wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear receptor coactivator 3 (NCoA-3) (EC 2.3.1.48) (ACTR) (Amplified in breast cancer 1 protein) (AIB-1) (CBP-interacting protein) (pCIP) (Class E basic helix-loop-helix protein 42) (bHLHe42) (Receptor-associated coactivator 3) (RAC-3) (Steroid receptor coactivator protein 3) (SRC-3) (Thyroid hormone receptor activator molecule 1) (TRAM-1) (Q9Y6Q9)
Organism: Homo sapiens (Human)
Function: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit.
Subcellular location: Cytoplasm. Nucleus. Note=Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus.
Interaction partners:
- CREB-binding protein
- Histone acetyltransferase p300
- Estrogen receptor
- Histone-arginine methyltransferase CARM1
- Nuclear receptor coactivator 2
- Estrogen receptor beta
- Androgen receptor
- Nuclear receptor coactivator 1
- Retinoic acid receptor RXR-alpha
- Progesterone receptor
Sequence:
MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC
Protein: BTB domain-containing protein (Q38DB4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPRSAGVRERQKRTREDSKTSGQLHKRQKVLPATATHLADDTSAEPFSQEDVDRENLTNHGPLAAYSSSSVMEAASLRNELKEHVSRCQLIVRNVGSLVQQRESSTAAMATLPSLCSISPREVVRLNVGGEIFTVPLQLLLKKDGGDTYFDMLFRYGAAGGEDSPYPTSFQPPLLDDTGALFIDRDPGTFRFILNYLRGSRMLSMLSEDRLSMLKTDAQYFQLHGLIKELSDESKETGIKFNPGPGVNLERNKFRVVYSIATIGENFLITGCHRITFEILNSEYVGIGLISDMCVMSDQEFHKTLHCCVYYMTGVFYSNFPHHRKEDRLEALDKGDFVSLMVDMNKRVAEYTLKGSVKTIPLGNARKLRFAVVMKMNSRIRIVPEEEARKLPLFRRRLYSSDVDSVDNALSLADERDGFTQLSQNSGAGAVELPTAMTLFSQLQQQQHQRQLPPPQGAVQDSGDPNAVDPSLPFLDDGNGGTVRPLTLDFTAEDIFPVDVDETEAFHHRSAPQEGE
Protein: Cytotoxic and regulatory T-cell molecule (Class-I MHC-restricted T-cell-associated molecule) (CD antigen CD355) (Q149L7)
Organism: Mus musculus (Mouse)
Function: Mediates heterophilic cell-cell adhesion which regulates the activation, differentiation and tissue retention of various T-cell subsets. Interaction with CADM1 promotes natural killer (NK) cell cytotoxicity and IFNG/interferon-gamma secretion by CD8+ T-cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM1 in vivo. Regulates CD8+ T-cell proliferation in response to T-cell receptor (TCR) activation. Appears to be dispensable for CD8+ T-cell-mediated cytotoxicity. Interaction with SCRIB promotes the late phase of cellular polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG, IL17 and IL22 production. By interacting with CADM1 on CD8+ dendritic cells, regulates the retention of activated CD8+ T-cells within the draining lymph node. Required for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells. Interaction with CADM1 promotes the adhesion to gut-associated CD103+ dendritic cells, which may facilitate the expression of gut-homing and adhesion molecules on T-cells and the conversion of CD4+ T-cells into CD4+ CD8+ T-cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18329370, ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:24687959}; Single-pass type I membrane protein {ECO:0000255}. Note=In a subset of CD4+ T-cells, colocalizes with SCRIB at the immunological synapse during the late phase of T-cell activation. {ECO:0000269|PubMed:18329370}.
Interaction partners:
- Cell adhesion molecule 1
- Nectin-2
Sequence:
MWWGALSLLFWVPVQAAFLKMETVTVEEGQTLTLTCVTSQTKNVSLQWLAPSGFTIFLNQHPALKSSKYQLLHHSATQLSISVSNVTLREEGVYTCLHYGSSVKTKQVRVTVLVTPFQPTVEALVLRRQNGEKSVVLKCSTERSKPPPQITWLLGEGLEIYGELNHEFEADGKICNTSSMLIARAYGKNSTVHCIIQHEGLHGRKLVAPFQFEDLVADQETSDQETSDAPEQSSLSSQALQQPTSTVSMMENSSIPETDKEEKEHATQDPGLSTEASAQHTGLARRKSGILLLTLVSFLIFILFIIVQLFIMKLRKAHVVWKKESEISEQALESYRSRSNNEETSSQENSSQAPQSKRCMNYITRLYSGAKTKKSAQHWKLGGKHSRVPESIV
Protein: scyllo-inositol 2-dehydrogenase (NAD(+)) (EC 1.1.1.370) (P40332)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the reversible NAD(+)-dependent oxidation of scyllo-inositol (SI) to 2,4,6/3,5-pentahydroxycyclohexanone (scyllo-inosose or SIS). Is required for SI catabolism that allows B.subtilis to utilize SI as the sole carbon source for growth. Cannot use NADP(+) instead of NAD(+).
Interaction partners:
- Inosose isomerase
- scyllo-inositol 2-dehydrogenase
- Inosose dehydratase
- 5-deoxy-glucuronate isomerase
- 3D-
- Uncharacterized oxidoreductase YfiI
- Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase
- scyllo-inositol 2-dehydrogenase
- Uncharacterized HTH-type transcriptional regulator YisR
- Uncharacterized oxidoreductase YrbE
Sequence:
MEHQVRCAVLGLGRLGYYHAKNLVTSVPGAKLVCVGDPLKGRAEQVARELGIEKWSEDPYEVLEDPGIDAVIIVTPTSTHGDMIIKAAENGKQIFVEKPLTLSLEESKAASEKVKETGVICQVGFMRRFDPAYADAKRRIDAGEIGKPIYYKGFTRDQGAPPAEFIKHSGGIFIDCSIHDYDIARYLLGAEITSVSGHGRILNNPFMEQYGDVDQALTYIEFDSGAAGDVEASRTSPYGHDIRAEVIGTEGSIFIGTLRHQHVTILSAKGSSFDIIPDFQTRFHEAYCLELQHFAECVRNGKTPIVTDIDATINLEVGIAATNSFRNGMPVQLDVKRAYTGM
Protein: Large ribosomal subunit protein mL52 (39S ribosomal protein L52, mitochondrial) (L52mt) (MRP-L52) (Q7JWG9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q86TS9}.
Interaction partners:
- Large ribosomal subunit protein mL55
- GH05406p
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein mL38
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL1m
- Large ribosomal subunit protein mL42
- Large ribosomal subunit protein uL14m
- Small ribosomal subunit protein mS31
- Large ribosomal subunit protein uL13m
Sequence:
MLKITKICLASSATSTAQRSIALTAPRAIDQKWRAAKGLPENPNAFGPLTNLPDYTYLDGRPTPLGANQKRRLIKQQEIATRIVELSGELEFAKQRHERLKANAESEKQRLIRSKLKPKGHFLLKK
Protein: Ferric uptake regulation protein (B6EHL8)
Organism: Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
Sequence:
MSDNNQALKKAGLKVTLPRLKILEILQQPESQHISAEDLYKKLIDIGEEIGLATVYRVLNQFDDAGIVTRHHFEGGKSVFELATQHHHDHLVCLDCGKVIEFSDDLIEERQKDIANKYNVRLTNHSLYLYGHCITGDCIENTTAHNG
Protein: SLIT-ROBO Rho GTPase activating protein 2B (A0A286YEY3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTCSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENLDATSDKQRLMEMYNNVFCPPMKFEFQPHMGDMASQLCAQQPVQSELLQRCQQLQSRLSTLKIENEEVKKTMEATLQTIQDIVTVEDFDVSDCFQYSNSMESVKSTVSETFMSKPSIAKRRANQQETEQFYFTVRECYGF
Protein: Nicastrin (Q54JT7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Probable gamma-secretase subunit PEN-2
- Gamma-secretase subunit Aph-1
- Presenilin-A
- Presenilin-B
Sequence:
MKIKNYFIIVFIIIVLSTDVISSQSSIEDKMYTSLNSYPCTRIMTLNGQIGCSSSHGGDSGILYLIDSDESYHNYFSYNQQKDIIVVFDSNYFNKTLVLEMYSKKKMNGALVLTDIGKTYPYSPEDQYPIKQFGLYPDSNLNWNPNGDGFTYMNFPFPMFALELKTSIIIRNLSTINRDGKYPAYGAELDSFMQGAINAETCLRRGFCEPVGGQSIWSSFSEVIDQSKPIILVMLPIDATAFFRDLATGTDQSGYALTVLLSMLNTLQGVDKTKWDKEVIFAMWNSERWGYVGSTNFVNDLLNFNCTSLDSNNQNSCSSPPMLDLTFEQIKFENIYAIIEFNQIGRPVNSGKKTPNKLDIYNLVFHPNGGAGANQLMDVFSQSTQSYENSTIQFQKTTQNELPPCSSMSFIKEINKKSAPNFIGTLVITDHDYQYNNPYFGDEQDNSGNINTTTSTLFDMVQVFSKSIDLLAGGNGTVKVDDLFIREINVCLTQSITCNWVTKLMSTFPYNPIPNFYSGVYGVSPVNHITPIETRFIFRMATYLTQHRTNATNCTSDNDCDTSSSICVNKVCLYSNTHYHNAISLAFSFDNSKSSWTIVNTSYPVFVESNWDYTTVRLFQVGSYANEIWFLVSGLIELLLSVGIIFYIKKYLSKRYKLL
Protein: Huntingtin-interacting protein K (Huntingtin yeast partner K) (Q9NX55)
Organism: Homo sapiens (Human)
Function: Component of several N-terminal acetyltransferase complexes. Inhibits the N-terminal acetylation activity of the N-terminal acetyltransferase NAA10-NAA15 complex (also called the NatA complex). Has chaperone-like activity preventing polyglutamine (polyQ) aggregation of HTT in neuronal cells probably while associated with the NatA complex. May play a role in the NatA complex-mediated N-terminal acetylation of PCNP.
Subcellular location: Nucleus {ECO:0000269|PubMed:20154145}. Cytoplasm {ECO:0000269|PubMed:20154145}. Note=Within the NatA/HYPK complex, may localize to ribosomes. {ECO:0000269|PubMed:20154145}.
Interaction partners:
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 50
- Huntingtin
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- N-alpha-acetyltransferase 11
- Testis-specific protein 10-interacting protein
- N-alpha-acetyltransferase 60
Sequence:
MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN
Protein: Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) (Q8AX86)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03205}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000256|HAMAP-Rule:MF_03205}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000256|HAMAP-Rule:MF_03205}.
Interaction partners:
- Very long chain fatty acid elongase 6
- Elongation of very long chain fatty acids protein 6
- Elongation of very long chain fatty acids protein 7
- Elongation of very long chain fatty acids protein 7
- Elongation of very long chain fatty acids protein 2
- Acyl-CoA 6-desaturase
- 3-hydroxy-3-methylglutaryl-CoA lyase.
- Very-long-chain 3-oxoacyl-CoA reductase-B
- 20beta-hydroxysteroid dehydrogenase type 2
- Very-long-chain 3-oxoacyl-CoA reductase-A
Sequence:
METFSHRVNSYIDSWMGPRDLRVTGWFLLDDYIPTFIFTVMYLLIVWMGPKYMKNRQAYSCRALLVPYNLCLTLLSLYMFYELVMSVYQGGYNFFCQNTHSGGDADNRMMNVLWWYYFSKLIEFMDTFFFILRKNNHQITFLHVYHHATMLNIWWFVMNWVPCGHSYFGATFNSFIHVLMYSYYGLSAVPALRPYLWWKKYITQGQLVQFVLTMFQTSCAVVWPCGFPMGWLYFQISYMVTLILLFSNFYIQTYKKRSGSRKSDYPNGSVNGHTNGVMSSEKIKHRKARAD
Protein: Polyadenylate-binding protein (PABP) (A3KFU5)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
Sequence:
MNAAASSYPMASLYVGDLHSDVTEAMLYEKFSPAGPVLSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVMKGKPIRIMWSQRDPSLRKSGVGNVFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYAFVHFETQEAADKAIEKMNGMLLNDRKVFVGRFKSRKEREAELGAKAKEFTNVYIKNFGEEVDDGNLKELFSQFGKTLSVKVMRDSSGKSKGFGFVSYEKHEDANKAVEEMNGKEMSGKAIFVGRAQKKVERQAELKRKFEQLKQERISRYQGVNLYIKNLDDTIDDEKLRREFSPFGSITSAKVMLEDGRSKGFGFVCFSSPEEATKAVTEMNGRIVGSKPLYVALAQRKEERKAHLTNQYMQRVAGMRALPASAILNQFQPAAGGYFVPAVPQAQGRPPYYTPNQLAQMRPNPRWQQGGRPQGFQGMPSALRQSGPRPALRHLAPTGNAPASRGLPTTAQRVGVPTAVPNLAPRAAVAAAAPRAVAPYKYASSVRSPHPAIQPLQAPQPAVHVQGQEPLTASMLAAAPPQEQKQMLGERLFPLIQTMHSNLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHHAKKEAAQKVGTVAAATS
Protein: Uteroglobin (Club cell phospholipid-binding protein) (CCPBP) (Club cells 10 kDa secretory protein) (CC10) (PCB-binding protein) (Secretoglobin family 1A member 1) (P17559)
Organism: Rattus norvegicus (Rat)
Function: Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2.
Subcellular location: Secreted.
Interaction partners:
- Surfactant protein C
- Pneumo secretory protein 1
- Pulmonary surfactant-associated protein B
- Pulmonary surfactant-associated protein A
- Secretoglobin, family 3A, member 1
- Aquaporin-5
- Pulmonary surfactant-associated protein D
- Keratin, type II cytoskeletal 5
- Tumor protein 63
- Homeobox protein Nkx-2.1
Sequence:
MKIAITITVLMLSICCSSASSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV
Protein: Gzmm protein (B7ZP17)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEVCWSLLLLLALKTLWAGNRFETQIIGGREAVPHSRPYMASLQKAKSHVCGGVLVHRKWVLTAAHCLSEPLQNLKLVLGLHNLHDLQDPGLTFYIREAIKHPGYNHKYENDLALLKLDRRVQPSKNVKPLALPRKPRSKPAEGTWCSTAGWGMTHQGGPRARALQELDLRVLDTQMCNNSRFWNGVLIDSMLCLKAGSKSQAPCKGDSGGPLVCGKGQVDGILSFSSKTCTDIFKPPVATAVAPYSSWIRKVIGRWSPQSLV
Protein: Protein GLUTAMINE DUMPER 2 (Q9SW07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable subunit of an amino acid transporter involved in the regulation of the amino acid metabolism. Stimulates amino acid export by activating nonselective amino acid facilitators.
Subcellular location: Membrane {ECO:0000269|Ref.8}; Single-pass membrane protein {ECO:0000269|Ref.8}.
Interaction partners:
- Probable E3 ubiquitin-protein ligase LOG2
- Probable E3 ubiquitin-protein ligase LUL2
- Probable E3 ubiquitin-protein ligase LUL1
- Cysteine proteinase RD21A
- Protein DA1-related 2
- Amino acid transporter ANT1
- E3 ubiquitin-protein ligase AIRP1
- WAT1-related protein At1g44800
- E3 ubiquitin-protein ligase RHA2B
- WAT1-related protein At2g40900
Sequence:
MQTMEGRQYNYQDSINASSSMVVPHSPWHSPVPYLFGGLAAMLALICVALLILACSYWRLSGSAERDLEAGDDAKPDNDTNKTKHTEMPEKFLVIMAGDVRPTYLATPATRSEQSCTCGDHNEEEGRRG
Protein: Calponin homology domain-containing protein (Q9XXA2)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Zygote defective protein 9
- Kinesin-like protein
- CAP-Gly domain-containing linker protein 1 homolog
- Tubulin alpha chain
- Dynein heavy chain, cytoplasmic
- Kinesin-like protein
- Exchange factor for Arf-6
- Protein CLASP-1
- Gamma-tubulin complex component
- Protein CLASP-3
Sequence:
MVVNVFISAVTTDTLSRKEAVAWVNNLLKSHFTKVEEMASGAAYCQLTHLLFNAINLKKVKFNPRSEPDVLNNWKVLTTTWKDLGIDKPVDVEKMKKAKFQDNMEFLQWFYKFYNANLTTEPEEYDAVGARFGEDLPALKGSTGSRPVAAPARPVAAAPPKPRPAAPAVAAPAVKASVPPTVRNGTRPAPATSAGTRRADPSASEELLKQEIEKHKAASDEWETTAKEMETEREYYYSILQRVESLANEAEESGSSTVDVAALKTILYAGNEDTEQVDEIENEHLVESLQANLDDTETF
Protein: Propanediol utilization protein PduV (Q9XDM6)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: May play a role in the spatial distribution of the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation, perhaps being involved in cytoskeleton dynamics. This subunit is directly targeted to the BMC (By similarity). Might bind GTP (Probable).
Subcellular location: Bacterial microcompartment {ECO:0000305|PubMed:25646976}. Note=Probably found on the exterior of the BMC. {ECO:0000305|PubMed:25646976}.
Interaction partners:
- Bacterial microcompartment shell protein PduU
- Bacterial microcompartment shell protein PduT
- Phosphate propanoyltransferase
- Bacterial microcompartment shell protein PduK
- Corrinoid adenosyltransferase PduO
- Propanediol dehydratase large subunit
- Propanediol dehydratase medium subunit
- Propanal dehydrogenase
- Propanediol dehydratase small subunit
- Bacterial microcompartment shell protein PduB
Sequence:
MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPFSPGFTAPMNRPTIGLVTKADLAEPQRISLVAEWLTQAGAQQIFITSALNNSGLDAVLDFLNSKEPLCLTK
Protein: Vacuolar protein sorting-associated protein 54 (CPF1 genetically-interacting protein 1) (Temperature-sensitive clathrin synthetic mutation protein 3) (Q12071)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. Seems also to be involved in protein transport from Golgi to the plasma membrane and is required for the integrity of the actin cytoskeleton.
Subcellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Mitochondrion membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=May also be mitochondrial.
Interaction partners:
- Vacuolar protein sorting-associated protein 52
- Vacuolar protein sorting-associated protein 53
- Vacuolar protein sorting-associated protein 51
- t-SNARE affecting a late Golgi compartment protein 2
- GTP-binding protein YPT6
- t-SNARE affecting a late Golgi compartment protein 1
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 3
- Protein transport protein DSL1
Sequence:
MSISETPHNKSQGLQKAAGRPKIVVPEGSPSRNSDSGSFTIEGDTSLNDDLLSISGSVTPRARRSSRLSLDSITPRRSFDSRTLSVANSRSFGFENETHSGSMDFSPLGNNSIYEIVMNTRRKNWLNYPTVADIPQVSLSKNDLDDHWKTHVIEYVKNIKSDYQIFQSTNNIRNMNQMEQLKELREGENMHEESFEANLRQGDAELINSIPDFYFSDKFQLDNPRTFHKVLDAIDLFLTKLDMKRQAERDEAFSELRDRLNDFLDIVETLLVTEISKSSHKFFHALSEVDNIQKRALDTMSELKELAQNIKTIDAENIRKKISHLEMIFKRKNVEKLEQGLLQAKLVLNKTDECKSMYEENKLDNCLELIKSIDYLIKGDDSINEDVQSWTRCWPYKLSNLRTIPALSATREFLTNMKIEIGGKFSLQLSILLIDDLRSFCKSIKPKETLHRIQTGSNDKKQTIFTDNFSSKITELIVRLNRCEELTSAFDLYREKSITELKSIIKIYLPTENAHADNNHDEKHLNNGSTSGSKLSRLIKEQTPAEFQSMLVNIFTHALEALRRLYGHQKLLLDISLNELASVKSPNENQHNMITQLDIRTGINEIIRIIQLRTGKIIAVRRELNLSLRYDYFLKFYAICVIFIQECEVLSGEFLTKYLSNVLASQIKHYANAQSSKNYRNIKKKIDAEEWIPYIVDSSIQSDVNDIVSSIDIDPLSWTTILDMVGGSHDCENGRSEDKEKDEGNETYQGHRKSVVVGDKTFVASSSLLATIEVIKELMVLSINLPSIYLSNFEKLCYDALQYYNSSAMASVTQPGNSLLKTGRNLSIMGESLDCLAEFVIIVQRFYQRLSNSNRDFEPFDASHYTTLLGQFQASSNKIYMANAPPPPV
Protein: Proto-oncogene vav (p95vav) (P27870)
Organism: Mus musculus (Mouse)
Function: Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.
Interaction partners:
- B-cell linker protein
- Tyrosine-protein kinase ZAP-70
- Growth factor receptor-bound protein 2
- Lymphocyte cytosolic protein 2
- Tyrosine-protein kinase SYK
- Cell division control protein 42 homolog
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- SH2/SH3 adapter protein Nck1
- Tyrosine-protein kinase BTK
- Tyrosine-protein kinase ITK/TSK
Sequence:
MELWRQCTHWLIQCRVLPPSHRVTWEGAQVCELAQALRDGVLLCQLLNNLLPQAINLREVNLRPQMSQFLCLKNIRTFLSTCCEKFGLKRSELFEAFDLFDVQDFGKVIYTLSALSWTPIAQNKGIMPFPTEDSALNDEDIYSGLSDQIDDTAEEDEDLYDCVENEEAEGDEIYEDLMRLESVPTPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFMKPLQRFLKPQDMETIFVNIEELFSVHTHFLKELKDALAGPGATTLYQVFIKYKERFLVYGRYCSQVESASKHLDQVATAREDVQMKLEECSQRANNGRFTLRDLLMVPMQRVLKYHLLLQELVKHTQDATEKENLRLALDAMRDLAQCVNEVKRDNETLRQITNFQLSIENLDQSLANYGRPKIDGELKITSVERRSKTDRYAFLLDKALLICKRRGDSYDLKASVNLHSFQVRDDSSGERDNKKWSHMFLLIEDQGAQGYELFFKTRELKKKWMEQFEMAISNIYPENATANGHDFQMFSFEETTSCKACQMLLRGTFYQGYRCYRCRAPAHKECLGRVPPCGRHGQDFAGTMKKDKLHRRAQDKKRNELGLPKMEVFQEYYGIPPPPGAFGPFLRLNPGDIVELTKAEAEHNWWEGRNTATNEVGWFPCNRVHPYVHGPPQDLSVHLWYAGPMERAGAEGILTNRSDGTYLVRQRVKDTAEFAISIKYNVEVKHIKIMTSEGLYRITEKKAFRGLLELVEFYQQNSLKDCFKSLDTTLQFPYKEPERRAISKPPAGSTKYFGTAKARYDFCARDRSELSLKEGDIIKILNKKGQQGWWRGEIYGRIGWFPSNYVEEDYSEYC
Protein: Proprotein convertase subtilisin/kexin type 6 (H3BLN2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDPQVKWLQQQEVKRRVKRQARSDSLYFNDPIWSNMWYMHCTDKNSRCRSEMNVQAAWKRGYTGKNVVVTILDDGIERNHPDLAPNYDSYASYDVNGNDYDPSPRYDASNENKHGTRCAGEVAASANNSYCIVGIAYNAKIGGIRMLDGDVTDVVEAKSLGIRP
Protein: DNA polymerase kappa, putative (EC 2.7.7.7) (Q384G4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCGGEENGGLDQAHVSYSGSASEQNIAEMIVDPSASRQPTAFQLTLDCNKAGMGNVDKERVEAIIRNVSEGSSFLMNEQRKAEGREKQLQELKRKSSLFTQLLDGERNAAQRKQWELKVSKIEQELEATRRLXTYIHLDMDMFYAAVXIKKHPEYAAIPLAI
Protein: Syndecan-4 (SYND4) (Amphiglycan) (Ryudocan core protein) (P31431)
Organism: Homo sapiens (Human)
Function: Cell surface proteoglycan that bears heparan sulfate. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
Subcellular location: [Isoform 1]: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:9169435}. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000269|PubMed:9169435}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Fibronectin
- Protein kinase C alpha type
- Fibroblast growth factor 2
- Syndecan-2
- Frizzled-7
- Syntenin-1
- Glypican-1
- Thrombospondin-1
- PDZ domain-containing protein GIPC1
- Tudor-interacting repair regulator protein
Sequence:
MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA
Protein: Complement C8 gamma chain (A0A8I6AEX7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MWTSGLCFLWHWTVDSDLEQCTPPPPCPITYCHRTAMLSPGAVLFFTLILMASSLGQRTRKPYGSTSPISTIQAQANFNAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHIAPQGAAMAASTFRKLDGICWQVRQLYGITGVPGRFLLQAPRARGPVHVVVAETDYQSFAILYLEQARRLSVKLYTRTLPVSDSALNAFEERVRGANLTEDQIFFFPKYDNTYKREHRPLLHSFITLFKLRDNSEFQGQALQHLVLY
Protein: Probable phospholipase A2 homolog 2 (EC 3.1.1.4) (Q9XG81)
Organism: Oryza sativa subsp. japonica (Rice)
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Os02g0676000 protein
- Os06g0712300 protein
- Os04g0615100 protein
- Os09g0513100 protein
- Lipoxygenase
- Phospholipase A2 homolog 3
- Os05g0357800 protein
- Os01g0307562 protein
- phospholipase D
- phospholipase D
Sequence:
MRFFLKLAPRCSVLLLLLLVTASRGLNIGDLLGSTPAKDQGCSRTCESQFCTIAPLLRYGKYCGILYSGCPGERPCDALDACCMVHDHCVDTHNDDYLNTMCNENLLSCIDRVSGATFPGNKCNVGQTASVIRGVIETAVFAGKILHKRDDGQ