wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylserine synthase 1 (PSS-1) (PtdSer synthase 1) (EC 2.7.8.29) (Serine-exchange enzyme I) (Q99LH2)
Organism: Mus musculus (Mouse)
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10938271}; Multi-pass membrane protein {ECO:0000269|PubMed:10938271}. Note=Highly enriched in the mitochondria-associated membrane (MAM).
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphatidylethanolamine N-methyltransferase
- Choline/ethanolaminephosphotransferase 1
- Phosphatidylserine synthase 2
- Cholinephosphotransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipase A1 member A
- Phospholipase D1
- Lysophospholipid acyltransferase 5
- Phospholipase D2
Sequence:
MASCVGSRTLSKDDVNYRMHFRMINEQQVEDITIDFFYRPHTITLLSFTIISLMYFAFTRDDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLFLNFEQVKSLMYWLDPNLRYATREADIMEYAVNCHVITWERIVSHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGIYLFMIIWQLTELNTFFLKHIFVFQASHPLSWGRILFIGCITAPTVRQYYAYLTDTQCKRVGTQCWVFGVIGFLEAIVCIKFGQDLFSKTQILYVMLWLLCVAFTTFLCLYGMVWYAEHYGHREKTYSECEDGTYSPEISWHHGKGSKGSEDSPPKHSSNHESHSSRRRNRHSKSKVTNGVGKK
Protein: MIF4G domain-containing protein (SLBP-interacting protein 1) (hSLIP1) (A9UHW6)
Organism: Homo sapiens (Human)
Function: Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18025107}. Nucleus {ECO:0000269|PubMed:18025107}.
Interaction partners:
- Histone RNA hairpin-binding protein
- ATP-dependent RNA helicase DDX19A
- ATP-dependent RNA helicase DDX19B
- CBP80/20-dependent translation initiation factor
- Eukaryotic translation initiation factor 4 gamma 1
Sequence:
MGEPSREEYKIQSFDAETQQLLKTALKDPGAVDLEKVANVIVDHSLQDCVFSKEAGRMCYAIIQAESKQAGQSVFRRGLLNRLQQEYQAREQLRARSLQGWVCYVTFICNIFDYLRVNNMPMMALVNPVYDCLFRLAQPDSLSKEEEVDCLVLQLHRVGEQLEKMNGQRMDELFVLIRDGFLLPTGLSSLAQLLLLEIIEFRAAGWKTTPAAHKYYYSEVSD
Protein: HIV-1 Tat specific factor 1 (Q5H918)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGTNLDGNDEFDEQLRMQELYGDGKDGDTQTDAGGEPDSLGQQPTDTPYEWDLDKKAWFPKITEDFIATYQANYGFSNDGASSSTANVEDVHARTAEEPPQEKAPEPTDARKKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDNQGNLKGDGLCCYLKRESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSMQQ
Protein: Small ubiquitin-related modifier 4 (SUMO-4) (Small ubiquitin-like protein 4) (Q6EEV6)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may modulate protein subcellular localization, stability or activity. Upon oxidative stress, conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. May also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I.
Interaction partners:
- SUMO-conjugating enzyme UBC9
- E3 SUMO-protein ligase PIAS4
- E3 SUMO-protein ligase RanBP2
- E3 SUMO-protein ligase NSE2
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- Small ubiquitin-related modifier 1
- Cellular tumor antigen p53
- EP300-interacting inhibitor of differentiation 3
- Non-structural maintenance of chromosomes element 4 homolog A
Sequence:
MANEKPTEEVKTENNNHINLKVAGQDGSVVQFKIKRQTPLSKLMKAYCEPRGLSVKQIRFRFGGQPISGTDKPAQLEMEDEDTIDVFQQPTGGVY
Protein: NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (RUB-activating enzyme) (Ubiquitin-activating enzyme E1-like protein) (O65041)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the dimeric ECR1-AXR1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-ECR1 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of RCE1 (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- NEDD8-activating enzyme E1 regulatory subunit AXL
- NEDD8-activating enzyme E1 regulatory subunit AXR1
- Probable NEDD8-conjugating enzyme Ubc12-like
- NEDD8-conjugating enzyme Ubc12
- NAD
- NEDD8-like protein RUB3
- F12F1.16 protein
- E3 ubiquitin-protein ligase UPL3
- E3 ubiquitin-protein ligase UPL4
- Ubiquitin carboxyl-terminal hydrolase 3
Sequence:
MADLDVPPQVPQSKTRDLDKLLLRHGNLVDPGFVPGPGLRDDIRDYVRILVIGAGGLGCELLKDLALSGFRNLEVIDMDRIEVTNLNRQFLFRIEDVGKPKAEVAAKRVMERVSGVEIVPHFSRIEDKEIEFYNDFNIIALGLDSIEARKYINGVACGFLEYNEDDTPKRETIKPMVDGGTEGFKGHARVILPGVTPCFECTIYLFPPQVKFPLCTLAETPRNAAHCIEYAHLIQWETVHRGKTFDPDEPEHMKWVYDEAIRRAELFGIPGVTYSLTQGVVKNIIPAIASTNAIISAACALETLKIVSACSKTLVNYLTYNGGEGLYTEVTKFERDTECLVCGPGILIELDTSVTLSKFIEMLEDHPKLLLSKASVKQGENTLYMQAPPVLEEFHRPKLSKPLYDLMGRVQKDTIHVFGQRALKNNEKESCTTKVRVVFKGADGVADMDTAIGA
Protein: Cullin-associated NEDD8-dissociated protein 2 (Cullin-associated and neddylation-dissociated protein 2) (Epididymis tissue protein Li 169) (TBP-interacting protein of 120 kDa B) (TBP-interacting protein 120B) (p120 CAND2) (O75155)
Organism: Homo sapiens (Human)
Function: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- TATA-box-binding protein
- Cullin-3
Sequence:
MSTAAFHISSLLEKMTSSDKDFRFMATSDLMSELQKDSIQLDEDSERKVVKMLLRLLEDKNGEVQNLAVKCLGPLVVKVKEYQVETIVDTLCTNMRSDKEQLRDIAGIGLKTVLSELPPAATGSGLATNVCRKITGQLTSAIAQQEDVAVQLEALDILSDMLSRLGVPLGAFHASLLHCLLPQLSSPRLAVRKRAVGALGHLAAACSTDLFVELADHLLDRLPGPRVPTSPTAIRTLIQCLGSVGRQAGHRLGAHLDRLVPLVEDFCNLDDDELRESCLQAFEAFLRKCPKEMGPHVPNVTSLCLQYIKHDPNYNYDSDEDEEQMETEDSEFSEQESEDEYSDDDDMSWKVRRAAAKCIAALISSRPDLLPDFHCTLAPVLIRRFKEREENVKADVFTAYIVLLRQTQPPKGWLEAMEEPTQTGSNLHMLRGQVPLVVKALQRQLKDRSVRARQGCFSLLTELAGVLPGSLAEHMPVLVSGIIFSLADRSSSSTIRMDALAFLQGLLGTEPAEAFHPHLPILLPPVMACVADSFYKIAAEALVVLQELVRALWPLHRPRMLDPEPYVGEMSAVTLARLRATDLDQEVKERAISCMGHLVGHLGDRLGDDLEPTLLLLLDRLRNEITRLPAIKALTLVAVSPLQLDLQPILAEALHILASFLRKNQRALRLATLAALDALAQSQGLSLPPSAVQAVLAELPALVNESDMHVAQLAVDFLATVTQAQPASLVEVSGPVLSELLRLLRSPLLPAGVLAAAEGFLQALVGTRPPCVDYAKLISLLTAPVYEQAVDGGPGLHKQVFHSLARCVAALSAACPQEAASTASRLVCDARSPHSSTGVKVLAFLSLAEVGQVAGPGHQRELKAVLLEALGSPSEDVRAAASYALGRVGAGSLPDFLPFLLEQIEAEPRRQYLLLHSLREALGAAQPDSLKPYAEDIWALLFQRCEGAEEGTRGVVAECIGKLVLVNPSFLLPRLRKQLAAGRPHTRSTVITAVKFLISDQPHPIDPLLKSFIGEFMESLQDPDLNVRRATLAFFNSAVHNKPSLVRDLLDDILPLLYQETKIRRDLIREVEMGPFKHTVDDGLDVRKAAFECMYSLLESCLGQLDICEFLNHVEDGLKDHYDIRMLTFIMVARLATLCPAPVLQRVDRLIEPLRATCTAKVKAGSVKQEFEKQDELKRSAMRAVAALLTIPEVGKSPIMADFSSQIRSNPELAALFESIQKDSASAPSTDSMELS
Protein: Cyclase-like protein 4 (OsCYL4) (Q6YX89)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May be involved in the control of plant responses to environmental stresses.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:25974367}.
Interaction partners:
- Os01g0772400 protein
- Malate synthase
- L-2-hydroxyglutarate dehydrogenase, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Probable NADPH:quinone oxidoreductase 1
- Probable NADPH:quinone oxidoreductase 2
Sequence:
MAPTPLFLLLLLTGVTAEPAHPGYAEGDGSSCDVAAVAVAERREEFDGGRIVDISHYYREEMPEWESADGTGGGFLRLVRSMRNGSDIANFSELRLTAHSGTHVDAPGHVFDHYYHAGFDVDTLDLAILNGPALLVDVPRDSNITANVMESLHIPKGVRRVLFRTLNTDRKLMWKKEFDTSYVGFMKDGAQWLIDNTDIRLVGVDYLSVGAFDECIPAHLVFLEKREVILVEALHLEHVTPGIYTLHCLPLRLRGSEGSPARCILIK
Protein: Protein RecA (Recombinase A) (P42442)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
Interaction partners:
- LexA repressor
- Regulatory protein RecX
- DNA repair protein RadA
- DNA polymerase I
- DNA polymerase IV
- ATP-dependent DNA helicase RecQ
- DNA-directed RNA polymerase subunit beta
- DNA repair protein RecN
- DNA gyrase subunit B
- Crossover junction endodeoxyribonuclease RuvC
Sequence:
MAPKKTATKATAAKGNDRQKALDAALALIEKDFGKGAVMRLGDENRPPIQTISSGNTAIDIALGIGGFPRGRIVEVYGPESSGKTTVALHAIAQAQKAGGIAAFIDAEHALDPDYARKLGVDTDALLVSQPDTGEQALEIADMLVRSGAIDIIVIDSVAALTPKAEIEGEMGDSHVGLQARLMSQALRKMTGALYNSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRCDIRRIQTLKDGQDAIGNRTRLKVVKNKVSPPFKIAEFDIMYGEGISRESSVIDLAVDNGIVKKSGSWFTYEGEQLGQGKEKVRLSLKENPELTDELEDKIFKKLGVGKYAAASDELTDDPVELVPNVDFDDEADTEADAED
Protein: Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (MAP2 RNA trans-acting protein 1) (MARTA1) (Q99PF5)
Organism: Rattus norvegicus (Rat)
Function: Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs (By similarity). Binds to the dendritic targeting element and may play a role in mRNA trafficking.
Subcellular location: Nucleus {ECO:0000269|PubMed:12358751}. Cytoplasm {ECO:0000269|PubMed:12358751}. Note=A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites.
Interaction partners:
- 14-3-3 protein zeta/delta
- Heterogeneous nuclear ribonucleoprotein D0
- Poly
- Ribonuclease 3
- ELAV-like protein 1
- Poly
- RAC-alpha serine/threonine-protein kinase
- Heterogeneous nuclear ribonucleoprotein A1
- Endoribonuclease Dicer
- mRNA decay activator protein ZFP36
Sequence:
MSDYSTGGPPPGPPPPAGGGGGAAGAGGGPPPGPPGAGDRGGGGPGGGGPGGGGASGGPSQPPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNNTPDFGFGGQKRQLEDGDQPDSKKLASQGDSIGSQLGPIHPPPRTSMTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRVGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDGTGPEKIAHIMGPPDRCEHAARIINDLLQSLRSGPPGPPGAPGMPPGGRGRGRGQGNWGPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQLPPNGDPNFKLFVIRGSPQQIDHAKQLIEEKIEGPLCPVGPGPGGPGPAGPMGPFHPGPFNQGPPGAPPHAGGPPPHQYPPQGWGNTYPEWQPPAPHDPNKAAAAATDPNAAWAAYYSHYYQQPPGPVPGPAPAPAAPPAQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAQVATGGGPGAPPGSQPDYSAAWAEYYRQQAAYYGQTPGPGGPQPPSTQQGQQQATEANGYELHL
Protein: Forkhead box protein D1 (FoxD1) (Brain factor 2) (BF-2) (xBF-2) (Xbf2) (Q9PSY4)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor that down-regulates bmp4 signaling in both mesoderm and ectoderm. Regulates mesoderm patterning by repressing ventral mesoderm genes and promoting the expression of dorsolateral genes. Can also neuralize ectodermal cells directly. Inhibits neural crest migration. The transcription factors foxd1 and foxg1 mutually repress each other to pattern the forebrain.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:9811586}.
Interaction partners:
Sequence:
MTLSSDMSDVLAEETDIDVVGEEDEPRAEEEEEEDGELLMPRSPHCSSTKDPYKAAGSGGVGRSALVKPPYSYIALITMSILQSPKKRLTLSEICDFISSRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPESADMFDNGSFLRRRKRFKRQQVPELVLREPGHFLPASAYGYGPYSCAYGIQIQPFHPHSALIAFQQQQQHQQQQARHQQQQARHQQQQARHQQQPPSLPSMAAPALMPPAAQDLSRTCTFYPHQLSPAALPPSLQSKSSSALARSTFSIESIIGGDLNPGPKAAGVPVISRALVTFSSSEAAAALGGNLQPGTVLTNH
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (H0Y548)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWSMALDDIALHCCSPGSPVLTGWMASMLCSVTSKRAWTS
Protein: Exostosin-2 (EC 2.4.1.224) (Exostosin glycosyltransferase 2) (Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Heparan sulfate co-polymerase subunit EXT1) (Multiple exostoses protein 2) (Q93063)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. Required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10679296}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:35137078}; Single-pass type II membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10679296}; Single-pass type II membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:O77783}. Note=The active heparan sulfate polymerase complex composed of EXT1 and EXT2 is localized to the Golgi apparatus. If both proteins are individually detected in the endoplasmic reticulum, the formation of the complex promotes their transport to the Golgi. {ECO:0000269|PubMed:10679296}.
Interaction partners:
- Exostosin-1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Homeobox protein aristaless-like 4
- 1-aminocyclopropane-1-carboxylate synthase-like protein 1
- Probable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2
- Hematopoietically-expressed homeobox protein HHEX
- Heparan sulfate 2-O-sulfotransferase 1
- Proton-coupled zinc antiporter SLC30A8
- Heat shock protein 75 kDa, mitochondrial
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
Sequence:
MCASVKYNIRGPALIPRMKTKHRIYYITLFSIVLLGLIATGMFQFWPHSIESSNDWNVEKRSIRDVPVVRLPADSPIPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYALKKYVDDFGVSVSNTISREYNELLMAISDSDYYTDDINRACLFVPSIDVLNQNTLRIKETAQAMAQLSRWDRGTNHLLFNMLPGGPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVYSPLSAEVDLPEKGPGPRQYFLLSSQVGLHPEYREDLEALQVKHGESVLVLDKCTNLSEGVLSVRKRCHKHQVFDYPQVLQEATFCVVLRGARLGQAVLSDVLQAGCVPVVIADSYILPFSEVLDWKRASVVVPEEKMSDVYSILQSIPQRQIEEMQRQARWFWEAYFQSIKAIALATLQIINDRIYPYAAISYEEWNDPPAVKWGSVSNPLFLPLIPPQSQGFTAIVLTYDRVESLFRVITEVSKVPSLSKLLVVWNNQNKNPPEDSLWPKIRVPLKVVRTAENKLSNRFFPYDEIETEAVLAIDDDIIMLTSDELQFGYEVWREFPDRLVGYPGRLHLWDHEMNKWKYESEWTNEVSMVLTGAAFYHKYFNYLYTYKMPGDIKNWVDAHMNCEDIAMNFLVANVTGKAVIKVTPRKKFKCPECTAIDGLSLDQTHMVERSECINKFASVFGTMPLKVVEHRADPVLYKDDFPEKLKSFPNIGSL
Protein: Transcription factor E2FA (E2F transcription factor-3) (AtE2F3) (Q9FNY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The binding of retinoblastoma-related proteins represses transactivation. Regulates gene expression both positively and negatively. Activates the expression of E2FB. Involved in the control of cell-cycle progression from G1 to S phase. Stimulates cell proliferation and delays differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11891240}. Nucleus {ECO:0000269|PubMed:11891240}. Note=Interaction with DPA induces an exclusive nuclear localization, but an interaction with DPB has no effect.
Interaction partners:
- Transcription factor-like protein DPA
- Retinoblastoma-related protein 1
- Transcription factor-like protein DPB
- Cyclin-dependent kinase A-1
- Cyclin-D3-1
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-1
- Cyclin-A2-3
- Cyclin-A2-1
Sequence:
MSGVVRSSPGSSQPPPPPPHHPPSSPVPVTSTPVIPPIRRHLAFASTKPPFHPSDDYHRFNPSSLSNNNDRSFVHGCGVVDREEDAVVVRSPSRKRKATMDMVVAPSNNGFTSSGFTNIPSSPCQTPRKGGRVNIKSKAKGNKSTPQTPISTNAGSPITLTPSGSCRYDSSLGLLTKKFVNLIKQAKDGMLDLNKAAETLEVQKRRIYDITNVLEGIDLIEKPFKNRILWKGVDACPGDEDADVSVLQLQAEIENLALEEQALDNQIRQTEERLRDLSENEKNQKWLFVTEEDIKSLPGFQNQTLIAVKAPHGTTLEVPDPDEAADHPQRRYRIILRSTMGPIDVYLVSEFEGKFEDTNGSGAAPPACLPIASSSGSTGHHDIEALTVDNPETAIVSHDHPHPQPGDTSDLNYLQEQVGGMLKITPSDVENDESDYWLLSNAEISMTDIWKTDSGIDWDYGIADVSTPPPGMGEIAPTAVDSTPR
Protein: V-type proton ATPase subunit f (V-ATPase subunit f) (P0C5R9)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Accessory component of the V0 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.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30910982, ECO:0000305|PubMed:29526695}; Multi-pass membrane protein {ECO:0000269|PubMed:29526695, ECO:0000269|PubMed:30910982}. Vacuole membrane {ECO:0000269|PubMed:26928762, ECO:0000269|PubMed:30910982}; Multi-pass membrane protein {ECO:0000269|PubMed:30910982}.
Interaction partners:
- V-type proton ATPase subunit e
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit a, vacuolar isoform
- V0 assembly protein 1
- V-type proton ATPase subunit B
- Vacuolar ATPase assembly integral membrane protein VMA21
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit c
- V-type proton ATPase subunit F
Sequence:
MRPVVSTGKAWCCTVLSAFGVVILSVIAHLFNTNHESFVGSINDPEDGPAVAHTVYLAALVYLVFFVFCGFQVYLARRKPSIELR
Protein: Probable phosphomannomutase PmmA (PMM) (Phosphomannose mutase) (O86374)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- mannose-6-phosphate isomerase
- Mannose-1-phosphate guanylyltransferase
- Probable phosphomannomutase PmmB
- Conserved protein
- Glycogen phosphorylase
- Exonuclease
Sequence:
MSWPAAAVDRVIKAYDVRGLVGEEIDESLVTDLGAAFARLMRTEDARPVVIGHDMRDSSPSLADAFAAGVTGQGLDVVRVGLASTDQLYFASGLLDCPGAMFTASHNPAAYNGIKMCRAAAKPVGADTGLTAIRDDLIAGVARYDGTPGTIADQDVLVDYGAFLRSLVDTSGLRPLRVAVDAGNGMAGHTAPAVLGVIDSITLLPSYFELDGSFPNHEANPLDPANLVDLQAYVRDTGADIGLAFDGDADRCFVVDERGQPVSPSTVTALVAARELNREIGATIIHNVITSRAVPELVAERGGTPLRSRVGHSYIKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQSRPLSELTADYQRYESSGEINFTVVDSSACVEAVLKSFGNRIVSIDHLDGVTVDLGDDSWFNLRSSNTEPLLRLNVEGRSVGDVDAVVRQVSAEIAAQSAHAKAGP
Protein: Thyroxine 5-deiodinase (EC 1.21.99.3) (5DIII) (DIOIII) (Type 3 DI) (Type III iodothyronine deiodinase) (Q91ZI8)
Organism: Mus musculus (Mouse)
Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P55073}; Single-pass type II membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P55073}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Protein delta homolog 1
- Monocarboxylate transporter 8
Sequence:
MPRQAASRLVVGEGEGPPGASGPAATMLRSLLLHSLRLCAQTASCLVLFPRFLGTAFMLWLLDFLCIRKHFLRRRHPDHPEPEVELNSEGEEMPPDDPPICVSDDNRLCTLASLKAVWHGQKLDFFKQAHEGGPAPNSEVVRPDGFQSQRILDYAQGTRPLVLNFGSCTUPPFMARMSAFQRLVTKYQRDVDFLIIYIEEAHPSDGWVTTDSPYVIPQHRSLEDRVSAARVLQQGAPGCALVLDTMANSSSSAYGAYFERLYVIQSGTIMYQGGRGPDGYQVSELRTWLERYDEQLHGTRPHRF
Protein: DNA excision repair protein ERCC-1 (P07992)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:24036546}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:24036546}. Nucleus {ECO:0000269|PubMed:24036546}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:24036546}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000269|PubMed:24036546}.
Interaction partners:
- DNA repair endonuclease XPF
- DNA repair protein complementing XP-A cells
- Structure-specific endonuclease subunit SLX4
- UV excision repair protein RAD23 homolog B
- Structure-specific endonuclease subunit MUS81
- DNA excision repair protein ERCC-5
- General transcription and DNA repair factor IIH helicase subunit XPD
- DNA repair protein complementing XP-C cells
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Structure-specific endonuclease subunit SLX1
Sequence:
MDPGKDKEGVPQPSGPPARKKFVIPLDEDEVPPGVAKPLFRSTQSLPTVDTSAQAAPQTYAEYAISQPLEGAGATCPTGSEPLAGETPNQALKPGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIHGRLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDLALCPGLGPQKARRLFDVLHEPFLKVP
Protein: Treacle ribosome biogenesis factor 1 (A0A6I8PRA0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XAPAPGKVGDVTPQVKGGALPPAKRAKKPEEESESSEEGSESEEEAPAGTRSQVKASEKILQVRAASAPAKGTPGKGATPAPPGKAGAVASQTKAGKPEEDSESSSEESSDSEEETPAAKALLQAKASGKTSQVGAASAPAKESPRKGAAPAPPGKTGPAVAKAQAGKREEDSQSSSEESDSEEEAPAQAKPSGKAPQVRAASAPAKESPRKGAAPAPPRKTGPAAAQVQVGKQEEDSRSSSEESDSDREALAAMNAAQVKPLGKSPQVKPASTMGMGPLGKGAGPVPPGKVGPATPSAQVGKWEEDSESSSEESSDSSDGEVPTAVAPAQEKSLGNILQAKPTSSPAKGPPQKAGPVAVQVKAEKPMDNSESSEESSDSADSEEAPAAMTAAQAKPALKIPQTKACPKKTNTTASAKVAPVRVGTQAPRKAGTATSPAGSSPAVAGGTQRPAEDSSSSEESDSEEEKTGLAVTVGQAKSVGKGLQVKAASVPVKGSLGQGTAPVLPGKTGPTVTQVKAEKQEDSESSEEESDSEEAAASPAQVKTSVKKTQAKANPAAARAPSAKGTISAPGKVVTAAAQAKQRSPSKVKPPVRNPQNSTVLARGPASVPSVGKAVATAAQAQTGPEEDSGSSEEESDSEEEAETLAQVKPSGKTHQIRAALAPAKESPRKGAAPTPPGKTGPSAAQAGKQDDSGSSSEESDSDGEAPAAVTSAQKDSNSKPARSKTLAPAPPERNTEGSSESSEEELPLTQVIKPPLIFVDPNRSPAGPAATPAQAQAASTPRKARASESTARSSSSESEDEDVIPATQCLTPGIRTNVVTMPTAHPRIAPKASMAGASSSKESSRISDGKKQEGPATQVSKKNPASLPLTQAALKVLAQKASEAQPPVARTQPSSGVDSAVGTLPATSPQSTSVQAKGTNKLRKPKLPEVQQATKAPESSDDSEDSSDSSSGSEEDGEGPQGAKSAHTLVGPTPSRTETLVEETAAESSEDDVVAPSQSLLSGYMTPGLTPANSQASKATPKLDSSPSVSSTLAAKDDPDGKQEAKPQQAAGMLSPKTGGKEAASGTTPQKSRKPKKGAGNPQASTLALQSNITQCLLGQPWPLNEAQVQASVVKVLTELLEQERKKVVDTTKESSRKGWESRKRKLSGDQPAARTPRSKKKKKLGAGEGGEASVSPEKTSTTSKGKAKRDKASGDVKEKKGKGSLGSQGAKDEPEEELQKGMGTVEGGDQSNPKSK
Protein: Phytoene dehydrogenase (Q4W8B6)
Organism: Brevundimonas sp. NBRC 101024
Interaction partners:
Sequence:
MRAAVIGSGFGGLSLAIRLQTAGIQTTVFEARDLPGGRAYVYKDKGYTFDAGPTVITDPSALEELFEGAGRKLSDYVELLPVAPFYRLCWEDGDVFDYVNGQDELDRQIVARNPADKEGYRRFLAYSQDLLKEGYLKLGAVPFLDFASMVKAAPELMRLQAWRSVYDKVAGYIQDEHLRQAFSFHSLLVGGNPFATSSIYALIHALERRWGVWFPRGGTGALIQAMVRLFQDLGGEIRLNSPVERITLANGRADGVVVGGQALAFDMVASNADVVHTYQRLLGQEPRGRKEGARLASKRHSMSLFVIYFGLKRVHPEVRHHTVLFGPRYRELIGEIFKGPDLPQDFSLYLHAPTRTDPSLAPEGCDAFYVLAPVPHLASADIDWAVEGPRYRDRVLAYLEQHYIPGLTAHLDTCRIFTPVDFRDQLNAHQGSAFSLEPILTQSAYFRVHNRDDQIPNLYFVGAGTHPGAGVPGVVGSAKATAGLMIEDAGRTA