLTEESYKDSTLIMQLLRDNLNLWVTDSAGDDNAEEK |
1433_HELAN | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAAASSPREENVYLAKLAEQAERYEEMVEFMEKVVAAADGGEELTIEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEGHVSTIRDYRSKIESELSSICDGILKVLDSKLIGSASGGDSKVFYLKMKGDYYRYLAEFKTGDERKLAAENTLSAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEDSYKDSTLIMQLLRDNLTLWTSDMQDDTAEEVKEAPKPDDQ |
1433_LILLO | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MSPAEPSREENVYMAKLAEQAERYEEMVEFMEKVARTVDTEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVALIKDYRGKIEAELSKICDGILKLLDSHLVPSSTAPESKVFYLKMKGDYHRYLAEFKSGAERKEAAESTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDINEEAGDEIKEASKAVEGQ |
1433_MESCR | PROTEIN NAME: 14-3-3-like protein | FUNCTION: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MSSESSREENVYMAKLAEQAERYEEMVEFMEKVAKMTDTEELSVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVSTIKEYRGKIETELSKICDGILNLLESHLIPSASTAESKVFYLKMKGDYHRYLAEFKTGAERKEAAENTLLAYKSAQDIALAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDNAEEGGDEIKEAAAKRESGEEKPQQ |
1433_NEOCA | PROTEIN NAME: 14-3-3 protein homolog | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAEEIKNLRDEYVYKAKLAEQAERYDEMAEAMKNLVENCLDEQQPKDELSVEERNLLSVAYKNAVGARRASWRIISSVEQKELSKQHMQNKALAAEYRQKVEEELNKICHDILQLLTDKLIPKTSDSESKVFYYKMKGDYYRYISEFSGEEGKKQAADQAQESYQKATETAEGHSPATHPIRLGLALNYSVFFYEILNLPQQACEMAKRAFDDAITEFDNVSEDSYKDSTLIMQLLRDNLTLWTSDLQADQQQQEGGEKPAEQADQ |
1433_OENEH | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MATAPSPREENVYLAKLAEQAERYEEMVEFMEKVCAAADSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNDDHVSTIRDYRSKIETELSNICGGILKLLDSRLIPSAASGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLSAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLANEAFDEAIAELDTLEEESYKDSTLIMQLLRDNLTLWTSDMQDDGGDEIKEAAPKPDEQY |
1433_PEA | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MAAAHTPREENVYMAKLAEQAERYEEMVEFMEKVSANADSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEDHVAVIRDYRSKIESELSNICDGILKLLDTRLIPSASSGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLTGYKSAQDIANAELPPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDGADEIKEAAPKADEQQ |
1433_POPEU | PROTEIN NAME: 14-3-3-like protein | FUNCTION: Is associated with a DNA binding complex to bind to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes. {ECO:0000250|UniProtKB:Q01526}. | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000255}. | LAEQAERYEEMVEFMEK |
1433_SPIOL | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | RNLLSVAYKNVVGARRASWRIISSIEQKEESRGNEDHVSVIRDYRSRIEKELSDNCDGILKLLDTKLVPAASSGDSKVFYLKMKGDYHRYLAEFKTGAQRKEAAESTLTAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFVEAIAELDTLGEDSYKDSTLIMQLLRDNLTLWTSDMQDEAADEITEEAAKQQKAVNNNKIAY |
1433_TOBAC | PROTEIN NAME: 14-3-3-like protein | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKEREKQVYLARLAEQAERYDEMVEAMKTVAKMDVELTVEERNLVSVGYKNVIGARRASWRILSSIEQKEESKGHDQNVKRIKTYQQRVEDELTKYALTLSVIDEHVVPSSTSGESTVFYYKMKGDYYRYLAEFKSGDDRKEAADQSLKAYEAATATASADLAPTHPIRLGLALNFSVFYYEILNSPERACHLAKQAFDEAIAELDSLSEESYKDSTLIMQLLRDNFTLWTSDLEEGGEHSKGDERQGEN |
1433_TRIHA | PROTEIN NAME: 14-3-3 protein homolog | null | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MGHEDAVYLAKLAEQAERYEEMVENMKIVASEDRDLTVEERNLLSVAYKNVIGARRASWRIVTSIEQKEESKGNSSQVTLIKEYRQKIENELAKICDDILEVLDQHLIPSAKSGESKVFYHKIKGDYHRYLAEFAIGDRRKDSADKSLEAYKAATEVAQTELPPTHPIRLGLALNFSVFYYEILNAPDQACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSSEAETPARLMPLLRRRPLLRLPSRRRRAQG |
1433_XENLA | PROTEIN NAME: 14-3-3-like protein | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. | null | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | AKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLDLLDRFLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVASSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKSAFDEAIRELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGEEADNVEGDN |
143B1_ONCMY | PROTEIN NAME: 14-3-3 protein beta/alpha-1 | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNDLVQKAKLAEQAERYDDMAAAMKAVTEQGGELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIEAELQDICKDVLALLDNYLIANATQAESKVFYLKMKGDYYRYLSEVASGDSKKTTVENSQQAYQEAFDISKKDMQPTHPIRLGLALNFSVFYYEILNSPEQACSLAKAAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN |
143B2_ONCMY | PROTEIN NAME: 14-3-3 protein beta/alpha-2 | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKNDLVQKAKLAEQAERYDDMAGAMKSVTEQGGELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQAMAKEYREKIETELQDICNDVLGLLDKYLIANATAAESKVFYLKMKGDYYRYLSEVAAGDAKKTTVDNSQQAYQDAFDISKKEMQPTHPIRLGLALNFSVFFYEILNNPEKACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLKGHLTLWTSENQGDEGETGEGEN |
143BA_DANRE | PROTEIN NAME: 14-3-3 protein beta/alpha-A | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKSDLVQKAKLAEQAERYDDMAASMKAVTEGGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIEAELQEICNDVLGLLEKYLIPNASQAESKVFYLKMKGDYYRYLSEVASGDSKRTTVENSQKAYQDAFEISKKEMQPTHPIRLGLALNFSVFYYEILNTPEQACSLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN |
143BA_XENLA | PROTEIN NAME: 14-3-3 protein beta/alpha-A | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKSELVQKAKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLDLLDRFLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVASSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKSAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGEEADNVEGDN |
143BB_DANRE | PROTEIN NAME: 14-3-3 protein beta/alpha-B | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKSDLVQKAKLAEQAERYDDMAAAMKAVTEGGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIETELQDICSDVLGLLEKYLIANASQAESKVFYLKMKGDYYRYLSEVASGDSKATTVENSQKAYQDAFDISKKDMQPTHPIRLGLALNFSVFYYEILNSPENACQLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGEEAGENEN |
143BB_XENLA | PROTEIN NAME: 14-3-3 protein beta/alpha-B | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MDKSELVQKAKLSEQAERYDDMAASMKAVTELGAELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNDKRQQMAREYREKVETELQDICKDVLDLLDRFLVPNATPPESKVFYLKMKGDYYRYLSEVASGDSKQETVANSQQAYQEAFEISKSEMQPTHPIRLGLALNFSVFYYEILNSPDKACSLAKSAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSETQGEEADNVEGDN |
143G1_DANRE | PROTEIN NAME: 14-3-3 protein gamma-1 | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKSVTELNEALSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELETVCQDVLNLLDNFLIKNCGETQHESKVFYLKMKGDYYRYLAEVATGEKRAAVVESSEKSYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDEGGEGNN |
143G1_ONCMY | PROTEIN NAME: 14-3-3 protein gamma-1 | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKSVTELNEALSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKMEMVRAYREKIEKELETVCRDVLNLLDNFLIKNCNETQHESKVFYLKMKGDYYRYLAEVATGEKRVGVVESSEKSYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQZDDEGGETNN |
143G2_ONCMY | PROTEIN NAME: 14-3-3 protein gamma-2 | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKSVTELNEALSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLNLLDNYLIKNCNETQHESKVFYLKMKGDYYRYLAEVATGEKRATVIESSEKAYNEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYQDSTLIMQLLRDNLTLWTSDQQDDEGGEGNKD |
143GA_XENLA | PROTEIN NAME: 14-3-3 protein gamma-A | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKAVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELETVCQDVLSLLDNFLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
143GB_XENLA | PROTEIN NAME: 14-3-3 protein gamma-B | FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. | MVDREQLVQKARLAEQAERYDDMAAAMKAVTELNEALSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLNLLDNFLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN |
148R_ASFB7 | PROTEIN NAME: Uncharacterized membrane protein EP148R {ECO:0000305} | null | SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | MKKIFLTMTPLPYMNHLPENHYFLSLTVVISIIHLFTTCVPQHNHSTHFPYLNHARHLNHVLHPSHARHPNHVLHLNRVLHPNRVVHLNHVLHLNHVLHLNHVLHLNHVLHPNHVLHLNPILHPNHYLVSRYYPISRHYLHKIFRLFM |
14KD_CERSP | PROTEIN NAME: 14 kDa peptide of ubiquinol-cytochrome c2 oxidoreductase complex | FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | MFSFIDDIPSFEQIKARVRDDLRKHGWEKRWNDSRLVQKSRELLNDEELKIDPATWIWKRMPSREEVAARRQRDFETVWKYRYRLGGFASGALLALALAGIFSTGNFGGSSDAGNRPSVVYPIE |
14KD_DAUCA | PROTEIN NAME: 14 kDa proline-rich protein DC2.15 | FUNCTION: May be connected with the initiation of embryogenesis or with the metabolic changes produced by the removal of auxins. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | MGSKNSASVALFFTLNILFFALVSSTEKCPDPYKPKPKPTPKPTPTPYPSAGKCPRDALKLGVCADVLNLVHNVVIGSPPTLPCCSLLEGLVNLEAAVCLCTAIKANILGKNLNLPIALSLVLNNCGKQVPNGFECT |
14KL_BRUA1 | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
14KL_BRUA2 | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
14KL_BRUA4 | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNIFKQTCVGAFAVIFGATSIAPTMAAPLNLERPVINHNVEQVRDHRRPPRHYNGHRPHRPGYWNGHRGYRHYRHGYRRYNDGWWYPLAAFGAGAIIGGAVSQPRPVYRAPRMSNAHVQWCYNRYKSYRSSDNTFQPYNGPRRQCYSPYSR |
14KL_BRUAB | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
14KL_BRUC2 | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
14KL_BRUME | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
14KL_BRUO2 | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
14KL_BRUSI | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
14KL_BRUSU | PROTEIN NAME: Lectin-like protein BA14k | FUNCTION: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | SIMILARITY: Belongs to the BA14k family. {ECO:0000305}. | MNSFRKTCAGALALIFGATSIVPTVAAPMNMDRPAINQNVIQARAHYRPQNYNRGHRPGYWHGHRGYRHYRHGYRRHNDGWWYPLAAFGAGAIIGGAISQPRPVYRAPAGSPHVQWCYSRYKSYRASDNTFQPYNGPRKQCRSPYSR |
165R_IIV6 | PROTEIN NAME: Putative metalloproteinase 165R | null | null | SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}. | MKINTTDVRTAIYHSLQQWQSVSLLTFKEEYYDENADIKVSFVKGKHNDGWDFDGKGRILAHAFFPSGSMRGVVHLDYDEDWDFASLKQVLLHELGHTFGLGHSSDNKSIMFPWNSSSVDNVNQDDKNGIEWLYGLKNKWAKLSPPVTKPPVTKPPVTKPILTTVPRFPVPTTQVPIIQPRFGNPTTHSPTTRHPLQKIPIQPRFGHSNPPIRYNPPIRYNPKHPLSPPFKSIPNSLLNVVNSSITNLYVYFPNTWNSSIIKFN |
169L_IIV6 | PROTEIN NAME: Uncharacterized protein 169L | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | MFSNISNQKLVLFFTIILIALCPFVYYLWDNEILGIGNWGRKRKDTFEDKNCSTEIEHAIEEHKRKNKEKKEAKEKRLAPGRVKISTYDVNNENYLLGDVNDELQPNIPGYLTKETAYPFDCEPDDRSNRWL |
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