wanglab/gogpt-training-data huggingface dataset:
Protein: RIB43A-like with coiled-coils protein 1 (Q8N443)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9D0B8}.
Interaction partners:
- Protein Tob2
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 11
- Protein BTG3
- CCR4-NOT transcription complex subunit 6-like
Sequence:
MYNIKQSTDTKEAAAIEARRNREKERQNRFFNVRNRVMGVDVQALNNQVGDRKRREAAERSKEAAYGTSQVQYDVVVQMLEKEEADRTRQLAKKVQEFREQKQQLKNGREFSLWDPGQVWKGLPTYLSYSNTYPGPASLQYFSGEDLDRDTRLRMQQGQFRYNLERQQQEQQQAKVDENYTDALSNQLRLAMDAQATHLARLEESCRAAMMCAMANANKAQAAVQAGRQRCERQREQKANLAEIQHQSTSDLLTENPQVAQHPMAPYRVLPYCWKGMTPEQQAAIRKEQEVQRSKKQAHRQAEKTLDTEWKSQTMSSAQAVLELEEQERELCAVFQRGLGSFNQQLANEQKAQQDYLNSVIYTNQPTAQYHQQFNTSSR
Protein: Cytochrome c oxidase subunit 6C-2 (Cytochrome c oxidase polypeptide VIc-2) (P11951)
Organism: Rattus norvegicus (Rat)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P04038}; Single-pass membrane protein {ECO:0000250|UniProtKB:P04038}.
Interaction partners:
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit 6, mitochondrial
Sequence:
MSSGALLPKPQMRGLLAKRLRVHIVGAFVVALGVAAAYKFGVAEPRKKAYADFYRNYDSMKDFEEMRQAGVFQSAK
Protein: Brain-derived neurotrophic factor (proBDNF) (A0A0E3SU01)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU364086}.
Interaction partners:
Sequence:
MTILFLTMVISYFGCMKAAPMKEANIRGQGGLAYPGVRTHGTLESVNGPKAGSRGLTSLADTFEHVIEELLDEDQKVRPNEENNKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR
Protein: Cytochrome c oxidase polypeptide IV, mitochondrial (G8BCY3)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Complex III subunit 9
- Cytochrome c oxidase subunit
- quinol--cytochrome-c reductase
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome c oxidase subunit
- Uncharacterized protein
Sequence:
MLSRSLRIVSQRRLLSTTRILANKAPQTTTEVKTAQDLAEVTGPASLIGPGAKPGTIPTDWDQSTGLQRLELLGKREGVDVFDMEMPITEGKGTMDDPFLVPTYIGYRYVGCKGTAELDHKPYWMKVEEGKPSRCWHCGTVLKTKYLGEPGMAH
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (Q8IPB1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKIDTCVLRFAKLTENALEPVRGSAKAAGVDLRSAYDVVVPARGKAIVKTDLQVQVPEGSYGRVAPRSGLAVKNFIDVGAGVVDEDYRGNLGVVLFNHSDVDFEVKHGDRIAQFICERIFYPQLVMVDKLEDTERGEAGFGSTGVKDLPAAKAQNGNGEKAAEPEGAAPAPVAT
Protein: Ubiquitin-conjugating enzyme E2 G2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme G2) (Ubiquitin carrier protein G2) (Ubiquitin-protein ligase G2) (P60604)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD). Required for sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent proteasomal degradation.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:23223569}. Lipid droplet {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:23223569}.
Interaction partners:
- E3 ubiquitin-protein ligase AMFR
- Lipid droplet-regulating VLDL assembly factor AUP1
- E3 ubiquitin-protein ligase MARCHF6
- Ubiquitin-conjugating enzyme E2 J1
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-conjugating enzyme E2 G1
- ER membrane protein complex subunit 3
- Polyubiquitin-C
- E3 ubiquitin-protein ligase parkin
- FAS-associated factor 2
Sequence:
MAGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFPAILSFPLDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQSVEKILLSVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL
Protein: Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate synthase) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (P-Rib-PP synthase) (PRPP synthase) (PRPPase) (P9WKE3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) and of the decaprenylphosphoryl-arabinose (DPA), an essential precursor for the mycobacterial cell wall biosynthesis. Catalyzes the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P) to yield phosphoribosyl diphosphate (PRPP) and AMP. It can also use GTP, CTP and UTP as diphosphoryl donors.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
Interaction partners:
- 3-methyl-2-oxobutanoate dehydrogenase subunit beta
- Multifunctional 2-oxoglutarate metabolism enzyme
- Bifunctional protein GlmU
- Transketolase
- Amidophosphoribosyltransferase
- Ribokinase
- Ribose-5-phosphate isomerase B
- Probable phosphoglucomutase PgmA
- Orotate phosphoribosyltransferase
- GMP synthase
Sequence:
MSHDWTDNRKNLMLFAGRAHPELAEQVAKELDVHVTSQDAREFANGEIFVRFHESVRGCDAFVLQSCPAPVNRWLMEQLIMIDALKRGSAKRITAVMPFYPYARQDKKHRGREPISARLIADLLKTAGADRIVTVDLHTDQIQGFFDGPVDHMRGQNLLTGYIRDNYPDGNMVVVSPDSGRVRIAEKWADALGGVPLAFIHKTRDPRVPNQVVSNRVVGDVAGRTCVLIDDMIDTGGTIAGAVALLHNDGAGDVIIAATHGVLSDPAAQRLASCGAREVIVTNTLPIGEDKRFPQLTVLSIAPLLASTIRAVFENGSVTGLFDGDA
Protein: Protein SNA3 (P14359)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Vacuole lumen. Cytoplasmic vesicle membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Sorted via late endosomes to the vacuolar lumen in a ubiquitin-independent manner.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- Protein SNA2
- Polyubiquitin
- Carboxypeptidase S
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40A fusion protein
- Protein COS5
- Ubiquitin carboxyl-terminal hydrolase 4
- Plasma membrane proteolipid 3
- Uncharacterized protein YCR043C
Sequence:
MDRDHINDHDHRMSYSINKDDLLLMVLAVFIPPVAVWKRKGMFNRDTLLNLLLFLLLFFPAIIHACYVVYETSSERSYDLSRRHATAPAVDRDLEAHPAEESQAQPPAYDEDDEAGADVPLMDNKQQLSSGRT
Protein: Interferon regulatory factor 7B (D2SR00)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Interferon regulatory factor 3
- TNF receptor-associated factor 6-like
- Serine/threonine-protein kinase TBK1
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon-like
- Myeloid differentiation primary response protein MyD88
- TNF receptor-associated factor 6-like
- TIR domain-containing adapter molecule 1-like
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MTEVRGSALTMQSRNPKPQFADWLIEQVWTGQYAGLYFVGNNKFRVPWNHISRKDCCEDDSKIFRAWAVVSGKINTHPNDKAKWKTNFRCVLNNLTKRFMMVEDHSKDSDDPHKVYLIINNESNYGSPHIEEIAVEDYDIDIHSSLTSTGYTPPGMEHDNLLKLVNTLDLNQHTEEWAENYIHTHHPVVPEDCYPFQPLTEPQPVSQNHSPPPVPVPIQQPYDHVNQDALLNLPAAQPSLCDLEITISYRRREMLKTQVSGPLVQLHYQCDIPEPNAQTLCFPSTDGLLDHKQIEYTNRILGSVQRGLLLEVRNTGIYGYRQDKCHVFSSTSDPREAHPEPRKMPQNEMVQLLSFDKYMTDLIAFKENRGGSPDYTIHMCFGEKFPDGKPLEKKLIIVKVVPLICRHFHEVAQGEGASSLQNDNISLQISHHNSLMELISATWPDGPQHTMGQYF
Protein: Archaic translocase outer mitochondrial membrane 40 (Q38E31)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLKEWLRGKQSEEPVAQAEPVKRGALGVDVESSLEPSQEEIIAQREDAFRRKLAASAKEGPPSPGKVVAYDTLLRPLQRLLLDGNAAETQEGLTISVARNAQNVMMSTKTMLVSPQMSNWELSLQMNGFSDIVVATYNTLSRWSLMYQRVSSTGALLFAQCMAQRQQGMTQGTVVGMIQYPWVQGGCTQVQYVKDQSFSVSHAQRLIRGFYLGSNLSWDALTKGTSLSYAGCITNPSKTGSLAAEWSPSKGEWKVGLTRSDWASDVEFAMQLEYTKKGQSGLMGLLSFGTKKQFVGGGSVSTAMLGFSQLKAVVEVPFGGDRSGFNQFMCMYNALYDIHSGGLKHGVVFTA
Protein: Transcriptional repressor NrdR (P0A8D0)
Organism: Escherichia coli (strain K12)
Function: Represses transcription of the class Ib RNR genes nrdHIEF but has much smaller effect on transcription of the class Ia RNR genes nrdAB and class III RNR genes nrdDG. By binding to nrdR boxes in the promoter regions to alter promoter activity, nrdR differentially regulates nrdAB, nrdHIEF and nrdD transcription in aerobic growth.
Interaction partners:
- Riboflavin biosynthesis protein RibD
- Transcription antitermination protein NusB
- Protein NrdI
- 6,7-dimethyl-8-ribityllumazine synthase
- Anaerobic ribonucleoside-triphosphate reductase
- Alpha-2-macroglobulin
- Thiamine-monophosphate kinase
- Bifunctional ligase/repressor BirA
- Arginine repressor
- Ribonucleoside-diphosphate reductase 2 subunit beta
Sequence:
MHCPFCFAVDTKVIDSRLVGEGSSVRRRRQCLVCNERFTTFEVAELVMPRVVKSNDVREPFNEEKLRSGMLRALEKRPVSSDDVEMAINHIKSQLRATGEREVPSKMIGNLVMEQLKKLDKVAYIRFASVYRSFEDIKEFGEEIARLED
Protein: Cardiac ryanodine receptor 2 (Q8WN72)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Interaction partners:
Sequence:
ALLPMLSSLFEHIGQHQFGEDLILEDVQVSCYRILTSLYALGTSKSIYVERQRSALGECLAAFAGAFPIAFLETHLDKHNIYSIYNTKSSRERAALNLPTNVEDVCPNIPSLEKLMEEIVELAESGIRYTQMPHVMEVILPMLCSYMSRWWEHGPENNPERAEMCCTALNSE
Protein: Uncharacterized protein YDR514C (Q04408)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ferulic acid decarboxylase 1
Sequence:
MSSSTKCKKAYEAVVKMVTHRFNSKAVRNYHQPQGLNRSLATRNAARVRGMVPSRRGGVGLYKSSSSKLMNKLGRQKTWINEFEHFNSLHEIAYTPNIALSSEIQKYLKALETNYRSIYEKSSELLDKKLEEIDKKWIEKNGCIPDASKDDVEKNLRKQYLADVQDVKNEHIPVMNCEPGGSQFKYLCKTIELLSSNKTICFAIDVEAFEFDTDIVTEIGIAIYDPRENIYSLMPIIRSYHLIVAEALPLRNKKFVCDFKDCFLLGESLVLPLEQCVEFIQSLINFYMKCETDQDTTWERAFVGHAIAGDIKWLKKIGVHVPELDNELTKPEDSTESKGVRKHVKMLDTEKIYSMCYGKKGSSLGKLLRLFHLPHAFLHNAGNDAYYTLLLMLKLGDYNFRKQIGADDLETMGYRIREWFKREADEPKILPMSYVLSVMNANNSKPKVDDKGRKKPRDLVPQTEFSGSHWFQNARAAFKSTLV
Protein: Heat stress transcription factor A-8 (AtHsfA8) (AtHsf-03) (Heat shock factor protein 5) (HSF 5) (Heat shock transcription factor 5) (HSTF 5) (Q9S7U5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- S-protein homolog 18
Sequence:
MVKSTDGGGGSSSSSSVAPFLRKCYDMVDDSTTDSIISWSPSADNSFVILDTTVFSVQLLPKYFKHSNFSSFIRQLNIYGFRKVDADRWEFANDGFVRGQKDLLKNVIRRKNVQSSEQSKHESTSTTYAQEKSGLWKEVDILKGDKQVLAQELIKVRQYQEVTDTKMLHLEDRVQGMEESQQEMLSFLVMVMKNPSLLVQLLQPKEKNTWRKAGEGAKIVEEVTDEGESNSYGLPLVTYQPPSDNNGTAKSNSNDVNDFLRNADMLKFCLDENHVPLIIPDLYDDGAWEKLLLLSPSRKKTKKQENIVKKGKDDLTLEEEEEDGTMELDKSYMLKLISEEMEKPDDFEFGQLTPERSRNLEILTEQMELLASNE
Protein: Methylenetetrahydrofolate reductase 1 (EC 1.5.1.20) (Q10258)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Major methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine. Performs 80 to 85 percent of the total methylenetetrahydrofolate reductase activity of the cells.
Interaction partners:
- Methylenetetrahydrofolate reductase 2
- Methylenetetrahydrofolate dehydrogenase [NAD
- Serine hydroxymethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Probable serine hydroxymethyltransferase, cytosolic
- Probable thymidylate synthase
- Probable aminomethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, mitochondrial
- Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Uncharacterized protein C57A7.07c
Sequence:
MKISDKLLHPDWKEKVTYSYEFFPPKTSTGVQNLYNRIDRMKTWGRPMFVDVTWGAGGTSSELTPGIVNVIQTDFEVDTCMHLTCTNMSTEMIDAALKRAHETGCRNILALRGDPVKDTDWTEGESGFRYASDLVRYIRTHYNDEFCIGVAGYPEGYSPDDDIDESIKHLKLKVDEGADFIVTQMFYDVDNFIAWVDKVRAAGINIPIFPGIMPIQAWDSFIRRAKWSGVKIPQHFMDTLVPVKDDDEGVRERGVELIVEMCRKLIASGITRLHFYTMNLEKAVKMIIERLGLLDENLAPIVDTNNVELTNASSQDRRINEGVRPIFWRTRNESYVSRTDQWDELPHGRWGDSRSPAFGEFDAIRYGLRMSPKEITTSWGSPKSYSEIGDLFARYCEKKISSLPWSDLPISDEADLIRDQLLSMNRNAFLTINSQPALNGEKSSHPVFGWGPPNGYVFQKPYVEFFVHPSLLNELKETVKKLNSVSYFVTNKNGDLDTNSQYEIPNAVTWGVFPNREIIQPTIVESTSFLAWKDEAYSLGMEWANAYSPDSISRKLLVSMMKEWFLCVIVDNDFQNGQSLFDVFNKMRSLKDIHPELYYANAS
Protein: Elongation factor 2 (Q54JV1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Small ribosomal subunit protein eS30
- Glutathione S-transferase domain-containing protein
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL3
Sequence:
MVNFTIDQIRSIMDRRENIRNMSVIAHVDHGKTTLTDSLIQRAGIIADKVSGNAGYMSCRPDEQLRGITIKSSSVSLHFEMPKDEKLPTGCSSHEFLINLIDSPGHVDFSSEVTAALRVTDGALVVIDCVEGVCVQTETVLRQAMAERIKPVLFVNKVDRFLLELQLNSEDAYLSFTRAIESVNVVIGSFGCTGENNEFGNGMMGDINLSPEKGTIAFGSGLHGWGFTIGKFAKLYASKFGVSEEKLMSRLWGDNYFDQESKKWKTSNVPSSDDGSGEAKPLQRAFCQFILDPIYKLTRAVIDEDQDRIDSMLKVLNISLSPEDAELKGKNLIKSIMRKFLPASDAILSMVVSHLPSPLEAQKYRVSHLYEGPMDDKCALAIANCDPNGPLMMYVSKMIPTSDKGRFYAFGRVFSGTIRTGQKVRIMGPDYVPGKKDDLYLKSIQRTVLMMGRKIELLDDCPCGNIIGLVGVDQFLVKSGTISTEETAHNIRVMKFSVSPVVRVAVQPKNPSELPKLIEGLKILAKADPCVLCITETSGEHIVAGAGELHLEICLKDLEEDHAGIEIITSDPVVSFCESVSEESKIMCLAKSPNKHNRIYMKSEPLSSDLTDDIDNGLVAFNQDVKSRANYLYDKHSWDKNDAVNIWSFGPEYKGPNVLVNKTKGVQYLHEIKDSMVSAFQWISNEGVLCGEKMRSIRFNVYDVMLHADAIHRGSGQFIPTTRRVMYASQLSAQPTLLEPMYLVDISTPESGISGIYSVLNRRRGVVIGEERRIGTPLFNIKAYLPVMESFGLTADLRSSTAGQAFPQCVFDHWSSIGIVGQDKRSTEVASSIRKRKGLNPKLPTLEEYNEKL
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q57XG6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MAMPGYAATASVILMMVPQSSDADTATAAHASVYKALCSVLQLQAGKIKAPDQEQEWQNAMETINDVNMTLGGPAWVNQFLKPDGTQKQWDPQTSPAKENSHWASSWAEWAASAERVFKKHGADSRPSNFSKLSITDQQLKLARTRMSLILEQASTLQTKIKSLQAAIDNAEPAKIKKLLTEAAIGTGEAAKEFTDAGKTSAARASAAFCGAGTVTGTDDCLADILICVCTQGNSDIPTGANKICSDHASNHAPKAHNLAAENDIKNQYDALVKDCNFNTEEEITPDKMLTALRSLESHIKIFKTDAYFGTTDGAATCDGTRTNGVCFKMPKYKTGKKGMQELAWATKIETAAAAMRAGATAASTSNALAASLTLLSKAAEGLASESKLFAAATTGQSSGNQPATDHLRATKEAERVCKTANDNQKECENLKDKGCVFNPKGGEGKKCTLSEEAKKKVEKENQEKWWNDGKRESNRYTRHTKKKDCEKENEGHKPGEKANCGRIEDKCNDSSFFVNKKMALSMAAAVMSLVAF
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (A0A1D8PFU3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Polyubiquitin
- Vacuolar protein sorting-associated protein 27
- Class E vacuolar protein-sorting machinery protein HSE1
- ESCRT-III subunit protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Nucleotide exchange factor SIL1
- ESCRT-III subunit protein
- Vacuolar-sorting protein SNF7
Sequence:
MKNSVKETTELDNISRALVELLKKNHDSFKSLFNVQLDLLKLFDKQVNNLEATGYCDYEVAYALYMIIIQLIAVMKDKSNSKTADIYNGIQQSIRKKASNFKKVLGYFKNDDDEKDEDPLINRFKSLSGEKTHPATKIKKELIYREWITPVELERTLREKHVLLIDYRPKKDYLHNHIKFDNLINIEPRQIESLPESSTDSDLEEVLRVSLSEEEFQMFLIRNKFDLIVVYNYNYGSTSKERLYGILDLLEKENPFTSLIGILLNNKYISSRLKIAPSFLSGGILNWYHTLGADYLETSSIKNGDCLKEETRYLTSFSDYLSNSKESSPSEVTLANENNSAYIRPVQKKVEQFDSIPPKSTATVYSSPKVELPLTPTSSTPNSPAPPLQPLSSNGKSPNNVTAKDVTVSSKKSQFLESYATGLVNLGNSCYMNCVIQCLAATPQLTSFFFPTITESFSDHSYKRHINVNNKLGTKGMLTTSFVELILSMLNNNGRSFSPSKFKKIMGSLSPARQFASFDQQDCIEFLNFLLDALHEDLNQVTIADPQERKMITELTPEQEKNREILPVRLASTIEWERYLKLNFSIIVDYFQGQYLSQLKCLECGFTSTTYNAFSILSLPIPEKLNKSMKVSLDECLQEFVTTELLDDNNKWYCPNCKKFTKSTKKIAITRLPQVLIINFKRFKMTASGGFHKLETFVTYPVNEELDMTPYWPDVGSTISANNSMSIEREKEILSTFPVRSQVPPFKYKLFGVANHYGNLTTGHYTAYVHKSSDSKKARNWCYFDDSRVTFNKSPNDVLNKNAYCLFFQRI
Protein: Sialidase-3 (EC 3.2.1.18) (Ganglioside sialidasedis) (Membrane sialidase) (N-acetyl-alpha-neuraminidase 3) (Q9UQ49)
Organism: Homo sapiens (Human)
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.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10861246, ECO:0000269|PubMed:17708748, ECO:0000269|PubMed:26251452, ECO:0000269|PubMed:28646141}; Peripheral membrane protein {ECO:0000269|PubMed:10861246, ECO:0000269|PubMed:17708748}. Membrane, caveola {ECO:0000269|PubMed:12011038}. Early endosome membrane {ECO:0000269|PubMed:26251452}; Peripheral membrane protein {ECO:0000305|PubMed:26251452}. Recycling endosome membrane {ECO:0000269|PubMed:26251452}; Peripheral membrane protein {ECO:0000305|PubMed:26251452}. Lysosome membrane {ECO:0000269|PubMed:26251452}; Peripheral membrane protein {ECO:0000305|PubMed:26251452}. Note=Associates with the external leaflet of the plasma membrane (By similarity). S-acylated NEU3 likely spans the lipid bilayer with a portion of C-terminus exposed to the cytosol and the catalytic region facing the extracellular space (PubMed:28646141). {ECO:0000250|UniProtKB:Q9JMH7, ECO:0000269|PubMed:28646141}.
Interaction partners:
- Arylsulfatase A
- 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
- Alpha-galactosidase A
- Galactosylceramide sulfotransferase
- Galactocerebrosidase
- Mucolipin-1
Sequence:
MEEVTTCSFNSPLFRQEDDRGITYRIPALLYIPPTHTFLAFAEKRSTRRDEDALHLVLRRGLRIGQLVQWGPLKPLMEATLPGHRTMNPCPVWEQKSGCVFLFFICVRGHVTERQQIVSGRNAARLCFIYSQDAGCSWSEVRDLTEEVIGSELKHWATFAVGPGHGIQLQSGRLVIPAYTYYIPSWFFCFQLPCKTRPHSLMIYSDDLGVTWHHGRLIRPMVTVECEVAEVTGRAGHPVLYCSARTPNRCRAEALSTDHGEGFQRLALSRQLCEPPHGCQGSVVSFRPLEIPHRCQDSSSKDAPTIQQSSPGSSLRLEEEAGTPSESWLLYSHPTSRKQRVDLGIYLNQTPLEAACWSRPWILHCGPCGYSDLAALEEEGLFGCLFECGTKQECEQIAFRLFTHREILSHLQGDCTSPGRNPSQFKSN
Protein: IQ calmodulin-binding motif-containing protein 1 (Q8BP00)
Organism: Mus musculus (Mouse)
Function: Involved in ciliogenesis. The function in an early step in cilia formation depends on its association with CEP290/NPHP6 (By similarity). Involved in regulation of the BBSome complex integrity, specifically for presence of BBS2 and BBS5 in the complex, and in ciliary targeting of selected BBSome cargos. May play a role in controlling entry of the BBSome complex to cilia possibly implicating CEP290/NPHP6 (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15051}. Note=Localization to the centrosome depends on the interaction with CEP290. {ECO:0000250|UniProtKB:Q15051}.
Interaction partners:
- Centrosomal protein of 290 kDa
- Nephrocystin-1
- X-linked retinitis pigmentosa GTPase regulator
- Nephrocystin-4
- Protein fantom
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Nephrocystin-3
- Ataxin-10
- Intraflagellar transport protein 122 homolog
- Inversin
Sequence:
MKPAGTDPRILSLAAEVAKSPEQNVPVILLKLKEIINNTPLGSSELKKVKQDIYCYDLIQYCLLVLSQDSSRIQGGWSTISQLTQILSHCCVGLEPGEDGEEFYKELLPSAAENFLILGRRLQTCFINATKGEEQDKLLHFFQIVTDSLFWLLGGHVQLIQNVLQSDHFLHLLQTDNVQIGASVMTLLQNILQINSGNLLKIEGKALHSILDEILFKLLSTPSPVIRSTATKLLLVLAESHQEILILLRLSACYKGLRSLLNKQETLTEFSRELRQLVDLLTPKIHQEVEEQKLHKAACLIQAYWKGFQTRKRLKKLPSAVIALQRSFRSKRTKMMLELNRQKEEEDLRLKLQLQRQRAMRLSRESRLNMLEIIHPGQVEKYNREMEEKSALTIQKHWRGYRERKNFRQQRPSLTEYKAAVTLQRAVLKFLAKCRKKKKLFASWHGLQELTDARRVELKQQVDDYVKRHPCSQMSEAASRELHAQAQERLQHYFMGRAIEERAQQHREALMAQISTNIEQLMKAPSLKEAEGKEPEQFLSRSRPVAAKAKQAHLTTLKHIQAPWWKKLGEEPGDEVDVPKDELSIDLGMLFIGGTKPP
Protein: Probable basic-leucine zipper transcription factor R (Q54GH2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable transcriptional regulator.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Probable basic-leucine zipper transcription factor G
- Probable serine/threonine-protein kinase ifkC
- Probable serine/threonine-protein kinase ifkB
- Probable serine/threonine-protein kinase ifkA
- Eukaryotic translation initiation factor 2 subunit 1
Sequence:
MDNFENPLLAPDQDVLLYLLDGYSQLQQLQKQQFNIHDDNINYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIGSPQIMNENIETNSNDPQYLERLQSIQQQQHQCQTQIQQQLQNYQQQYEDQYQQRQQQYQDQYQKPYSSPPLNFNSIPPITNNNNNNNNNNNNNNNNNNSNSNSNSNSNSNSNSNSNSNSNSNNNNINNNICINNNDISIFLLNNQIQLQPLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPTQPTQPTKPIQLTQPIQLTQPTLLEELKDISIQQQLLSAIQQTAQSPQQIHPLQQLQPYQLQSYQQIQASQQLQPYQQLIQLQQLQLQQLEEEKRQQQKQLLLQQQQLQEQQEKLQQQLLQQQKQQLKQKVKQQKQQHQKQQPQQQQQSIQIPPELQNYILNNNNNNNNNNTNKTLSPISEMIQNQFLNNQQTILNQNNSTLQLPTPFYSPQQQQQQHTPISSFIPPPSLPSSPPSPPSPPSPPPQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQQQQLQQQQLQQQHQLKESYESKESIKKYNQNIASRNYRLKKKDYIKEIENKIATLSLENNRLEKENGSIRTNGSIEMMRMEPESMKMLMDGKLIIENIKHALIIDDEKSLIYLLHQYHRTIDQRYSLLEKEVNKLINPYTQLRLCCIGYVPKSSPLVLNIFQGPESDKWLNLFKIEANITPEQSIKIDSLRFQYGKVSSRLSNELLELDLIIKRFFIKNVLPTPDTPLLNSDYYSEGELIPNTTTESIAPLNNFELLDFASKLESLKNKIILNASLGLDTFATLCSILTPKQEALLLVRVNLFCIDLHHHDILGEVWTNVNQISNSLSNPLTSFSDSMKKINFSFLQLDNNNNNYHYKIN