wanglab/gogpt-training-data huggingface dataset:
Protein: Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Potential peptide; Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gamma (Gamma-LPH); Melanocyte-stimulating hormone beta (Beta-MSH) (Melanotropin beta); Beta-endorphin; Met-enkephalin] (P01189)
Organism: Homo sapiens (Human)
Function: Stimulates the adrenal glands to release cortisol.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01193}. Note=Melanocyte-stimulating hormone alpha and beta-endorphin are stored in separate granules in hypothalamic POMC neurons, suggesting that secretion may be under the control of different regulatory mechanisms. {ECO:0000250|UniProtKB:P01193}.
Interaction partners:
- Melanocortin receptor 3
- Melanocyte-stimulating hormone receptor
- Mu-type opioid receptor
- Melanocortin receptor 4
- Adrenocorticotropic hormone receptor
- Melanocortin receptor 5
- Melanocortin-2 receptor accessory protein
- Proenkephalin-B
- Leptin
- Corticoliberin
Sequence:
MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPMFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSSGSSGAGQKREDVSAGEDCGPLPEGGPEPRSDGAKPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRLREGDGPDGPADDGAGAQADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE
Protein: Platelet-activating factor receptor (PAF-R) (PAFr) (Q62035)
Organism: Mus musculus (Mouse)
Function: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- G-protein coupled receptor 135
- Toll-like receptor 4
- Guanine nucleotide-binding protein subunit alpha-14
Sequence:
MEHNGSFRVDSEFRYTLFPIVYSVIFILGVVANGYVLWVFANLYPSKKLNEIKIFMVNLTMADLLFLITLPLWIVYYYNEGDWILPNFLCNVAGCLFFINTYCSVAFLGVITYNRYQAVAYPIKTAQATTRKRGISLSLIIWVSIVATASYFLATDSTNLVPNKDGSGNITRCFEHYEPYSVPILVVHVFIAFCFFLVFFLIFYCNLVIIHTLLTQPMRQQRKAGVKRRALWMVCTVLAVFIICFVPHHVVQLPWTLAELGYQTNFHQAINDAHQITLCLLSTNCVLDPVIYCFLTKKFRKHLSEKFYSMRSSRKCSRATSDTCTEVIVPANQTPIVSLKN
Protein: Signal recognition particle 54 kDa protein (EC 3.6.5.-) (G3V480)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364034}. Nucleus speckle {ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum {ECO:0000256|RuleBase:RU364034}.
Interaction partners:
Sequence:
MVLADLGRKITSALRSLSNATIINEEVLNAMLKEVCTALLEADVNIKLVKQLRENVKSAIDLEEMASGLNKRKMIQHAVFKELVKLVDPGVKAWTPTKGKQNVIMFVGLQGSGKTTTCSKLAYYYQRKGWKTCLICADTFRAGAFDQLKQNATKARIPFYGSYTEMDPVIIASEGVEKFKNENFEIIIVDTSGRHKQEDSLFEEMLQVANAIQPDNIVYVMDASIGQACEAQAKAFKDKVDVASVIVTKLDGHAKGGGALSAVAATKSPIIFIGTGEHIDDFEPFKTQPFISKLLGMGDIEGLIDKVNELKLDDNEALIEKLKHGQFTLRDMYEQFQNIMKMGPFSQILGMIPGFGTDFMSKGNEQESMARLKKLMTIMDSMNDQGGDMSKNVSQSQMAKLNQQMAKMMDPRVLHHMGGMAGLQSMMRQFQQGAAGNMKGMMGFNNM
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (O35803)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
HSPKKQKNGYEKKRVPEATPLLDASSLEYLFAQGQYDLIKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEPSRCHSNDSGNVLYEVMVTGNLGIQWRQKPNVLPVEKEKNKLKRKKLDYIKHKKEDARNKLREEWNSFSYFPEITHIVIKESVVSINKQDNKNMELKLSSHEGALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTDIAFNKLRQEGSEEGMYVLRWSCTDFDNILIAVSCFEKSEVLGNQKQFKNFQIEVQKGRYSLHGSVDHFPSLRDLMNHLKKQILRTDNISFVLKRCCQSKPREISNLLVATKKAQEWQPVYSMSQLSFDRILKKDIIQGEHLGRGTRTHIYSGTLLDYKDDEGIAEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDALTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSDIGPFIKLSDLGIPVSVLTRQECIERNPWIAPECVEDSKNLSVAADKWSFGTTLWEIRYDGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKHPITEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICMEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAIQICKGMDYLG
Protein: NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3) (P25963)
Organism: Homo sapiens (Human)
Function: Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10655476}. Nucleus {ECO:0000269|PubMed:10655476, ECO:0000269|PubMed:16648481, ECO:0000269|PubMed:9566872}. Note=Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export. {ECO:0000269|PubMed:10655476, ECO:0000269|PubMed:9566872}.
Interaction partners:
- S-phase kinase-associated protein 1
- NF-kappa-B essential modulator
- NF-kappa-B inhibitor beta
- Proto-oncogene c-Rel
- F-box/WD repeat-containing protein 1A
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Nuclear factor NF-kappa-B p105 subunit
- Cullin-1
- Transcription factor p65
Sequence:
MFQAAERPQEWAMEGPRDGLKKERLLDDRHDSGLDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEFTEDELPYDDCVFGGQRLTL
Protein: Chitinase-like protein PB1E7.04c (EC 3.2.1.-) (Q9C105)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase gde1
Sequence:
MRLISSLLLLVYSARLALSLNLTNQTAVLGYWGSNLAGKMGDRDQKRLSSYCQNTTYDAIILSSVIDFNVDGWPVYDFSNLCSDSDTFSGSELKKCPQIETDIQVCQENGIKVLLSIGGYNGNFSLNNDDDGTNFAFQVWNIFGSGEDSYRPFGKAVVDGFDLEVNKGTNTAYSAFAKRMLEIYASDPRRKYYISAAPTCMVPDHTLTKAISENSFDFLSIHTFNSSTGEGCSGSRNSTFDAWVEYAEDSAYNTNTSLFYGVVGHQNGSNGFISPKNLTRDLLNYKANSTLFGGVTIWDTSLAAMSYDNSSETFVEAIHKILDTKSKHSSSKSSHDSSQGLESTSSIALNPTSSISSTSSSSSTSSAISTISQDHTKTVTSVSDEPTTITASGATSVTTTTKTDFDTVTTTIVSTSTLISASDSTSIIVSSYVSTVTQPASTRVQTTTVSSISTSVKQPTASVASSSVSVPSSSSVQPQSSTPISSSSSASSPQSTLSTSSEVVSEVSSTLLSGSSAIPSTSSSTPSSSIISSPMTSVLSSSSSIPTSSSSDFSSSITTISSGISSSSIPSTFSSVSSILSSSTSSPSSTSLSISSSSTSSTFSSASTSSPSSISSSISSSSTILSSPTPSTSSLMISSSSIISGSSSILSSSISTIPISSSLSTYSSSVIPSSSTLVSSSSSLIVSSSPVASSSSSPIPSSSSLVSTYSASLSNITHSSLSLTAMSSSSAIPTSVNSSTLITASSSNTLLSSITSSSAIVSSTTVSNISSNLPSATASSQSQLTNSSTLATSLYLSSSSSRTISTSSTNEYNTSFHAPTVSSTTSSSSTTSLAANKGVNSNSITSLNLESTSSVTSTAYTTDSVTSTTALTSQGPSSSVVSSSLSSTTSLSTSIPVTSSVAPAVTSTGSETSSVVGSGTDSATSSSWTAETSSSAITSSVAASVTPTSSSSASSWSSSSEVDPSTAASATGSSTSSIATASVSGSSTSSVATASATDSSTSSIAAASVTGSSTSSVATASVTDSSTSSVATASATDSSTSSIAVASVTGSSTSSVATASATDSSTSSVATASITGSLSSSIATASVTGSPTSSVTAVSSTSSVEGTASSTIAAAASAATLSSDAASGSSTVTSSATASSSSSAATTADSSVTTDTPSNDFNANVDTAGLWYVSALSSYSVPAGFAWTTIDGFSVVMPSANAYKKRSLPIKATANPALNGAGTWKTIHTSATTTAA
Protein: Gap junction protein (E7FBZ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
- Tight junction protein 1a
- Gap junction alpha-1 protein
- Casein kinase I isoform delta-A
- Casein kinase I isoform delta-B
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
Sequence:
MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILVLGTAVESAWGDEQSAFKCNTLQPGCENVCYDKSFPISHVRFWVLQIIFVSMPTLLYLSHVVFLMNKEEKLNKKEDKLRDIQSKGGDVDVLLRKIETRKFKYGLEDHGKIKMRGGIFYTYIVSIVLKSVFEIVFLLIQWHLYGFKLSAVYTCEKFPCPHKVDCFLSRPTEKTVFIIFMLVVSLVSLALNVFEFFYVIFKRMKDQIRESEKKFDSACNIKPCPRNLSGYEYYNDCSAPVPNLGYNLDTVDKSNSSDNYDKQANEQNWTNYSTEQNQLGHSQRFPYPEKVTLGKDLLLLKELEPRPSSRASSRARPDDLDI
Protein: Galactan beta-1,4-galactosyltransferase GALS3 (EC 2.4.1.-) (Beta-1,4-galactan synthase) (Galactan synthase 3) (O65431)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of beta-1,4-galactan. Beta-1,4-galactans are abundant polysaccharides in plant cell walls and are found as side-chain of rhamnogalacturonan I, which is a major component of pectin.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:O22807}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable arabinosyltransferase ARAD2
- Probable pectin methylesterase CGR3
- Probable arabinosyltransferase ARAD1
- Protein trichome birefringence-like 10
- Galacturonosyltransferase 8
- Probable pectin methyltransferase QUA3
- Rhamnogalacturonan I rhamnosyltransferase 1
- Hexosyltransferase GAUT11
- Probable galacturonosyltransferase 7
- Probable pectin methylesterase CGR2
Sequence:
MAMVKEKEQNTKDKKLLVGVIWNFSAELKLTFMALLVLCTLATLLPFIPSSFSLSTSDFRFCISRFSSAVPLNTTTTVEESSSSPSPEKNLDRVLDNGVIKRTFTGYGSAAYNFVSMSAYRGGVNSFAVIGLSSKPLHVYGHPSYRCEWVSLDPTQDPISTTGFKILTDWGYGRIYTTVVVNCTFSSISAVNPQNSGGTLILHATTGDPTLNLTDSISVLTEPPKSVDFDLYNSTKKTKKYDYLYCGSSLYGNLSPQRVREWIAYHVRFFGERSHFVLHDAGGIHEEVFEVLKPWIELGRVTLHDIRDQERFDGYYHNQFMIVNDCLHRYRFMTKWMFFFDVDEFLHVPVKETISSVMESLEEYSQFTIEQMPMSSRICYSGDGPARTYRKWGIEKLAYRDVKKVPRRDRKYAVQPENVFATGVHMSQNLQGKTYHKAESKIRYFHYHGSISQRREPCRQLFNDSRVVFENTPYVLDTTICDVGLAVRTFELRTIGDRLLRTRQ
Protein: Gamma-tubulin complex component 2 (GCP-2) (hGCP2) (Gamma-ring complex protein 103 kDa) (h103p) (hGrip103) (Spindle pole body protein Spc97 homolog) (hSpc97) (Q9BSJ2)
Organism: Homo sapiens (Human)
Function: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome. Plays a role in neuronal migration.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:9566967}.
Interaction partners:
- Tubulin gamma-1 chain
- Gamma-tubulin complex component 5
- Gamma-tubulin complex component 4
- Gamma-tubulin complex component 6
- Gamma-tubulin complex component 3
- Mitotic-spindle organizing protein 1
- Tubulin gamma-2 chain
- Mitotic-spindle organizing protein 2A
- Mitotic spindle organizing protein 2B
- CDK5 regulatory subunit-associated protein 2
Sequence:
MSEFRIHHDVNELLSLLRVHGGDGAEVYIDLLQKNRTPYVTTTVSAHSAKVKIAEFSRTPEDFLKKYDELKSKNTRNLDPLVYLLSKLTEDKETLQYLQQNAKERAELAAAAVGSSTTSINVPAAASKISMQELEELRKQLGSVATGSTLQQSLELKRKMLRDKQNKKNSGQHLPIFPAWVYERPALIGDFLIGAGISTDTALPIGTLPLASQESAVVEDLLYVLVGVDGRYVSAQPLAGRQSRTFLVDPNLDLSIRELVHRILPVAASYSAVTRFIEEKSSFEYGQVNHALAAAMRTLVKEHLILVSQLEQLHRQGLLSLQKLWFYIQPAMRTMDILASLATSVDKGECLGGSTLSLLHDRSFSYTGDSQAQELCLYLTKAASAPYFEVLEKWIYRGIIHDPYSEFMVEEHELRKERIQEDYNDKYWDQRYTIVQQQIPSFLQKMADKILSTGKYLNVVRECGHDVTCPVAKEIIYTLKERAYVEQIEKAFNYASKVLLDFLMEEKELVAHLRSIKRYFLMDQGDFFVHFMDLAEEELRKPVEDITPPRLEALLELALRMSTANTDPFKDDLKIDLMPHDLITQLLRVLAIETKQEKAMAHADPTELALSGLEAFSFDYIVKWPLSLIINRKALTRYQMLFRHMFYCKHVERQLCSVWISNKTAKQHSLHSAQWFAGAFTLRQRMLNFVQNIQYYMMFEVMEPTWHILEKNLKSASNIDDVLGHHTGFLDTCLKDCMLTNPELLKVFSKLMSVCVMFTNCMQKFTQSMKLDGELGGQTLEHSTVLGLPAGAEERARKELARKHLAEHADTVQLVSGFEATINKFDKNFSAHLLDLLARLSIYSTSDCEHGMASVISRLDFNGFYTERLERLSAERSQKATPQVPVLRGPPAPAPRVAVTAQ
Protein: Uncharacterized protein YfdQ (P76513)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YfdP
- Uncharacterized protein YfdR
- Uncharacterized protein YfdS
- Uncharacterized protein YfdT
Sequence:
MSQNLDATAINQIHALISAQGVNEIISKIGADAVALPENFRIHDLEKFNLNRFRFRGALSTASIDDFTRYSKDLADEGTRCFIDADNMRAVSVLNLGTIDEPGHADNTATLKLKKTAPFSALLSVNGERNSQKSLAEWIEDWADYLVGFDANGDAIQATKAAAAIRKITIEANQTADFEDNDFSGKRSLMESVEAKTKDIMPVAFEFKCVPFEGLKERPFKLRLSIITGDRPVLVLRIIQLEAVQEDMANEFRDLLVEKFKDSKVETFIGTFTA
Protein: Homeobox protein Nkx-2.5 (Cardiac-specific homeobox) (Homeobox protein CSX) (Homeobox protein NK-2 homolog E) (P42582)
Organism: Mus musculus (Mouse)
Function: Transcription factor required for the development of the heart and the spleen. During heart development, acts as a transcriptional activator of NPPA/ANF in cooperation with GATA4. May cooperate with TBX2 to negatively modulate expression of NPPA/ANF in the atrioventricular canal. Binds to the core DNA motif of NPPA promoter. Together with PBX1, required for spleen development through a mechanism that involves CDKN2B repression. Positively regulates transcription of genes such as COL3A1 and MMP2, resulting in increased pulmonary endothelial fibrosis in response to hypoxia (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19483677}.
Interaction partners:
- Transcription factor GATA-4
- T-box transcription factor TBX5
- Myocyte-specific enhancer factor 2A
- Myocyte-specific enhancer factor 2C
- T-box transcription factor TBX20
- Heart- and neural crest derivatives-expressed protein 2
- Serum response factor
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Myosin-6
- Natriuretic peptides A
Sequence:
MFPSPALTPTPFSVKDILNLEQQQRSLASGDLSARLEATLAPASCMLAAFKPEAYSGPEAAASGLAELRAEMGPAPSPPKCSPAFPAAPTFYPGAYGDPDPAKDPRADKKELCALQKAVELDKAETDGAERPRARRRRKPRVLFSQAQVYELERRFKQQRYLSAPERDQLASVLKLTSTQVKIWFQNRRYKCKRQRQDQTLELLGPPPPPARRIAVPVLVRDGKPCLGDPAAYAPAYGVGLNAYGYNAYPYPSYGGAACSPGYSCAAYPAAPPAAQPPAASANSNFVNFGVGDLNTVQSPGMPQGNSGVSTLHGIRAW
Protein: (2Z,6E)-farnesyl diphosphate synthase (EC 2.5.1.68) (Cis-prenyltransferase) (Short-chain Z-isoprenyl diphosphate synthase) (Z-FPP synthase) (Z-FPPS) (Z-Polyprenyl diphosphate synthase) (Z-isoprenyl diphosphate synthase) (Q47SS3)
Organism: Thermobifida fusca (strain YX)
Function: Catalyzes the condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Only geranyl diphosphate (GPP) can be used as isoprenyl acceptor.
Interaction partners:
- Putative polyprenyl synthase / dimethylallyltranstransferase
- Trans,polycis-polyprenyl diphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Phosphatidate cytidylyltransferase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Trans-hexaprenyltranstransferase
Sequence:
MGLLRIPLYRLYERRLERALSNAPKPRHVGVILDGNRRWARLSGLSSPKEGHRAGAEKIFELLDWCDEVGVQVVTLWLLSTDNLARPPEELEPLFEIIENTVRRLCNEGRRVNPMGALDLLPASTAQVMKEAGTTTERNPGLLVNVAVGYGGRREIADAVRSLLLEEAAKGTTLEELAERLDLDDIAKHLYTRGQPDPDLLIRTSGEQRLSGFLLWQSAHSEFYFCEVFWPAFRKIDFLRALRSYSVRQRRFGC
Protein: Cell division ATP-binding protein FtsE (P0A9R7)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter FtsEX involved in cellular division. Important for assembly or stability of the septal ring.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10048040, ECO:0000269|PubMed:3323846}; Peripheral membrane protein {ECO:0000269|PubMed:10048040}; Cytoplasmic side {ECO:0000305}. Note=Associated with the membrane through an interaction with FtsX (PubMed:10048040). Localizes to the septal ring at the later stages of cell growth and remains there until division is complete (PubMed:14729705). This localization is dependent on localization of FtsZ, FtsA and ZipA, but not on the downstream division proteins FtsK, FtsQ or FtsI (PubMed:14729705). {ECO:0000269|PubMed:10048040, ECO:0000269|PubMed:14729705}.
Interaction partners:
- Cell division protein FtsX
- Cell division protein FtsZ
- Cell division protein FtsA
- Cell division protein ZipA
- Cell division protein FtsQ
- Probable peptidoglycan glycosyltransferase FtsW
- Cell division protein FtsL
- DNA translocase FtsK
- Peptidoglycan D,D-transpeptidase FtsI
- Signal recognition particle receptor FtsY
Sequence:
MIRFEHVSKAYLGGRQALQGVTFHMQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDINLISRRSYRMLTLSDGHLHGGVGHE
Protein: Conserved oligomeric Golgi complex subunit 1 (G5EE66)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 5
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 4
- Immediate early response 3-interacting protein 1
- Putative syntaxin-5
- t-SNARE coiled-coil homology domain-containing protein
- Probable coatomer subunit gamma
Sequence:
MDVDRLMRDLSVEQLENIQQNLEKEMEGKRESLREMVGRRYRDVLEASSEVRHVCSLADKLASDIANTRVGYQSTHVRTGGREEQKAGEHLYAVNYLVSSIGGDSGEPLDDVVALCMVEHLQKQLISNHSSPMIHKNARALTNRIVATRSELEFQNCSTLLDISRSDWATNQLAAIALLQGKDISQLLELYLEKRFEHVTHLIEDSATILNIVDEMKKTLAVVEELFVHGELIHAIHSVCNGQYKCELIREMCADQAYSFEKTINEDMDRVWRHLREKLSGRGAGTLPSQLVGEKCAAWIEKTCAVTHKLVAEVCEYFDNLDQIIDLLQAITASLKQDWPRIGSNRSVYDKLLQTAVVDKAKILLIQMIESIELFAKKRFESTSDGPQTAIFDERTYHPDSQSHIGISTQLYNCVKTLWESLEQTNEKCAQFETICTPMADMATSNALKETMATNVLQLLLRLCELHSDKQEGSARFLARARLALALVHSESTLICKLLDKDSQRITSLNQRLHSIIEKNLGDFCEVVVDEHITVASLSEYLESFEGGMYALRLVMEFQTVDLPDVGEVTVPIALSPPLQSILFDISSCLAEASVAHLLTKKIRKRLDEHVSHRMAQLIGERVEELKDSWHLPSRSTLQVLFDCQLIGAMFPSERMRSVCSSIESHLDPFDVSLLSPLLAANVKLVYTRTQVLFSCLVADTLSSKEVQLPQSFSKIQDVSVHIEQPSRIPMVPRLDRTMNGDKKNGGARLKNNKYLANPQQGSSKSTPSLSAFYDRISSSWFGGANN
Protein: Scarecrow-like protein 11 (AtSCL11) (GRAS family protein 31) (AtGRAS-31) (Q9LTI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein PAT1 homolog
- Transcription factor bHLH154
- Monomeric G-protein
Sequence:
MDALLQVSVDGFRFENGSGSCCKPRNNLESGNNLFPDFHESQNQSSPNDSPPTVCLDNSPVLKYINDMLMDEEDFVGISRDDLALQAAERSFYEIIQQQSPESDQNTSSSSDQNSGDQDFCFPSTTTDSSALVSSGESQRKYRHRNDEEDDLENNRRNKQPAIFVSEMEELAVKLEHVLLVCKTNQEEEEERTVITKQSTPNRAGRAKGSSNKSKTHKTNTVDLRSLLTQCAQAVASFDQRRATDKLKEIRAHSSSNGDGTQRLAFYFAEALEARITGNISPPVSNPFPSSTTSMVDILKAYKLFVHTCPIYVTDYFAANKSIYELAMKATKLHIVDFGVLYGFQWPCLLRALSKRPGGPPMLRVTGIELPQAGFRPSDRVEETGRRLKRFCDQFNVPFEFNFIAKKWETITLDELMINPGETTVVNCIHRLQYTPDETVSLDSPRDTVLKLFRDINPDLFVFAEINGMYNSPFFMTRFREALFHYSSLFDMFDTTIHAEDEYKNRSLLERELLVRDAMSVISCEGAERFARPETYKQWRVRILRAGFKPATISKQIMKEAKEIVRKRYHRDFVIDSDNNWMLQGWKGRVIYAFSCWKPAEKFTNNNLNI
Protein: RAB30, member RAS oncogene family (E9PMJ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSMEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYASNKVITVLVGNKIDLAERREVSQQRAEEFSEAQDMYYLETSAKESDNVEKLFLDLAC
Protein: Glycerate 3-kinase (EC 2.7.1.31) (D-Glycerate-3-kinase) (Glycerate kinase 2) (GK2) (P77364)
Organism: Escherichia coli (strain K12)
Interaction partners:
- 2-hydroxy-3-oxopropionate reductase
- Putative purine permease YbbY
- Allantoinase
- Glyoxylate/hydroxypyruvate reductase B
- Glycerate 2-kinase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- 2-hydroxy-3-oxopropionate reductase
- Probable phosphoglycerate mutase GpmB
- Glyoxylate/hydroxypyruvate reductase A
Sequence:
MKIVIAPDSFKESLSAEKCCQAIKAGFSTLFPDANYICLPIADGGEGTVDAMVAATGGNIVTLEVCGPMGEKVNAFYGLTGDGKTAVIEMAAASGLMLVAPEKRNPLLASSFGTGELIRHALDNDIRHIILGIGGSATVDGGMGMAQALGVRFLDADGQALAANGGNLARVASIEMDECDPRLANCHIEVACDVDNPLVGARGAAAVFGPQKGATPEMVEELEQGLQNYARVLQQQTEINVCQMAGGGAAGGMGIAAAVFLNADIKPGIEIVLNAVNLAQAVQGAALVITGEGRIDSQTAGGKAPLGVASVAKQFNVPVIGIAGVLGDGVEVVHQYGIDAVFSILPRLAPLAEVLASGETNLFNSARNIACAIKIGQGIKN
Protein: Phosphatidylinositide phosphatase SAC2 (EC 3.1.3.25) (Inositol polyphosphate 5-phosphatase F) (Sac domain-containing inositol phosphatase 2) (Sac domain-containing phosphoinositide 4-phosphatase 2) (hSAC2) (Q9Y2H2)
Organism: Homo sapiens (Human)
Function: Inositol 4-phosphatase which mainly acts on phosphatidylinositol 4-phosphate. May be functionally linked to OCRL, which converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol, for a sequential dephosphorylation of phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of inositol, thus playing an important role in the endocytic recycling. Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms. Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation. Negatively regulates STAT3 signaling pathway through inhibition of STAT3 phosphorylation and translocation to the nucleus. Functionally important modulator of cardiac myocyte size and of the cardiac response to stress (By similarity). May play a role as negative regulator of axon regeneration after central nervous system injuries (By similarity).
Subcellular location: Membrane, clathrin-coated pit {ECO:0000269|PubMed:25869669}. Early endosome {ECO:0000269|PubMed:25869669}. Recycling endosome {ECO:0000269|PubMed:25869669}. Note=Also found on macropinosomes. {ECO:0000250|UniProtKB:Q8CDA1}.
Interaction partners:
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Inositol polyphosphate 5-phosphatase OCRL
- Phosphatidylinositol 4-kinase type 2-alpha
- Synaptojanin-1
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR4
- Synaptojanin-2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
Sequence:
MELFQAKDHYILQQGERALWCSRRDGGLQLRPATDLLLAWNPICLGLVEGVIGKIQLHSDLPWWLILIRQKALVGKLPGDHEVCKVTKIAVLSLSEMEPQDLELELCKKHHFGINKPEKIIPSPDDSKFLLKTFTHIKSNVSAPNKKKVKESKEKEKLERRLLEELLKMFMDSESFYYSLTYDLTNSVQRQSTGERDGRPLWQKVDDRFFWNKYMIQDLTEIGTPDVDFWIIPMIQGFVQIEELVVNYTESSDDEKSSPETPPQESTCVDDIHPRFLVALISRRSRHRAGMRYKRRGVDKNGNVANYVETEQLIHVHNHTLSFVQTRGSVPVFWSQVGYRYNPRPRLDRSEKETVAYFCAHFEEQLNIYKKQVIINLVDQAGREKIIGDAYLKQVLLFNNSHLTYVSFDFHEHCRGMKFENVQTLTDAIYDIILDMKWCWVDEAGVICKQEGIFRVNCMDCLDRTNVVQAAIARVVMEQQLKKLGVMPPEQPLPVKCNRIYQIMWANNGDSISRQYAGTAALKGDFTRTGERKLAGVMKDGVNSANRYYLNRFKDAYRQAVIDLMQGIPVTEDLYSIFTKEKEHEALHKENQRSHQELISQLLQSYMKLLLPDDEKFHGGWALIDCDPSLIDATHRDVDVLLLLSNSAYYVAYYDDEVDKVNQYQRLSLENLEKIEIGPEPTLFGKPKFSCMRLHYRYKEASGYFHTLRAVMRNPEEDGKDTLQCIAEMLQITKQAMGSDLPIIEKKLERKSSKPHEDIIGIRSQNQGSLAQGKNFLMSKFSSLNQKVKQTKSNVNIGNLRKLGNFTKPEMKVNFLKPNLKVNLWKSDSSLETMENTGVMDKVQAESDGDMSSDNDSYHSDEFLTNSKSDEDRQLANSLESVGPIDYVLPSCGIIASAPRLGSRSQSLSSTDSSVHAPSEITVAHGSGLGKGQESPLKKSPSAGDVHILTGFAKPMDIYCHRFVQDAQNKVTHLSETRSVSQQASQERNQMTNQVSNETQSESTEQTPSRPSQLDVSLSATGPQFLSVEPAHSVASQKTPTSASSMLELETGLHVTPSPSESSSSRAVSPFAKIRSSMVQVASITQAGLTHGINFAVSKVQKSPPEPEIINQVQQNELKKMFIQCQTRIIQI