wanglab/gogpt-training-data huggingface dataset:
Protein: Osteoclast-associated immunoglobulin-like receptor (Osteoclast-associated receptor) (hOSCAR) (Polymeric immunoglobulin receptor 3) (PIgR-3) (PIgR3) (Poly-Ig receptor 3) (Q8IYS5)
Organism: Homo sapiens (Human)
Function: Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation.
Subcellular location: [Isoform 1]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- TYRO protein tyrosine kinase-binding protein
- Tyrosine-protein kinase SYK
- Dendritic cell-specific transmembrane protein
- Tumor necrosis factor ligand superfamily member 11
- Nuclear factor of activated T-cells, cytoplasmic 1
- Tartrate-resistant acid phosphatase type 5
- Cathepsin K
Sequence:
MALVLILQLLTLWPLCHTDITPSVPPASYHPKPWLGAQPATVVTPGVNVTLRCRAPQPAWRFGLFKPGEIAPLLFRDVSSELAEFFLEEVTPAQGGIYRCCYRRPDWGPGVWSQPSDVLELLVTEELPRPSLVALPGPVVGPGANVSLRCAGRLRNMSFVLYREGVAAPLQYRHSAQPWADFTLLGARAPGTYSCYYHTPSAPYVLSQRSEVLVISWEGEGPEARPASSAPGMQAPGPPPSDPGAQAPSLSSFRPRGLVLQPLLPQTQDSWDPAPPPSDPGV
Protein: Lathosterol oxidase (EC 1.14.19.20) (C-5 sterol desaturase) (Delta(7)-sterol 5-desaturase) (Delta(7)-sterol C5(6)-desaturase) (Lathosterol 5-desaturase) (Sterol-C5-desaturase) (Q9EQS5)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol in cholesterol biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:4019441}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 7-dehydrocholesterol reductase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Squalene synthase
- Lanosterol synthase
- Delta
- 3-beta-hydroxysteroid-Delta
- Lanosterol 14-alpha demethylase
- Ergosterol biosynthesis 28 homolog
- Methylsterol monooxygenase 1
- Transmembrane 7 superfamily member 2.
Sequence:
MDLVLSAADYYFFTPYVYPATWPEDNIIRQTVSLLVVTNLGAYILYFFCATLSYYFVYDHSLMKHPQFLKNQVSREIMFTVKSLPWISIPTVSLFLLELRGYSKLYDDIGDFPNGWIHLIMSVISFLFFTDMLIYWIHRGLHHRLLYKHIHKPHHIWKIPTPFASHAFHPVDGFLQSLPYHIYPFVFPLHKVVYLGLYVLVNVWTISIHDGDFRVPQIFRPFINGSAHHTDHHMLFDYNYGQYFTLWDRIGGSFKHPSSFEGKGPHSYVKNMTEKESNSLAENGCKSKKLCNGEFTKNE
Protein: Vesicle transport protein SFT2A (SFT2 domain-containing protein 1) (pRGR1) (Q8WV19)
Organism: Homo sapiens (Human)
Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEKLRRVLSGQDDEEQGLTAQVLDASSLSFNTRLKWFAICFVCGVFFSILGTGLLWLPGGIKLFAVFYTLGNLAALASTCFLMGPVKQLKKMFEATRLLATIVMLLCFIFTLCAALWWHKKGLAVLFCILQFLSMTWYSLSYIPYARDAVIKCCSSLLS
Protein: Endonuclease III homolog 2, chloroplastic (AtNTH2) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2) (DNA glycosylase/AP lyase 2) (B9DFZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:19372224}.
Interaction partners:
- Endonuclease III homolog 1, chloroplastic
- Putative DNA glycosylase At3g47830
- N-glycosylase/DNA lyase OGG1
- DNA-
- DNA glycosylase superfamily protein
- At1g19480
- DNA-
- At3g50880
- DNA-
- Formamidopyrimidine-DNA glycosylase
Sequence:
MILTGAASTFPIVARVLNAMNRRMYAATTLSSAKSISAESLNLRSDSNSEAAHGASESETRVSLRKKRIKQDDLEPVKKCSARETKARKDMCGLPDIEDSPYKKTNGTASSRTRKLNSYIKSTEASPSASSIKTAGLGIPPENWEKVLEGIRKMKPSEEAPVNAVECDRTGSFLPPKERRFYVLIGTLLSSQTKEHITGAAVERLHQNGLLTPEAIDKADESTIKELIYPVGFYTRKATNVKKVAKICLMEYDGDIPRTLEELLSLPGVGPKIAHLVLHVAWNDVQGICVDTHVHRICNRLGWVSKPGTKQKTSSPEETRVALQQWLPKGEWVAINFLLVGFGQTICTPLRPHCGTCSITEICPSAFKETPSTSSKLKKSIKSKKL
Protein: CCN family member 5 (Connective tissue growth factor-like protein) (CTGF-L) (WNT1-inducible-signaling pathway protein 2) (WISP-2) (Q9Z0G4)
Organism: Mus musculus (Mouse)
Function: May play an important role in modulating bone turnover. Promotes the adhesion of osteoblast cells and inhibits the binding of fibrinogen to integrin receptors. In addition, inhibits osteocalcin production (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Proto-oncogene Wnt-1
Sequence:
MRGNPLIHLLAISFLCILSMVYSQLCPAPCACPWTPPQCPPGVPLVLDGCGCCRVCARRLGESCDHLHVCDPSQGLVCQPGAGPSGRGAVCLFEEDDGSCEVNGRRYLDGETFKPNCRVLCRCDDGGFTCLPLCSEDVRLPSWDCPRPRRIQVPGRCCPEWVCDQAVMQPAIQPSSAQGHQLSALVTPASADGPCPNWSTAWGPCSTTCGLGIATRVSNQNRFCQLEIQRRLCLSRPCLASRSHGSWNSAF
Protein: Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (A0A0U1RNF2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASSSRESSFSSCSSSCDLDDEGVRGTCEDASLCKRFAVSIGYWHDPYIEHLVRQSKERKAPEINRGYFARVHGVSQLIKAFLRKTECHCQILNLGAGMDTTFWKLKDEGLLPNKYFEVDFPMIVTRKLLTIKSKPLLFRPIMELHPEDTLQMGNHMLDSKRYAIIGADLRDLSELEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAASSFETAMFINYEQVNMDDRFGQIMIENLRRRSCDLAGVETCKSLESQKERLLLNGWETASAVNMMELYSGLPRAEVNRIESLEFLDEMELLEQLMRHYCLCWATRGGQELGLKEITY
Protein: Tachykinin-like peptide-III (P.nigriventer tachykinin peptides III) (PnTkP-III) (U29-ctenitoxin-Pn1c) (U29-CNTX-Pn1c) (P86300)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDR
Protein: DDB1- and CUL4-associated factor 5 (WD repeat-containing protein 22) (Q80T85)
Organism: Mus musculus (Mouse)
Function: Is a substrate receptor for the CUL4-DDB1 E3 ubiquitin-protein ligase complex (CRL4), involved in the ubiquitination of a set of methylated non-histone proteins, including SOX2. The complex CRL4-DCAF5 is also involved in the ubiquitination of methylated DNMT1 and E2F1 (By similarity).
Interaction partners:
- DNA damage-binding protein 1
- DDB1- and CUL4-associated factor 4
- DDB1- and CUL4-associated factor 12
- DDB1- and CUL4-associated factor 10
- DNA damage-binding protein 2
- DDB1- and CUL4-associated factor 11
- DDB1- and CUL4-associated factor 6
- DET1- and DDB1-associated protein 1
- Short transient receptor potential channel 4-associated protein
- Cullin-4B
Sequence:
MKRRAGLGGSMRSVVGFLSQRGLHGDPLLTQDFQRRRLRGCRNLYKKDLLGHFGCVNAIEFSNNGGQWLVSGGDDRRVLLWHMEQAIHSRVKPIQLKGEHHSNIFCLAFNSGNTKVFSGGNDEQVILHDVESSETLDVFAHEDAVYGLSVSPVNDNIFASSSDDGRVLIWDIRESPHGEPFCLANYPSAFHSVMFNPVEPRLLATANSKEGVGLWDIRKPQSSLLRYGGNLSLQSAMSVRFNSNGTQLLALRRRLPPVLYDIHSRLPVFQFDNQGYFNSCTMKSCCFAGDRDQYILSGSDDFNLYMWKIPADPEAGGIGRVVNGAFMVLKGHRSIVNQVRFNPHTYMICSSGVEKIIKIWSPYKQPGCTGDLDGRIEDDSRCLYTHEEYISLVLNSGSGLSHDYANQSVQEDPRMMAFFDSLVRREIEGWSSDSDSDLSESTILQLHAGVSERSGYTDSESSASLPRSPPPTVDESADNAFHLGPLRVTTTNAVASTPATPTCEDASSRQQRLSALRRYQDKRLLALSNESDSEENVCEAELDTDLFPRPRSPSPEDGSSSPSSSTSSEDEEELNQRRATTRQRNAMRRRQKTARDERPTGPAKSTNTYIGEDNYDYPQIKVDDLSPSPDSSPERSASTLDVQPSRAPPAANMESVERKIYKAYKWLRCSYISYSNNKDGETSLMAEEADEGRAGTSHKDNPTPSSSKEACLTATAQRDQDLPSEGCSSDACKEGTSAGNPNSGAGHEHSSHPWAEVPEGTSQDTNNSGPLEHSFETKKLNGKALSKALSSRAEEPPASPGPKASGSTLNSASGNCPRTQSDDSEERSLDTVCANHNNGRLHPRPLHPHNNGQSSGELETVACSSPGHLDTDHDSPSLTGTFLHKDCCGSEMACETPSAGMREDPPDPSGLDSSKVVHGQSGLKRHRIELEDTESENSSSEKKLKT
Protein: Catalase (EC 1.11.1.6) (Q5B0L2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- FMN-dependent dehydrogenase family protein
- Kynureninase 1
- Kynureninase 2
- propanoyl-CoA C-acyltransferase
- propanoyl-CoA C-acyltransferase
- Lipid transfer protein, putative
Sequence:
MGQNDDQKTYRYNESPVYTTSNGCPVMDPQASQRVGPNGPLLLQDFNLIDLLAHFDRERIPERVVHAKGAGAYGEFEVTDDISDITVIDMLKGVGKKTKTFVRFSTVGGEKGSPDSARDPRGFACKFYTEEGNWDWVFNNTPVFFLRDPSKFPMFIHTQKRNPQTNLKDATMFWDYLSTHQEAVHQVMHLFSDRGTPYSYRHMNGYSGHTYKWIKPDGTFNYVQLHLKTDQGNKTFTDAEATRLAAENPDWHTQDLFNAIARGEYPSWTCYVQTLSPEQAEKFRWNIFDLTKVWPQSEVPLRRFGRFTLNKNPENYFAEVEQAAFSPSHLVPGVEPSADPVLQARLFSYPDTHRHRLGTSNYQSIPVNCPLRAFTPFHRDGAMSVNGNHGANPNYPSTFRPLQYKPVKASQEHEKWAGSVVTEQLPVTDEDFVQANGLWKVLGRQPGQQENFVGNVAGHLCNAHPRVRQATYGMFRRVNADLGKRIEKATEKKATEARARL
Protein: FI04466p (Q9VMM7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- U3 small nucleolar RNA-associated protein 18 homolog
- Nucleolar protein 10
- RE67794p
- KRR1 small subunit processome component homolog
- Protein Aatf
- LD10780p
- LD47749p
- LD31322p
- FI03455p
- Probable U3 small nucleolar RNA-associated protein 11
Sequence:
MVQALDYDCEAQGQDIPQAIQLLGEMNSNVKQVTDLVEGMLQRVKRGELTTEYGLSFLEVKYHMLLDYLINLTYVVLRKCSGETIEGDPSIERLIEIRTVLEKIRPIDHKLRYQIDKLVKTATTGVSSSTDPILYKPNPDDMMSSAGGAGRDEDDGEDDSDEEDEDDDEEDEDEAGAAKMPRKAATAGKSGVYVPPRIKPVYYDGDERDADKEKKALDRAKKRAITSSMLQDLKEEYLDAPTEISSGSRAQQMLSQAQKEKQEYEETYLMRLPVTKAEKHRQRKLTTLGTLGDEILGEISRESALRGDGSKKRKLAKKGKGKKRGGKKRKFH
Protein: DnaJ homolog subfamily B member 1 (M0QZD0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIE
Protein: PLASMODESMATA CALLOSE-BINDING PROTEIN 4 (AtPDCB4) (Q93V72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:19223515}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19223515}. Cell junction, plasmodesma {ECO:0000269|PubMed:19223515}.
Interaction partners:
- Uncharacterized protein
- Protein PHLOEM PROTEIN 2-LIKE A9
- UDP-glycosyltransferase 87A1
- Alpha-glucan water dikinase 2
Sequence:
MSVLLPLCLIISMFTYSNAAYCLCKEGNEQVLQKAIDYACGNGADCTQIQPTGACYQPNTVKNHCDVAVNSYYQKKASSGATCDFNGAASPSTTPPSTASNCLTGSSSSGTPTTGTPTTGTPTSGTPTTGTPTTGTPTTGTPTSGTPTSGFPNTGTPNTGTNTGMPNSNGMPTSSSSSVFPGTTLGPTGSGGLGDPNAGEKLSVRTNTVVFLLTGVAAMLVI
Protein: Large ribosomal subunit protein uL2 (60S ribosomal protein L8) (P62917)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS4, X isoform
- Large ribosomal subunit protein P1
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein uS5
Sequence:
MGRVIRGQRKGAGSVFRAHVKHRKGAARLRAVDFAERHGYIKGIVKDIIHDPGRGAPLAKVVFRDPYRFKKRTELFIAAEGIHTGQFVYCGKKAQLNIGNVLPVGTMPEGTIVCCLEEKPGDRGKLARASGNYATVISHNPETKKTRVKLPSGSKKVISSANRAVVGVVAGGGRIDKPILKAGRAYHKYKAKRNCWPRVRGVAMNPVEHPFGGGNHQHIGKPSTIRRDAPAGRKVGLIAARRTGRLRGTKTVQEKEN
Protein: Gonadotropin subunit beta-2 (W5UK74)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU004069}.
Interaction partners:
Sequence:
MSVPASSFLLLCFLMNSFSPAQSYILPHCEPVNETVSVEKDGCPKCLVFQTAICSGHCFTKEPVYKSPFSSIYQHVCTYRDVRYETVRLPDCRPGVDPHVTYPVALSCECSLCTMDTSDCTIESLNPDFCMTQKEYILDY
Protein: Protein sidekick-2 (Q6V4S5)
Organism: Mus musculus (Mouse)
Function: Adhesion molecule that promotes lamina-specific synaptic connections in the retina and is specifically required for the formation of neuronal circuits that detect motion. Acts by promoting formation of synapses between two specific retinal cell types: the retinal ganglion cells W3B-RGCs and the excitatory amacrine cells VG3-ACs. Formation of synapses between these two cells plays a key role in detection of motion. Promotes synaptic connectivity via homophilic interactions.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8AV57}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV57}. Synapse {ECO:0000269|PubMed:20219992, ECO:0000305|PubMed:26287463}.
Interaction partners:
Sequence:
MFSSMWRLPLWTLLALHRIHSAGAQDDVPPYFKTEPVRTQVHLEGNRLVLTCMAEGSWPLEFKWLHNNRELTRFSLEYRYMITSLDRTHAGFYRCIVRNRMGALLQRQTEVQVAYMGSFEEGEKRQSVNHGEAAVIRAPRISSFPRPQVTWFRDGRKIPPSSRIAITLENTLVILSTVAPDAGRYYVQAVNDKNGDNKTSQPITLAVENVGGPADPIAPTIIIPPKNTSVVAGTSEVTMECVANARPLIKLHIVWKKDGAPLSSGISDYNRRLTIANPTVSDAGYYECEAMLRSSSVAPVTRGAYLSVLEPPQFVREPERHITAEMEKVVDIPCRAKGVPPPSITWYKDAALVEVGKLTRFKQRSDGGLQISGLLPDDTGMLQCFAHNAAGEAQTSTYLAVTSIAPNITRGPLDSTVIDGMSVVLACETSGAPRPAITWQKGERILASGSVQLPRFTLLESGSLLISPTHISDAGTYTCLATNSRGVDEASADLVVWARTRITKPPQDQSVIKGTQASMVCGVTHDPRVTVRYVWEKDGATLAVETNPRIRLDRNGSLHISQTWSGDIGTYTCRVLSAGGNDSRNAHLRVRQLPHAPEHPVATLSTVERRAINLTWAKPFDGNSPLMRYVLEMSENNAPWTILLASVDPEATSVMVKGLVPARSYQFRLCAVNDVGKGQFSKDTERVSLPEEPPTAPPQNVIASGRTNQSIMIQWQPPPESHQNGILKGYIIRYCLAGLPVGYQFKNITDADVNNLLLEDLIIWTNYEIEVAAYNSAGLGVYSSKVTEWTLQGVPTVPPGNVHAEATNSTTIRFTWNAPSPQFINGINQGYKLIAWEPAQEEEVTMVTARPNFQDSIHVGFVSGLKKFTEYFTSVLCFTTPGDGPRSSPQLVRTHEDVPGPVGHLSFNDILDTSLKVSWQEPGEKNGILTGYRISWEEYNRTNTRVTHYLPNVTLEYRVTGLTALTTYTIEVAAMTSKGQGQVSASTISSGVPPELPGAPTNLGISNIGPRSVTLQFRPGYDGKTSISRWVVEAQVGVIGEGEEWLLIYQLGNEPDARSMEVPDLNPFTYYSFRMRQVNIVGTSPPSQPSRKIQTLQAPPDIAPANVTLRTASETSLWLRWMPLPEMEYNGNPESVGYKIKYGRSDGHGKTLSHTVQDRVEREYTIEDLEEWTEYRVQVQAFNAIGSGPWSQAVVGRTRESVPSSGPTNVSALATTSSSMLVRWSEIPEADRNGLVLGYKVRYKEKDSDSQPRFWLVEGNSSRSAQLTGLGKYVLYEVQVLAFTRIGDGSPSHPPILERTLDDVPGPPMGILFPEVRTTSVRLIWQPPAAPNGIILAYQITHRLNATTANTATVEVLAPSARQYMATGLKPESVYLFRITAQTRKGWGEAAEALVVTTEKRDRPQPPSKPVVQQEDVKARSVLLSWEPGSDGLSPVRYYTIQTRELPSGRWALHSASVSHNASAFTVDRLKPFTSYKFRVKATNDIGDSEFSEESESLTTLQAAPDEAPTILSVTPHTTTSVLIRWQPPSEDKINGILLGFRIRYRELLYDGLRGFTLRGINNPGAKWAELTSLYSMRNLTRPSLTQYELDNLSKHRRYEIRMSIYNAVGEGPLSPPQEVFVGEAVPTAAPQNVAIHSATATQLDVTWEPPPLDNQNGDIQGYKIYFWEVQRRNLTERVKTLFLAENSVKLKNLTGYTAYMVSVAAFNAAGDGPRSTPTRGQTQQAAPSAPGSVKFSELTTTSVNVSWDAPQFPNGPLEGYRLVYEPCTPVDGVSKIVTVDVKGNSPLWLKVKDLAEGMTYRFRIKAKTFTYGPEIEANITTGPGEGAPGPPGVPIIVRYSSAIAIHWSSGDPGKGPITRYVIEARPSDEGLWDILIKDIPKEVTSYTFSMDILKPGVSYDFRVIAVNDYGFGTPSSPSQSVPAQKASPFYEEWWFLVVIALVGLIFILLLVFVLIIRGQSKKYSKKTDSGGNTKSGALGHGEMLSLDESSFPALELNNRRLSVKNSFCRKNGLYTRSPPRPSPGSLHYSDEDVTKYNDLIPAESSSLTEKPSEISDSQGSDSEYEVDTNTQKAHSFVNHYISDPTYYNSWRRQQKGISRAQAYSYTESDSGEPDHVTVPNSNSTQQGSLFRPKASRTPTPQNPPNPQSQQSTLYRPPSSLAPGSRAPIAGFSSFV
Protein: Velvet complex subunit B (C8VTS4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination. The velvet complex acts as a global regulator for secondary metabolite gene expression. Component of the velB-VosA heterodimeric complex that plays a dual role in activating genes associated with spore maturation and repressing certain development-associated genes. The velB-VosA complex binds DNA through the DNA-binding domain of vosA that recognizes an 11-nucleotide consensus sequence 5'-CTGGCCGCGGC-3' consisting of two motifs in the promoters of key developmental regulatory genes. The vosA-velB complex binds to the beta-glucan synthase fksA gene promoter in asexual spores for repression.
Subcellular location: Nucleus {ECO:0000269|PubMed:18556559}. Cytoplasm {ECO:0000269|PubMed:18556559}. Note=VeA increases the nuclear localization of VelB. {ECO:0000269|PubMed:18556559}.
Interaction partners:
- Protein-methionine methyltransferase laeA
- Developmental and secondary metabolism regulator veA
- Spore development regulator vosA
- C2H2 type master regulator of conidiophore development brlA
- Conidiophore development regulator abaA
- Sexual development regulator velC
- GATA-factor
- Uncharacterized protein
- Uncharacterized protein
- Importin subunit alpha
Sequence:
MYAVEDRAHSGHHPPPLSMDRIPPPSTMYPSSAGPSAMVSPAGQPEPESLSTVHDGRIWSLQVVQQPIRARMCGFGDKDRRPITPPPCIRLIVKDAQTQKEVDINSLDSSFYVVMADLWNADGTHEVNLVKHSATSPSISTAMSSSYPPPPHPTSSDYPASYQTNPYGQPVGQPVGQPVGYAGVGNYYGGSTQLQYQNAYPNPQAQYYQPMYGGMAQPQMPAAQPVTPGPGGMFTRNLIGCLSASAYRLYDTEDKIGVWFVLQDLSVRTEGIFRLKFSFVNVGKSVSDLPQSDIAEVINKGTAPILASTFSEPFQVFSAKKFPGVIESTPLSKVFANQGIKIPIRKDGVKGQGSRGRHSDEDDGLDNEY
Protein: Beta-soluble NSF attachment protein (SNAP-beta) (N-ethylmaleimide-sensitive factor attachment protein beta) (P85969)
Organism: Rattus norvegicus (Rat)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus.
Subcellular location: Membrane {ECO:0000269|PubMed:19343716}; Peripheral membrane protein {ECO:0000269|PubMed:19343716}.
Interaction partners:
- Vesicle-associated membrane protein 2
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Syntaxin-5
- Syntaxin-1A
- Vesicle-associated membrane protein 8
- Synaptobrevin homolog YKT6
- Multifunctional fusion protein
- Syntaxin-16
- Vesicle-fusing ATPase
- Vesicle transport through interaction with t-SNAREs homolog 1B
Sequence:
MDNAGKEREAVQLMAEAEKRVKASHSFLRGLFGGNTRIEEACEMYTRAANMFKMAKNWSAAGNAFCQAAKLHMQLQSKHDSATSFVDAGNAYKKADPQEAINCLNAAIDIYTDMGRFTIAAKHHITIAEIYETELVDIEKAIAHYEQSADYYKGEESNSANKCLLKVAAYAAQLEQYQKAIEIYEQVGANTMDNPLLKYSAKDYFFKAALCHFIVDELNAKLALEKYEEMFPAFTDSRECKLLKKLLEAHEEQNSEAYTEAVKEFDSISRLDQWLTTMLLRIKKSIQGDGEGDGDLK
Protein: Large ribosomal subunit protein uL18 (60S ribosomal protein L5) (A2RUM7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGFVKVVKNKAYFKRYQVKFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNRFGMDKIYEGQVEVTGDEYNVESIDGQPGAFTCYLDAGLARTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHIMGQNVADYMRYLMEEDEDAYKKQFSQYIKNSVTPDMMEEMYKKAHAAIRENPVYEKKPKKEVKKKRWNRPKMSLAQKKDRVAQKKASFLRAQERAAES
Protein: Cyclin-dependent kinase 5 activator 1 (p35) (Q22695)
Organism: Caenorhabditis elegans
Function: Activator of the kinase cdk-5 (By similarity). In several motor neurons, promotes the polarized trafficking of synaptic vesicles and dense-core vesicles. In the ventral nerve cord, regulates the synaptic localization of the glutamate receptor, glr-1. In DA motor neurons, regulates axonal transport of synaptic vesicle precursors by inhibiting dynein-mediated retrograde transport. Regulates the polarized distribution of dense-core vesicles in DB motor neurons. May regulate these processes in association with cdk-5. May also play a role in GABAergic synaptic vesicle localization in the ventral nerve cord.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20510931}. Cell projection, dendrite {ECO:0000269|PubMed:20510931}. Cell projection, axon {ECO:0000269|PubMed:20510931}. Note=Presynaptic localization in the axon and punctate localization in the dendrite. {ECO:0000269|PubMed:20510931}.
Interaction partners:
- Cyclin-dependent-like kinase 5
- Nuclear migration protein nudC
- Protein nud-2
- Cyclin-dependent kinase 17
- Lissencephaly-1 homolog
- Dynein heavy chain, cytoplasmic
Sequence:
MGANLTSPLPHHHRTQTTSVCNHLFSPGDGGPTFAPQRDSNTSSRSSSNAKESVLMQGWNWSKRNIQPVMSRRSLPKSGSSSEATSSKSSDSLVSFTRNVSTSTSSQYGKISISLDRNQNYKSVPRPSDTTTIIPNYYSLREEFRRGLQINTRQDLVNNNLASNDLSVIGSPKHVPRPRSVLRDDNANCDISPIAEQENVPSEASTSELLRGLGIFISNNCDVSDFDPAHLVTWLRSVDRSLLLQGWQDIAFINPANLVFIFLLVRDVLPDERHLIHTLEELHAWILSCLYVSYSYMGNEISYPLKPFLIGNDRNTFWNRCVAMVTSHSRQMLLLNSSSTFFSEVFTDLKHCSSSE
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (F4IK69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At2g35736
- Zinc finger CCCH domain-containing protein 14
Sequence:
MDDSCAVCAENLEWVGYGSCGHREVCSTCVVRLRFILNDRRCCICKTECPVVFVTKALGDYTKTISDFSTTFPSVPKEGRVGSFWYHEETNVYFDDLNHYTRIKAMCRLSCNLCNDTNKTRPKKEPNHCVRFKSVEHLKDHLNHQHKLHMCSLCLVGRKVFICEQKLFTKGQLNQHISSGDSEVDGSESERGGFTGHPMCEFCKRPFYGDNELYTHMSREHYTCHICQRLKPGQYEYYGNYDDLEVHFRSDHFLCEDETCLAKKFIVFQIEAELKRHNAIDHGGRMSRSQQNASLQIQASFQYPNSRRGRRRSSLREPNLVLLESQASYAFNDDNNLPQHVGRSGNSRLGESSFPPLSVQANQGQSRFGQNSESLVSNTTTTRQRHRANQGQSRFGQNSESLVSNTTTTRQRHQTNRSATSGSSQAWPALNRGPAEISITSRVQSSGASAQSQSRHHDRVESTRTLASAVPQDARTTVGGCSSGSSLSSANATKRNNHHSSSTPKMSETRSLAQPSHSDSPQISAVKNRRSSSTSANAGNIQVAQGVSDVQSDNKSLVEKIHASLGHDEELFMAFKNTSGKYRHGSIDARTYLEYVKGYGLSHLVLDMARLCPDPQRQKELIDTHNACLKGGNKGKAVKVESSSDSKGDRFVDTVRKLQFSDKSQDKDKDKDAYRSDKGKTKVTTLVNSSSAGVGLGDTGKQPKKTSKFLRTRLGEKSMAAVLDLRNSNPEPEPEPKNDNSKRSQNSPGGLPLRGAWKRGSAKLFV
Protein: Lon protease homolog, mitochondrial (EC 3.4.21.53) (Q09769)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:16823372}.
Interaction partners:
- ATP-dependent zinc metalloprotease YME1 homolog
- Mitochondrial inner membrane m-AAA protease component yta12
- GrpE protein homolog
- Probable mitochondrial-processing peptidase subunit alpha
- 10 kDa heat shock protein, mitochondrial
- Heat shock protein 78
- Intermediate cleaving peptidase 55
- Mitochondrial acidic protein mam33
- Heat shock protein 60, mitochondrial
- Probable ketol-acid reductoisomerase, mitochondrial
Sequence:
MITRLSGACLRRSGAKRNWPREHLVHRSLLASFSTTQRVLKCSVGPFRTSNVVFKSKEPKDNKPLDNKNDPKKTHNEDESHTNESLPSTDKKKKKDNDDFKQNLKSSSNKTEEKYSATQASKSKNDEFELGGEENEDEMPLNGEFNKNVPAKYSVPDVYPQLLALPIARRPLFPGFYKAIVTKNPSVSEAIKELIKKRQPYIGAFLLKDENTDTDVITNIDQVYPVGVFAQITSIFPAKSGSEPALTAVLYPHRRIRITELIPPKEDADSAASSDAAELETDKSSNLSSNGEVKSDLKQDNGKEEPEKEVESTPSILQNFKVSLVNVENVPNEPFKRQDPVIKAVTSEIMNVFKDIANVSPLFREQIANFSISQTSGNVFDEPAKLADFAAAVSAADHRELQEVLEATNIGDRLQKALYVLKKELLNAQLQHKINKEIEQKITQRHKEYLLTEQLKQIKRELGQELDSKEALVTEFKKRTESLSMPDHVKKVFNDELSKFQHLEPMAAEFNITRNYLDWITQLPWGKRSVENFDLDHAKEVLDRDHYGLKDVKDRVLELVAVGKLRGTMQGKIMCLVGPPGVGKTSVGKSIASALNREFFRFSVGGLTDVAEIKGHRRTYIGAMPGKIVQALKKVQTENPLILIDEIDKVGKSHQGDPASALLELLDSEQNSAFLDYYMDIPLDVSSVLFVCTANTIDTIPPPLLDRMEVIELSGYVSAEKVNIAKGYLIPQAKAACGLKDANVNISDDAIKGLISYYAHESGVRNLKKSIEKIFRKTSFSIVKEIDDELNSKEKSTGKSGKKTSPQSSEDAANKEASSVPLKVPDKVNIEIEEKDLTKYLGPPIYTSQRLYDTTPPGVVMGLGWTPMGGVSMYVETIVKNILSSNSTPSLERTGQLGDVMKESSEISYSFSKSFLSKHFPNNKFFEHARLHMHCPEGSISKDGPSAGITMATSLLSLALDTPVPATTAMTGELTLTGKILRIGGLREKTVAAKLSGMKEILFPKSNLADWEQLPDYVKEGLTGVPVAWYDDVFKRVFSNIDAEKCNNLWPNLIKSSSKQHQISPSH