wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger and BTB domain-containing protein 8B (Q8NAP8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEMQSYYAKLLGELNEQRKRDFFCDCSIIVEGRIFKAHRNILFANSGYFRALLIHYIQDSGRHSTASLDIVTSDAFSIILDFLYSGKLDLCGENVIEVMSAASYLQMNDVVNFCKTYIRSSLDICRKMEKEAAVAAAVAAAAAAAAAAAAAAAHQVDSESPSSGREGTSCGTKSLVSSPAEGEKSVECLRESPCGDCGDCHPLELVVRDSLGGGSADSNLSTPPKRIEPKVEFDADEVEVDVGEQLQQYAAPLNLAHVEEALPSGQAVDLAYSNYHVKQFLEALLRNSAAPSKDDADHHFSRSLEGRPEGAGVAMSSMMDVQADWYGEDSGDVLVVPIKLHKCPFCPYTAKQKGILKRHIRSHTGERPYPCETCGKRFTRQEHLRSHALSVHRSNRPIICKGCRRTFTSHLSQGLRRFGLCDSCTCVTDTPDDDDDLMPINLSLVEASSESQEKSDTDNDWPIYVESGEENDPAGDDSDDKPQIQPNLSDRETLT
Protein: V-type proton ATPase subunit a (Q9VE75)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- V-type proton ATPase subunit d 1
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase subunit B
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit H
- V-type proton ATPase subunit E
- V-type proton ATPase subunit
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase proteolipid subunit
Sequence:
MGDMFRSEEMALCQMFIQPEAAYTSVSELGETGCVQFRDLNVNVNAFQRKFVTEVRRCDELERKIRYIETEIKKDGIVLPDIQDDIPRAPNPREIIDLEAHLEKTESEMIELAQNEVNMKSNYLELTELRKVLENTQGFFSDQEVLNLDSSNRAGGDNDAAAQHRGRLGFVAGVINRERVFAFERMLWRISRGNVFLKRSDLDEPLNDPATGHPIYKTVFVAFFQGEQLKNRIKKVCTGFHASLYPCPSSHNEREEMVRNVRTRLEDLKLVLSQTEDHRSRVLATVSKNLPSWSIMVKKMKAIYHTLNLFNMDVTKKCLIGECWVPTNDLPVVQKALSDGSAAVGSTIPSFLNVIDTNEQPPTFNRTNKFTRGFQNLIDAYGVASYRECNPALYTCITFPFLFAVMFGDLGHGLILVLFGAWMVLCERKLARIRNGGEIWNIFFGGRYIILLMGLFAMYTGLVYNDVFSKSMNLFGSRWFNNYNTTTVLTNPNLQLPPNSSAVGVYPFGMDPVWQLADNKIIFLNSFKMKLSIIFGVLHMVFGVCMSVVNFTHFKRYASIFLEFVPQILFLLLLFGYMVFMMFFKWFSYNARTSFQPETPGCAPSVLIMFINMMLFKNTEPPKGCNEFMFESQPQLQKAFVLIALCCIPWMLLGKPLYIKFTRKNKAHANHNGQLTGNIELAEGETPLPTGFSGNEENAGGAHGHDDEPMSEIYIHQAIHTIEYVLSTISHTASYLRLWALSLAHAQLSEVLWQMVLSLGLKMSGVGGAIGLFIIFGAWCLFTLAILVLMEGLSAFLHTLRLHWVEFMSKFYEGMGYAFQPFSFKAILDGEEEE
Protein: S phase cyclin A-associated protein in the endoplasmic reticulum N-terminal domain-containing protein (Q8C0H1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MMASFQRSNSHDKVRRIVAEEGRTARNLIAWSVPLESKDDDGKPKCQTGGKSKRTIQGTHKTTKQNTAVECKITSTTGEKHFDKSPTKTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDYYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIQSPSTDRMNVTSTARRSLNFGSLPGAVTAPCLAPTGVSWADKVKAHHTGSAPPEATPAQSCAPMTVQKTSRKNERKDAEGWETVQRGRPVRSRSTAVIPKVSLVTETLRSKDDSDKENICLLPEESIQKGKLEDRCSTVESLSKDSLLHSSDHPLSERTQFTVCILDDVKNSGSSQDSSVHTSEIPAIDSDAVCVAPQNTTALPTDRVPAETTGMVTEMTDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSGSLSFCGVSLDWNDVLADYEARESWRQNTSWGDIVEEEPARLPGHGIHMHEKLSSPSRKRTIAEFKKKY
Protein: Calcitonin receptor (CT-R) (C1A/C1B) (P32214)
Organism: Rattus norvegicus (Rat)
Function: This is a receptor for calcitonin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The calcitonin receptor is thought to couple to the heterotrimeric guanosine triphosphate-binding protein that is sensitive to cholera toxin.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30988}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30988}.
Interaction partners:
- Receptor activity-modifying protein 1
- Receptor activity-modifying protein 3
- Islet amyloid polypeptide
- Receptor activity-modifying protein 2
- Calcitonin
- Pro-adrenomedullin
- Calcitonin gene-related peptide 2
- Calcitonin gene-related peptide type 1 receptor
- Guanine nucleotide-binding protein G
- Nuclear factor of activated T-cells 1
Sequence:
MRFLLLNRFTLLLLLLVSPTPVLQAPTNLTDSGLDQEPFLYLVGRKKLLDAQYKCYDRIQQLPPYEGEGPYCNRTWDGWMCWDDTPAGVMSYQHCPDYFPDFDPTEKVSKYCDENGEWFRHPDSNRTWSNYTLCNAFTPDKLHNAYVLYYLALVGHSMSIAALIASMGIFLFFKNLSCQRVTLHKNMFLTYILNSIIIIIHLVEVVPNGDLVRRDPMHIFHHNTYMWTMQWELSPPLPLSAHEGKMDPHDSEVISCKILHFFHQYMMACNYFWMLCEGIYLHTLIVMAVFTEDQRLRWYYLLGWGFPIVPTIIHAITRAVYYNDNCWLSTETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRQTHEAEAYMYLKAVKATMVLVPLLGIQFVVFPWRPSNKVLGKIYDYLMHSLIHFQGFFVATIYCFCNHEVQVTLKRQWAQFKIQWSHRWGRRRRPTNRVVSAPRAVAFAEPGGLPIYICHQEPRNPPVSNNEGEEGTEMIPMNVIQQDSSA
Protein: Berberine bridge enzyme-like D-1 (NtBBLd) (EC 1.1.1.-) (A0A1S3YTK9)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (By similarity). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids (By similarity).
Subcellular location: Vacuole {ECO:0000250|UniProtKB:F1T160}.
Interaction partners:
Sequence:
MKRNISMFLQLLLIILMMISFLFTSLLVPSVSATTLNTISTCLINYKVSNFSVYPTRNHAGNSYYNLLDFSIQNLRFAACSKPKPTVIIVPESKEQLVSSVLCCRQGSYEIRVRCGGHSYEGTSSVSFDGSPFVVIDLMKLDGVSVDVDSETAWVQGGATLGQTYYAISRASNVHGFSAGSCPTVGVGGHISGGGYGFLSRKYGLAADNVVDALLVDAEGRLLDRKAMGEEIFWAIRGGGGGIWGIIYAWKIRLLKVPKTVTSFIIPRPGSKRYVSQLVHKWQLVAPKLEDEFYLSISMSSPSKGNIPIEINAQFSGFYLGTKTEAISILNEAFSELGVLEGDCKEMSWIESTLFFSELDDVANSSDVSRLKERYFENKSYFKAKSDYVKTPISVGGIMTALNVLEKEPNGHVILDPYGGAMQRISEEAIAFPHRKGNLFGIQYLVVWKEKDNNNIVKSNIGYIEWIREFYNTMAPHVSSSPRAAYVNYMDLDLGVMDDYLLPCTSTTASANHAVERARVWGEKYFLNNYDRLVKAKTKIDPLNVFRHQQGIPPLFASMQEYTYSSK
Protein: Pre-mRNA-splicing factor 6 (P19735)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome.
Subcellular location: Nucleus.
Interaction partners:
- LSM complex subunit LSM4
- Small nuclear ribonucleoprotein Sm D3
- 13 kDa ribonucleoprotein-associated protein
- Spliceosomal protein DIB1
- Small nuclear ribonucleoprotein G
- U4/U6 small nuclear ribonucleoprotein PRP3
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein-associated protein B
- Small nuclear ribonucleoprotein E
Sequence:
MERPSFLDQEPPAGYVPGIGRGATGFSTKEKQVVSNDDKGRRIPKRYRENLNNHLQSQPKDDEDDEAANVFKTLELKLAQKKKKRANEKDDDNSVDSSNVKRQFADLKESLAAVTESEWMDIPDATDFTRRNKRNRIQEQLNRKTYAAPDSLIPGNVDLNKLTEEREKLLQSQIDENLAQLTKNASNPIQVNKPNAATDALSYLKDLENDRVNSLSDATLEDLQKMRTILKSYRKADPTNPQGWIASARLEEKARKFSVAKKIIENGCQECPRSSDIWLENIRLHESDVHYCKTLVATAINFNPTSPLLWFKAIDLESTTVNKYRVVRKALQEIPRDEGLWKLAVSFEADKAQVIKMLEKATQFIPQSMDLLTAYTNLQSYHNAKMTLNSFRKILPQEPEIWIISTLLEERNNPDIPVDKLVSLLKEGLLELSKNGYKATLSAWLKRAEALNDAPNSNLTCQAIVYAILEWLRESGEYESELNNVDQILEKMPHSKVQIAVLKKLIQWDPCDTVLWSRLKMATESYHKIEELLAFFQELLFQTKNSDDIRANMREKSPGLLMMYVSEYWKAQKGDTRQTLVLIDQIIDFAPHNLDLRFFKIKLLGRSLQLDELRDFFQQTFSSLEDFKISGTERLYYKYVNFLRYQDLNEEAIKFLNERCLKSFPICHKFFLQLGQIYHSMGNIEMSRETYLSGTRLVPNCPLLWVSLSKIDEIDLKNPVRARSILDRGLLKNPDDVLFYIAKIQMEIRLGNLDQAELLVTQALQKFPSNALLWVEQIKLFKHGNKSSLKKTIFQDALRRTQNDHRVLLEIGVSFYAEAQYETSLKWLERALKKCSRYGDTWVWLFRTYARLGKDTVDLYNMFDQCEPTYGPEWIAASKNVKMQYCTPREILLRLMNDK
Protein: Tumor necrosis factor receptor superfamily member 18 (Activation-inducible TNFR family receptor) (Glucocorticoid-induced TNFR-related protein) (CD antigen CD357) (Q9Y5U5)
Organism: Homo sapiens (Human)
Function: Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Tumor necrosis factor ligand superfamily member 18
- Tumor necrosis factor receptor superfamily member 4
- Forkhead box protein P3
- Cytotoxic T-lymphocyte protein 4
- Tumor necrosis factor receptor superfamily member 9
- Interleukin-2 receptor subunit alpha
- T-cell immunoreceptor with Ig and ITIM domains
- T-lymphocyte activation antigen CD80
- T-cell surface glycoprotein CD4
- CD27 antigen
Sequence:
MAQHGAMGAFRALCGLALLCALSLGQRPTGGPGCGPGRLLLGTGTDARCCRVHTTRCCRDYPGEECCSEWDCMCVQPEFHCGDPCCTTCRHHPCPPGQGVQSQGKFSFGFQCIDCASGTFSGGHEGHCKPWTDCTQFGFLTVFPGNKTHNAVCVPGSPPAEPLGWLTVVLLAVAACVLLLTSAQLGLHIWQLRSQCMWPRETQLLLEVPPSTEDARSCQFPEEERGERSAEEKGRLGDLWV
Protein: Natriuretic peptide Na-NP (D9IX97)
Organism: Naja atra (Chinese cobra)
Function: Natriuretic peptide that dose-dependently induces the rapid relaxation of rat aortic strips phenylephrine-precontracted. Acts by stimulating cGMP production in a dose-dependent manner (by probably activating NPR1 and/or NPR2). May also show potent hypotensive effects.
Subcellular location: Secreted {ECO:0000269|PubMed:21050868}.
Interaction partners:
Sequence:
MVGLSRLAGGGLLLVLALLPLALDGKPAPEALHKPPTGLRTSLAALRILGYLRPDSKQSRAARDRMLHPEQQVGGGGDSRPLQDETNKGKGSSCFGQKIDRIGSMSGMGCRTQGKPPPALPTAPAALRILEYLRPDSKRSRATRDRMLHPEQQVGGGGGGGSRVI
Protein: Geranyltranstransferase (EC 2.5.1.10) (Q60AN0)
Organism: Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Interaction partners:
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Squalene synthase
- Octaprenyl diphosphate synthase
- Exodeoxyribonuclease 7 small subunit
Sequence:
MNPERSLSDFMRSSQERVERALDARLPAADRMPERLHQAMRYSVLGGGKRMRPLLTYATGQTIGVAADLLDGPACAVEFIHVYSLIHDDLPAMDDDDLRRGKPTCHKAYDEATAILAGDGLQALAFHVLAQDPSIAVPAENRIAMIETLAKASGPAGMVGGQAIDLASVGKKLDLPGLENMHIRKTGALIRASVRLACLARPGLPAEQFDRLDHYAKCIGLAFQIQDDILDEESDTQTLGKTRGKDRDHNKPNYPALLGLSGAKEKAEEMHEAALESLAGFGPEADLLRELARFIIQRQS
Protein: DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-alkyladenine DNA glycosylase) (3-methyladenine DNA glycosidase) (ADPG) (N-methylpurine-DNA glycosylase) (Q04841)
Organism: Mus musculus (Mouse)
Function: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Subcellular location: Cytoplasm {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Methylated-DNA--protein-cysteine methyltransferase
- N-glycosylase/DNA lyase
- Endonuclease III-like protein 1 lyase)
- DNA repair nuclease/redox regulator APEX1
- Uracil-DNA glycosylase
- DNA repair protein XRCC1
Sequence:
MPARGGSARPGRGALKPVSVTLLPDTEQPPFLGRARRPGNARAGSLVTGYHEVGQMPAPLSRKIGQKKQRLADSEQQQTPKERLLSTPGLRRSIYFSSPEDHSGRLGPEFFDQPAVTLARAFLGQVLVRRLADGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYLIYGMYFCLNVSSQGAGACVLLRALEPLEGLETMRQLRNSLRKSTVGRSLKDRELCSGPSKLCQALAIDKSFDQRDLAQDDAVWLEHGPLESSSPAVVVAAARIGIGHAGEWTQKPLRFYVQGSPWVSVVDRVAEQMDQPQQTACSEGLLIVQK
Protein: Rrp9p (Q5A213)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ribosome biosynthesis protein
- Nucleolar protein 58
- Utp9p
- Utp13p
- 13 kDa ribonucleoprotein-associated protein
- SnoRNA-binding rRNA-processing protein
- Nucleolar protein 56
- Nan1p
- rRNA-processing protein
- SnoRNA-binding rRNA-processing protein
Sequence:
MAGDPFLSDPSKKRKRSNKLTSKTKRSKSSTPTPTPTPTPNTNHQDDDISSGSDSENGHANGTNENDHGDNESELSSDEEFADETVNDKRRRLAKQYLENLKQNEHELYDEFDAKDLDDDILARRLQKDIAETKGYVYKFVGDKIKDQLDEEYPLELITTRIGCKNLTSMTINYPFLYTVSKDMEIIKWDINETHKKPKRIKHTKGGNKYFEINTINPQLNHHWQQINCIAASPDGKYIVTGGSDSRLIIWSSENLTCLKVLPTRSSVNSIVFRRNSDQLFAACADLRIRTYSINQFTQLEILYGHQDNISDISALAKETCVSVGSRDKTAMFWKIAEESRLTFRGGDSLEKTNKKKKRHYHQEEEEAETENDESTFYNEGSIDVVSMIDESHFVTGSDNGNVALWSLAKKKPLTTKRLSHGLQPQFTPIQASSESNEELALQQIPKPQPYWITAIHGVPYSDIFITGSFNGTIKIWKLEEPSLRSFKLLGEIKQNNLNGCIVKIDSVEIPNTKKLKIYVLLSKEHKFGRWLGKLPGARNALVNFTVNL
Protein: Large ribosomal subunit protein uL15m (39S ribosomal protein L15, mitochondrial) (Q9VPF6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL9m
- Ribosomal protein
- Large ribosomal subunit protein uL4m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL20m
Sequence:
MAHLRETSDKALKLLRTLPRVQIGNLRPNPNSKQNDKRGRAQHGGDKHGAGNKGSGQRQNFMRLGYETGNQPFYLRFPYEPYYKGHHLKRQYPPISLLQLQVLIDTNRIDISQPIDISTLCNSGLLKLKPAEMEYGFQLTDDGLDNFQAKINIEVQHASEAVIAAIEKNGGVIRTAYYDPRSLHMLANPKKWFEKGVPIPSRMLPPQDAVDYYTDPKNRGYLANPEAISQDRLVLAQKYGYQLPKIEEDSAYEMLTTAKDPRQVFYGLEPGWLINIVDKTIIKRKQ
Protein: Frizzled-7-B (Fz-7-B) (Xfz7-B) (Q8AVJ9)
Organism: Xenopus laevis (African clawed frog)
Function: Receptor for Wnt proteins. Acts in both canonical and non-canonical Wnt pathways. Although different papers report differing Wnt preferences, wnt5a, wnt8b and wnt11 have been proposed as synergists. In the canonical Wnt pathway, acts via beta-catenin to promote the expression of the dorsal genes siamois, twin and nodal3 and to establish the dorsal axis of the embryo and induce dorsal mesoderm formation. In a non-canonical Wnt/planar cell polarity (PCP) pathway, acts with sdc4 and dvl2/dsh to regulate convergent extension cell movements during gastrulation. Triggers phosphorylation of dvl2/dsh and its translocation to the plasma membrane. In a third branch of Wnt signaling, acts in a non-canonical pathway via trimeric G proteins, and independently of dvl2/dsh, to recruit protein kinase C (PKC) to the membrane and thus activate PKC. PKC signaling controls cell sorting and tissue separation during gastrulation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:O75084}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75084}. Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. {ECO:0000250|UniProtKB:O75084}.
Interaction partners:
Sequence:
MLAPVSLLFCLFLQLCPSAQQYHGEKGISVPDHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLEQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDNSPSGPTARPTLNLPDSITFQPHPHRDFTCPRQLKVPPYLGYRFLGEKDCGAPCEPGKANGLMYFKEEEVRFARLWVGIWAILCGISTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAYTAGFLLEERAVCVERFSEDSYRTVAQGTKKEGCTILFMILYFFGMASSIWWVILALTWFLSAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDVLSGVCYVGINSVDSLRGFVLAPLFVYLFLGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVMYTVPATIVLACYFYEQAFRDTWEKTWLVHTCKGYAVPCPNYNFAPMSPDFTVFMIKYLMTMIVGITSSFWIWSGKTLQSWRRFYHRLGNGSKGETAV
Protein: Profilin-3 (Pollen allergen Zea m 12) (ZmPRO3) (allergen Zea m 12) (P35083)
Organism: Zea mays (Maize)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-1
- Actin-1
- Uncharacterized protein.
- Actin-depolymerizing factor
- Actin-depolymerizing factor
- Actin-depolymerizing factor
- Actin-depolymerizing factor 7
- Actin-depolymerizing factor 1
- Expansin-B9
- Expansin-B10
Sequence:
MSWQTYVDEHLMCEIEGHHLSSAAIVGHDGAVWAQSTAFPQFKPEEMTNIIKDFDEPGFLAPIGLFLGPTKYMVIQGEPGAVIRGKKGSGGITVKKTGQALVIGIYDEPMTPGQCNMVVERLGDYLVEQGL
Protein: Transcription factor SOX-14 (SRY-related protein CH60) (Q9W7R6)
Organism: Gallus gallus (Chicken)
Function: Acts as a negative regulator of transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Sulfhydryl oxidase 1
Sequence:
MSKPSDHIKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSEAEKRPYIDEAKRLRAQHMKEHPDYKYRPRRKPKNLLKKDRYVFPLPYLGETDPLKAAGLPVGATDSLLSSPEKARAFLPPTSAPYSLLDPSQFSSSAIQKMTEVPHTLATGTLPYASTLGYQNGAFGSLSCPSQHTHTHPSPTNPGYVVPCNCTAWSASSLQPPVAYILFPGMTKTGIDPYSSAHATAM
Protein: Transportin-1 (Importin beta-2) (Karyopherin beta-2) (Q8BFY9)
Organism: Mus musculus (Mouse)
Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. May mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (By similarity). In vitro, mediates nuclear import of SRP19 (By similarity). Mediates the import of histones H2A, H2B, H3 and H4. Mediates nuclear import of ADAR/ADAR1 in a RanGTP-dependent manner (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein A1
- RNA-binding protein FUS
- Kinesin-like protein KIF17
- GTP-binding nuclear protein Ran
- Importin-7
- mRNA decay activator protein ZFP36
- Heterogeneous nuclear ribonucleoprotein D0
- Transportin-3
- Heterogeneous nuclear ribonucleoprotein M
- Exportin-1
Sequence:
MVWDRQTKMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEAEVRKNVCRALVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHEEDGIEEEDDDDDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQAMLNNAQPEQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV
Protein: Uncharacterized protein (Q581S5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDLNFERPFFMEFGDFKNGYNREEAEAGINEAIRKQRKLRLQSHVEGIMLGCGIGEAAKQSVHKGVYKPQTTINPSLLCEEDAQPSAGGDEVNSNNGGSRPCPPLDGAALLETSPSAVMKDFATVDVQVETLQEVAEQLDQNIRVARERIGQGCAPFTFEDVLEALTIVLTVVEKGDPTVKVLLPIQPEGSEPLEGAEEVADFAYSNIVPLTVALSSTIYATEWMLQYTLTFINSIGVETEEEAQLHLELRARCVRLLGEINRFTAFAIAFKMKCEMYVAFDDLRNETEFNIGGILDSVEEDLKETMQLQFPRRRRRVLKVQRSIFKRLQRALVLLHELDTCWTPVMMLQKVWKDEFLAESYERIYTIIAPTFFSATLGFVDSSLYIESDSSNSVPEPNNPSCPIQRAPSQCSISRHGRQVGSAKPRVVAERQSKKLVLGQVKTLRVEEKRSFEKISYLVKGTVNRTVGMQLCLGARYSLVEFGEEHDKNWDFVANEPKDPQDVNAYVMELVKKFIRILRQRTKNTDDTDALVP
Protein: Adipokinetic hormone receptor, isoform A (Adipokinetic hormone receptor, isoform B) (Adipokinetic hormone receptor, isoform D) (GH19447p) (Q9VM96)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAKVAEENDHRDLSNWSNVNDTNGTIHLTKDMVFNDGHRLSITVYSILFVISTIGNSTVLYLLTKRRLRGPLRIDIMLMHLAIADLMVTLLLMPMEIVWAWTVQWLSTDLMCRLMSFFRVFGLYLSSYVMVCISLDRYFAILKPLKRSYNRGRIMLACAWLGSVVCSIPQAFLFHLEEHPAVTGYFQCVIFNSFRSDFDEKLYQAASMCSMYAFPLIMFIYCYGAIYLEIYRKSQRVLKDVIAERFRRSNDDVLSRAKKRTLKMTITIVIVFIICWTPYYTISMWYWLDKHSAGKINPLLRKALFIFASTNSCMNPLVYGLYNIRGRMNNNNPSVNNRHTSLSNRLDSSNQLMQKQLTNNSLLNGRGQVMAAAVSATTKLANVVSLKGTANGNGSAAAAGTVPITPPLTVTIAPLATDDEANDDSCLSAVTIRCQDQSPIRQK
Protein: Cathepsin D (EC 3.4.23.5) (O93428)
Organism: Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus hamatus)
Function: Acid protease active in intracellular protein breakdown.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q9DEX3}.
Interaction partners:
Sequence:
MKMLLLCVFSALALTNDALVRIPLKKFRSIRRQLTDSGKRAEELLADHHSLKYNLSFPASNAPTPETLKNYLDAQYYGEIGLGTPPQPFTVVFDTGSSNLWVPSIHCSLLDIACLLHHKYNSGKSSTYVKNGTAFAIQYGSGSLSGYLSQDTCTIGDLAIDSQLFGEAIKQPGVAFIAAKFDGILGMAYPRISVDGVAPVFDNIMSQKKVEQNVFSFYLNRNPDTEPGGELLLGGTDPKYYTGDFNYVNVTRQAYWQIRVDSMAVGDQLSLCTGGCEAIVDSGTSLITGPSVEVKALQKAIGAFPLIQGEYMVNCDTVPSLPVISFTVGGQVYTLTGEQYILKVTQAGKTMCLSGFMGLDIPAPAGPLWILGDVFMGQYYTVFDRDANRVGFAKAK
Protein: Sialidase-3 (EC 3.2.1.18) (Ganglioside sialidase) (Membrane sialidase) (N-acetyl-alpha-neuraminidase 3) (Q9JMH7)
Organism: Mus musculus (Mouse)
Function: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3. Plays a role in the regulation of transmembrane signaling through the modulation of ganglioside content of the lipid bilayer and by direct interaction with signaling receptors, such as EGFR. Desialylates EGFR and activates downstream signaling in proliferating cells. Contributes to clathrin-mediated endocytosis by regulating sorting of endocytosed receptors to early and recycling endosomes (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14970224, ECO:0000269|PubMed:17708748}; Peripheral membrane protein {ECO:0000269|PubMed:17708748}. Membrane, caveola {ECO:0000250|UniProtKB:Q9UQ49}. Early endosome membrane {ECO:0000269|PubMed:17708748}; Peripheral membrane protein {ECO:0000269|PubMed:17708748}. Recycling endosome membrane {ECO:0000269|PubMed:17708748}; Peripheral membrane protein {ECO:0000269|PubMed:17708748}. Lysosome membrane {ECO:0000250|UniProtKB:Q9UQ49}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UQ49}. Note=Associates with the external leaflet of the plasma membrane (PubMed:17708748). S-acylated NEU3 likely spans the lipid bilayer with a portion of C-terminus exposed to cytosol and the catalytic region facing the extracellular space (By similarity). {ECO:0000250|UniProtKB:Q9UQ49, ECO:0000269|PubMed:17708748}.
Interaction partners:
- Arylsulfatase A
- Galactocerebrosidase
- Galactosylceramide sulfotransferase
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Alpha-galactosidase A
- Neuferricin
Sequence:
MEEVPPYSLSSTLFQQEEQSGVTYRIPALLYLPPTHTFLAFAEKRTSVRDEDAACLVLRRGLMKGRSVQWGPQRLLMEATLPGHRTMNPCPVWEKNTGRVYLFFICVRGHVTERCQIVWGKNAARLCFLCSEDAGCSWGEVKDLTEEVIGSEVKRWATFAVGPGHGIQLHSGRLIIPAYAYYVSRWFLCFACSVKPHSLMIYSDDFGVTWHHGKFIEPQVTGECQVAEVAGTAGNPVLYCSARTPSRFRAEAFSTDSGGCFQKPTLNPQLHEPRTGCQGSVVSFRPLKMPNTYQDSIGKGAPATQKCPLLDSPLEVEKGAETPSATWLLYSHPTSKRKRINLGIYYNRNPLEVNCWSRPWILNRGPSGYSDLAVVEEQDLVACLFECGEKNEYERIDFCLFSDHEVLSCEDCTSPSSD