wanglab/gogpt-training-data huggingface dataset:
Protein: Protein Wnt-7b (P28047)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway. Required for normal fusion of the chorion and the allantois during placenta development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P56706}. Secreted {ECO:0000269|PubMed:15923619}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 5
- Frizzled-4
- Frizzled-2
- Protein-serine O-palmitoleoyltransferase porcupine
- Frizzled-1
- Frizzled-10
- Wnt inhibitory factor 1
- Palmitoleoyl-protein carboxylesterase NOTUM
- Frizzled-7
- Low-density lipoprotein receptor-related protein 6
Sequence:
MHRNFRKWIFYVFLCFGVLYVKLGALSSVVALGANIICNKIPGLAPRQRAICQSRPDAIIVIGEGAQMGIDECQHQFRFGRWNCSALGEKTVFGQELRVGSREAAFTYAITAAGVAHAVTAACSQGNLSNCGCDREKQGYYNQAEGWKWGGCSADVRYGIDFSRRFVDAREIKKNARRLMNLHNNEAGRKVLEDRMKLECKCHGVSGSCTTKTCWTTLPKFREVGHLLKEKYNAAVQVEVVRASRLRQPTFLRIKQLRSYQKPMETDLVYIEKSPNYCEEDAATGSVGTQGRLCNRTSPGADGCDTMCCGRGYNTHQYTKVWQCNCKFHWCCFVKCNTCSERTEVFTCK
Protein: Obg-like ATPase 1 (Q6FXN6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167}.
Interaction partners:
Sequence:
MPPKKQVEEKKVLLGRPGNNLKAGIVGLANVGKSTFFQAITRSPLGNPANYPFATIDPEEARVIVPSPRFDELVNIYKPASEVPAHLTVYDIAGLTKGASAGEGLGNAFLSHIRAVDSIYQVVRCFDDAEIIHIEGDVDPVRDLEIISTELRLKDIEFSQKALEAAEKIAKRGGQSLEVKQKKEEMALIERIIKLLEDGQRVYNQTWTPKEVEVINSLYLLTAKPTIYLINLSERDYIRKKNKHLLRIKEWVDKYSPGDLIIPFSVSLEEKLSHMSIEEGEEELKQLGTTSALPKIITTMRQKLDLISFFTCGPDEVREWTIRNGTKAPQAAGVIHNDLMNTFILAQVMKYSDVIEYKDDNAIKAAGKLLQKGKDYVVEDGDVIYFRAGAGKN
Protein: 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial (24-OHase) (Vitamin D(3) 24-hydroxylase) (EC 1.14.15.16) (Cytochrome P450 24A1) (Cytochrome P450-CC24) (Q09128)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase with a key role in vitamin D catabolism and calcium homeostasis. Via C24-oxidation pathway, catalyzes the inactivation of both the vitamin D precursor calcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3)). With initial hydroxylation at C-24 (via C24-oxidation pathway), performs a sequential 6-step oxidation of calcitriol leading to the formation of the biliary metabolite calcitroic acid. Hydroxylates at C-24 or C-25 other vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S-hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:2026586}.
Interaction partners:
- Vitamin D 25-hydroxylase
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- Vitamin D-binding protein
- Vitamin D3 receptor
- Parathyroid hormone
- Fibroblast growth factor 23
- Sodium-dependent phosphate transport protein 2A
- Sodium-dependent phosphate transport protein 2C
- Klotho
- Adrenodoxin, mitochondrial
Sequence:
MSCPIDKRRTLIAFLRRLRDLGQPPRSVTSKASASRAPKEVPLCPLMTDGETRNVTSLPGPTNWPLLGSLLEIFWKGGLKKQHDTLAEYHKKYGQIFRMKLGSFDSVHLGSPSLLEALYRTESAHPQRLEIKPWKAYRDHRNEAYGLMILEGQEWQRVRSAFQKKLMKPVEIMKLDKKINEVLADFLERMDELCDERGRIPDLYSELNKWSFESICLVLYEKRFGLLQKETEEEALTFITAIKTMMSTFGKMMVTPVELHKRLNTKVWQAHTLAWDTIFKSVKPCIDNRLQRYSQQPGADFLCDIYQQDHLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQAQRRLLQEVQSVLPDNQTPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKPTVLGEYALPKGTVLTLNTQVLGSSEDNFEDSHKFRPERWLQKEKKINPFAHLPFGIGKRMCIGRRLAELQLHLALCWIIQKYDIVATDNEPVEMLHLGILVPSRELPIAFRPR
Protein: Lost on transformation protein 1 (Q9EPT3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAQQFLSTSEEESVRTKGMAPFRCQKCGKSFVTLEKFTIHNYSHSRERPFKCSKAECGKAFVSKYKLMRHMATHSPQKIHQCTHCEKTFNRKDHLKNHLQTHDPNKISYACDDCGKKYHTMLGYKRHLALHSASNGDLTCGVCTLELGSTEVLLDHLKSHAEEKANQAPREKKYQCDHCDRCFYTRKDVRRHLVVHTGCKDFLCQFCAQRFGRKDHLTRHTKKTHSQELMQENMQAGDYQSNFQLIAPSTSFQIKVDPMPPFQLGAAPENGLDGGLPPEVHGLVLAAPEEAPQPMPPLEPLEPLEPLEPLEPMQSLEPLQPLEPMQPLEPMQPLEPMQPLEPLEPLEPMQPLEPMQPLEPMQPMLPMQPMQPMQPMLPMPEPSFTLHPGVVPTSPPPIILQEHKYNPVPTSYAPFVGMPVKADGKAFCNVGFFEEFPLQEPQAPLKFNPCFEMPMEGFGKVTLSKELLVDAVNIAIPASLEISSLLGFWQLPPPTPQNGFVNSTIPVGPGEPLPHRITCLAQQQPPPLPPPPPLPLPQPLPVPQPLPQPQMQPQFQLQIQPQMQPQMQLQPLQLQLPQLLPQLQPQQQPDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEEEQEEAEEEAEEGAEEGAEPEAQAEEEEEEEEAEEPQPEEAQIAGLVYKKWTV
Protein: Thymocyte expressed, positive selection associated 1 (E9PPW8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTGGTNKTSSSISEILDKVQEDAEDVLFSLGFGQEDHKDTSRIPARFFTTPSQAKGIDFQLFLKSQVRRIEMEDPCLMLASFLHHHNSMWSDRIGFKEET
Protein: Rhombotin-2 (Cysteine-rich protein TTG-2) (LIM domain only protein 2) (LMO-2) (T-cell translocation protein 2) (P25791)
Organism: Homo sapiens (Human)
Function: Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- LIM domain-binding protein 1
- Erythroid transcription factor
- T-cell acute lymphocytic leukemia protein 1
- LIM domain-binding protein 2
- Protein lyl-1
- Endothelial transcription factor GATA-2
- Transcription factor E2-alpha
- Runt-related transcription factor 1
- Transcription factor 12
- Zinc finger protein ZFPM1
Sequence:
MSSAIERKSLDPSEEPVDEVLQIPPSLLTCGGCQQNIGDRYFLKAIDQYWHEDCLSCDLCGCRLGEVGRRLYYKLGRKLCRRDYLRLFGQDGLCASCDKRIRAYEMTMRVKDKVYHLECFKCAACQKHFCVGDRYLLINSDIVCEQDIYEWTKINGMI
Protein: Zinc finger CCCH-type antiviral protein 1-like (Q96H79)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein mono-ADP-ribosyltransferase PARP11
Sequence:
MAEPTVCSFLTKVLCAHGGRMFLKDLRGHVELSEARLRDVLQRAGPERFLLQEVETQEGLGDAEAEAAAGAVGGGGTSAWRVVAVSSVRLCARYQRGECQACDQLHFCRRHMLGKCPNRDCWSTCTLSHDIHTPVNMQVLKSHGLFGLNENQLRILLLQNDPCLLPEVCLLYNKGEALYGYCNLKDKCNKFHVCKSFVKGECKLQTCKRSHQLIHAASLKLLQDQGLNIPSVVNFQIISTYKHMKLHKMLENTDNSSPSTEHSQGLEKQGVHAAGAAEAGPLASVPAQSAKKPCPVSCEK
Protein: CHCH domain-containing protein (Q8BW15)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPRGSRSAAARPVSRPAPPPAHPPPSAAAPAPAAPGQPGLMAQMASTAAGVAVGSAVGHVMGSALTSAFSGGNSEPAQPAVKQAPARPASHPLQMGPCSYEIKQFLDCSTTQSDLTLCEGFSEALKQCKYNHGLSSLP
Protein: Small ribosomal subunit protein uS10y (40S ribosomal protein S20-2) (Q9STY6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein eL8z
- Small ribosomal subunit protein uS12y
- Small ribosomal subunit protein uS17x
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein uS9x
- Large ribosomal subunit protein eL8y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS21y
Sequence:
MAYEPMKPTKAGLEAPLEQIHKIRITLSSKNVKNLEKVCTDLVRGAKDKRLRVKGPVRMPTKVLKITTRKAPCGEGTNTWDRFELRVHKRVIDLFSSPDVVKQITSITIEPGVEVEVTIADS
Protein: Octopamine receptor Oamb (Octopamine receptor in mushroom bodies) (Q7JQF1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for octopamine (OA) which is a neurotransmitter, neurohormone and neuromodulator in invertebrates. Stimulates intracellular accumulation of cAMP and Ca(2+) following ligand binding. Required for ovulation. Following activation on mature follicle cells by OA, induces activity of the metalloprotease Mmp2 which leads to breakdown of the posterior follicle wall, resulting in ovulation. Ligand binding probably also leads to activation of CamKII which is also required for ovulation. Modulates sleep/wake behavior by acting in neurons of the pars intercerebralis to promote wakefulness. Plays a role in courtship conditioning where the courtship behavior of males rejected by already mated females is inhibited with further females. Required in the mushroom body for appetitive olfactory learning. Specifically conveys the short-term reinforcing effects of sweet taste. In insulin-producing cells of the brain, plays a role in inhibiting transcription of insulin-like peptide Ilp3. Also plays a role in social behavior by modulating male agression.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tyramine beta-hydroxylase
- MIP05841p)
- G protein alpha s subunit subunit alpha)
Sequence:
MNETECEDLIKSVKWTEPANLISLAVLEFINVLVIGGNCLVIAAVFCSNKLRSVTNFFIVNLAVADLLVGLAVLPFSATWEVFKVWIFGDLWCRIWLAVDVWMCTASILNLCAISLDRYVAVTRPVTYPSIMSTKKAKSLIAGIWVLSFFICFPPLVGWKDQKAVIQPTYPKGNHTLYYTTTMSSSEDGQLGLDSIKDQGEASLPPSPPHIGNGNAYNPYDPGFAPIDGSAEIRIAAIDSTSTSTTATTTTTASSSSTTETEMDLDLLNAPPQNRPQTISGSCPWKCELTNDRGYVLYSALGSFYIPMFVMLFFYWRIYRAAVRTTRAINQGFKTTKGSKGIGSRFEEQRLTLRIHRGRGSNQQDSMHSNGSTQSTTTTLGTPSPERLSKYATRRLHHHDKIKISVSYPSSENISELAGHGDVGHERRQSGNALFAVHYNGTNGRESTESQLYRQQQQHGVASSCYLQVGKGLPELARRQSNTSEAGGSGHSRPANKKMGRRNIKAQVKRFRMETKAAKTLAIIVGMFIFCWCPFFTMYIIRPFCQDCVDPLLFSVLFWLGYCNSAVNPMIYALFSKDFRFAFKRIICRCFCSRQSVSLKSSRRGSDMSAIRIRARTPSITPSAAAHSFGDESELHHSEMSNDPR
Protein: Acyl carrier protein 5, chloroplastic (O04652)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- EMBRYO DEFECTIVE 3147
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Putative acyl-activating enzyme 19
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 6
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- 3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
Sequence:
MATSFCSSISMQAPFSATTTRFCLNKQATIFNNEKTNNLSFSLRRLMPARLAVSCAVKQETVEKVSEIVKKQLSLTDDQKVTAGTKFTELGADSLDTVEIVMGLEEEFGITMAEERAKEIATVQQAAELIEELVQEKTA
Protein: Transmembrane protein, putative (DUF3537) (Q94AL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- FBD-associated F-box protein At5g60610
- Ubiquitin carboxyl-terminal hydrolase-related protein
- Expressed protein family protein)
- FKBP12-interacting protein of 37 kDa
- Probable non-intrinsic ABC protein 5
- Probable E3 ubiquitin-protein ligase ARI5
- 30-kDa cleavage and polyadenylation specificity factor 30
- Glycerophosphodiester phosphodiesterase GDPD4
- Protein RFT1 homolog
Sequence:
MATNGSSEHLLPETTRPSAIINKQQPEFPASRFTFMSLVLWFDQSNFGTALLSWSVFFLLVVIVPLISHFLLVCSDCDFHHRRPYDVIVQLSLSIFAGISFVSLSIWSRKFGMRRFLFLDKLWDVSDKVRIEYEAEIQRSLKRLMIFVLPSLTLEATYRIWWYISGFNQIPYIINPILSHVVACTLQLSSWLYRNSLFIIVCILYKITCHLQTLRLDDFARCFASEITDVRSALGEHQKIRRNLRIVSHRFRRFILLSLILVTATQFMALLTTTRASVAVNIYEVGELALCSLSLVTGVFICLRSATKITHKAQSVTSLAAKWNVCATVDSFDHLDGETPTGSIIESQVSLRGNAIETSDDEEGEGDDDLDNTKIHPIYANTISYQKRQALVTYLENNKAGITVYGFLVDRSWLNTIFGIELALLLWLLNKTIVNIP
Protein: Tyrosine-protein kinase receptor TYRO3 (EC 2.7.10.1) (Etk2/tyro3) (TK19-2) (Tyrosine-protein kinase DTK) (Tyrosine-protein kinase RSE) (Tyrosine-protein kinase TIF) (P55144)
Organism: Mus musculus (Mouse)
Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Growth arrest-specific protein 6
- Vitamin K-dependent protein S
- Tubby-related protein 1
- CD209 antigen-like protein A
- Lactadherin
- T-cell immunoglobulin and mucin domain-containing protein 4
- Tumor necrosis factor
Sequence:
MALRRSMGWPGLRPLLLAGLASLLLPGSAAAGLKLMGAPVKMTVSQGQPVKLNCSVEGMEDPDIHWMKDGTVVQNASQVSISISEHSWIGLLSLKSVERSDAGLYWCQVKDGEETKISQSVWLTVEGVPFFTVEPKDLAVPPNAPFQLSCEAVGPPEPVTIYWWRGLTKVGGPAPSPSVLNVTGVTQRTEFSCEARNIKGLATSRPAIVRLQAPPAAPFNTTVTTISSYNASVAWVPGADGLALLHSCTVQVAHAPGEWEALAVVVPVPPFTCLLRNLAPATNYSLRVRCANALGPSPYGDWVPFQTKGLAPARAPQNFHAIRTDSGLILEWEEVIPEDPGEGPLGPYKLSWVQENGTQDELMVEGTRANLTDWDPQKDLILRVCASNAIGDGPWSQPLVVSSHDHAGRQGPPHSRTSWVPVVLGVLTALITAAALALILLRKRRKETRFGQAFDSVMARGEPAVHFRAARSFNRERPERIEATLDSLGISDELKEKLEDVLIPEQQFTLGRMLGKGEFGSVREAQLKQEDGSFVKVAVKMLKADIIASSDIEEFLREAACMKEFDHPHVAKLVGVSLRSRAKGRLPIPMVILPFMKHGDLHAFLLASRIGENPFNLPLQTLVRFMVDIACGMEYLSSRNFIHRDLAARNCMLAEDMTVCVADFGLSRKIYSGDYYRQGCASKLPVKWLALESLADNLYTVHSDVWAFGVTMWEIMTRGQTPYAGIENAEIYNYLIGGNRLKQPPECMEEVYDLMYQCWSADPKQRPSFTCLRMELENILGHLSVLSTSQDPLYINIERAEQPTESGSPEVHCGERSSSEAGDGSGVGAVGGIPSDSRYIFSPGGLSESPGQLEQQPESPLNENQRLLLLQQGLLPHSSC
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase BAT2, chloroplastic (EC 2.3.1.51) (EC 2.3.1.n4) (Lysophosphatidyl acyltransferase 1) (Protein BRASSICA ACYLTRANSFERASE 2) (Q9LLY4)
Organism: Brassica napus (Rape)
Function: Plastidial enzyme of the prokaryotic glycerol-3-phosphate pathway that converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at position sn-2. Utilizes palmitoyl-ACP (16:0-ACP) to produce phosphatidic acid containing a saturated group at position sn-2, which is characteristic of lipids synthesized by the prokaryotic pathway. In vitro, can use 16:0-CoA as acyl donor.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:10398728}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 
- 
- 
- 1-acylglycerol-3-phosphate O-acyltransferase
- 1-acylglycerol-3-phosphate O-acyltransferase
- 
- BnaCnng10420D protein
- 
- 
- Phosphatidate cytidylyltransferase
Sequence:
MDVASAPGVSSHPPYYSKPICSSQSSLIRIPINKGCCFARSSNLITSLHAASRGVTRRTSGVQWCYRSIRFDPFKVNDKNSRTVTVRSDLSGAATPESTYPEPEIKLSSRLRGICFCLVAGVSAIVLIVLMITGHPFVLLFDRYRRKFHHFIAKLWASISIYPFYKTDIQGLENLPSSDTPCVYVSNHQSFLDIYTLLSLGQSYKFISKTGIFVIPVIGWAMSMMGVVPLKRMDPRSQVDCLKRCMELVKKGASVFFFPEGTRSKDGRLGPFKKGAFTIAAKTGVPVVPITLMGTGKIMPTGSEGILNHGDVRVIIHKPIYGSKADLLCDEARNKIAESMNLVS
Protein: Poly(U)-specific endoribonuclease-B protein (F4JNE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MCDHSLSPQVQKEQWQDYKRPASEQHYSDEVETYGNLEPSQLELSGLSEACNKLWELDLNRLVPGRDYQIDCGDGKRVHERADMAEGLLFSWVSEEVSRKPTFARFCSLLDNYNPNEGYKEVVTEEERQEQAAFIEEISRTSVIKYLHRYLVLKDVAPGSYLEFKRMLTSLWFDLYGRGGTSGSSSAFEHVFVGEIKQSGGEQVSGFHNWLQFYLEEAKGTVDYQGYIFPRRRGEIPDSETQLLTIQFEWNGVLKSVSSTLVGVSPEFELALYTMCFFMGTEDNHIQLGPYNVNVKCYRLGNNRIGSAFPIAES
Protein: Glucose 1,6-bisphosphate synthase (EC 2.7.1.106) (PMMLP) (Phosphoglucomutase-2-like 1) (Q6PCE3)
Organism: Homo sapiens (Human)
Function: Glucose 1,6-bisphosphate synthase using 1,3-bisphosphoglycerate as a phosphate donor and a series of 1-phosphate sugars, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-phosphate, as acceptors. In vitro, also exhibits very low phosphopentomutase and phosphoglucomutase activity which are most probably not physiologically relevant.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:17804405}.
Interaction partners:
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, brain form
- Glycogen phosphorylase, muscle form
- Uridine phosphorylase 2
- Glycogen debranching enzyme
- Phosphopentomutase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Uridine phosphorylase 1
Sequence:
MAENTEGDLNSNLLHAPYHTGDPQLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGQVTSSCSSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLVDTSPLKRDPLQDICRRYMEDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAALFGWWMFDCWKKNKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIIDLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVYEKYGYHISKTSYFLCYEPPTIKSIFERLRNFDSPKEYPKFCGTFAILHVRDVTTGYDSSQPNKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDQSDTALLEEELKKLIDALIENFLQPSKNGLIWRSV
Protein: Valine--tRNA ligase (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (P9WFS9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
Interaction partners:
- Arginine--tRNA ligase
- Threonine--tRNA ligase
- Leucine--tRNA ligase
- Cysteine--tRNA ligase
- Histidine--tRNA ligase
- Glutamate--tRNA ligase
- Dihydrofolate synthase/folylpolyglutamate synthase
- Tyrosine--tRNA ligase
- Probable conserved integral membrane protein
- Isoleucine--tRNA ligase
Sequence:
MTASPHPAADMLPKSWDPAAMESAIYQKWLDAGYFTADPTSTKPAYSIVLPPPNVTGSLHMGHALEHTMMDALTRRKRMQGYEVLWQPGTDHAGIATQSVVEQQLAVDGKTKEDLGRELFVDKVWDWKRESGGAIGGQMRRLGDGVDWSRDRFTMDEGLSRAVRTIFKRLYDAGLIYRAERLVNWSPVLQTAISDLEVNYRDVEGELVSFRYGSLDDSQPHIVVATTRVETMLGDTAIAVHPDDERYRHLVGTSLAHPFVDRELAIVADEHVDPEFGTGAVKVTPAHDPNDFEIGVRHQLPMPSILDTKGRIVDTGTRFDGMDRFEARVAVRQALAAQGRVVEEKRPYLHSVGHSERSGEPIEPRLSLQWWVRVESLAKAAGDAVRNGDTVIHPASMEPRWFSWVDDMHDWCISRQLWWGHRIPIWYGPDGEQVCVGPDETPPQGWEQDPDVLDTWFSSALWPFSTLGWPDKTAELEKFYPTSVLVTGYDILFFWVARMMMFGTFVGDDAAITLDGRRGPQVPFTDVFLHGLIRDESGRKMSKSKGNVIDPLDWVEMFGADALRFTLARGASPGGDLAVSEDAVRASRNFGTKLFNATRYALLNGAAPAPLPSPNELTDADRWILGRLEEVRAEVDSAFDGYEFSRACESLYHFAWDEFCDWYLELAKTQLAQGLTHTTAVLAAGLDTLLRLLHPVIPFLTEALWLALTGRESLVSADWPEPSGISVDLVAAQRINDMQKLVTEVRRFRSDQGLADRQKVPARMHGVRDSDLSNQVAAVTSLAWLTEPGPDFEPSVSLEVRLGPEMNRTVVVELDTSGTIDVAAERRRLEKELAGAQKELASTAAKLANADFLAKAPDAVIAKIRDRQRVAQQETERITTRLAALQ
Protein: Secreted aspartic protease 10 (ACP 10) (Aspartate protease 10) (EC 3.4.23.24) (Candidapepsin-10) (Q5A651)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Required for cell surface integrity and cell separation during budding.
Subcellular location: Secreted {ECO:0000269|PubMed:16269404}. Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MDLVIMNFVFLLYLTSVVKCSIKLDFNKVSTPSKYTKRDALPMPLINDKILYTTELEIGSNKDKVSVSIDTGSYDLWVMSNDAVCYKVSEFQTEGAPQLPDIFNDIDQDYSCTFNGTYNSKSSKTFKNTSEDFSIGYVDGSAAQGVWGYDSVQFGQYGVTGLKIGIANRSSVSDGILGIGIANGYDNFPVLLQKQGLINKIAYSVYLNSSNSTTGTILFGAIDHAKYKGALSTVPVDSKSQLSVNVTNLKTKNGNVASGGHSILLDTGSTFSIFPDEWIDALGHSLNATYDEDESVYEIECDGYDEHFFGFSIGDSDFSVPIQDLKTEKDGQCYLAIMSNSVIGGGGILFGDDILRQIYLVYDLQDMTISVAPVVYTEDEDIEEILNPNEDQNEVPTSTSFTQSASSSGSQPSSTISGENMDKNTTSSSSGNCQTRSWIAILSALFLVYIHII
Protein: Zinc finger and BTB domain-containing protein 21 (Zinc finger protein 295) (Q9ULJ3)
Organism: Homo sapiens (Human)
Function: Acts as a transcription repressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:15629158}. Note=Colocalizes with ZBTB14 in nucleus in HEK293 cells.
Interaction partners:
Sequence:
MEGLLHYINPAHAISLLSALNEERLKGQLCDVLLIVGDQKFRAHKNVLAASSEYFQSLFTNKENESQTVFQLDFCEPDAFDNVLNYIYSSSLFVEKSSLAAVQELGYSLGISFLTNIVSKTPQAPFPTCPNRKKVFVEDDENSSQKRSVIVCQSRNEAQGKTVSQNQPDVSHTSRPSPSIAVKANTNKPHVPKPIEPLHNLSLTEKSWPKDSSVVYAKSLEHSGSLDDPNRISLVKRNAVLPSKPLQDREAMDDKPGVSGQLPKGKALELALKRPRPPVLSVCSSSETPYLLKETNKGNGQGEDRNLLYYSKLGLVIPSSGSGSGNQSIDRSGPLVKSLLRRSLSMDSQVPVYSPSIDLKSSQGSSSVSSDAPGNVLCALSQKSSLKDCSEKTALDDRPQVLQPHRLRSFSASQSTDREGASPVTEVRIKTEPSSPLSDPSDIIRVTVGDAATTAAASSSSVTRDLSLKTEDDQKDMSRLPAKRRFQADRRLPFKKLKVNEHGSPVSEDNFEEGSSPTLLDADFPDSDLNKDEFGELEGTRPNKKFKCKHCLKIFRSTAGLHRHVNMYHNPEKPYACDICHKRFHTNFKVWTHCQTQHGIVKNPSPASSSHAVLDEKFQRKLIDIVREREIKKALIIKLRRGKPGFQGQSSSQAQQVIKRNLRSRAKGAYICTYCGKAYRFLSQFKQHIKMHPGEKPLGVNKVAKPKEHAPLASPVENKEVYQCRLCNAKLSSLLEQGSHERLCRNAAVCPYCSLRFFSPELKQEHESKCEYKKLTCLECMRTFKSSFSIWRHQVEVHNQNNMAPTENFSLPVLDHNGDVTGSSRPQSQPEPNKVNHIVTTKDDNVFSDSSEQVNFDSEDSSCLPEDLSLSKQLKIQVKEEPVEEAEEEAPEASTAPKEAGPSKEASLWPCEKCGKMFTVHKQLERHQELLCSVKPFICHVCNKAFRTNFRLWSHFQSHMSQASEESAHKESEVCPVPTNSPSPPPLPPPPPLPKIQPLEPDSPTGLSENPTPATEKLFVPQESDTLFYHAPPLSAITFKRQFMCKLCHRTFKTAFSLWSHEQTHN
Protein: Putative pyridoxal kinase BUD17 (EC 2.7.1.35) (Bud site selection protein 17) (P53727)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase BUD16
- Uncharacterized protein YGR017W
- Putative pyridoxal reductase
- Probable pyridoxal 5'-phosphate synthase subunit SNO2
- Probable pyridoxal 5'-phosphate synthase subunit SNO3
- Pyridoxal 5'-phosphate synthase subunit SNO1
- Probable pyridoxal 5'-phosphate synthase subunit SNZ3
- Probable pyridoxal 5'-phosphate synthase subunit SNZ2
- Pyridoxal 5'-phosphate synthase subunit SNZ1
Sequence:
MTSTLHTTKKVLSIQSHVIHGYVGNKAATFPLQYRGWDVDVLNTVQFSNHSGYAHFTGFKCSTEELVDIVEKGLIGSLRIKYDAVLSGYLPNVQALQKVAGIVGQLCEGSENVKWILDPVLGDNGRLYVDRECVAVYQDILQNFKIFLATPNQFEMELLVGMSIRTLDDAKQAFKLFHKKYPRVSRIVVTSLELSEFLSNDTYVVAGFDCSASEEIFFYEIPKINAKFSGSGDLISAMLTDSLLGDRRCTQLSLSASLGQVLWLVTSILQKTYDLNIAERGPQDSTIDIKDLKLIQCRDILKQDLIPSIGKPKTIKI
Protein: Small nuclear ribonucleoprotein Sm D1 (snRNP core protein D1) (Q8IIA8)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365054}.
Interaction partners:
- Sm protein F
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein G
- Sm protein B
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- U1 small nuclear ribonucleoprotein 70 kDa homolog, putative
- Pre-mRNA-processing-splicing factor 8, putative
- U5 small nuclear ribonucleoprotein component, putative
- Splicing factor 3B subunit 2, putative
Sequence:
MKLVHFLMKLTNENVTIELKNGTLITGIITAVDIKMNTHMKNVKVVIKNKNIAEYNVNTKQFLSLEHVTIRGNNIRYFILSDSLPLDSLLVEDTTPKKISKDKSFLHRDKGMSKGAKGRGRKLSKR
Protein: Ikaros (IKAROS family zinc finger 1 (Ikaros)) (O93581)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
METEEAQEMSQITGRDSPMNANEGGEDQDEAMPVPEDLSASTGLQHNNRTDKPLACNIKVEARSDEENGLSCEMNGEAEECAAEDLRILDGSGAKVNGSHAGPDSKPAAYPTAGGIRLPNGKLKCDICGIVCIGPNVLMVHKRSHTEERKSVLEQQKGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCAYCGRSYKQRSSLEEHKERCHNYLQCMGLQNSIYTVKEENSQNEQREDMPASERALVLDRIANNVAKRKSSMPQRFVGENRLSELSFESGSGELMQPHVIDQAINSAISYLGAESLRPLVQTSPGSADMVVSPLYNLHKSQTAEGNGVSAKDSAAEHLLLLSKSKSASVDKDGSPSPSGQDSTDTESNNEERSAGVSGTAATGGLIYLTNHMAPGMRNGGLPGVKEEQQRHFEALRAAGMDLSIASSEGFKVLSGDGEELRAYRCIHCRVLFLDHVMYTIHMGCHGFRDPFECNLCGYRSQDRYEFSSHITRGEHRI
Protein: Rac GTPase activating protein 1 (F8VUW9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREML