wanglab/gogpt-training-data huggingface dataset:
Protein: Quaking related 54B, isoform E (A0A0B4KFT9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD36772p
- Quaking related 58E-2, isoform A
- QKR58E-3
Sequence:
MTEKYDGNGDFSAFNDDDNDFGGKPRKPGGSIGAPGGAHNGDASAHDHGHHGGDPGGNVQINEKANEYIRDCMAERNRMDRKFPIAEKLLEGEIEKVQTTGRIPSREQKYADIYREKPLRISQRVLVPIREHPKFNFVGKLLGPKGNSLRRLQEETLCKMTVLGRNSMRDRVKEEELRSSKDPKYAHLNSDLHVEISTIAPPAEAYARIAYAMAELRKYLIPDSNDIIRQEQLRELMDSTSLNDNDNAKSGYKKTSHMQGGNNVLGGGSINPIGGVKNTPHHSYRSSQPSSFSKNVLAPKQKVMSILEKARTAMDETYGRGYDDGLGYDPHQSYDSYSYGTHGHGPHGPPANILGGVGGISGGGGRGGHYESSDYEPDYGRREYYQHSPGYSAGGGGGVGLGTGGASQSNAIGGSGLSSNHNRSHVNRXNLLDPSSASGGRGTNPAATTQNLTMKSQPNSSNNFLPNHGASECQNGKNINPNYYYNSNGSSKVNQQQLQQSQPNLPPQLSGHNNNSSNGSRASNMINTSSHNNCNSNFHPVGEKNSNDVSFISSYRLGPMDGQKSANSNNINNHTLGSKNHSNNTTTTASVPNMLLVRPANPSLHIGTFPFLPVQFF
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q08DN4)
Organism: Bos taurus (Bovine)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MAQKENAYPWPYGRQTAQPGLNTLPQRVLRKEPVTPSALVLMSRSNAQPTAAPGQKVVENSSGTPNIPKRSFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLQHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSRTFDEQRTATIMEELADALTYCHAKKVIHRDIKPENLLLGLRGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRTHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPPSVPLGAQDLIYKLLKHNPSERLPLAQVSAHPWVRTHSRRVLPPSAPQSVP
Protein: Ubiquitin-like protein 3 (Membrane-anchored ubiquitin-fold protein) (HsMUB) (MUB) (Protein HCG-1) (O95164)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein 5
- Ubiquitin-like protein NEDD8
- Small ubiquitin-related modifier 1
Sequence:
MSSNVPADMINLRLILVSGKTKEFLFSPNDSASDIAKHVYDNWPMDWEEEQVSSPNILRLIYQGRFLHGNVTLGALKLPFGKTTVMHLVARETLPEPNSQGQRNREKTGESNCCVIL
Protein: Transcription initiation factor TFIID subunit 5 (Transcription initiation factor TFIID 100 kDa subunit) (TAF(II)100) (TAFII-100) (TAFII100) (Q8C092)
Organism: Mus musculus (Mouse)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C. TAF5 is involved in two modules of TFIID, in TFIID-A together with TAF3 and TBP, and in TFIID-B with TAF8. Involved in contacts between TFIID and TFIIF in the PIC.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 10
- TATA-box binding protein associated factor 4
- Transcription initiation factor TFIID subunit 9
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
Sequence:
MAALAEEQTEVAVKLEPEGPPTLLPPQAGDGAGEGSGGTPNNGPNGGGGGNVAVAAAAGGDGGTPKPGVAVSAAAPAGAAPVPAAPAEAGAPHDRQTLLAVLQFLRQSNLREAEEALRREARLLEEAVAGSGAPGELDGAGAEAASALLSRVTASVPGSAAPEPPGTGASVTSVFSGSASGPAAPGKVASVAVEDQPDVSAVLSAYNQQGDPTMYEEYYSGLKHFIECSLDCHRAELSQLFYPLFVHMYLELVYNQHENEAKSFFEKFHGDQECYYQDDLRVLSSLTKKEHMKGNETMLDFRTSKFVLRIYRDSYQLLKRHLQEKQNNQIWNIVQEHLYIDIFDGMPRSKQQIDAMVGSLAGEAKREANKSKVFFGLLKEPEIEVPLDDEDEEGENEEGKPKKKKPKKDSIGSKSKKQDPNAPPQNRIPLPELKDSDKLDKIMNMKETTKRVRLGPDCLPSICFYTFLNAYQGLTAVDVTDDSSLIAGGFADSTVRVWSVTPKKLRSVKQASDLSLIDKESDDVLERIMDEKTASELKILYGHSGPVYGASFSPDRNYLLSSSEDGTVRLWSLQTFTCLVGYKGHNYPVWDTQFSPYGYYFVSGGHDRVARLWATDHYQPLRIFAGHLADVNCTRYHPNSNYVATGSADRTVRLWDVLNGNCVRIFTGHKGPIHSLTFSPNGRFLATGATDGRVLLWDIGHGLMVGELKGHTDTVCSLRFSRDGEILASGSMDNTVRLWDAVKAFEDLETDDFTTATGHINLPENSQELLLGTYMTKSTPVVHLHFTRRNLVLAAGAYSPQ
Protein: Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (Thioredoxin reductase TR3) (Q9Z0J5)
Organism: Rattus norvegicus (Rat)
Function: Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis (By similarity). Maintains mitochondrial thioredoxin in a reduced state. May play a role in redox-regulated cell signaling.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9988709}.
Interaction partners:
- Thioredoxin, mitochondrial
- Selenocysteine lyase
- Selenide, water dikinase 1
- Thioredoxin
- Cystathionine gamma-lyase
- Kynurenine--oxoglutarate transaminase 1
- thioredoxin-disulfide reductase
- Thioredoxin reductase 1, cytoplasmic
- Thioredoxin-dependent peroxide reductase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
Sequence:
MAAIVAALRGSSGRFRPQTRVLTRGTRGAAGAASAAGGQQNFDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVAQPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGVDKAGKVTQLSAKHIVIATGGRPKYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVPLRGFDQQMASLVTEHMESHGTRFLKGCVPSLIRKLPTNQLQVTWEDLASGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQKIIVDAQEATSVPHIYAIGDVAEGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKPLEFTVADRDASQCYIKMVCMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKLHISKRSGLDPTVTGCUG
Protein: Non-specific lipid transfer protein GPI-anchored 14 (AtLTPG-14) (Protein LTP-GPI-ANCHORED 14) (Protein SENESCENCE ASSOCIATED GENES 27) (Xylogen like protein 7) (AtXYLP7) (AtXYP10) (O64865)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable lipid transfer protein.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- BTB/POZ domain-containing protein At2g30600
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Aldo-keto reductase family 4 member C8
- Disease resistance family protein / LRR family protein
- Exocyst complex component EXO70E2
- Non-specific lipid transfer protein GPI-anchored 12
Sequence:
MESRKINLMATAIALIVVAMVVAAADDKTKDKEECTEQLVGMATCLPYVQGQAKSPTPDCCSGLKQVLNSNKKCLCVIIQDRNDPDLGLQINVSLALALPSVCHAAADVTKCPALLHLDPNSPDAQVFYQLAKGLNKTGPASAPTGSSPGPISISPTSGSDDGNNSGRTTSVPGRNHAQSFYKQWLGLEVVFHFFVIFYIFILV
Protein: Putative magnesium-dependent phosphatase YER134C (EC 3.1.3.48) (P40081)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Magnesium-dependent phosphatase which may act as a tyrosine phosphatase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Putative uncharacterized protein YGR259C
- Uncharacterized transcriptional regulatory protein YNR063W
- Protein DOS2
- Vacuolar basic amino acid transporter 5
- Vacuolar-sorting protein BRO1
- pH-response regulator protein palA/RIM20
- Vacuolar membrane protein YOR292C
Sequence:
MTGYPDVAAFDLDYTIWPCYCDTHLHGPFKPVKSSNGEVLTIICRDGYELTIYKDIPRILGDLKDNGVKLMTASRTWAPEIAQEILKIFKVKYAGVVTPLANLFDEFQWGERSKIGHLRDGLKDLYNTSDLKSKKICLFDDESRNKEVEKYGVKFVYVRDPENGPSWKLYQDYLSGKV
Protein: Transcription factor LBX1 (Ladybird homeobox protein homolog 1) (Q2PYN8)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that controls hypaxial muscle development by down-regulating myod1 and cdkn1b/p27, thereby allowing myoblasts to proliferate before the onset of terminal differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MTSKDEAKSSASSVEERRRNALDLLPPPANSNKPLTPFSIEDILNKPSVRRSYTICGTAHLLSSADKPPAAGLPLSSRALLSQTSPLCALEELASKTFKGLEVSVLQAAEGRDGMTIFGQRQTPKKRRKSRTAFTNHQIYELEKRFLYQKYLSPADRDQIAQQLGLTNAQVITWFQNRRAKLKRDLEEMKADVESTKKMSPSAVEAVLTISELEESGSERGNSRSRSPQLGLTSNHMPLSPSXPLTDQHASKECSEDEEDVEIDVDD
Protein: Proliferating cell nuclear antigen (PCNA) (O02115)
Organism: Caenorhabditis elegans
Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular location: Nucleus.
Interaction partners:
- Flap endonuclease 1
- Replication factor C subunit 4
- Replication factor C subunit 2
- DNA ligase 1
- DNA mismatch repair protein
- Probable DNA polymerase delta small subunit
- DNA polymerase delta catalytic subunit
- DNA polymerase eta
- Replication factor C subunit 1
- Probable replication factor C subunit 5
Sequence:
MFEAKLANAGLLKKIVESIKDLVTDAPFDCSETAMSLQAMDSSHVALVSLKLEVGLFDTYRCDRTINLGLSLANMSKALKCANNDDTCMLKYEENEGDSIIFTFADPKRDKTQDVTVKMMDIDSEHLGIPDQDYAVVCEMPAGEFQKTCKDLSTFSDSLNITATKAGIVFTGKGDIGSSVVTYSPSSNTDDETEAVTLEVKDPVNVNFSIKYMNQFTKATALSDRVRLSLCNDVPVVVEYPIEENGYLRFYLAPKIDDDENMD
Protein: Putative portal protein (H9C192)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MADNKFGGKPRVRVTSDGLVNVMTGMGTGRDRRMFNRFQFGVMQDFTELESAYIENWIARAIIDNPVNDATREWREFASDKEATEIRVAEKKYSLQAVTQESFKWAGVYGGAGALMITDQPFEKPLDVKKIKKGSLKRLLVLDRMFINGQAFNVTNPIEANYMLPDFYVVNGGTQRIHYSHFVKAPGAPMPARLRMLNGGWDDSKLRRCMEDIKDAVSAKSGIAAMIQEANIDVINRKNLANDLSSGDMDETIANRYNIFGMMKSLYRIGLLDEEEKLDRKQLSFSGLGEVLNALMEWTSGSAGQPMTRLFGVQAKGMGDSGQGDMNNYYNNVRGEQESQYRPFLKRIDEVLIRSTLGTMPDGLEFEFSPLSQPTDTELSAQRLADAQADEIRLNQGVVLPSQVARKLMEQGVYGLNESDIANLESDEKAERDGDYEFQLAELARANGENANTPPSANPTSQAE
Protein: BES1/BZR1 homolog protein 1 (Q9S7F3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Shaggy-related protein kinase eta
- Shaggy-related protein kinase iota
- Transcription factor BIM1
- Protein BRASSINOSTEROID INSENSITIVE 1
- Filaggrin-like protein
- Expressed protein
Sequence:
MTASGGGSTAATGRMPTWKERENNKKRERRRRAIAAKIFTGLRSQGNYKLPKHCDNNEVLKALCLEAGWIVHEDGTTYRKGSRPTETTVPCSSIQLSPQSSAFQSPIPSYQASPSSSSYPSPTRFDPNQSSTYLIPYLQNLASSGNLAPLRISNSAPVTPPISSPRRSNPRLPRWQSSNFPVSAPSSPTRRLHHYTSIPECDESDVSTVDSCRWGNFQSVNVSQTCPPSPTFNLVGKSVSSVGVDVSVKPWEGEKIHDVGIDDLELTLGHNTKGRG
Protein: Copper metallothionein 1-2 (Cu-MT) (Cu-metallothionein) (Copper chelatin) (Copper thionein) (P0CX81)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protects the cell against copper toxicity by tightly chelating copper ions. May also act as a depository for copper designated for the effective transfer into the apo forms of copper proteins.
Interaction partners:
Sequence:
MFSELINFQNEGHECQCQCGSCKNNEQCQKSCSCPTGCNSDDKCPCGNKSEETKKSCCSGK
Protein: TuSp1 (Q1I128)
Organism: Trichonephila antipodiana
Interaction partners:
Sequence:
SGATSQAASQSASSSYSSAFAQAASSALATSSAISRAFASVSSASAASSLAYNIGLSAARSLGIASDTALAGALAQAVGGVGAGASASAYANAIARAAGQFLATQGVLNAGNASALAGSFARALSASAESQSFAQSQAYQQASAFQQAAAQSAAQSASRAGSTSSSTTTTTSGATSQAASQSASSSYSSAFAQAASSSLATSSAISRAFASVSSASAASSLAYNIGLSAARSLGIASDTALAGALAQAVGGVGAGASASAYANAIARAAGQFLATQGVLNAVNASSLGSALANALSDSAANSAVSGNYLGVSQNFGRIAPVTGGTAGISVGVPGYLRTPSSTILAPSNAQIISLGLQTTLAPVLSSSGLSSASASARVSSLAQSLASALSTSRGTLSLSTFLNLLSSISSEIRASTSLDGTQATVEVLLEALAALLQVINGAQITDVNVSSVPSVNAALVSALVA
Protein: Acyl carrier protein MbtL (ACP) (Mycobactin synthase protein L) (P9WQF1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Acyl carrier protein involved in the formation of acyl-S-ACP intermediates within the mycobactin biosynthesis process. The aliphatic chains carried by ACP are subsequently transferred on to the mycobactin core by MbtK.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable fatty acid synthase Fas
- Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase MbtM
- Acyl-[acyl-carrier-protein] dehydrogenase MbtN
- Meromycolate extension acyl carrier protein
- Phenyloxazoline synthase MbtB
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit I
- Malonyl CoA-acyl carrier protein transacylase
- NADH-quinone oxidoreductase subunit E
Sequence:
MTSSPSTVSTTLLSILRDDLNIDLTRVTPDARLVDDVGLDSVAFAVGMVAIEERLGVALSEEELLTCDTVGELEAAIAAKYRDE
Protein: Defective proboscis extension response 6, isoform F (X2J8X8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein alpha, isoform A
- Dpr-interacting protein beta, isoform C
- Common Dpr-interacting protein
- Enhancer of split m4 protein
- Dpr-interacting protein zeta, isoform A
Sequence:
MPIAHPLPLCVAWLLLLVVIVMSDMTNGGVQGPIEGYNSLDDLLTTTPTPGQAALLLPTAPTAAYTHPKWMEPYFDPSTPRNVTALMGKSAYLSCRVRNLANKTVSWIRHRDIHILTVGSYTYTSDQRFQATHHQDTEDWTLQIKWAQKRDAGMYECQISTQPVRSYFVRLNVVVPTATILGGPDLHVDKGSTINLTCTVKFSPEPPAYIFWYHHEEVINYDSSRGGVSVITEKGDVTTSFLLIQNADLADSGKYSCAPSNADVASVRVHVLNVRAIISGEHPEAMQTGSSGCQYNWLTIVLLLGLVLCYSSQQCSSAVPASLTSSLPLPSQLPLPAAAAATTTATGESASSESVTAARASAATTTTTTATRKRCPAVKSCRQTAGRVLTKRSCHR
Protein: Probable sodium/metabolite cotransporter BASS3, chloroplastic (Bile acid transporter 3) (Bile acid-sodium symporter family protein 3) (Q8RXE8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function as sodium-coupled metabolite transporter across the chloroplast envelope.
Subcellular location: Membrane {ECO:0000305|PubMed:19542295}; Multi-pass membrane protein {ECO:0000305|PubMed:19542295}. Plastid, chloroplast envelope {ECO:0000305|PubMed:19542295}.
Interaction partners:
- Probable sodium/metabolite cotransporter BASS4, chloroplastic
Sequence:
MTLIASLSLPPPAIQRQSLSEFHNLPAKSQSFNCQFRSSSSPLSSLHSSSLSNFLDFRLRRRNSGLVPVVACSTTPFMGRVGLHWRDGNMSLLSFCGGTDVTEKADSSQFWSALLPFVVALTAVAALSYPPSFTWVSKDLYAPALGGIMLSIGIQLSVDDFALAFKRPVPLSVGFVAQYVLKPLLGVLVANAFGMPRTFYAGFILTCCVAGAQLSSYASSLSKADVAMSILLTSSTTIASVIFTPLLSGLLIGSVVPVDAVAMSKSILQVVLVPITLGLVLNTYAKPVVTLLQPVMPFVAMVCTSLCIGSPLSINRSQILSAEGLGLIVPIVTFHAVAFALGYWFSKIPGLRQEEEVSRTISLCTGMQSSTLAGLLASQFLGSSQAVPAACSVVVMAIMGLCLASFWGNGFRIRDVLSLSTPQSTGYTAES
Protein: Hydrolase (Q59WF0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glutamate dehydrogenase
- NAD-specific glutamate dehydrogenase
- Transaminase A
- Aspartate aminotransferase
- Aspartate aminotransferase
- Glutamate synthase
- Large ribosomal subunit protein eL31
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase
- Pyruvate carboxylase
Sequence:
MSNQVLKSPLSKSIKIALIQLKAGADKAANLTKVTKFIDDAVTKSTGVNLVMLPECFNSPYAVDQFRNYAEDIPQGETTQLLSSLAQKYKIYIIGGSIPEKGENDKIYNTSLTFNPQGEIIAKHRKAHLFDIDIPNGITFQESLTLSGGDKATVFKLGEYGNVGLGICYDIRFPELASIASRYPYNSFAMFYPGAFNTTTGPLHWHLLARARAVDNETFVVLCSPARDVEGGGYQAYGHSLVADPFGNIIAEAGEGEEILYAELDPALLPKARDGIPVHYQRRFDIYGDFVGEGKAKVSDK
Protein: Kinase (EC 2.7.-.-) (Q54XR3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Kinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
Sequence:
MHIFYLVNSKKSKVNNSESFIKDDRKYNLEIDLNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNNMENENNSDNNSMKIDQFPHQVGGHSAMLSVNGNICKPLINRELQFYEFSQLKNNIHSFFISPFLANFFGVVEVLKSKNDIVTDLDQSQNQEAQQQQQQQQQQQQQQQQQQQQQQKPSLGSPKSSQQSYMSNQQQINYSNIINNKNKKKVKECKHPSGTQQKYIVLSDLTSSYNSPCIVDIKIGTRQRGVICSSTTSTSHGIRVCGMKIYCPQLGEMITFDRYFGRTLDGNTLEESLFHFFTSNMFFNNNNNNINNSNDNFNNNKNFISCDFHLQRINLIESILEKLGQIECILSNKNDPFPFKIYSSSLLIIYEGKPNEILNQSLINNINNINNSSNNNNNNNNNNNNNNSNINSIISDCMNIGFSDIDSTSSSCTTTPSQSPITNILDSNIQSSTDSYTNSVENNSNNNNNNNDNIIISVSNSISIQRNINKSLESNSCISSNNSMIEDMEDGFHSFGSEEEIDDSCVSSDLDSDSDEMPSNRSTRSNSGNFSGSKPQPSKFIQNAVKMIDFAHAIPIIEKEAQEDDGYLFGINNLQLLLFKIKSRLLLSLSVQKEQQNQQQQQQQQQQQQQNQQQNNSSELSSPSSSFSSLNNSMINNRNDDCGNLEFSFNKMFNHHHQQNTVINTN
Protein: m7GpppX diphosphatase (EC 3.6.1.59) (Hint-related 7meGMP-directed hydrolase 1) (Nuclear histidine triad (HIT) motif protein 1) (Scavenger mRNA-decapping enzyme DcpS) (Q9P7C9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Has no activity towards mRNA molecules longer than 25 nucleotides. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP. Inhibits mRNA translation. Binds to the m7GpppG cap analog.
Subcellular location: Cytoplasm. Nucleus. Note=Predominantly nuclear.
Interaction partners:
- Putative acetyltransferase C18B11.09c
- mRNA decapping complex subunit 2
- mRNA-capping enzyme subunit beta
- Probable guanine deaminase
- ADP-ribosylation factor guanine nucleotide-exchange factor sec71
- mRNA-decapping enzyme subunit 1
Sequence:
MEESSAAKIQLLKEFKFEKILKDDTKSKIITLYGKIRNEVALLLLEKTAFDLNTIKLDQLATFLQDTKLVENNDVFHWFLSTNFQDCSTLPSVKSTLIWPASETHVRKYSSQKKRMVCETPEMYLKVTKPFIETQRGPQIQWVENILTHKAEAERIVVEDPDPLNGFIVIPDLKWDRQTMSALNLMAIVHATDIASIRDLKYKHIPLLENIRNKVLTEVPKQFSVDKNQLKMFVHYLPSYYHLHVHILHVDHETGDGSAVGRAILLDDVIDRLRNSPDGLENVNITFNIGEQHFLFQPLTNMNA
Protein: Zinc finger E-box-binding homeobox 1 (NIL-2-A zinc finger protein) (Negative regulator of IL2) (Transcription factor 8) (TCF-8) (P37275)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting microRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:25190660}.
Interaction partners:
- C-terminal-binding protein 1
- C-terminal-binding protein 2
- Histone deacetylase 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- Cadherin-1
- Mothers against decapentaplegic homolog 3
- Twist-related protein 1
- Histone acetyltransferase p300
- Vimentin
- Zinc finger E-box-binding homeobox 2
Sequence:
MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPYCDRGYKRFTSLKEHIKYRHEKNEDNFSCSLCSYTFAYRTQLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLIPVNGRPRTGLKTSQCSSPSLSASPGSPTRPQIRQKIENKPLQEQLSVNQIKTEPVDYEFKPIVVASGINCSTPLQNGVFTGGGPLQATSSPQGMVQAVVLPTVGLVSPISINLSDIQNVLKVAVDGNVIRQVLENNQANLASKEQETINASPIQQGGHSVISAISLPLVDQDGTTKIIINYSLEQPSQLQVVPQNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNDSTCLLCDDCPGDINALPELKHYDLKQPTQPPPLPAAEAEKPESSVSSATGDGNLSPSQPPLKNLLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWFEKMQAGQISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANPINIAIPTVTAQLPTIVAIADQNSVPCLRALAANKQTILIPQVAYTYSTTVSPAVQEPPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSEKEEEEEDKEMEELQEEKECEKPQGDEEEEEEEEEVEEEEVEEAENEGEEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA
Protein: Gcp-like domain-containing protein (A0A0H2UN08)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKVLAFDTSSKALSLAILEDKQVLAETTINIKKNHSITLMPAIDFLMASLDWTPKDLDRIVVAEGPGSYTGLRIAVATAKTLAHTLNIELVGMSSLLALVPHQQEGLFVPLMDARRNNVYAGFYENAKPVMAEAHLSFEEVLEKVKGTSQVTFVGEVGPFVEQIQKHLPRTDYKETLPNAANLALLAWDKEADSLHDFVPNYLKRVEAEENWLKNHTESGESYIKRL
Protein: Gamma-aminobutyric acid receptor subunit rho-2 (GABA(A) receptor subunit rho-2) (GABAAR subunit rho-2) (GABA(C) receptor) (P28476)
Organism: Homo sapiens (Human)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-2 GABA receptor could play a role in retinal neurotransmission.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P56476}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P56476}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit rho-1
- Gamma-aminobutyric acid receptor subunit rho-3
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit theta
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit gamma-3
- Gamma-aminobutyric acid receptor subunit alpha-5
- Gamma-aminobutyric acid receptor subunit alpha-2
- Gamma-aminobutyric acid receptor subunit epsilon
- Gamma-aminobutyric acid receptor subunit alpha-1
Sequence:
MPYFTRLILFLFCLMVLVESRKPKRKRWTGQVEMPKPSHLYKKNLDVTKIRKGKPQQLLRVDEHDFSMRPAFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLAFSSASNKSMTFDGRLVKKIWVPDVFFVHSKRSFTHDTTTDNIMLRVFPDGHVLYSMRITVTAMCNMDFSHFPLDSQTCSLELESYAYTDEDLMLYWKNGDESLKTDEKISLSQFLIQKFHTTSRLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVSLGITTVLTMTTIITGVNASMPRVSYVKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKERKLREKFPCMCGMLHSKTMMLDGSYSESEANSLAGYPRSHILTEEERQDKIVVHLGLSGEANAARKKGLLKGQTGFRIFQNTHAIDKYSRLIFPASYIFFNLIYWSVFS
Protein: TEPSIN adaptor related protein complex 4 accessory protein (I3L4S7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MVGALVPFQLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKV
Protein: FI09914p (Q9VMH4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- small monomeric GTPase
- Transport and Golgi organization protein 1
- Protein transport protein SEC23
- Protein SEC13 homolog
- Secretory 16, isoform I
- Protein transport protein Sec31A
- Secretory 24AB, isoform A
- Guanine nucleotide exchange factor MSS4 homolog
- Secretory 24CD, isoform C
- Syntaxin-5
Sequence:
MAHTRRPSDGLLARVNFPLYAVDMLTSRHILVAGGGGSSKTGVANGFEIYELYHNGSHFCAEEVLRHETGANVVMNFAVRNGGRRGYLCAGQEAHCQMYYVQPRVQSEEDGNGNGVGVGDGKPAPEERPHENGNVRQRNAHSGVEPVANGHRPPLSTADILRQFRRLHFDIQAADVIQTDFLKGAEPLQRVVRISGNGRLMATGGTDGKLRVWTFPQMTLAAELAAHSKEIDDLDFSPDSKLIASISKDAQGLVWDLASGQLQHKLQWKTPEGAKYLFKRCRYGTVEAQKDNYRLFTIANPLGKVGKQRGFLQHWDCASGQLRQAVAIDESLSSLAVRDDGRFVAVGTMFSGSVSMYIAFSLQRVLHIPHAHSMFVTGLQFLPITNEEGPPISSDTEAAVLSISVDNKVCIHSLSQRRTIPAWIAIVFLIVMIFAVFVLCSYIGI
Protein: WW domain binding protein VOPP1 (EGFR-coamplified and overexpressed protein) (ECop) (Glioblastoma-amplified secreted protein) (Putative NF-kappa-B-activating protein 055N) (Vesicular, overexpressed in cancer, prosurvival protein 1) (Q96AW1)
Organism: Homo sapiens (Human)
Function: Increases the transcriptional activity of NFKB1 by facilitating its nuclear translocation, DNA-binding and associated apoptotic response, when overexpressed.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:20571887}; Single-pass type I membrane protein {ECO:0000269|PubMed:20571887}. Late endosome membrane {ECO:0000269|PubMed:30285739}; Single-pass membrane protein {ECO:0000269|PubMed:30285739}. Lysosome membrane {ECO:0000269|PubMed:30285739}; Single-pass membrane protein {ECO:0000269|PubMed:30285739}. Note=When overexpressed, localizes in the nucleus and perinuclear regions. {ECO:0000269|PubMed:15735698}.
Interaction partners:
Sequence:
MRRQPAKVAALLLGLLLECTEAKKHCWYFEGLYPTYYICRSYEDCCGSRCCVRALSIQRLWYFWFLLMMGVLFCCGAGFFIRRRMYPPPLIEEPAFNVSYTRQPPNPGPGAQQPGPPYYTDPGGPGMNPVGNSMAMAFQVPPNSPQGSVACPPPPAYCNTPPPPYEQVVKAK