wanglab/gogpt-training-data huggingface dataset:
Protein: Casein kinase I isoform gamma-3 (CKI-gamma 3) (EC 2.7.11.1) (Q62763)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Regulates fast synaptic transmission mediated by glutamate (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- Protein smoothened
- cAMP-dependent protein kinase catalytic subunit alpha
- Beta-adrenergic receptor kinase 1
- G protein-coupled receptor kinase 3
Sequence:
MDNKKKDKDKSDDRMARPSGRSGHSTRGTGSSSSGVLMVGPNFRVGKKIGCGNFGELRLGKNLYTNEYVAIKLEPMKSRAPQLHLEYRFYKQLGSGDGIPQVYYFGPCGKYNAMVLELLGPSLEDLFDLCDRTFSLKTVLMIAIQLISRMEYVHSKNLIYRDVKPENFLIGRPGNKAQQVIHIIDFGLAKEYIDPETKKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCENFPEEMATYLRYVRRLDFFEKPDYDYLRKLFTDLFDRKGYMFDYEYDWIGKQLPTPVGAVQQDPALSSNREAHQHRDKIQQSKNQSADHRAAWDSQQANPHHLRAHLAADRHGGSVQVVSSTNGELNTDDPTAGRSNAPITAPTEVEVMDETKCCCFFKRRKRKTIQRHK
Protein: Rifin (B9ZSH6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHCYNILLFSFTLIILLLSSSQVNNQMNHYNTAHMKNTEPIKSYRSLCECELYTSMYDDDPEMKEILHDFDRQTSQRFEEYNERLLENKQKCKEQCEKDIQKIILKDKLEKELMDKFATLHTDIQSDAIPTCVCEKSIADKMEKECLRCAQNLGGIVAPSSGVLAGIAEGALIVWKPAAIKAAKAAAAKAASDAATQAGMNAVRLEIKKLLEMFTGKPGYVDLLPIVKESTYKNGSALVDSAKKLFVESGKLEGLDRMPVFYNTVIDYPGPSNIKGFGKIGSDAYEAAFTSQKGTLEATKVGEVNTTYGGCQTAITASVIAIVVIILIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Short-form leptin receptor 3 (R9QTF6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKTMILSAMLTFLVHILIISHSAVLVEPVEVSPHGDLLDLPWQTELCCSSTPAQLHHGGEEEDTGSAPSDTGHPHTLQCLFRNFTSTLGPHPESELSRATCWDILCRVDETWDNVICDLKHPATSSDTSIPGSVALSLQHLTTLPDIEVNSTHGTDCVGEDSITCSVALHVVSSIVVVTANVSNTTAGPLVMLSVPPRTSQRLWKPSPPLNLTHTQTTEGELILSWSDPQPHASPVQLSYEVRYNTSQSTSHPNWLHVNVSGAQWVSLTGLRPGLQYTLQIRSHHPALPHLWSDWSQQHRIRLENVTYLPERVVASFGDSVTVYCVCNDLRVNASTMVWILNSRDRLPKSQYAAVNDRVSKITVRPSEQRLSGTLHCCQPFGEMYSCNYHYSTIYIKDPVIDISCVTSGDLDSMTCRWNNLPIGGINFMSRVADLSCDVMEEAERVGVPVGVVRQAKCESSGYRGVKSCNLQPIRVTSCYKLWMEAKTDNSTRSHPVYITPMDHVKPHPPSRLEAVSMPSGVLKLAWVPPELPIYDMQYQVRYALSTGKGPSILAVLALQTESWAEVLEPDVCGVYNVQVRCMHINGSGTWSDWSHLLYTTTHNSRAPDQGPDFWRVFQEDPASMQTNVTLLFEHSPIVEPTYCVEELVVQHQDSGDTVTEERIGLVSSYSFEWRGEVHSVTVKAQNSQGSSTRNTHMTLDRHPKRKSLLKNTLNGNVLYL
Protein: All-trans-retinol dehydrogenase [NAD(+)] ADH4 (EC 1.1.1.105) (Alcohol dehydrogenase 2) (Alcohol dehydrogenase 4) (Alcohol dehydrogenase class II) (Alcohol dehydrogenase II) (Q64563)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the NAD-dependent oxidation of either all-trans-retinol or 9-cis-retinol (By similarity). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (By similarity). Also catalyzes the reduction of benzoquinones (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MGTQGKVITCKAAIAWKTDSPLCIEEIEVSPPKAHEVRIKVIATCVCPTDINATNPKKKALFPVVLGHECAGIVESVGPGVTNFKPGDKVIPFFAPQCKKCKLCLSPLTNLCGKLRNFKYPTIDQELMEDRTSRFTSKERSIYHFMGVSSFSQYTVVSEANLARVDDEANLERVCLIGCGFTSGYGAAINTAKVTPGSACAVFGLGCVGLSAVIGCKIAGASRIIAIDINSEKFPKAKALGATDCLNPRDLDKPVQDVITELTGGGVDFSLDCAGTAQTLKAAVDCTVVGWGSCTVVGAKVDEMNISTVDMILGRSVKGTFFGGWKSVDSVPNLVTDYKNKKFDLDLLVTHALPFDKINDAIDLMNQGKSIRTILTF
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q960T3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNGSVRFCEKCKIIKPDRAHHCSVCSCCVLKMDHHCPWVNNCVNFYNYKYFVLFLGYALVYCLYVAFTSLHDFVEFWKVGAGQLNASGMGRFHILFLFFIAIMFAISLVSLFGYHIYLVLVNRTTLESFRAPIFRVGGPDKNGYNLGRYANFCEVFGDDWQYWFLPVFSSRGDGYSYPTSSDQSRVSTSSPTQRYDAMGDTTTSRLDGNPTDKLIGASPLDTTNHHHNQSPHQVRSTSVLPTQLLQIQPPSTCRDELNERQQKLANGQSLDCSTPAAMSSPDERGVNGAAVYIEMIGDHPLTSADPAKGFPRPPNGDLPV
Protein: ChpADiploid state maintenance protein chpA (C8VTA5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- SGT1 and CS domain protein
- Heat shock protein 90
- Puatative oxidoreductase
Sequence:
MATKCVHKGCGKVFTDPEEPCVYHPGPPVFHEGQKGWNCCKPRVLTFEEFMEIPPCTTGKHSAVDDTPAPAQKKDTPAESQPPVAAPVPVRDSGVPRPVAHSPAIPPPSNAPTPVPEEPESDDPELAIPENATCRRRGCGGTYKPDVSRDEERCVYHPGQPVFHEGSKGWSCCKRRVLEFDEFLKIEGLRGEEEASFCREGQACWRGEG
Protein: HUWE1-associated protein modifying stress responses 1 (Telomere attrition and p53 response 1 protein) (Q14CZ0)
Organism: Homo sapiens (Human)
Function: Acts as a central player within a network of stress response pathways promoting cellular adaptability. The E3 ligase HUWE1 assists HAPSTR1 in controlling stress signaling and in turn, HUWE1 feeds back to promote the degradation of HAPSTR1. HAPSTR1 represents a central coordination mechanism for stress response programs. Functions as a negative regulator of TP53/P53 in the cellular response to telomere erosion and probably also DNA damage. May attenuate p53/TP53 activation through the E3 ubiquitin ligase HUWE1.
Subcellular location: Nucleus {ECO:0000269|PubMed:35776542}. Cytoplasm {ECO:0000269|PubMed:35776542}.
Interaction partners:
Sequence:
MEERKEEGEAEIQEHGPEHWFSKWERQCLAEAEQDEQLPPELQEEAAAAAQPEHKQQKLWHLFQNSATAVAQLYKDRVCQQPGLSLWVPFQNAATAVTNLYKESVDTHQRSFDIGIQIGYQRRNKDVLAWVKKRRRTIRREDLISFLCGKVPPPRNSRAPPRLTVVSPNRATSTETSSSVETDLQPFREAIALHGLSGAMASISVRSSTPGSPTHVSSGSNASRRRNGLHDVDLNTFISEEMALHLDNGGTRKRTSAQCGDVITDSPTHKRNRMI
Protein: Unique cartilage matrix-associated protein [Cleaved into: Unique cartilage matrix-associated protein C-terminal fragment (Ucma-C) (Gla-rich protein) (GRP)] (Q6NWB6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Thrombospondin 4a
- Fin bud initiation factor
- Gamma-glutamyl carboxylase.
- Secretion-regulating guanine nucleotide exchange factor
- Plakophilin 3b
- Zinc finger protein 536
- Copine-8
- Copine 8.
- Matrix Gla protein.
- Anoctamin
Sequence:
MSWTQPALLTCLLVLSAITLFDGADSAVSDKRDAVNPQGALRKIFMPEADAASFFKRRSRRAVKTQDEINAEQRQRLAADERRREYHEEQRNKYENYAEEENDEQDERTREKTEQWREFHYDGLDPSYEYNRHTI
Protein: NAD--protein ADP-ribosyltransferase modA (EC 2.4.2.31) (RNA polymerase ADP-ribosylase modA) (P39421)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: ADP-ribosyltransferase that efficiently ADP-ribosylates both alpha subunits of host RNA polymerase RPOA. The ModA-induced ADP-ribosylation of RPOA alpha subunits inhibits transcription from viral early promoters.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04141}. Note=This protein is injected from the virion into the bacterial cell. {ECO:0000255|HAMAP-Rule:MF_04141}.
Interaction partners:
Sequence:
MKYSVMQLKDFKIKSMDASVRASIREELLSEGFNLSEIELLIHCITNKPDDHSWLNEIIKSRLVPNDKPLWRGVPAETKQVLNQGIDIITFDKVVSASYDKNIALHFASGLEYNTQVIFEFKAPMVFNFQEYAIKALRCKEYNPNFKFPDSHRYRNMELVSDEQEVMIPAGSVFRIADRYEYKKCSTYTIYTLDFEGFNL
Protein: Ent-copalyl diphosphate synthase 4 (EC 5.5.1.13) (Terpene synthase 5) (IrTPS5) (A0A1W6QDJ1)
Organism: Isodon rubescens (Rabdosia rubescens)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSSSSIVTSLLRPTTAADGVLPRQMAQVNSSCNIWRSKAKVGGINYFNPGNIKCVEEVHKSRQVVVAALKSLEYETEKPTNQDVVSEKMRVLSERIETMLQNMDEGEISISPYDTAWVALVEDTDGRPQFPTSLEWISNNQLADGSWGDRKFVIYDRILNTLACVVALTTWNMHPHKCNRGLRFIRDNMEKLENENEELMPIGFEVVFPSLIEAAQKLGIEIPHIDSPCIKKIQAMRDFKLKRIPMELLHKKPTSLLHSLEGMQGLVWEKLLDFRSDGSFLCSPSSTAYALQHTKDELCLQYLLKAVKKFNGGVPNVYPVDMFEHLWCVDRLQRLGICRYFRVQIKEMLDYVYKYWTDKGICWARNTNVQDVDDTAMGFRLLRMHGYDVSTDVFKQFEKAGEFCCFPGQSTHAITGMYNVYRTSQIMFDGEDILADAKNYSATFLHQKRLANELVDKWIITKDLPGEVGYALDVPFFASLPRLEARFFLEQYGGDDDVWIGKTLYRMPYVNSDTYLELAKLDYKKCQAVHQLEWKSIQKWYRDCKLGEFGLGEKRLLLAYFLAASTAFEPEKKGERLAWAKTAFLVETIASQQLSHEQKREFADEFEHGSSLNMENGGSYKTRTRLVEILSNTVSQLSFETLVAEGRDIKQQLSNTWQKWLKTWEEGGNLGEAEAQLLLQTLHLSSGLDESSFSHPKYHQLLEVTCKVCNQLRLFQNRKAHDAQGGISDLVIGTTFQIEASMQELVKLVFTKSSEDLDSITKQSFFAIARSFYYTAYCDAGAINSHIYKVLFENID
Protein: Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14] (Q9TZP5)
Organism: Caenorhabditis elegans
Function: Putative inactive caspase. In the germline, binds caspase ced-3 zymogen and prevents ced-3 autoactivation. Does not affect the caspase activity of mature ced-3 and ced-4-mediated mature ced-3 activation. Negatively regulates germline apoptosis by inhibiting autocleavage of caspase ced-3. Involved in fertility.
Subcellular location: [Isoform b]: Cytoplasm {ECO:0000269|PubMed:19575016}.
Interaction partners:
- Cell death protein 4
- Apoptosis regulator ced-9
- Cell death protein 3
- histone acetyltransferase
Sequence:
MMCEDASDGKKIDETRKYRNNRSSKCRAIIINNVVFCGMEKRIGSDKDKKKLSKLFERLGYQSTSYDNLKSSEILETVRQFTQSNHGDSLIITIMSHGDQGLLYGVDGVPVQMLDIIDLMCTASLAKKPKWLMCVCCRGDRIDRAVRCDGFIDNFFDRFPKFFQFMKSKFPSHQTSSSQADLLVSFSTSPGFLSFRDETKGTWYIQELYRVIIENAKDTHLADLLMETNRRVVEKYEADKVVIVCKQAPEFWSRFTKQLFFDV
Protein: Protein transport protein Sec61 subunit alpha-like 2 (Q90YL4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61619}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- SEC63 homolog, protein translocation regulator.
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit gamma
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL23
- 40S ribosomal protein S15
- Small ribosomal subunit protein uS13
- FAU ubiquitin-like and ribosomal protein S30 fusion b
Sequence:
MAIKFLEVIKPFCAVLPEIQKPERRIQFKEKVLWTAITLFIFLVCCQIPLFGIMSSDSADPFYWMRVIMASNRGTLMELGISPIVTSGLIMQLLAGAKIIEVGDTPKDRALFNGAQKLFGMIITIGQAVVYVMTGMYGDPSEMGAGICLLIIIQLFVAGLIVLLLDELLQKGYGLGSGISLFIATNICETIVWKAFSPTTVNTGRGTEFEGAIIALFHLLATRTDKVRALREAFYRQNLPNLMNLIATIFVFAVVIYFQGFRVDLPIKSARYRGQYNTYPIKLFYTSNIPIILQSALVSNLYVISQMLSTRFSGNFLVNLLGTWSDTSTGGPARAYPVGGLCYYLSPPESFGTVLEDPIHAIIYIIFMLGSCAFFSKTWIEVSGSSAKDVAKQLKEQQMVMRGHRETSMVHELNRYIPTAAAFGGLCIGGLSVMADFLGAIGSGTGILLAVTIIYQYFEIFVKEQSEVGSVGALLF
Protein: Two-component response regulator ORR8 (Type A response regulator 8) (OsRR8) (Q4GZK3)
Organism: Oryza sativa subsp. indica (Rice)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Interaction partners:
Sequence:
MSSPHVLVVDDTHVDRHVVSMALMRHNVRVTAVESVMQALMFLDSEHDVDMIVSDYCMPDMTGYNLLMEVKKSPKLAHLPVVIASSDNIPERIRKCLDGGAKDYILKPVKIVDVPRIMKYI
Protein: Dipeptidyl peptidase 10, isoform A (EC 3.4.14.1, EC 3.4.14.2, EC 3.4.14.4, EC 3.4.14.5) (Dipeptidyl peptidase 10, isoform C) (RE27507p) (Q9VMB4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037847}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037847}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MPEQDNYDDELVSSNPNQRNWRGILIALLVIIIVLALIVTSVVLLTPPDEGPRVKGQRIKLQDIVDGLFVPQHSNGSWIDGEEFLYQDHLGRICLLNAANRSERVLMSNVTFKTLSPFTFTISADKRYLLLAQNVVKLFRHSYLAQYTLYDIQTSESIKLRHSPHQDEWPYLHYARFTPAGNALVWVQSYDIYYREEVRSASVHRITHDAVPGVVYNGIPDWLYEEEILHANNAIWMSDNGQLMLYATFNDTHVQEQHFAWYGTTGPSAGGAAAAAAVGAGGAGTGSPGAGGSNPHASLYPEIRSLRYPKPGTQNPTVTLRVADLKDPLKVHITDLHPPQIIANEDHYFSSASWVSHSKIAVVWLNRPQNISVVSVCKAPLFQCIETHRVSGDGRGWVDTVAVPLFAANASIYVAISPLRDGLFGYFRHIVHVDIDKNRVLPLTHGPYEVNRLLHWDQLDNWIYFLGTPERLPSQQHLYRVSALPARQGQALRSPDCLTCPAVSQWSEGYDEGHTKSPPKLVTAWDDDWEDSEEAEAQPPQPALPVEQQPPGRGQSAPLPPPPSDCLYHEAKFPISRQAKYVLIDCLGPVVPTSILYGLKSAAADSAKTKRHSTQQEEPPTEGGDEKPGEEPKSQFLELLVIVQNNTRLKEKMAKTAMPQIKTFPVMISGGYHAQVRLYLPPVLREDEITRYPTILHVYSGPGSQLVTDHWHVDWNTYLSGSKDYIVVEIDGRGSAGQGYQLLHEVYKRLGSVEVSDQLEVSEYLRDNLHFIDSRRMGVWGWSYGGYTAALALAGQQSIFQCGISVSPVTNWKLYDSTYAERYLSFPNVTDNYKGYEESDLSKYVDNLRDRQFLLVHGTADDNVHVQQSMVLARSLTSKGVLYKQQIYPDEGHSLSGVKRHLYRSMTAFFEDCFKKLVPPESKAGLGNGGDMQQQ
Protein: Ribosome assembly protein 4 (Notchless protein homolog 1) (Ribosome biogenesis factor rsa4) (O74855)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in ribosome biogenesis. Required for processing and efficient intra-nuclear transport of pre-60S ribosomal subunits. Interacts with the AAA-ATPase Midasin, which is essential for the ATP-dependent dissociation of a group of nonribosomal factors from the pre-60S particle.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Midasin
- Ribosome biogenesis protein nsa2
- Nucleolar GTP-binding protein 2
- Ribosome biogenesis protein NOP53
- Probable nucleolar GTP-binding protein 1
- Protein sda1
- Pre-rRNA-processing protein crb3/ipi3
- Ribosome biogenesis protein rlp24
- Probable metalloprotease arx1
- Ribosome biogenesis protein erb1
Sequence:
MATLLPPKSKRQKKESLNPTTIEIPEKFPLVNVQFRASDDSNELASLLVPGNSSVRQLEALLNQLLENSDDPVPYNFALHHEDETIEIQDNLYTSVFHNGLMKTEDHLTLLYTPQAVFRVRAVTRCTASMNGHDGTIISAQFSPSTSSRLVTGSGDFTARLWDCDTQTPIATMKGHTNWVSCVAWAPDASIIATGSMDNTIRFWDPKKGSPIGDALRRHTKPIMALCWQPLHLAPDSGPYLLASGSKDNTVRIWNVKLRTLLFTLSGHTAPITCVRWGGQNWIYSSSYDKTIRIWDAKDGKCLHILKGHAARVNHLSLSTEHVLRSGAYDHTDFKPKSFSDERRKAKERYEACLKQSGERLVSASDDLQLILWDPQKSTKPITKMHGHQKVVNHASFSPDGRCIATASFDSSVRLWDGKTGKFLATLRGHVAAVYQCAWSTDSRLLVSSSQDTTLKVWDVRSKKMKFDLPGHEDQVFAVDWSPDGQRVASGGADKAVRIWSH
Protein: AP-3 complex subunit mu (AP-3 adaptor complex mu3A subunit) (Adaptor-related protein complex 3 subunit mu) (Mu-adaptin 3A) (Mu3-adaptin) (P38153)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. Required for the transport via the ALP pathway, which directs the transport of the cargo proteins PHO8 and VAM3 to the vacuole.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:10559961, ECO:0000269|PubMed:14562095}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10559961, ECO:0000305}; Peripheral membrane protein {ECO:0000269|PubMed:10559961, ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:14562095, ECO:0000305}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000269|PubMed:10559961, ECO:0000305}.
Interaction partners:
- AP-3 complex subunit sigma
- AP-3 complex subunit delta
- AP-3 complex subunit beta
- AP-1 complex subunit gamma-1
- AP-1 complex subunit sigma-1
- AP-1 complex subunit mu-1-I
- AP-2 complex subunit sigma
- AP-2 complex subunit beta
- AP-1 complex subunit beta-1
- AP-2 complex subunit alpha
Sequence:
MYLSFYITDTKNKLIFQYLLGATAPSFKHLWTRVQSTCPQLLEDSSSDDYLDHSMVGRDLEVYKYFSVINKLNYWCLASTSKSKGPLDCFTFLETIDRILLEYFDKDKLSIKKIVNNYDRISLIFNCCVEAGEPNVSDMLYVNKIKEAVPERSDLSKFISSTAHNLQQAVQLPQQRQQQLQQNQISRGSNSLIENEEIVPWRTSRASKHENNELYVDLLETFHVVFEKKKSHLRLLTGSIHGIVDVRSYLNDNPLVAVKLNTMGNDIGIPSLHDCVEINDGVFSPSNITFIPPDGKFRLLEYSVDLSSQVKQSGVRMNSIGLMSLHFQNGLGKDSDEFELSLNIENFKKVSQVDDLKIDLQFNVENADPNEIAYKIKILRNTHGRFENSIIMGQGQWIFDKSTATGTVPVLRGCIEYENTGPNFTKKVDLQTVSLEYSYIGQSASGIYVEAIDIVSGLTIGKNTKLYKGAKYKTQTGNFQVRL
Protein: Oligogalacturonide ABC transporter, permease component (E0SDC7)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}. Cell membrane {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Oligogalacturonide ABC transporter, permease component
- Predicted rhamnose oligosaccharide ABC transport system, substrate-binding component
- Oligogalacturonide ABC transporter, ATPase component
- Predicted rhamnose oligosaccharide ABC transport system, substrate-binding component
- ABC transporter, inner membrane component
- ABC transporter, membrane spanning protein
- Multiple sugar ABC transporter, membrane-spanning permease protein MsmF
- ABC-type sugar transport systems, permease component
- Sugar ABC transport system, permease protein
- Galactan ABC transport system, permease component
Sequence:
MADIHSPLSAQAIAAAEVRRTLRREKINAGFRYTILLAVGILMLYPLAWMFSASFKPNHEIFTTLSLWPAHATWDGFINGWKTGTEYNFGHYMINTFKYVIPKVALTVISSTIVAYGFARFEIPWKNFWFATLIATMLLPSTVLLIPQYIMFREMGMLNSYLPLYVPVAFATQGFFVFMLIQFLRGVPRDMEEAAQIDGCNSWQVLWYVVVPILKPAIISVALFQFMWSMNDFIGPLIYVYSVDKYPIALALKMSIDVTEGAPWNEILAMASISILPSIIIFFMAQRYFVQGVTSSGIKG
Protein: Methyltransferase like 17 (G3V353)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MENQVQTLTSYLWSRHLPVEPEELQRRARHLEKKFLENPDLSQTEEKLRGAVLHALRKTTYHWQELSYTEGLSLVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDFGSGTGSVTWAAHSIWGQSLREYMCVDRSAAMLVLAEKLLKGGSESGEPYIPGVFFRQFLPVSPK
Protein: Rhesus theta defensin-1/3 subunit A (RTD-1 subunit A) (RTD-1a) (Demidefensin-2) (RTD-3) (P82270)
Organism: Macaca mulatta (Rhesus macaque)
Function: RTD-1 and RTD-3 have similar antimicrobial activities against the Gram-positive bacteria S.aureus 502A and L.monocytogenes, the Gram-negative bacteria S.typhimurium and E.coli ML35, and the fungi C.albicans 16820 and C.neoformans 271A.
Interaction partners:
- Defensin, alpha 4, corticostatin
- Neutrophil defensin 1
- B-defensin2-like
- Beta/alpha-defensin C-terminal domain-containing protein
- Defensin beta 4A
- Beta-defensin-like domain-containing protein
- Rhesus theta defensin-1/2 subunit B
- Beta/alpha-defensin C-terminal domain-containing protein
- Defensin alpha 6
- Ribonuclease P/MRP subunit p14
Sequence:
MRTFALLTAMLLLVALHAQAEARQARADEAAAQQQPGTDDQGMAHSFTWPENAALPLSESAKGLRCICTRGFCRLL
Protein: Protein aardvark (Suppressor of amiB protein 16) (Q54I71)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required to regulate pattern formation during multi-cellular stages of development and for the formation of adherens junctions. Plays a structural role during the regulation of stalk formation. Involved in cell signaling. Required for spore-cell differentiation. Overexpression increases number and size of cell junctions and reduces spore-cell formation.
Subcellular location: Cytoplasm. Cell junction.
Interaction partners:
Sequence:
MNDCGSLFNKKLFKMNLLFKHLKLQQHLKLQQKPLLNNSSINNNINNNNNNNNNNNSNNDSNNTNTNIFNNSFLNSDLIERLIIKFTIGYLKNNITEDYIEQILLENQNNFIKSTTTSNYILEENNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSSSSSSSILSKFNKLEEDNELELQKKQKQQLEQQEEELFNQFNFLEGIEDQNDFLSEQETIQKIKFLIKMTAKSMSNYSSPNTLIPSVSKTYISPFGLSSNGSTNNHNNNNNNNHHHHSNNGNLIESSNNVNNQLNVSNYNNNNSNHYDENNQFDIFLIPTEMLVHLLSFLSANDLWRISLTCKRIWYIVDVFKFWELLFEQTCPRIYYAMQFNSRWSNPTSFQSKMILCYIDRLPTDNYKNFDKSDESGQIKKIIGVMNENLHNPMILRETCYILKRLSYRQRKEDEHESLIARYGGISLILQAMKNHPYDAGVQEDACGALGNLTCDSPNNMGLYSNDNYLSVVEQGGIQLILQAMKNHMMNPGVQYNTSFVLRNLARNDVSESRVAIEGGIQSIATAMKNHPNHIGIQTQGCGALRNLGCNDSNKVLSAKEGGIGLILRAMRSFSSHPDLQLNGCGALRNLARNEDNKNMISRQNGIQLVLGAMSNHPDDPDVQDEGCAALINLAYQDEANEETIAREGGINLILKAMRNHPFHSGVQMQGRGALKNLSCNPKNKLTIARSGGIELMNIAMQNHPNFANRFLELSRILQVALEDGNI
Protein: Rab-3-interacting molecule unc-10 (Rim) (Uncoordinated protein 10) (Q22366)
Organism: Caenorhabditis elegans
Function: Regulates the efficiency of a post-docking step of the release pathway. Acts after vesicle docking likely via regulating priming. May regulate the conformational changes in syntaxin. Binding of vesicles via rab-3[GTP] to Rim may signal the presence of a docked synaptic vesicle. Rim may then signal to unc-13 to change the conformation of syntaxin from the closed to the open state. Syntaxin could then engage synaptobrevin on the docked vesicle to form SNARE complexes and to prime the vesicle for release. Not required for the development or the structural organization of synapses. May play a role in regulating entry into the dauer state.
Subcellular location: Synapse {ECO:0000250}.
Interaction partners:
- Phorbol ester/diacylglycerol-binding protein unc-13
- Variant SH3 domain protein
- Liprin-alpha
- Ras-related protein Rab-3
- ELKS/RAB6-interacting/CAST family member 2
- Acetylcholine regulator unc-18
- Syntaxin-1A homolog
- Synaptobrevin-1
- Putative complexin-1
- ATP-grasp domain-containing protein
Sequence:
MDDPSMMPDLSHLSAEEREIIENVFKRQKDEEAKETQISQKASEELSELDKQITERKETSKKLVGTQDDAICQICQKTKFADGIGHKCFYCQLRSCARCGGRAQSKNKAIWACSLCQKRQQILAKTGKWFQPEEQPQPKISGSEPSPSPQPLTDDNVPEPQQRRAEPPDKMNTPNYQNNQQPRGMGMQPNHNQTQQNFMNQNQNSNQHPNQNHNQNQMQNPHQNQNHVQNNHQGANNHQQNNRRAMQQQPMSQNQANQINQMNQNQNQQQSHNQNMTQNQRNQTGPQNQQRTNDSRTMKQTPQQQPSQYQNNVGAAHQHHNQHGQQEQHHQQMNEQRTDNNRMRENTNGQGGMFNRQPSLEQTTPMNKYNHVEDDGMNQRPTFYTGNSENDQRQFDGQMQQGSQQNNQNQNQNNRNLRKNTVSRVTEEDYASSSNFESKKQRNNSSQSQSNTQGVRACPSTDDHLNRVKNRLHRQLRSMSSSEEDIIAGGGGNTLKMSTSAVVASGGKTAFHDDMGASNVQRLSEECNSEKDLLRYIYGDHKNSDSSSLGAGVGGSGGGGVLSGNSVLKSKSHALLKGSYQGGLDMQANRRRDKSLSLSPSRNDHFGTGSISGGDLLASRIRTFLSHPVTWQPSADQKKLIGHMILHRTENSAANGDLGLKIVGGRRTDTGKLGAFITQVKPGSVADTIGRLRPGDEVVEWNGQSLQNATYEQVYDSIAASRYDTSVELIVSRSAIIPGGDDFLNLTPSQMSSSAYSRVPSAYPSQFQRQLPNPDLFLDIHPALQQLSLPHSQSAVFPHNNTLTSRNRSTSSYYYSDVPDLGVPSNREMQESQAFGTGHIFGRIEVSFVYSHHDRQLSVALVRGFDLPPRSDGTPRNPYVKIFLLPDRSEKSRRQSAVIAETLMPVWDEVFYYNGLTEPMLLQRVLELTVWDYDKFGTNSFLGETLIDLASVPLDGEHSLMCILVDMDDDNPLRTVISIFKFHVIILTFLQRLKLRKASYNAPTRRPQSELNYYDHSSNYYDHISQNIDKQPHHHHLAPNDEENDEYIDDDELENDIDLATGGGARKSRTYRREKGMHGGHGYADWTQNHQRQSGYTSDHGYGRQNMIGRAYNRRQQRRPRSATALSQMEREDMYDPTRKHRDDNEYSMRESVRHGSQYYLGDQPLYEDGRYKISQGQMTPKQHNQQHQPHPLSQAHQQQQTAGVQPQHHQGFQQQQHPQQPNQQMQQMQPPMPNQGYYSDGSETLSVHSTNSMPTTMTTVNRRNMNANNTSNDNTSFAETPTANTNRVPIKETKQNSLASSSSVAGGGSAANNVMKERKKSLMTRFIPGRGAEGKRTGFARSEEVGIPGNLSSDRLTEPTPPFLKQASKESTDSAHSDKFARQCWLPVLADGPLGTFVDNLGPGQVVGRQVLASPVLGEIQIALMAGRSGIDVEIIKAKNLVVKPGVKVCPAPYVKVYLMEGKQCIAKAKTNAATKTTSPLFQQHLIFNDSPKKKTLQVTVLGDYGRMERKVFMGISQIRLEDLELGSQPLIGWYKLFHSSSLAGTGPVRKDSDVSVGGAQQ