wanglab/gogpt-training-data huggingface dataset:
Protein: Small nuclear ribonucleoprotein G (snRNP-G) (Sm protein G) (Sm-G) (SmG) (P62308)
Organism: Homo sapiens (Human)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. As part of the U7 snRNP it is involved in histone 3'-end processing.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000305}.
Interaction partners:
- U4/U6 small nuclear ribonucleoprotein Prp31
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein F
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- U6 snRNA-associated Sm-like protein LSm3
- Small nuclear ribonucleoprotein-associated protein N
- Splicing factor 3B subunit 3
- Protein BUD31 homolog
- U7 snRNA-associated Sm-like protein LSm10
- U1 small nuclear ribonucleoprotein 70 kDa
Sequence:
MSKAHPPELKKFMDKKLSLKLNGGRHVQGILRGFDPFMNLVIDECVEMATSGQQNNIGMVVIRGNSIIMLEALERV
Protein: Ferredoxin (P68164)
Organism: Datura metel (Devil's trumpet) (Datura fastuosa)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:7586063, ECO:0000269|PubMed:7764481}.
Interaction partners:
Sequence:
ATYKVKLVTPDGPVEFDCPDDVYILDRAEEEGHDLPYSCRAGSCSSCAGKVTAGTVDQSDGNYLDDDQMAEGFVLTCVAYPQSDVTIETHKEEELTG
Protein: NAD-dependent epimerase/dehydratase domain-containing protein (Q57X60)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Electron transfer protein, putative
- Acyl carrier protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Reiske iron-sulfur protein, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MKSGKLLIFGGTGFVGSVVVRKALQRGWRVICATRGGVPIHGSPLYNDFTSLQQKHGDTLSQGVAHDTCHVPQPLEFVSLDATSRLQVFQFMDDHPDASAIISCIGLLTRDHEMARRVCGDANVNIAAALYERRAVARRMVLISAEPVGTRAGFFLNSRWALKGYFMGKRVAERAVLENLGDDGAVLRPGFIYGTRHVPLGEGCVPVPLWPIGKPLEAVLRPLHLHGLLVPPISVDVVAEAAVRLAEAPGPSTVLDYYGMQQVCGLPQDGHHVLGGDKTNKEECGDNNQSNK
Protein: Poly(rC)-binding protein 2 (Alpha-CP2) (CTBP) (CBP) (Putative heterogeneous nuclear ribonucleoprotein X) (hnRNP X) (Q61990)
Organism: Mus musculus (Mouse)
Function: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein (By similarity). Binds also poly(rU) (By similarity). Acts as a negative regulator of antiviral signaling (By similarity). Negatively regulates cellular antiviral responses mediated by MAVS signaling (By similarity). It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation (By similarity). Negativeley regulates the cGAS-STING pathway via interaction with CGAS, preventing the formation of liquid-like droplets in which CGAS is activated (By similarity). Together with PCBP1, required for erythropoiesis, possibly by regulating mRNA splicing.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15366}. Cytoplasm {ECO:0000250|UniProtKB:Q15366}. Note=Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q15366}.
Interaction partners:
- Poly
- Serine/arginine-rich splicing factor 3
- DNA endonuclease RBBP8
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoprotein A3
- Natural resistance-associated macrophage protein 2
- Cytotoxic granule associated RNA binding protein TIA1
- Polypyrimidine tract-binding protein 1
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein D0
Sequence:
MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLESPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWAGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
Protein: Skeletal muscle myosin heavy chain II-b (Skeletal muscle myosin heavy chain II-b transcript variant 3) (Skeletal muscle myosin heavy chain II-b transcript variant 4) (Skeletal muscle myosin heavy chain II-b transcript variant 5) (Skeletal muscle myosin heavy chain II-b transcript variant 6) (Skeletal muscle myosin heavy chain II-b transcript variant 7) (Skeletal muscle myosin heavy chain II-b transcript variant 8) (Skeletal muscle myosin heavy chain IIb transcript variant 9) (Q1WJJ3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSDAEMAVFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVDAKESYVKATVQSREGGKVTAKTEGGATVTVKDDQVFSMNPPKYDKIEDMAMMT
Protein: Tricarboxylate transport protein, mitochondrial (Citrate transport protein) (CTP) (Mitochondrial citrate carrier) (CIC) (Solute carrier family 25 member 1) (Tricarboxylate carrier protein) (P53007)
Organism: Homo sapiens (Human)
Function: Mitochondrial electroneutral antiporter that exports citrate from the mitochondria into the cytosol in exchange for malate. Also able to mediate the exchange of citrate for isocitrate, phosphoenolpyruvate, cis-aconitate and to a lesser extend cis-aconitate, maleate and succinate. In the cytoplasm citrate is important in the regulation of glycolysis through a feedback mechanism and in the production of acetyl-CoA which is needed for the synthesis of fatty acids, sterols, prostaglandins, dolichol and coenzyme Q (CoQ). Required for proper neuromuscular junction formation (Probable).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8JZU2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Citrate synthase, mitochondrial
- Clathrin heavy chain 2
- ATP-citrate synthase
- Mitochondrial ribosomal protein L40
- Splicing factor ESS-2 homolog
- DNA polymerase epsilon subunit 2
- Integral membrane protein DGCR2/IDD
- Progranulin
- Developmentally-regulated GTP-binding protein 1
- UPF0235 protein C15orf40
Sequence:
MPAPRAPRALAAAAPASGKAKLTHPGKAILAGGLAGGIEICITFPTEYVKTQLQLDERSHPPRYRGIGDCVRQTVRSHGVLGLYRGLSSLLYGSIPKAAVRFGMFEFLSNHMRDAQGRLDSTRGLLCGLGAGVAEAVVVVCPMETIKVKFIHDQTSPNPKYRGFFHGVREIVREQGLKGTYQGLTATVLKQGSNQAIRFFVMTSLRNWYRGDNPNKPMNPLITGVFGAIAGAASVFGNTPLDVIKTRMQGLEAHKYRNTWDCGLQILKKEGLKAFYKGTVPRLGRVCLDVAIVFVIYDEVVKLLNKVWKTD
Protein: Presequence protease, mitochondrial (EC 3.4.24.-) (Pitrilysin metalloproteinase 1) (Q8K411)
Organism: Mus musculus (Mouse)
Function: Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. It is also able to degrade amyloid-beta protein 40, one of the peptides produced by APP processing, when it accumulates in mitochondrion. It is a highly efficient protease, at least toward amyloid-beta protein 40. Cleaves that peptide at a specific position and is probably not processive, releasing digested peptides intermediates that can be further cleaved subsequently. It is also able to degrade amyloid-beta protein 42.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q5JRX3}.
Interaction partners:
- Amyloid-beta precursor protein
Sequence:
MWRFSGRRGLCAVQRLSCGRVHHRVWREKSDQACERALQYKVGEKIHGFTVNQVTPVPELFLTAVKLSHDNTGARYLHLAREDKNNLFSVQFRTTPMDSTGVPHVLEHTVLCGSQKYPCRDPFFKMLNRSLSTFMNAMTASDYTIYPFSTQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENPRDPQTPLIFKGVVFNEMKGAFTDNERIFSQHLQNKLLPDHTYSVVSGGDPLCIPELTWEQLKQFHATHYHPSNARFFTYGNFQLEGHLKQIHEEALSKFQRLEQSTAVPAQPHWDKPREFHITCGPDSLATETAKQTTVSVSFLLPDITDTFEAFTLSLLSSLLIAGPNSPFYKALIESGLGTDFSPDVGYNGYTREAYFSVGLQGIAEKDVKTVRELVDRTIEEVIEKGFEDDRIEALLHKIEIQTKHQSASFGLTLTSYIASCWNHDGDPVELLQIGSQLTRFRKCLKENPKFLQEKVEQYFKNNQHKLTLSMKPDDKYYEKQTQMETEKLEQKVNSLSPADKQQIYEKGLELQTQQSKHQDASCLPALKVSDIEPSMPFTKLDIGLAAGDIPVQYCPQPTNGMVYFRAFSSLNTLPEDLRPIVPLFCSVLTKLGCGILNYREQAQQIELKTGGMSVTPHVLPDDSQLDTYEQGVLFSSLCLERNLPDMMHLWSEIFNNPCFEEEEHFKVLVKMTAQELSNGISDSGHLYAALRASKTLTPSGDLQETFSGMDQVKVMKRIAEMTDIKPILRKLPRIKKYLLNCDNMRCSVNATPQQMPQAEKEVENFLRNVGRSKKERKPVRPHIVEKPTPSGPSGAAHVSGSQIVRKLVTDPTFKPCQMKTHFVLPFPVNYIGECVRTVPYADPDHASLKILARLMTAKFLHTEIREKGGAYGGGAKLTHSGIFTLYSYRDPNSIETLQSFGKAVDWAKSGKFTQQDIDEAKLSVFSTVDSPVAPSDKGMDHFLYGLSDEMKQAYREQLFAVNHDKLTSVSHKYLGIGKSTHGLAILGPENSKIAKDPSWIIK
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (Q7JUF8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MQQKPRNNGYPGTLICAVLLVLLSTGVSGQKQYSKARKLELREDVRRMFQHAYDGYLRHASNYDELRPLTCDGHDTWGSYSLTLIDALDTLATMGNFTEFRRAARLLEEKMDFDRDINVSVFETNIRIVGGLLSAHLLSKRAGVELEPGWPCKGPLLRLAEDVARRLLPAFVTNTGMPYGTVNLRYGVPKGETSITCTAGVGTFLIEFGTLSRLTGKTIYEDVAMKAVHALWAYRSPIGLFGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLNRPELLELFHEARAAIDKYMRKEDWYVWVGMNKGRVTLPVFQSLEAFWPGILSIIGDTEPALRTISRYIGVWKKYGFLPEFYNIAAGEASPNREVYPLRPELIESAMYLYRATGNEYLLEFGEHMLETLEFSAKTKCGYATIRNVVTHEKENRMESFFLAETSKYLYLLFDEENFLHNDGSGGELLSTEDDVCVVQAGAYIFNTEAHPMDMSALHCCHAHNEDIYTSLDLQRFSPRAILERSKKRQVAVQEQWVPQCHPENNEFFNKEDESVQAQDSEKEQEREQSGTSTTMAVDIEVFDEFQQPAGDLLVSNFEQIREERELNESLHRNVVARNQLTVSDLDEFFAQRRESFASASEALNYVKTFMGNYTMDVAFIRGLQLYDTNMSSVLGTGAQKEYESRMRTLWQLYELQQQYVANIRVIQGLGLLTFPADGDRIPSHLTEVLDSLDKSAHLEHMDLQDLETRVSNTSSPQLAHIREVILKARNAYAIAMVNTSAMQEFAIRIYLSGTSEAGVRIHPLLEDGELSEEARKRPLKLAEERALFSYARRIVDFRKRMAETVDRLQTLMQDIPPPKRKEATTDSQAADASTVYTQTKAQMAAPAQQPEPSQEEKQSTQIQKGKLAENGSGLGEEESGCVWSQLVQTILRKTTVQRVKFDEAVLQENTRKALEKYARKELPHHLFACHRPEYIEGFAYRDFYPEAL
Protein: AP-4 complex subunit beta-1 (AP-4 adaptor complex subunit beta) (Adaptor-related protein complex 4 subunit beta-1) (Beta subunit of AP-4) (Beta4-adaptin) (Q9Y6B7)
Organism: Homo sapiens (Human)
Function: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal (Probable).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10066790, ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:22472443}; Peripheral membrane protein {ECO:0000269|PubMed:10066790}.
Interaction partners:
- AP-4 complex subunit sigma-1
- AP-4 complex subunit epsilon-1
- AP-4 complex subunit mu-1
- AP-2 complex subunit alpha-1
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- AP-1 complex subunit sigma-1A
- AP-5 complex subunit zeta-1
- AP-5 complex subunit mu-1
- AP-2 complex subunit alpha-2
Sequence:
MPYLGSEDVVKELKKALCNPHIQADRLRYRNVIQRVIRYMTQGLDMSGVFMEMVKASATVDIVQKKLVYLYMCTYAPLKPDLALLAINTLCKDCSDPNPMVRGLALRSMCSLRMPGVQEYIQQPILNGLRDKASYVRRVAVLGCAKMHNLHGDSEVDGALVNELYSLLRDQDPIVVVNCLRSLEEILKQEGGVVINKPIAHHLLNRMSKLDQWGQAEVLNFLLRYQPRSEEELFDILNLLDSFLKSSSPGVVMGATKLFLILAKMFPHVQTDVLVRVKGPLLAACSSESRELCFVALCHVRQILHSLPGHFSSHYKKFFCSYSEPHYIKLQKVEVLCELVNDENVQQVLEELRGYCTDVSADFAQAAIFAIGGIARTYTDQCVQILTELLGLRQEHITTVVVQTFRDLVWLCPQCTEAVCQALPGCEENIQDSEGKQALIWLLGVHGERIPNAPYVLEDFVENVKSETFPAVKMELLTALLRLFLSRPAECQDMLGRLLYYCIEEEKDMAVRDRGLFYYRLLLVGIDEVKRILCSPKSDPTLGLLEDPAERPVNSWASDFNTLVPVYGKAHWATISKCQGAERCDPELPKTSSFAASGPLIPEENKERVQELPDSGALMLVPNRQLTADYFEKTWLSLKVAHQQVLPWRGEFHPDTLQMALQVVNIQTIAMSRAGSRPWKAYLSAQDDTGCLFLTELLLEPGNSEMQISVKQNEARTETLNSFISVLETVIGTIEEIKS
Protein: Histone deacetylase complex subunit SAP130a (EC 3.2.1.3) (Sin3A-associated protein a) (F1REK0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Family with sequence similarity 60, member A
- SIN3-HDAC complex-associated factor,-like.
- Histone deacetylase complex subunit SAP30L
- BRMS1 transcriptional repressor and anoikis regulator.
- Paired amphipathic helix protein Sin3a
- Inhibitor of growth protein
- Paired amphipathic helix protein Sin3a
- Paired amphipathic helix protein Sin3b
- SDS3 homolog, SIN3A corepressor complex component)
- Histone-binding protein RBBP4
Sequence:
MQYSHYVVGIASDIRQKMSSQQFPRAALPPSAAAAAPGQASADSSGAGTHSVGSEDSSREVDHPQDPSLGSSSGSIGGLASFRDDKQETVVVRPYPQVQAPGQSPALPQHVPIQPSPPVTLAAPSVHLLQGQQPSLTEGSVKATLKPPMPSRLIAPAPALSQGHIPVPAKVSGHITVPLESSIAPASIPVATISGQQGQSNLHQLMATNVQIFRGSAPLQIGSPATPHTFTSHLPRGAAAAAVMSSTKGPNVLRPAGGGSAGPSQPAAVQHIIHQPIQSRSLVTTSTAVLPTMVAPIPAARTQSPVINTTVTHATEMVHGRPVAIHPPPATINIQRPPTPRDTATRITLPSHPAIGGQKAQPPHTVTQKPIFNTVTPVAAATVAPILATNTVPSATTTGSAAHTQMTSSTIVTMTMASHSSHATAVTTSAIPVAKVVPQPIAHTSHSPRIQQEYSGERPNLIPISGHRSSPNPVTMEARSDNRPSVPVQFQYFLPTYPSPSYPLSHTYTPITSSVSTIRPYPVTAPAQSSALPAQTGVGVATTMHLNQMQLMALPSAQISTQNIQPASMTAQGIQPAPIGVQGLHAAAPISTQTVQQAPVTTQQPQSEAKPAGVVLAESPAFVTNPIGSTFSGTQPVTTIVQTHTGAGAPTLVSSPRPSILRKKPVTEGAVRKCLIQAQPSEPNAGRVDSGIRLSGSPRPAGVKPKPDIHVAMAPPVMAAVEALVGHVGEQQTLSTPVQHHSQAIPTLLAPPAPAPPSQPTAVLSALPATMAVTPPVPASMANAVASPTQPAASSTAALSSTLPEVKIKQEAEPMDTSQAVPLAPSLTGPAPSLSSQSSTLTVSSQPGELLPGASPRKKPRKQQHVISTEETEMVETNSTDEERASSRAPGNRMERHESPPREYVDEDGVRYVPVRPRPPHTHLRQYRNPWKAAYHHFQRYSDIRVKEEKKGSLQDMANQRGVACRAQGWKVHLCAAQLLQLSNLEHDVYSRLTTLQEGLIPKKRAGADDDLHRINELIQGNMQRCKLVMDQVTEARDTMMKVLDHKDRVLKLLNKNGTPKKSSKLKRKERA
Protein: Proprotein convertase subtilisin/kexin type 4 (EC 3.4.21.-) (Proprotein convertase 4) (PC4) (Q6UW60)
Organism: Homo sapiens (Human)
Function: Proprotein convertase involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues (By similarity). In males, important for ADAM2 processing as well as other acrosomal proteins with roles in fertilization and critical for normal fertilization events such as sperm capacitation, acrosome reaction and binding of sperm to zona pellucida (By similarity). Also plays a role in female fertility, involved in the regulation of trophoblast migration and placental development, may be through the proteolytical processing and activation of proteins such as IGF2. May also participate in folliculogenesis in the ovaries (By similarity).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:P29121}.
Interaction partners:
Sequence:
MRPAPIALWLRLVLALALVRPRAVGWAPVRAPIYVSSWAVQVSQGNREVERLARKFGFVNLGPIFPDGQYFHLRHRGVVQQSLTPHWGHRLHLKKNPKVQWFQQQTLQRRVKRSVVVPTDPWFSKQWYMNSEAQPDLSILQAWSQGLSGQGIVVSVLDDGIEKDHPDLWANYDPLASYDFNDYDPDPQPRYTPSKENRHGTRCAGEVAAMANNGFCGVGVAFNARIGGVRMLDGTITDVIEAQSLSLQPQHIHIYSASWGPEDDGRTVDGPGILTREAFRRGVTKGRGGLGTLFIWASGNGGLHYDNCNCDGYTNSIHTLSVGSTTQQGRVPWYSEACASTLTTTYSSGVATDPQIVTTDLHHGCTDQHTGTSASAPLAAGMIALALEANPFLTWRDMQHLVVRASKPAHLQAEDWRTNGVGRQVSHHYGYGLLDAGLLVDTARTWLPTQPQRKCAVRVQSRPTPILPLIYIRENVSACAGLHNSIRSLEHVQAQLTLSYSRRGDLEISLTSPMGTRSTLVAIRPLDVSTEGYNNWVFMSTHFWDENPQGVWTLGLENKGYYFNTGTLYRYTLLLYGTAEDMTARPTGPQVTSSACVQRDTEGLCQACDGPAYILGQLCLAYCPPRFFNHTRLVTAGPGHTAAPALRVCSSCHASCYTCRGGSPRDCTSCPPSSTLDQQQGSCMGPTTPDSRPRLRAAACPHHRCPASAMVLSLLAVTLGGPVLCGMSMDLPLYAWLSRARATPTKPQVWLPAGT
Protein: Ribonuclease D, putative (O07183)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MCPEPSHAGAAESEGTESEPTPLLRPAGGIPDLCVTVGEIAAAAELLDRGRGPFAVDAERASGFRYSGRAYLIQIRRAEAGTVLIDPVSHGGDPLTVLAPVAEVLSTNEWILHSADQDLPCLAEVGMRPPALYDTELAGRLAGFDRVNLAAMVERLLGLGLTKGHGAADWSKRPLPSAWLNYAALDVELLIELRAAISRVLAEQGKTDWAAQEFEHLRSFESRPPPAAARQDRWRRTSGIHKVHDRRGLAAVRELWTARDRIAQRRDIAPRRILPDSAIIDAAIADPKSVDDLVALPVFGGRNQRRSAAVWWAALAAARESPDPPEIAEPANGPPPPGRWVRRKPAAAARLDAARAALTEVSQRVRVPTENLVSPDLVRRLCWEWEDISQSSPDPIAAVEAYLRTGQARAWQLELVVPILTAALTGAPDAGAQGDDGS
Protein: Kinesin-like protein (Q382W3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Kinesin-like protein, putative
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin, putative
- Kinesin, putative
- Kinesin, putative
Sequence:
MENIRVVVRVRPFIPGENPQQCVTVHDRQIRVGDDRTFAFDKVFDMRATCDLVNSSVGDPLISAFVDGYTVSTIAYGQTGAGKTHTMSRLSRYVVERVHKILTNGAAEHSGLASPGARSNSLADAEAAATQPEFRFSAVEVYNDQISDLAVSASSSSAPRQVRTLSLREDNRCGVFIKGLTETAVDSAEGLLTLIERCISSRRTAMTQANETSSRSHCLLTVALVYRGKVGRFALVDLAGSERMKKAHGATPSAAGEGHSGAAASRVREGISINSGLLALGNVISALCARKSHVPYRASKLTRLLQPMLSGNSKTTMIACVSPVAASFEETLNTLKYANRVKSLRTTPLQMAAVSSMEDAQRAIEMLHQQLLEAKQVGCGQFSGMPSFPTGDVNAKLEELEEKLRVEQKLTQRLKDDLFNAEYTAMVEVEKRKSLEKRIALLELVEKERCVGRASTSTAEVSAVGSTVSCPRRSAESSDPSDEGGDIENNRKLLERLEAERDELEALKKQKETDSKRLAELDMGGQHSIGCDFDGSFSQENLLRDIALKERHIQELKQRNEEAVWALEDSKRNQEEVLSVKRRLEEDLANAVTKLESTEMEQQRKQAERNRLFALHEERLRKAEEMAETYRRRVEEATLQLNQRQCNEELIQQLQAQIPEMREELNRHVVAVREGQQREQKMAASYVQKVKKMKRQMRETEAQVSRLQVELQKKEREIARVKSNIADRFDRCLSKAHVERKQLLRNLQCDSSGRSSSVQREIDLELRALATIETDLDDLMLERCEMKARLDEVCGSPNVVNSCAVAAKGFECQSRRAGSPNSCSGAQAEASTDYSEALGDGNAVVKEQATNPLVFQTLRRLEEVEDSIDSLQEARKYHLQRVRRLQNSSASAQGSVTSRACELLQRSISDSFRQTS
Protein: V-type proton ATPase subunit C 1 (V-ATPase subunit C 1) (Vacuolar proton pump subunit C 1) (Q5FVI6)
Organism: Rattus norvegicus (Rat)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit D
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit F
- Renin receptor
- V-type proton ATPase subunit G
Sequence:
MTEFWLISAPGEKTCQQTWEKLHAATTKNNNLAVSSKFNIPDLKVGTLDVLVGLSDELAKLDAFVEGVVKKVAQYMADVLEDSKDKVQENLLASGVDLVTYITRFQWDMAKYPIKQSLKNISEIIAKGVTQIDNDLKSRASAYNNLKGNLQNLERKNAGSLLTRSLAEIVKKDDFVLDSEYLVTLLVVVPKLNHNDWIKQYETLAEMVVPRSSNVLSEDQDSYLCNVTLFKKAVDDFRHKARENKFIVRDFQYNEEEMRADKEEMNRLSTDKKKQFGPLVRWLKVNFSEAFIAWIHIKALRVFVESVLRYGLPVNFQAMLLQPNKKSVKKLREVLHELYKHLDSSAAAIIDAPMDIPGLNLSQQEYYPYVYYKIDCNLLEFK
Protein: Endothelin-2 (ET-2) (Preproendothelin-2) (PPET2) (Vasoactive intestinal contractor) (VIC) (P22389)
Organism: Mus musculus (Mouse)
Function: Vasoconstrictor.
Subcellular location: Secreted.
Interaction partners:
- Endothelin receptor type B
- Endothelin-1 receptor
- Endothelin-3
- Endothelin-1
Sequence:
MVSAWCSIALALLLALHEGKGQAAATLEQPASAPKGRGPHLRFRRCSCNSWLDKECVYFCHLDIIWVNTAGQTAPYGLGNPPRRRRRSLPKRCECSTAGDSACATFCHRRHWPEAVVAPSSQAPAAVLKTGKMWTAEGDLLRKLRDISATKLRFARLQPEVTRKAIPAYSRWRKR
Protein: Amyloid protein-binding protein 2 (Amyloid beta precursor protein-binding protein 2) (APP-BP2) (Q9DAX9)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa-Xaa-Gly degron at the C-terminus, leading to their ubiquitination and degradation. The CRL2(APPBP2) complex mediates ubiquitination and degradation of truncated SELENOV selenoproteins produced by failed UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron. May play a role in intracellular protein transport: may be involved in the translocation of APP along microtubules toward the cell surface.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q92624}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92624}. Membrane {ECO:0000250|UniProtKB:Q92624}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q92624}. Note=Associated with membranes and microtubules. {ECO:0000250|UniProtKB:Q92624}.
Interaction partners:
- Kelch domain-containing protein 3
- Kelch domain-containing protein 2
- Protein fem-1 homolog B
- Protein fem-1 homolog C
- Cullin-2
- Protein zer-1 homolog
- Kelch domain-containing protein 10
- Elongin-B
- Protein fem-1 homolog A-A
- Protein zyg-11 homolog B
Sequence:
MAAVELEWIPETLYNTAISAVVDNYIRSRRDIRSLPENIQFDVYYKLYQQGRLCQLGSEFCELEVFAKVLRALDKRHLLHHCFQALMDHGVKVASVLAYSFSRRCSYIAESDAAVKEKAIQVGFVLGGFLSDAGWYSDAEKVFLSCLQLCTLHDEMLHWFRAVECCVRLLHVRNGNCKYHLGEETFKLAQTYMDKLSKHGQQANRAALYGELCALLFAKSHYDEAYKWCVEAMKEITAGLPVKVVVDVLRQASKACVVKREFKKAEQLIKHAVYLARDHFGSKHPKYSDTLLDYGFYLLNVDNICQSVAIYQAALDIRQSVFGGKNIHVATAHEDLAYSSYVHQYSSGKFDNALFHAERAIGIITHILPEDHLLLASSKRVKALILEEIAIDCHNKETEQRLLQEAHDLHLSSLQLAKKAFGEFNVQTAKHYGNLGRLYQSMRKFKEAEEMHIKAIQIKEQLLGQEDYEVALSVGHLASLYNYDMNQYENAEKLYLRSIAIGKKLFGEGYSGLEYDYRGLIKLYNSIGNYEKVFEYHNVLSNWNRLRDRQYSVTDALEDVSSSPQSTEEVVQSFLMAQNVEGPSC
Protein: Prolyl 4-hydroxylase subunit alpha 2 (C9JCP0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLD
Protein: Zinc finger protein ZAT3 (Protein DUO1-ACTIVATED ZINC FINGER 2) (O65499)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the regulation of male germ cell division by DUO1.
Subcellular location: Nucleus {ECO:0000269|PubMed:24876252}.
Interaction partners:
- Transcription factor DUO1
- Protein HAPLESS 2
- Homeodomain-like superfamily protein
- Protein GAMETE EXPRESSED 2
- C2H2-like zinc finger protein
- Pectinesterase PPME1
- Protein DMP9
- C2H2-type zinc finger family protein
Sequence:
MNNNHSYDDRSFHIPLHPSNTSNPNPNLQFALSSSYDHSPKKKRTKTVASSSSSSPKSASKPKYTKKPDPNAPKITRPCTECGRKFWSWKALFGHMRCHPERQWRGINPPPNYRVPTAASSKQLNQILPNWVSFMSEEDHEVASCLLMLSNGTPSSSSIERFECGGCKKVFGSHQALGGHRASHKNVKGCFAITNVTDDPMTVSTSSGHDHQGKILTFSGHHKCNICFRVFSSGQALGGHMRCHWEKEEEPMISGALDLNVPPTIQDLSTSDTSGCCLDLRLGL
Protein: GH10101p (Mayday, isoform A) (Mayday, isoform B) (Q9VDY9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP10645p
Sequence:
MTFVNKLSKSFRWLRCSTLCAILFYMFFIGLILHSTSQKLQQQLKEQGTSSSSSSSSSSSSSSSSSSSSSTQADTKMAPNVGHNGAQRWPNTLQELEQQQQKHEQSMRLQPVANNLDSRNENNHRQPHPQSQKVQNASKSPNQPETVILAASNVNEKQILAKAFKRADRSRDGILSIQELGQYINRRIVEHIDEAIMNNAREFRRVDIGPADGLITWDEYHRFFLREHGMTEADIDEHDEIRHTALNRRAREDMMRDKARWSEAARTDLFTLTIDEYLSFRHPESSVSNLLELVDDLLRQFDQDGDDQLTLEEFSDLNVDDDDDLMRKSLISKTLVERREEFKRIIDKNHDGKADRGELLNYVNPKTPRYALQEAATLFSLCDENKDELLTLKEMTDHAEIFLQSKMIDTANSFHTEF