wanglab/gogpt-training-data huggingface dataset:
Protein: Anaphase-promoting complex subunit CDC26 (Cell division control protein 26) (P14724)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Anaphase-promoting complex subunit MND2
- Anaphase-promoting complex subunit SWM1
- Anaphase-promoting complex subunit DOC1
- Anaphase-promoting complex subunit 9
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit CDC23
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit CDC27
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 5
Sequence:
MIRRAPTTLQLSHDDVTSLIDDLNEQKLKQQLNIEKTKYFQGKNGGSLHSNTDFQDTSQNIEDNNNDNDNDIDEDDDMSSYNDKAASVAHTRVLNSLHLSTDSNTAHETSNANDNHNPFYIREE
Protein: Probable transcriptional regulator (Q9I1R1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transcriptional regulator
- Lipoprotein
- Putative 4-hydroxythreonine-4-phosphate dehydrogenase 2
- FAH family protein
- Probable transcriptional regulator
- DUF112 domain-containing protein
- Probable transcriptional regulator
- HTH-type transcriptional regulator PtxR
- Bistable expression regulator, BexR
- Probable transcriptional regulator
Sequence:
MSRIPDASIIHSRLRLRQLRLMLALEELGSLRRAADEIGMTQPAATKMLHEAEDLLGVELFERLPRGMRATPFGETLIYYSRMIFAELSGMREELVALESGNLGRVTVGAIPALASSLLTRTIATLKQSHPRLSMSIQVDTSDVLVQALQQDQLDVVLGRIPSGARTDDLVFDSLGEEELCVVVGAQNPLSQARKLDWGELQELTWVLQQHPSPMRGIVNQAFHNARIDLPSSIVETTSIMTLLSLLQQTDMIGITPRSVIEDYPGKHLLAILPIQLEPRLPPYGLITRRNRVHSSAMQTFMASVHAEQARHLAK
Protein: Uncharacterized protein (Q582N1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDFPKLMRLRVDDENMEKIHSVARKGQTDEVKRFVEQGIDPSIQNKFGCTALHLACKFGQVETAKYLSTLCDSHISWHGQKPLHLAVLSKKEDLVEALVAGARDRGRNVEAMLNEHDEFQVTEIGEHDIHSDGQTALHWCVALGSEYLPMLKLLLKLGASPTAKSKESMTSLMYAIITKNEEAMECMLDGAKSGQLRLDYQDKDGRTHLHHAILSNREDYAMRFIELGHGLDQEDDNHEPPLFHALRAAMPKLLAYLLENVDTFSVQQAPFHNGSTVMPERIQWLPFATNEQEQNECIALFQKRLSEVCAPQEAVVKKKKANIKKMHLAPSAPVRKRSVGRPKASK
Protein: ASI1-immunoprecipitated protein 3 (Bromo-adjacent homology domain-containing protein 1) (BAH domain-containing transcriptional regulator 1) (Protein REPRESSOR OF VERNALIZATION 1) (AtRVR1) (Q8RXT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00651}.
Interaction partners:
- Histone H3.1
Sequence:
MVLSRRFAQVSSDEEDDVPITRSKGRNSASPEESLGKRRKRKTVKLYEDFEEKEADRKKKRKGNKEDEDMAEGDDDQAEEETNPEAEEEEDEEEEEKPDDACPVGDSVNVTGKGKGKRTHFNQFAYDGNTYDLEVPVLLVPEDKSQKPYVAIIKDITQTKDGSMMILGQWFYRPEEAEKRGGGNWQSSDTRELFYSFHRDEVPAESVMHRCVVYFVPAHKQLPKRKNNPGFIVRKVYDTVEKKLWKLTDKDYEDSKQREIDVLVKKTMNVLGDLPDLESEDMLVDQENVLKAKRSFRKVNISPVDVRREEDASLKAETPGSGAGISSEHYAILEKFDSLTGDAHRDKCLGKLLEAVQHICYIPENKQAGDEAKVGSDASHLEQDEKDTKPENGKDEKFLWPDAAVPQVCALENASHASLASDFQKYNQKMRTLVFNLKNTALLARRLLNGELEPATILNMSPTELKEGLTADETTKKEPDDADRMQMTSVRCSRCSQLTVGLRDIIQAGHGDRYQLECVDCGYSWYASRDEVSTLTIVTDKPAQGTEKEDIEKNLTSPRETNKPKDEALKTNDSNADNNPEASKKPE
Protein: Sucrose-phosphate synthase 1 (EC 2.4.1.14) (Sucrose-phosphate synthase 1F) (AtSPS1F) (Sucrose-phosphate synthase 5.1) (AtSPS5.1) (UDP-glucose-fructose-phosphate glucosyltransferase) (Q94BT0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a major role in photosynthetic sucrose synthesis by catalyzing the rate-limiting step of sucrose biosynthesis from UDP-glucose and fructose- 6-phosphate. Involved in the regulation of carbon partitioning in the leaves of plants. May regulate the synthesis of sucrose and therefore play a major role as a limiting factor in the export of photoassimilates out of the leaf. Plays a role for sucrose availability that is essential for plant growth and fiber elongation. Required for nectar secretion.
Interaction partners:
- Probable sucrose-phosphatase 2
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Probable sucrose-phosphatase 1
- UTP--glucose-1-phosphate uridylyltransferase 1
- Probable sucrose-phosphatase 3b
- Probable sucrose-phosphatase 3a
- UTP--glucose-1-phosphate uridylyltransferase 2
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
Sequence:
MAGNDWVNSYLEAILDVGQGLDDARSSPSLLLRERGRFTPSRYFVEEVITGYDETDLHRSWVKAVATRSPQERNTRLENMCWRIWNLARQKKQHEEKEAQRLAKRRLEREKGRREATADMSEEFSEGEKGDIISDISTHGESTKPRLPRINSAESMELWASQQKGNKLYLVLISLHGLIRGENMELGRDSDTGGQVKYVVELARALGSMPGVYRVDLLTRQVSSPDVDYSYGEPTEMLTPRDSEDFSDEMGESSGAYIVRIPFGPKDKYIPKELLWPHIPEFVDGAMSHIMQMSNVLGEQVGVGKPIWPSAIHGHYADAGDATALLSGALNVPMLLTGHSLGRDKLEQLLRQGRLSKEEINSTYKIMRRIEGEELSLDVSEMVITSTRQEIDEQWRLYDGFDPILERKLRARIKRNVSCYGRFMPRMVKIPPGMEFNHIVPHGGDMEDTDGNEEHPTSPDPPIWAEIMRFFSNSRKPMILALARPDPKKNITTLVKAFGECRPLRELANLALIMGNRDGIDEMSSTSSSVLLSVLKLIDKYDLYGQVAYPKHHKQSDVPDIYRLAAKSKGVFINPAIIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDPHDQQSISEALLKLVADKHLWAKCRQNGLKNIHQFSWPEHCKTYLSRITSFKPRHPQWQSDDGGDNSEPESPSDSLRDIQDISLNLKFSFDGSGNDNYMNQEGSSMDRKSKIEAAVQNWSKGKDSRKMGSLERSEVNSGKFPAVRRRKFIVVIALDFDGEEDTLEATKRILDAVEKERAEGSVGFILSTSLTISEVQSFLVSGGLNPNDFDAFICNSGSDLHYTSLNNEDGPFVVDFYYHSHIEYRWGGEGLRKTLIRWASSLNEKKADNDEQIVTLAEHLSTDYCYTFTVKKPAAVPPVRELRKLLRIQALRCHVVYSQNGTRINVIPVLASRIQALRYLFVRWGIDMAKMAVFVGESGDTDYEGLLGGLHKSVVLKGVSCSACLHANRSYPLTDVISFESNNVVHASPDSDVRDALKKLELLKD
Protein: RE52752p (Q8IGP6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPPVQVQAANMSLGAMHCTRCADGFEPTEKIVNSNGELWHTQCFVCAQCFRPFQDGIFYEFEGRKYCERDFHVLFAPCCNKCGEFVIGRVIKAMSASWHPQCFRCQLCAKELADCGFIKNQNRALCHECNAKVKAEITGRYVCQKCHGLIDEEPLRFRGEVYHGYHFSCTACGTELDSTAREVKSRPGLAANDMNELYCLRCHDKMGIPICGACRRPIEERVVTALGKHWHVEHFVCAKCEKPFLGHRHYEKR
Protein: Calcium-binding protein F (Calcium-binding protein 6) (Q54QT9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSTNSDNDKIFQEVQKFVKNYDLNKDGSVTSFDIYRSFLKKMDGDIFKASQAAGVLCSTVDMDHDGKFTYQEIAKYCADEAKKNVEQNAEIAALADVEAMLLRFDKDKDKKLTKTEFVEYFKGNGHTPYSDRDQVLKIIDLDKDGCVSANELQEWFKKRRIDYARMVSARGPNC
Protein: NADPH:adrenodoxin oxidoreductase, mitochondrial (EC 1.18.1.6) (A0A0A0MTN9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|PIRNR:PIRNR000362}.
Interaction partners:
Sequence:
MEDKDREHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVPELQEAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKELREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH
Protein: G2/mitotic-specific cyclin-B1 (P24860)
Organism: Mus musculus (Mouse)
Function: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
Interaction partners:
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase PLK1
- Cell division cycle protein 20 homolog
- Cyclin-dependent kinase 2
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Baculoviral IAP repeat-containing protein 5
- Aurora kinase A
- Cell division cycle protein 27 homolog
- Growth arrest and DNA damage-inducible protein GADD45 alpha
- M-phase inducer phosphatase 3
Sequence:
MALRVTRNTKINAENKAKVSMAGAKRVPVTVTAASKPGLRPRTALGDIGNKVSEELQARVPLKREAKTLGTGKGTVKALPKPVEKVPVCEPEVELAEPEPEPELEHVREEKLSPEPILVDNPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDADDGADPNLCSEYVKDIYAYLRQLEEEQSVRPKYLQGREVTGNMRAILIDWLIQVQMKFRLLQETMYMTVSIIDRFMQNSCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTNNTYTKHQIRQMEMKILRVLNFSLGRPLPLHFLRRASKVGEVDVEQHTLAKYLMELSMLDYDMVHFAPSQIAAGAFCLALKILDNGEWTPTLQHYLSYSEDSLLPVMQHLAKNVVMVNCGLTKHMTVKNKYAASKHAKISTLAQLNCTLVQNLSKAVTKA
Protein: SERF-like protein YDL085C-A (Q3E7B7)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mitofissin
Sequence:
MARGNQRDLARQKNLKKQKDMAKNQKKSGDPKKRMESDAEILRQKQAAADARREAEKLEKLKAEKTRR
Protein: Peptide deformylase, mitochondrial (EC 3.5.1.88) (Polypeptide deformylase) (Q9HBH1)
Organism: Homo sapiens (Human)
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14532271, ECO:0000269|PubMed:15489958}.
Interaction partners:
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein bS6m
Sequence:
MARLWGALSLWPLWAAVPWGGAAAVGVRACSSTAAPDGVEGPALRRSYWRHLRRLVLGPPEPPFSHVCQVGDPVLRGVAAPVERAQLGGPELQRLTQRLVQVMRRRRCVGLSAPQLGVPRQVLALELPEALCRECPPRQRALRQMEPFPLRVFVNPSLRVLDSRLVTFPEGCESVAGFLACVPRFQAVQISGLDPNGEQVVWQASGWAARIIQHEMDHLQGCLFIDKMDSRTFTNVYWMKVND
Protein: Circumsporozoite protein (CS) (PbCSP) [Cleaved into: Circumsporozoite protein C-terminus] (P23093)
Organism: Plasmodium berghei (strain Anka)
Function: Essential sporozoite protein. In the mosquito vector, required for sporozoite development in the oocyst, migration through the vector hemolymph and entry into the vector salivary glands. In the vertebrate host, required for sporozoite migration through the host dermis and infection of host hepatocytes. Binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on the surface of host hepatocytes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15630135, ECO:0000269|PubMed:16207248, ECO:0000269|PubMed:21262960, ECO:0000269|PubMed:6985745}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:16207248}. Cytoplasm {ECO:0000269|PubMed:16207248}. Note=Localizes to the cytoplasm and the cell membrane in oocysts at day 6 post infection and then gradually distributes over the entire cell surface of the sporoblast and the budding sporozoites. {ECO:0000269|PubMed:16207248}.
Interaction partners:
Sequence:
MKKCTILVVASLLLVNSLLPGYGQNKSIQAQRNLNELCYNEGNDNKLYHVLNSKNGKIYNRNTVNRLLADAPEGKKNEKKNEKIERNNKLKQPPPPPNPNDPPPPNPNDPPPPNPNDPPPPNPNDPPPPNANDPPPPNANDPAPPNANDPAPPNANDPAPPNANDPAPPNANDPPPPNPNDPAPPNANDPPPPNPNDPAPPQGNNNPQPQPRPQPQPQPQPQPQPQPQPQPRPQPQPQPGGNNNNKNNNNDDSYIPSAEKILEFVKQIRDSITEEWSQCNVTCGSGIRVRKRKGSNKKAEDLTLEDIDTEICKMDKCSSIFNIVSNSLGFVILLVLVFFN
Protein: V-type proton ATPase subunit a (Q9JL11)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
EGQLEDPVTGEPATWMTFVISYWGEQIGQKIRKITDCFHCHVFPYLEQEEARFRTLQQLQQQSQELQEVLGETDRFLSQVLGRVQQLLPPWQVQIHKMKAVYLTLNQCSVNTTHKCLIAEVWCAARDLPTVQQALQSGSVSIQAARGLLPPCLSSFYFQSLLKLPLLWD
Protein: Basonuclin zinc finger protein 1 (F5GY04)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRCRNMFFSFKASLCGCGAATAPSLTAISCTLNCSCQSFKPGKINHRQCDQCKHGWVAHALSKLRIPPMYPTSQVEIVQSNVVFDISSLMLYGTQAIPVRLKILLDRLFSVLKQDEVLQILHALDWTLQDYIRGYVLQDASGKVLDHWSIMTSEEEVATLQQFLRFGETKSIVELMAIQEKEEQSIIIPPSTANVDIRAFIESCSHRSSSLPTPVDKGNPSSIHPFENLISNMTFMLPFQFFNPLPPALIGSLPEQYMLEQGHDQSQDPKQEVHGPFPDSSFLTSSSTPFQVEKDQCLNCPDAITKKEDSTHLSDSSSYNIVTKFERTQLSPEAKVKPERNSLGTKKGRVFCTACEKTFYDKGTLKIHYNAVHLKIKHKCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMNRNNRDKDLRNSLNLASSENYKCPGFTVTSPDCRPPPSYPGSGEDSKGQPAFPNIGQNGVLFPNLKTVQPVLPFYRSPATPAEVANTPGILPSLPLLSSSIPEQLISNEMPFDALPKKKSRKSSMPIKIEKEAVEIANEKRHNLSSDEDMPLQVVSEDEQEACSPQSHRVSEEQHVQSGGLGKPFPEGERPCHRESVIESSGAISQTPEQATHNSERETEQTPALIMVPREVEDGGHEHYFTPGMEPQVPFSDYMELQQRLLAGGLFSALSNRGMAFPCLEDSKELEHVGQHALARQIEENRFQCDICKKTFKNACSVKIHHKNMHVKEMHTCTVEGCNATFPSRRSRDRHSSNLNLHQKALSQEALESSEDHFRAAYLLKDVAKEAYQDVAFTQQASQTSVIFKGTSRMGSLVYPITQVHSASLESYNSGPLSEGTILDLSTTSSMKSESSSHSSWDSDGVSEEGTVLMEDSDGNCEGSSLVPGEDEYPICVLMEKADQSLASLPSGLPITCHLCQKTYSNKGTFRAHYKTVHLRQLHKCKVPGCNTMFSSVRSRNRHSQNPNLHKSLASSPSHLQ
Protein: Ionotropic receptor 93a (Q9VDH6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Integral part of various neural sensory systems in the antenna that provide the neural basis for the response to environmental changes in temperature (thermosensation) and humidity (hygrosensation). Together with Ir21a and Ir25a, mediates the response of the larval dorsal organ cool cells, a trio of cool-responsive neurons, to cooling and is required for cool avoidance behavior. Together with Ir25a and Ir40a, mediates the response of the hydrosensory sacculus neurons to changes in relative humidity, and is required for dry detection and humidiy preference behavior.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ionotropic receptor 40a
- Ionotropic receptor 68a, isoform A
- Ionotropic receptor 64a
- Ionotropic receptor 41a
- Ionotropic receptor 25a
- Ionotropic receptor 75d
- Ionotropic receptor 60a
- Ionotropic receptor 87a
- Ionotropic receptor 31a, isoform C
- Glycine--tRNA ligase
Sequence:
MNPGEMRPSACLLLLAGLQLSILVPTEANDFSSFLSANASLAVVVDHEYMTVHGENILAHFEKILSDVIRENLRNGGINVKYFSWNAVRLKKDFLAAITVTDCENTWNFYKNTQETSILLIAITDSDCPRLPLNRALMVPIVENGDEFPQLILDAKVQQILNWKTAVVFVDQTILEENALLVKSIVHESITNHITPISLILYEINDSLRGQQKRVALRQALSQFAPKKHEEMRQQFLVISAFHEDIIEIAETLNMFHVGNQWMIFVLDMVARDFDAGTVTINLDEGANIAFALNETDPNCQDSLNCTISEISLALVNAISKITVEEESIYGEISDEEWEAIRFTKQEKQAEILEYMKEFLKTNAKCSSCARWRVETAITWGKSQENRKFRSTPQRDAKNRNFEFINIGYWTPVLGFVCQELAFPHIEHHFRNITMDILTVHNPPWQILTKNSNGVIVEHKGIVMEIVKELSRALNFSYYLHEASAWKEEDSLSTSAGGNESDELVGSMTFRIPYRVVEMVQGNQFFIAAVAATVEDPDQKPFNYTQPISVQKYSFITRKPDEVSRIYLFTAPFTVETWFCLMGIILLTAPTLYAINRLAPLKEMRIVGLSTVKSCFWYIFGALLQQGGMYLPTADSGRLVVGFWWIVVIVLVTTYCGNLVAFLTFPKFQPGVDYLNQLEDHKDIVQYGLRNGTFFERYVQSTTREDFKHYLERAKIYGSAQEEDIEAVKRGERINIDWRINLQLIVQRHFEREKECHFALGRESFVDEQIAMIVPAQSAYLHLVNRHIKSMFRMGFIERWHQMNLPSAGKCNGKSAQRQVTNHKVNMDDMQGCFLVLLLGFTLALLIVCGEFWYRRFRASRKRRQFTN
Protein: Aldo-keto reductase family 1, member B10 (G5E895)
Organism: Mus musculus (Mouse)
Interaction partners:
- Sorbitol dehydrogenase
- L-xylulose reductase
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- glycerol kinase
- Dihydropteridine reductase
- Glycerol kinase 2
- Dihydrofolate reductase
- Glycerol kinase
- Tyrosine 3-monooxygenase
- Galactose mutarotase
Sequence:
MAAFVTLLTGAKMPIVGLGTWKSPPAKVREAVKVAIDAGYRHIDCAYVYQNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDPLLLEIPKIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRACGLFAASHNEDFPFHAEY
Protein: Afadin- and alpha-actinin-binding protein (ADIP) (Afadin DIL domain-interacting protein) (Q8CGZ2)
Organism: Rattus norvegicus (Rat)
Function: Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles. The function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome (By similarity). Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling (By similarity). Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin. Involved in ciliogenesis (By similarity). It is required for targeted recruitment of the BBSome, CEP290, RAB8, and SSTR3 to the cilia (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:12446711}. Nucleus {ECO:0000250|UniProtKB:Q9Y2D8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9Y2D8}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9Y2D8}. Note=Not found at cell-matrix AJs.
Interaction partners:
- Alpha-actinin-1
- Alpha-actinin-4
Sequence:
MGDWMTVTDPVLCTENKNLSQYTSETKMSPSSLYSQQVLCSATPLSKNVHGVFSAFCTGENIEQSISYLDQELTTFGFPSLYEESKSKEAKRELSIVALLNCMNELLVLQRKNLLAQESVETQNLKLGSDMDHLQSCYAKLKEQLEASRREMISLQERDRQLQCKNRNLHQLLKNEKEEVQKLQNIIASRATQYNHDVKRKEREYNKLKERLHQLVMNKKDKNIAMDVLNYVGRVDGKRGSWRTDKTEARNEDEMYKILLNDYEYRQKQILLENAELKKVLQQMKKEMISLLSPQKKKPRERAEDSTGTVVISDVEDDAGELSRDGVWSLSCDTVREQLTNSIRKQWRILKSHVEKLDNQASKVHSEGFHEEDVISRQDHEQETEKLELEIERCKEMIKAQQQLLQQQLATACDDDTTSLLRDCYLLEEKERLKEEWSLFKEQKKNFERERRSFTEAAIRLGLERKAFEEERASWVKQQFLNMTTFDHQNSENVKLFSAFSGSSDPDNLIVHPRPRQKKPHSVANGVPACTSKLAKSLPTSPSDFCPSRSCVSEHSPVSALTVTPEETKPNEVGRESTDQKWSVVSRPSSREGCYGGCSSAYTSSHVERDDLP
Protein: 5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1) (Nap1) (TILP) (Q9H6S1)
Organism: Homo sapiens (Human)
Function: Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14560022}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- Tumor necrosis factor
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon
- TRAF family member-associated NF-kappa-B activator
- NF-kappa-B essential modulator
- Tax1-binding protein 1
- Calcium-binding and coiled-coil domain-containing protein 2
- TANK-binding kinase 1-binding protein 1
- TNF receptor-associated factor 3
Sequence:
MDALVEDDICILNHEKAHKRDTVTPVSIYSGDESVASHFALVTAYEDIKKRLKDSEKENSLLKKRIRFLEEKLIARFEEETSSVGREQVNKAYHAYREVCIDRDNLKSKLDKMNKDNSESLKVLNEQLQSKEVELLQLRTEVETQQVMRNLNPPSSNWEVEKLSCDLKIHGLEQELELMRKECSDLKIELQKAKQTDPYQEDNLKSRDLQKLSISSDNMQHAYWELKREMSNLHLVTQVQAELLRKLKTSTAIKKACAPVGCSEDLGRDSTKLHLMNFTATYTRHPPLLPNGKALCHTTSSPLPGDVKVLSEKAILQSWTDNERSIPNDGTCFQEHSSYGRNSLEDNSWVFPSPPKSSETAFGETKTKTLPLPNLPPLHYLDQHNQNCLYKN
Protein: Metabotropic glutamate receptor-like protein H (Q54SH8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Autocrine proliferation repressor protein A
- Frizzled and smoothened-like protein B
- Frizzled and smoothened-like protein K
Sequence:
MKNILKILILILICINKINCLDGDGKQFRMIMLLSANVNDMGFNNMMNQGRIGVSKNLQIEDSRLIVVDGENDTKALVEPILQNEDIDFVICSSQGHTVACKYFADKYLKHPTVKTQFLIRGSGSSTANLIQFNYNFASCNYMSGYFAGLHTKTNKIGFLSPGAPKVNDAWVYAFWLGAKQVNPKIQFFYYNVGAFLNPDASERATNDLLERGCDVIGNTLDDFSSGITIMSKGYRTIGTNGFPQKLIYGEKILYSYAYNWTKLFLPIAMSVKAGITNNTNGYGDFNLDESKNFFNIEYSYGVSTDTINRMNQQITFLKSNSRFTHPYYCNEYLPEYTKKNNLNLSTSPTVNNLICIDHSTFLKINPPFPGMTYLGIYNISLVEVEFSQSIQNGFSITTGILIGITILMMIGIIKYSKTPSMRSASPIFLNFILAGGIIVYIGIIVWVGPMSTHSCNARLWLVTLGFSTLIGSLVVKNFRIWLIFDNPELKSIKITNYQLFPWVGACLVINIILMAILTSVGDLKQIDAMNIDSLGKYEYMKVCKMNSSGASTLYTILAYFAALLLVGVFVSWKIRIVDILEFNESGAIANTLYAISFCLFVIVPLMISPQDMQSETIILCTTGLFITTAALLIIFIPKFWRVFRKGANDSEINFNKKKSSSVATARAESGSKGSNGNASSGNRTNRRGNVVSGDFTDDSESSVGDENQKEKEKIKDDVANVTSGAVLAEFTDEASDTDNNEFNDIELSEQPPSIIVNDSENNN
Protein: Protein STU2 (Suppressor of tubulin 2) (P46675)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. Stabilizes both cytoplasmic and nuclear microtubules. Promotes mitotic spindle elongation in anaphase. Has microtubule polymerase activity by accelerating microtubule growth and inhibiting catastrophe. The polymerase activity is proposed to involve a tethering mechanism at the microtubule plus end: a curved, longitudinally microtubule lattice-associated tubulin heterodimer (that cannot be incorporated into the microtubule lattice) is bound via one TOG domain while the other TOG domain binds to an unpolymerized tubulin heterodimer leading to lateral association of these tubulin heterodimers; polymerization-induced straightening of the tubulin heterodimer releases the polymerase. Is involved in regulation of kinetochore-microtubule attachments in a tension-dependent manner involving its association with the NDC80 complex; the function may be independent of its microtubule polymerase activity. Can either stabilize or destabilize kinetochore attachments, depending on the level of kinetochore tension and whether the microtubule tip is assembling or disassembling.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:9382872}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:9382872}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:27156448}. Note=Localizes primarily to the spindle pole body (SPB) and to a lesser extent along spindle microtubules. {ECO:0000269|PubMed:9382872}.
Interaction partners:
- Protein BIM1
- Kinetochore protein NDC80
- Spindle pole body component 110
- Tubulin beta chain
- S-phase entry cyclin-5
- G2/mitotic-specific cyclin-2
- Mitosis inhibitor protein kinase SWE1
- Tubulin alpha-1 chain
- Nuclear fusion protein BIK1
- Kinetochore protein NUF2
Sequence:
MSGEEEVDYTTLPLEERLTYKLWKARLEAYKELNQLFRNSVGDISRDDNIQIYWRDPTLFAQYITDSNVVAQEQAIVALNSLIDAFASSSLKNAHNITLISTWTPLLVEKGLTSSRATTKTQSMSCILSLCGLDTSITQSVELVIPFFEKKLPKLIAAAANCVYELMAAFGLTNVNVQTFLPELLKHVPQLAGHGDRNVRSQTMNLIVEIYKVTGNNSDLLEEILFKKLKPIQVKDLHKLFAKVGDEPSSSKMLFEWEKRELEKKRSQEEEARKRKSILSNDEGEYQIDKDGDTLMGMETDMPPSKQQSGVQIDTFSMLPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQTKKLKSTSQNYSNLLGIYGHIIQKDANIQAVALAAQSVELICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSVIEAIRKALLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECTQLFNASMKEEKDGYSTLQRYLKDEVVPIVIQIVNDTQPAIRTIGFESFAILIKIFGMNTFVKTLEHLDNLKRKKIEETVKTLPNFSIASGSTHSTIETNKQTGPMENKFLLKKSSVLPSKRVASSPLRNDNKSKVNPIGSVASASKPSMVAANNKSRVLLTSKSLATPKNVVANSTDKNEKLIEEYKYRLQKLQNDEMIWTKERQSLLEKMNNTENYKIEMIKENEMLREQLKEAQSKLNEKNIQLRSKEIDVNKLSDRVLSLENELRNMEIELDRNKKRNDTNLQSMGTISSYSIPSSTVSSNYGVKSLSSALPFKEEEDVRRKEDVNYERRSSESIGDLPHRVNSLNIRPYRKNGTGVSSVSDDLDIDFNDSFASEESYKRAAAVTSTLKARIEKMKAKSRREGTTRT