wanglab/gogpt-training-data huggingface dataset:
Protein: Oxaloacetate tautomerase Fahd2a, mitochondrial (EC 5.3.2.2) (Fumarylacetoacetate hydrolase domain-containing protein 2A) (Q3TC72)
Organism: Mus musculus (Mouse)
Function: May have hydrolase activity.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:F1MLX0}.
Interaction partners:
- Homogentisate 1,2-dioxygenase
- Cilia- and flagella-associated protein 20
Sequence:
MLGFGRRRLFSALLQVQKRPCQPSRNMRLVQFQAPHLEEPHLGLESGVGGGVVDLNAFDSTLPKTMVQFLEQGETTLSVARRALATQLPVIPRSQVTFLAPVTRPDKVICVGLNYADHCQEQNVRVPKSPIIFSKFSSSIVGPYDEIILPPESKEVDWEVEMAVVIGKKGKHIKATDVMAHVAGFTVAHDVSARDWQMRNGKQWLLGKTFDTFCPLGPALVTKDTIADPHNLKICCRVNGEVVQSSNTNQMVFKTEYLIAWVSQFVTLYPGDLLLTGTPPGVGMFRKPPVFLKKGDEVQCEIEELGVIINKVV
Protein: Stac-like, isoform O (A0A0B4KER3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004278}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGISAHAAPASFWNHPRRIRRTPTSDRDGVDQCRPWICRRKDRRPAHPAANRPPESRVCGPSSTFRWDDWAAPAPRTRERATDCARMCMCTSRIPYSVARICARTTSMHSSRPASRSSSFIRRPLTRRQRMAVGGVTRRLWRTMRVYTIHQGRGVRRARAAQAVAAYLRDRRARIGKGWPAQGHGVRISATEQWADKPVVRRPGDPTRRVAAGAVPVLAERLPKVTGSSVKSSSGRRSRRRRIFGWRGPRGGSLSPQGGSMASYNGVLKDYSHSSLNEAFKSQNNVNFKLIKTVSDFSETLSRLYEEHATALQVAVSNYRKKNAELRKERPACHLAIFQAWETFLQEVETDSQACNDVASVLSRQVSRPMLDKSFHRKVQSRKIFTHRESFETIIAKTEEKLSKCRVDYKQCHLAHRQNPSQHSLTEYIDAHNAYVQQLHATNGMLEAYHTDTLPQQMQELEEIHNDLVAIVSDSLMQGAEVIAGKANDQAKRYNSLSNQCAAVSPQQDLVNFVRLLAQPSQAQKIPRRLFASPQAEVGEEAGDHNEMTPCLRNELVFDRHSTLSQRSALESLKREAIELELQIRQLQDSIEALNRTQTRGIEGQLYNKVNELQEDLSMKKFDLRAKQIHLAAIRAQKDLFVSKVEPTSPRNERKFSAATAPSMKTKWLKAFKSLKPAGSGSAQQADRRNGASSTASEPLRPNLDGSHHLQEYTYKKITACDVCSQILRGHTRQGLRCRICKLNAHGDCAPNLPRCQPKQKLLRRQKSTSELENRVDIEEETGADKSVQAKQMDGSVAGGSALPVPVLSERELGRAPPPDIPIVSVSELALQEQQQQQQQQQQQHQQQQRSLASVAQAAAVRAGRGVRPPPVAMPILGVQLQQQELQQQRGGLPVPSQDISSSSAPHSPRRQKLNLRMKSLSLDSPESSELHGQFRRRTQLPGTGASTSAGSGYYHGGSGGHLEHSTPPSNNSRLHWTNASKTITAPSSPSHPGRKLLYATRGMRGGSVDLPDEMEKSQSSASTSPCLSPKTHRLLPTNLYVIIYNFKARHADELDLKAGYKVTVIDNSDPDWWKGKVLGRVGYFPSKYCVRLNANEKPLQVTHNLQVSDSERGENLTLLRDQIVIQTGDEVNGMVMIRAAEHGQGYCPIKYLQEV
Protein: RUN domain-containing protein (RUND-1) (Q22585)
Organism: Caenorhabditis elegans
Interaction partners:
- CARD domain-containing protein
- Resistance to inhibitors of cholinesterase protein 19
- Rab GTPase-activating protein tbc-8
- Vacuolar protein sorting-associated protein 51 homolog
- Ras-related protein Rab-2
- Vacuolar protein sorting-associated protein 53 homolog
- Vps54_N domain-containing protein
Sequence:
MMNELEASDLLVELGQSLKKRASEDSKEIVDGLDFYDTMSETEWKSARLSSSHSDDIGSLNDALRVQQLEEEQERLNNSLFSLSSHFAQVQFRIKQMNEADPSDRLKLLSDLQKFAFKGCTDMNELQRLRSESESGNDVLDKQNERQKELLKQLREQVEDLERTAYENGEGELPSTDILKKQKAVLDKLREKIELNLDIDKMNQTEIQRQVDDALKQLVNPFKEKGQLVDQLQTQITDLERFVNFLQKENAENSNQTTPVRSMGSTPLSGAKSKNGSFLSGIIGCSTGRFQKNQLKNTLKGNHYGDERAHVQLAVDATQQVLEKYTLLTFDSATKGQLEEVQVENDEVFERSEEEVVTIVRKQLCLALKALLEHGMLSETVVHKRIPGLGCFVAKSSADEKSTSLSHIWDVILYFYNLKTGRDTTDAPVRKLSQSFKLDHVGGRSITSKQVLLTTIENIISTHARLKRSKDAHWKAFVSAALNEKKLPAWLRIIFRTRQVVEMCYNSWSYVARTGCEELYTLLEGLHKYSIHLPVDLALRPFEQIKDAF
Protein: U-box domain-containing protein 40 (EC 2.3.2.27) (Plant U-box protein 40) (RING-type E3 ubiquitin transferase PUB40) (Q9FL17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as an E3 ubiquitin ligase.
Interaction partners:
- Serine/threonine-protein kinase BSK6
- F-box/kelch-repeat protein KIB1
Sequence:
MEIQRPVINLMVLHSQHDKSDNLSRRESLAGKSKWRTSLSRSSSSSSSNNNSPTKTEIPAEFLCPISGSLMADPIIVSSGHSYERACVIACKTLGFTPTPPPDFSTVIPNLALKSAIHSWCERRCFPPPKPLNSAAAEKLILALMEKKPQRRKVSVSEKELIQAIRDKPSVRLNHAATELDRRPNYFNSSSDESIASSSRTLQLTTKPSCFSSPSSGEIESLEPNLTPEEEALLTKLKSNRISEIEEALISIRRITRIDESSRISLCTTRVISALKSLIVSRYATVQVNVTAVLVNLSLEKSNKVKIVRSGIVPPLIDVLKCGSVEAQEHSAGVIFSLALEDENKTAIGVLGGLEPLLHLIRVGTELTRHDSALALYHLSLVQSNRGKLVKLGAVQMLLGMVSLGQMIGRVLLILCNMASCPVSRPALLDSGGVECMVGVLRRDREVNESTRESCVAVLYGLSHDGGLRFKGLAMAANAVEELVKVERSGRERAKQKARRVLEVLRAKIEDDDLVENEEIDWEELLNSGDVSRSRCRLGGEKSCVNSAEF
Protein: Serum amyloid P-component (SAP) (P23680)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted.
Interaction partners:
- Histidine-rich glycoprotein
- Low affinity immunoglobulin gamma Fc region receptor II
- Beta-2-glycoprotein 1
- Afamin
- Mannose-binding protein A
- Inter-alpha-trypsin inhibitor heavy chain 4
- C4b-binding protein beta chain
- Carboxypeptidase B2
- Complement component C9
- Mannan-binding lectin serine protease 2
Sequence:
MDKLLLWMSVFTSLLSEAFAQTDLNQKVFVFPRESETDYVKLIPWLEKPLQNFTLCFRAYSDLSRSQSLFSYSVNSRDNELLIYKDKVGQYSLYIGNSKVTVRGLEEFPSPIHFCTSWESSSGIAEFWVNGKPWVKKGLQKGYTVKSSPSIVLGQEQDTYGGGFDKTQSFVGEIADLYMWDSVLTPENIHSVDRGFPPNPNILDWRALNYEINGYVVIKPRMWDNKSS
Protein: ShKT domain-containing protein (Q9XUS8)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable N-acetylgalactosaminyltransferase 7
- Acyltransferase 3 domain-containing protein
Sequence:
MRWTPILTTLLLLCVVLISVAGVKSTTKKGAVGGTAVRKTTVKKVAVKNKNIQRMNQKRWREPPRDCSDAPKHLKQTCLMIRRMDLATRRRLARQSVRQTRPNQVPNWLQPIPVPANARGQAAYHPYDCMTLLCLCPFFNGRNVNGQCVLSNGVVLNMSWRKEYRMMTEDERRRWHNALNTLKRNGEYDRLSRQHLEVGVGSGAHSGPGFLPWHREYLKRVEIALRMVDPTVFIPYWDSVMDSYLPDPRDSIMFSDLFVGGTDYYGNVVTGPFAYWRTIEGRSTILRNLGAEGQLFNENQVNTIVAQNTIENTLAYTAPQPGCPYPNNYGAIEYSHSNIHLWIGGDMKPPSTSANEPIFFMHHSFVDYLWELWRQLQQPRWLREQAYSADHPTCANWQHFSYAPMRPFPYLVNRDGLSNSYTDQMYRYAPRATCSHQRPNCGSPYLFCDTRGYPHCVSKIRLNGNCRGFEQNDACYASRCWWGRCVNANFAARMKGARTHANSTLIDLELAKEVSVNGTKVERVPLVKRISIKMTAPLFVDCYNRMPCCDSWAKNGGCQREPEFMSQYCQASCNTCTPSYNTTDACMDRHVNCVAWKADKMCSGKSADFMSENCRSSCGKCSLTRESQCFNNGKIIVIPVSQNLRESISDSLMSEVTNRIKKVKKVAAKEEVESTKKVRHN
Protein: Soluble inorganic pyrophosphatase PPA1 (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) (Q43187)
Organism: Solanum tuberosum (Potato)
Function: Catalyzes the irreversible hydrolysis of pyrophosphate (PPi) to phosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10092174}.
Interaction partners:
Sequence:
MSNENDDLSPQRRAPRLNERILSSISRRSVAAHPWHDLEIGPEAPSVFNVVIEISKGSKVKYELDKKTGLIKVDRILYSSVVYPQNYGFIPRTLCEDNDPMDVLVLMQEPVLPGCFLRARAIGLMPMIDQGEKDDKIIAVCADDPEYRHYTDIKQLPPHRLAEIRRFFEDYKKNENKDVAVDDFLPPNSAVNAIQYSMDLYAEYILHSLRK
Protein: Auxin-responsive protein IAA2 (Indoleacetic acid-induced protein 2) (Q9LG86)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 11
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 9
- Auxin response factor 7
- Auxin response factor 3
- Auxin response factor 15
- Auxin response factor 14
- Auxin response factor 1
- Auxin response factor 16
Sequence:
MAWRRGFGREEEDAAAAGESGLELCLGLPAYFSSSSSSKPSEGSTAAPAFALRSNGTNASKPSGAAAAAPVVGWPPVRSFRRNLASSSSSSSKQAPPPPSSSPQNGDKASKDGGAEKGMFVKINMDGVPIGRKVDLAAYGGYAQLSAAVDKLFRGLLAAQSAAADGEADAAAAGEMVGGGEYTLVYEDDEGDRMLVGDVPWQMFIATAKRLRVLKSSDLPPPSLMRAAGSRKRAAADS
Protein: 3'-5' exonuclease eri-1 (EC 3.1.-.-) (Enhanced RNAi protein) (O44406)
Organism: Caenorhabditis elegans
Function: RNA exonuclease that acts as a negative regulator of RNA interference (RNAi). Probably acts by degrading the 3'-overhangs of short interfering RNAs (siRNAs). Component of the ERI/DICER complex which is involved in processing amplified double-stranded RNA (dsRNA) intermediates during small-RNA-mediated gene-silencing or RNA interference (RNAi) (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14961122}.
Interaction partners:
- RNA-directed RNA polymerase
- Tudor domain-containing protein
- DRBM domain-containing protein
- Endoribonuclease dcr-1
- Reverse transcriptase domain-containing protein
- Protein lin-15B
- Helicase ATP-binding domain-containing protein
- CHHC U11-48K-type domain-containing protein
- Zc3h12a-like Ribonuclease NYN domain-containing protein
- Piwi-like protein ergo-1
Sequence:
MSADEPSPEDEKYLESLRDLLKISQEFDASNAKQNDEPEKTAVEVESAETRTDESEKSIDIPREQQLLPSERVEPLKSMVEPEYVKKVIRQMDTMTAEQLKQALMKIKVSTGGNKKTLRKRVAQYYRKENALLNRKMEPNADKTARFFDYLIAIDFECTCVEIIYDYPHEIIELPAVLIDVREMKIISEFRTYVRPVRNPKLSEFCMQFTKIAQETVDAAPYFREALQRLYTWMRKFNLGQKNSRFAFVTDGPHDMWKFMQFQCLLSNIRMPHMFRSFINIKKTFKEKFNGLIKGNGKSGIENMLERLDLSFVGNKHSGLDDATNIAAIAIQMMKLKIELRINQKCSYKENQRSAARKDEERELEDAANVDLTSVDISRRDFQLWMRRLPLKLSSVTRREFINEEYLDCDSCDDLTDDKNDEAAFQEKMAIREYLENKQTEDFAKIAAERGIFKIGEIKSYQTARPIIEDDDVDVESEEEDYGTEFEMLEVVERMPPVSSTLHTEVDLDAVWERDGGSDSERENLSNAPSLHEFPSSSTSSPHATSEHVTSSSPLHIDDDVDRVLNAPPKNSLASSSNRSSF
Protein: Hexitol phosphatase A (Mannitol-1-phosphatase) (EC 3.1.3.22) (Sorbitol-6-phosphatase) (EC 3.1.3.50) (Sugar-phosphatase) (EC 3.1.3.23) (P77625)
Organism: Escherichia coli (strain K12)
Function: Sugar-phosphate phosphohydrolase that appears to contribute to butanol tolerance. Catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate. Is also able to dephosphorylate other sugar phosphates in vitro including ribose-5-phosphate (Rib5P), 2-deoxyribose-5-phosphate, fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), and glucose-6-phosphate (Glu6P). Selectively hydrolyzes beta-D-glucose-1-phosphate (bGlu1P) and has no activity with the alpha form.
Interaction partners:
- Mannitol-1-phosphate 5-dehydrogenase
- Hexitol phosphatase B
- UPF0304 protein YfbU
- PTS system mannitol-specific EIICBA component
- PTS system mannitol-specific cryptic EIICB component
- Mannitol-specific cryptic phosphotransferase enzyme IIA component
- Uncharacterized transporter YfbS
- Sugar phosphatase YidA
- Kojibiose phosphorylase
Sequence:
MRCKGFLFDLDGTLVDSLPAVERAWSNWARRHGLAPEEVLAFIHGKQAITSLRHFMAGKSEADIAAEFTRLEHIEATETEGITALPGAIALLSHLNKAGIPWAIVTSGSMPVARARHKIAGLPAPEVFVTAERVKRGKPEPDAYLLGAQLLGLAPQECVVVEDAPAGVLSGLAAGCHVIAVNAPADTPRLNEVDLVLHSLEQITVTKQPNGDVIIQ
Protein: Cytochrome c3 (Formate dehydrogenase 2 subunit gamma (cytochrome c-553)) (FDH2 subunit gamma (cytochrome c-553)) (FDH2C) (Q727P6)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin (By similarity). Gamma chain of the formate dehydrogenase (FDH) that catalyzes the reversible two-electron oxidation of formate to carbon dioxide. The gamma subunit of formate dehydrogenase forms a c-type heme.
Subcellular location: Periplasm {ECO:0000269|PubMed:8566699}.
Interaction partners:
- Formate dehydrogenase 2 subunit beta
- Formate dehydrogenase 2 subunit alpha
- Formate dehydrogenase formation protein FdhE, putative
Sequence:
MRYLVISLFAVSLLMAGSALVGNAADAAKAPKKAIELKHGTSKRMHVMFNHTTHKDIACEQCHHDSPAPDKPYASCTDNDCHATPGPRERDTMSMFVAYHAKDTDRSCYGCHKKMAAQHPEFTGCRPCHMSQQARKEAAASEKK
Protein: Membrane sensor protein UhpC (P09836)
Organism: Escherichia coli (strain K12)
Function: Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. UhpC senses external glucose-6-phosphate and interacts with the histidine kinase UhpB, leading to the stimulation of the autokinase activity of UhpB.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Signal transduction histidine-protein kinase/phosphatase UhpB
- Transcriptional regulatory protein UhpA
- Low-affinity inorganic phosphate transporter PitB
- Hexose-6-phosphate:phosphate antiporter
Sequence:
MLPFLKAPADAPLMTDKYEIDARYRYWRRHILLTIWLGYALFYFTRKSFNAAVPEILANGVLSRSDIGLLATLFYITYGVSKFVSGIVSDRSNARYFMGIGLIATGIINILFGFSTSLWAFAVLWVLNAFFQGWGSPVCARLLTAWYSRTERGGWWALWNTAHNVGGALIPIVMAAAALHYGWRAGMMIAGCMAIVVGIFLCWRLRDRPQALGLPAVGEWRHDALEIAQQQEGAGLTRKEILTKYVLLNPYIWLLSFCYVLVYVVRAAINDWGNLYMSETLGVDLVTANTAVTMFELGGFIGALVAGWGSDKLFNGNRGPMNLIFAAGILLSVGSLWLMPFASYVMQATCFFTIGFFVFGPQMLIGMAAAECSHKEAAGAATGFVGLFAYLGASLAGWPLAKVLDTWHWSGFFVVISIAAGISALLLLPFLNAQTPREA
Protein: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase) (PGP synthase) (P0ABF8)
Organism: Escherichia coli (strain K12)
Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Phosphatidate cytidylyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- Phosphatidylglycerophosphatase A
- Phosphatidylglycerophosphatase C
- Phosphatidylglycerophosphatase B
- Phosphatidylserine decarboxylase proenzyme
- Cardiolipin synthase A
- Uncharacterized protein YnbB
- Nicotinamide-nucleotide amidohydrolase PncC
- CDP-diacylglycerol pyrophosphatase
Sequence:
MQFNIPTLLTLFRVILIPFFVLVFYLPVTWSPFAAALIFCVAAVTDWFDGFLARRWNQSTRFGAFLDPVADKVLVAIAMVLVTEHYHSWWVTLPAATMIAREIIISALREWMAELGKRSSVAVSWIGKVKTTAQMVALAWLLWRPNIWVEYAGIALFFVAAVLTLWSMLQYLSAARADLLDQ
Protein: Hyaluronan-mediated motility receptor (Intracellular hyaluronic acid-binding protein) (Receptor for hyaluronan-mediated motility) (CD antigen CD168) (P97779)
Organism: Rattus norvegicus (Rat)
Function: Receptor for hyaluronic acid (HA) (By similarity). Involved in cell motility (By similarity). When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including the PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity (By similarity). May act as a regulator of adipogenisis (By similarity).
Subcellular location: Cell surface {ECO:0000250|UniProtKB:Q00547}. Cytoplasm {ECO:0000250|UniProtKB:Q00547}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00547}.
Interaction partners:
- CD44 antigen
- Centromere protein F
- Protein regulator of cytokinesis 1
- Family with sequence similarity 83, member D
- DLG associated protein 5
- Breast cancer type 1 susceptibility protein homolog
- Dual specificity protein kinase TTK
- Centromere-associated protein E
Sequence:
MGGGVSYVGWLEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEEDLKEKDREILCLKQSLEEKVSFSKQIEDLTVKCQLLEAERDDLVSKDRERAESLSAEMQVLTEKLLLERQEYEKLQQNELQSQSLLQQEKELSAHLQQQLCSFQEEMTSERNVFKEQLKLALDELDAVQQKEEQSEKLVKQLEEETKSTAEQLRRLDDLLREKEIELEKRTAAHAQATVIAQEKYSDTAQTLRDVTAQLESYKSSTLKEIEDLKLENLTLQEKVAMAEKRVEDVQQQILTAESTNQEYAKVVQDLQNSSTLKEAEIKEITSSYLEKITDLQNQLRQQNEDFRKQLEEEGAKMTEKETAVTELTMEINKWRLLYEELYDKTKPFQQQLDAFEAEKQALLNEHGATQEQLSKIRDSYAQLLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRSQLAKRKQNELRLQGELDKALGIRHFDPPKAFCHESKENVTLKTPLKEGNPNCC
Protein: Cytochrome P450 4Z1 (EC 1.14.14.1) (CYPIVZ1) (Laurate 7-monooxygenase) (EC 1.14.14.130) (Q86W10)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase that catalyzes the in-chain oxidation of fatty acids. Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates lauric and myristic acids predominantly at the omega-4 and omega-2 positions, respectively. Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Displays an absolute stereoselectivity in the epoxidation of arachidonic acid producing the 14(S),15(R)-epoxyeicosatrienoic acid (EET) enantiomer. 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 cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15059886}; Single-pass type II membrane protein {ECO:0000269|PubMed:15059886}. Microsome membrane {ECO:0000269|PubMed:15059886}; Single-pass type II membrane protein {ECO:0000269|PubMed:15059886}.
Interaction partners:
- Cytochrome P450 4X1
Sequence:
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEFYPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESWVGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELFQHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFSSQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFSEADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLSQMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWEDPQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHSRPPQPVRQVVLKSKNGIHVFAKKVC
Protein: Vasculin (GC-rich promoter-binding protein 1) (D4PHA4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAQHDFAPAWLNFPTPPSSTKSSLNFEKHSENFAWTENRYDVNRRRHNSSDGFDSAIGRPNGGNFGRKEKNGWRTHGRNGTENINHRGGYHGGSSRSRSSIFHAGKSQGLHENNIPDNETGRKEDKRERKQFEAEDFPSLNPEYEREPNHNKSLAAGVWGLHAQTHTYPTKKISQAPLLEYPPNPKSRAPRMLVIKKGNTKDLQLSGFPVVGNLPSQPVKNGTGPSVYKGLVPKPAAPPTKPTQWKSQTKENKVGTSFPHESTFGVGNFNAFKSTAKNFSPSTNSVKECNRSNSSSPVDKLNQQPRLTKLTRMRTDKKSEFLKALKRDRVEEEHEDESRAGSEKDDDSFNLHNSNSTHQERDINRNFDENEIPQENGNASVISQQIIRSSTFPQTDVLSSSLEAEHRLLKEMGWQEDSENDETCAPLTEDEMREFQVISEQLQKNGLRKNGILKNGLICDFKFGPWKNSTFKPTTENDDTETSSSDTSDDDDV
Protein: Gamma-crystallin E (Gamma-2) (Gamma-E-crystallin) (Gamma-crystallin 3-1) (P02528)
Organism: Rattus norvegicus (Rat)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
Sequence:
MGKITFYEDRGFQGRHYECSTDHSNLQPYFSRCNSVRVDSGCWMLYEQPNFTGCQYFLRRGDYPDYQQWMGFSDSVRSCRLIPHSSSHRIRIYEREDYRGQMVEITDDCPHLQDRFHFSDFHSFHVMEGYWVLYEMPNYRGRQYLLRPGEYRRYHDWGAMNARVGSLRRIMDFY
Protein: Thimet oligopeptidase (EC 3.4.24.15) (Endo-oligopeptidase A) (Endopeptidase 24.15) (PZ-peptidase) (Soluble metallo-endopeptidase) (P24155)
Organism: Rattus norvegicus (Rat)
Function: Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the amyloid-beta precursor protein and generate amyloidogenic fragments (By similarity). Also acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47788}.
Interaction partners:
- Kininogen-1
- Prolyl endopeptidase
- Neurotensin/neuromedin N
- Metalloendopeptidase
- Metalloendopeptidase
- Metalloendopeptidase
- Neprilysin
- Calmodulin-1
- Metalloendopeptidase
- Membrane metallo-endopeptidase-like 1
Sequence:
MKPPAACAGDVVDTVSPCSTVNHLRWDLSAQQIRALTTQLIEQTKCVYDRVGAQDFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPNKDIRAASTEADKKLSEFDVEMSMRQDVYQRVVWLQEKIPKDSLKPEAARYLERLIKLGRRNGLHLPQDTQEKIKNIKKRLSLLCIDFNKNLNEDTTFLPFTREELGGLPEDFLNSLEKTEDGKLKVTLKYPHYFPLLKKCHVPETRRLLEEAFNCRCKEENCAILKELVSLRAQKSNLLGFRTHADYVLEMNMAKTSQTVATFLDELARKLKPLGEQERAVILELKEAECAKRGLPFDGRIHAWDMRYYMNQVEETRYRVDQNLLKEYFPMQVVTRGLLAIYQELLGLTFTLEEGAAAWHEDVRLYSVRDAASGEEIGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQLAIAAMVANFTKPTPDVPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFVEAPSQMLENWVWEKEPLMRMSQHYRTGGEAPEDLLEKLIKSRQANAGLFNLRQIVLAKVDQVLHTQTDVDPAEEYARLCQEILGVPATPGTNMPATFGHLAGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLSPKVGMDYRTSILRPGGSEDASTMLKQFLGRDPKQDAFLLSKGLQVEGCEPPAC
Protein: Ribosome-associated molecular chaperone SSB2 (EC 3.6.4.10) (Heat shock protein SSB2) (Hsp70 chaperone Ssb) (P40150)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23332755, ECO:0000305|PubMed:1394434}. Note=About 50% of the protein is associated with translating ribosomes, but sufficient Ssb exists in the cell for each ribosome to be associated with at least one Ssb molecule. {ECO:0000269|PubMed:1394434, ECO:0000269|PubMed:23332755, ECO:0000269|PubMed:9670014}.
Interaction partners:
- Zuotin
- Ribosome-associated molecular chaperone SSB1
- Mitochondrial protein import protein MAS5
- ATP-dependent molecular chaperone HSP82
- ATP-dependent molecular chaperone HSC82
- Heat shock protein STI1
- Protein SIS1
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL18
- Heat shock protein 104
Sequence:
MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSSNITISNAVGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDPVLSSKLKRGSKSKIEAALSDALAALQIEDPSADELRKAEVGLKRVVTKAMSSR
Protein: Core gene UL10 family protein (Envelope glycoprotein gM) (Glycoprotein M) (ORF39) (O40931)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MRASKSDRFLMSSWVKLLFVAVIMYICSAVVPMAATYEGLGFPCYFNNLVNYSALNLTVRNSAKHLTPTLFLEKPEMLVYIFWTFIVDGIAIVYYCLAAVAVYRAKHVHATTMMSMQSWIALLGSHSVLYVAILRMWSMQLFIHVLSYKHVLMAAFVYCIHFCISFAHIQSLITCNSAQWEIPLLEQHVPDNTMMESLLTRWKPVCVNLYLSTTALEMLLFSLSTMMAVGNSFYVLVSDAIFGAVNMFLALTVVWYINTEFFLVKFMRRQVGFYVGVFVGYLILLLPVIRYENAFVQANLHYIVAINISCIPILCILAIVIRVIRSDWGLCTPSAAYMPLATSAPTVDRTPTVHQKPPPLPAKTRARAKVKDISTPAPRTQYQSDHESDSEIDETQMIFI
Protein: FI03683p (Smooth, isoform B) (A1ZBN3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNNLNANASAFLWQVPPPQQLTPQSVQQQTVQSVQSMQSVQHSQLLQSAVVSQPRKFGGNKSNYNYMQNHAIMGPGGGPMGGIGGNPNIYRKRHSINTYNAGLYQTNEPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN