wanglab/gogpt-training-data huggingface dataset:
Protein: Amine oxidase [flavin-containing] (EC 1.4.3.21) (EC 1.4.3.4) (Monoamine oxidase) (MAO) (Z-MAO) (Q6NSN2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially oxidizes serotonin and tyramine. Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P21396}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P21396}; Cytoplasmic side {ECO:0000250|UniProtKB:P21396}.
Interaction partners:
- Catechol O-methyltransferase B
- Catechol O-methyltransferase A
- Transmembrane O-methyltransferase homolog
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Dopamine beta-hydroxylase
- Aromatic-L-amino-acid decarboxylase
- Amine oxidase
- Uncharacterized protein.
- Histamine N-methyltransferase
Sequence:
MTANAYDVIVIGGGISGLSAAKLLVDSGLNPVVLEARSRVGGRTYTVQNKETKWVDLGGAYIGPTQNRILRIAKQYGVKTYKVNEEESLVHYVKGKSYPFKGPFPPMWNPFAYMDYNNLWRTMDKMGMEIPKEAPWRAPHAEEWDKMTMQQLFDKICWTRSARRFATLFVNVNVTSEPHEVSALWFLWYVKQCGGTMRIFSTTNGGQERKFAGGANQISEGMARELGDRVKLSRAVCSIDQTGDLVEVRTVNEEVYKAKYVILAIPPGLNLKIHFNPELPPLRNQLIHRVPMGSVIKCMVYYKENFWRKKGYCGSMVIEEEDAPIGLTLDDTKPDGSVPAIMGFILARKSRKLANLTRDERKRRICEIYARVLGSEEALYPVHYEEKNWCEEEYSGGCYTAYFPPGIMTQFGRVLREPVGRLYFAGTETATEWSGYMEGAVQAGERASREVMCAMGKLHASQIWQSEPESMDVPARPFVTTFWERNLPSVGGFLKFMGVSSFLAAATAAGLVACKKGLLPRC
Protein: cDNA FLJ75083, highly similar to Homo sapiens amine oxidase (flavin containing) domain 2 (AOF2),mRNA (A8K2R3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPPYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
Protein: Bifunctional polynucleotide phosphatase/kinase (DNA 5'-kinase/3'-phosphatase) (Polynucleotide kinase-3'-phosphatase) [Includes: Polynucleotide 3'-phosphatase (EC 3.1.3.32) (2'(3')-polynucleotidase); Polynucleotide 5'-hydroxyl-kinase (EC 2.7.1.78)] (O13911)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the phosphorylation of DNA at 5'-hydroxyl termini and can dephosphorylate its 3'-phosphate termini. Has a role in the repair of breaks in single-stranded DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:11729194, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable tyrosyl-DNA phosphodiesterase
- Histidinol-phosphate aminotransferase
- Imidazole glycerol phosphate synthase hisHF
- DNA-
- Endonuclease III homolog lyase)
- Histidinol dehydrogenase
- ATP-dependent helicase rhp16
- Histidine biosynthesis bifunctional protein his7
- 1-
- ATP phosphoribosyltransferase
Sequence:
MSSKKRKSPPQESLTSYFEKSSKSSKKYGSQNKDSDSSSTCLQQKIEIQWSITDSLYIAKYGKLKKTKKFIAFDLDGTLIKTKSGRVFSKDAADWTWWHPSVVPKLKALYQDNYSLVIFSNQNGIPRKPSAGHTFQMKIRAIFESLDLPIVLYAAILKDKFRKPLTGMWNSFLKDVNRSIDLSFIKYVGDAAGRPGDHNSTDLKFAENIGIKFETPEQFFLGHSFVPPNFESFHPKNYLVRNSSSHPYHFKKSEHQEIVVLVGFPSSGKSTLAESQIVTQGYERVNQDILKTKSKCIKAAIEALKKEKSVVIDNTNPTIESRKMWIDIAQEFEIPIRCIHLQSSEELARHNNVFRYIHHNQKQLPEIAFNSFKSRFQMPTVEEGFTNVEEVPFKCLKDYEDTWNYWYE
Protein: Large ribosomal subunit protein eL32z (60S ribosomal protein L32-1) (P49211)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein eL22z
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18z
- Small ribosomal subunit protein eS24y
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL42z/eL42y
- Small ribosomal subunit protein eS1y
- Large ribosomal subunit protein uL6x
Sequence:
MAVPLLTKKVVKKRSAKFIRPQSDRRITVKESWRRPKGIDSRVRRKFKGVTLMPNVGYGSDKKTRHYLPNGFKKFVVHNTSELELLMMHNRTYCAEIAHNVSTKKRKAIVERASQLDVVVTNRLARLRSQEDE
Protein: Chromatin structure-remodeling complex subunit RSC7 (Nuclear protein localization protein 6) (Remodel the structure of chromatin complex subunit 7) (P32832)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. Together with HTL1, LDB7, RSC3, RSC30 components, defines a fungal-specific module within the RSC complex that plays a role in many cellular functions including the maintenance of cell wall integrity. Acidic protein important for nuclear protein localization.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nuclear protein STH1/NPS1
- Regulator of Ty1 transposition protein 102
- Chromatin structure-remodeling complex protein RSC58
- Chromatin structure-remodeling complex protein RSC6
- Chromatin structure-remodeling complex protein RSC8
- Chromatin structure-remodeling complex subunit RSC4
- Chromatin structure-remodeling complex protein RSC14
- Chromatin structure-remodeling complex subunit RSC9
- Chromatin structure-remodeling complex subunit RSC1
- Actin-like protein ARP9
Sequence:
MSDSEGGLASEVEHEKRSRSTSNRPNYAIDTEDLDIDENDENEDDDYREEEANEGVNEEEISDEEEQINKSGRNKRRHVDEEEDLSEDKGVTRSRNRSKFKKPVFPGIDDAEENLNPLKVVNEEYVLPDDPEGETKITADGDLLGGREFLVRTFTLTEKGNRKFMLATEPARIVGFRDSYLFFQTHPNLYKFILNQTQKNDLIDRGVLPYSYRNRQIALVTARGVFKEFGAKIIRGGKHITDDYYASELRTKGNVIEGKLAGDPIDKSARALETMMYPASENGINPAKNQVEFFEHRPHGHMSNSNIIASGSKLSSTNWLYQHSAACSRFNSDLFYDRVKVLLVDQQGLRDAYTNILHIPESTQSTTVLGWRRSKNDSPSDTSIVYETVIHDNDLNKPKTGLSEIPKEIYEDVVDEDVLRAITEQQNFEKCNEYI
Protein: AP-2 complex subunit alpha (Q22601)
Organism: Caenorhabditis elegans
Subcellular location: Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
- AP-2 complex subunit mu
- AP complex subunit sigma
- AP complex subunit beta
- NECAP PHear domain-containing protein
- Probable clathrin heavy chain 1
- EHS-1
- Numb-related protein 1
- ENTH domain-containing protein
- Intersectin-1
- Phosphatidylinositol-binding clathrin assembly protein unc-11
Sequence:
MPAVKGDGMRGLAVFISDIRNCKSKEAELKRINKELANIRSKFKGDKTLDGYQKKKYVCKLLFIFLLGNDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLIEQQSDLMKLIVQGIRNDLTSRNPVHVNLALQCISNMGSREMVEAFCTDLPKLLVSGETIDFVKQSAALCILKLFRNSPDSFQPGDYASRIVHLLNDSHMGVVTSAASLIEALSKKWPEEYKGAVPLAISRLSRIVTATYTDLQDYTYYFVPAPWLCVKLLRLLQNYPPPDDPSNKARLLECLEGILNKAQDAPKSKKVQHSNAKNAVLFEAIALIIHMDSEPQLLVRACNQLGTFLSHRETNLRYLALESMCLLATSEFSHDAVKKHQDTIINSLKTERDVSVRQRAVDLLYAMCDRSNANQIVAEMLAYLETADYSIREEMVLKVAILAEKYATDYTWYVDVILKLIRIAGDYVSEEVWYRVIQIVVNREDVQGYAAKTVFEALQRPACHENMVKVGGYILGEFGNFIAGDERSTAKIQFELLHSKFHLCSITTRCLLLTTYIKFCNLFPEIKPLVQQVFQTDHNLRNPDAELQQRSIEYLQMTKLASNDVLATILEVMPAFAEKESSLLAKLKKSKPQLEEIEREEKEKRSKPTAVMSEGSTSLVDFDSTNDTTASLADVFANNSGTGLGAQGDEVEIANKDDYLKFVTKSNAILWEDDYIQIGCKLETRNNLGRLGMFYGNKTSQPFNKFTPIITCPGALAVQLQAQAKPVEPVVAAGTQVQQLINFVCVQEFQKMPIMNIKFTFTDRAGAVQNFDKNFYLPLFISKFFEPTNMTSEQFFTRWKSLGAASQEAQKIFNALSPIEHATIESRLKGFGANLLTDVDPNPDNYVCAGIIHTQTQQIGTLIRLEPNKQAKMYRLTIRSSKDTVVQTLVDLLGNQF
Protein: Succinate dehydrogenase cytochrome b560 subunit, mitochondrial (P41956)
Organism: Caenorhabditis elegans
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity). Mediates resistance to enteropathogenic E.coli infection.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Putative succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Uncharacterized protein F42A8.1
- Probable fumarate hydratase, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- fumarate reductase
- Probable NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MINIPTAILCRLGARSSISRSFGTSIVTKSEAKTPIQKFGWEYLLKQRSKNRPIAPHLTVYQPQLTWMLSGFHRISGCVMAGTLLVGGIGFAVLPFDFTAFVDFIRSWNLPCAVTAVFKYIIAFPIIFHTLNGIRFLGFDLAKGVNNVGQIYKSGYLVSGLSAILALAIVFNSCQNKSNKTA
Protein: Collagen alpha-1(IV) chain (F1KQQ4)
Organism: Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MLARIPLQVTILLVICEQISLRGFVDAAACKGCAPPCICPGQKGEKGVQGFQGPRGHPGPPGLDGLEGNIGAPGLRGSEGDFGDPGVKGVRGERGFPGAPGNVGLPGLDGLPGMKGEMGIPGCNGTDGLPGIPGLAGPPGPHGPPGAAGQPGKQGPPGDGGINSVGRKGEAGEPGRAGAPGTRGLDGIPGQKGSKGDPGPAGPPGFPGPQGQKGRMGTRTPGMKGEKGLAGPPGPPGPPGNFAGASAPEETEVIQGPAGPPGLKGEKGRDGPVGPPGAPGLDGPPGYVGLKGQKGDPGDAGARGKRGKDGMMGLSGAKGETGARGVPGLDGYPGQKGAAGELGYSGRPGPEGDPGPPGEFGIGRGQPGPRGVQGIDGAPGPKGTAGRPGGMGPVGPRGHVGAPGPPGPPGPEGLPGYSEKGDRGKDGNPGYAGEAGPTGPLGECGKPGEQGLPGFDIQGPPGPEGRPGRDGYPGVPGDVGDPGMAGLKGFPGTGVKKVGPPGQIGLIGPPGENGRIGLDGRPGSPGLPGQKGDDCGYCPDGLPGQKGEAGAPGPDGYPGPPGPNGNMGERGAKGAAGKPGLPGPSGIQGSVGLPGLPGFPGLKGEAGDIIGPMENPQGYPGTKGERGPPGGVGLPGLPGPDGADGPRGPSGQPGPRGEKGLPGIDGKRGRDGMVGRPGLPGPPGDSFPGPPGPPGVKGERGEEGLPGLPGPRGPQGPMYSGLIKEIPGPDGFPGAPGLPGLRGDDGLPGLPGAPGIEGIPGQKGEDGSDGLPGAPGLDGAPGLPGMPGDDGLPGADGLRGQPGDAGLPGLPGLPGLPGEPGIGMPGQAGFPGPQGEDGLPGLAGAEGFPGRQGPRGAPGVKGQPGESGYPGLPGLPGLKGEKGLLGIDGKDGRVGKKGEPGYAGLPGQKGEAGVPGPDGLPGPKGETGKQGFPGLEGPPGLPGIPGLRGEDGTIGFPGLRGMPGDDGVPGIDGYPGSRGEPGLDGLPGEPGRQGEPGLPGKMGLAGLPGLPGMPGDSGAPGSKGLRGEPGRIAHHGLPGEPGLPGPEGPPGLPGLDGLPGMKGARGAPGRGFPGVPGLKGEPGDKGFDGPDGIDGYPGLPGMIGIPGPKGQTGDAGRNGERGFDGRPGIPGIKGERGADGLPGLPGLQGPPGFDGLQGQKGHRGIPGDAGFNGRAGLPGLPGIKGERGQDGQHGYPGEPGPVGAHGESGLTGAPGLQGEPGLPGRMGLPGQPGELGAPGFPGAPGLEGIPGIRGERGDDGLPGLPGIDGIPIQGPEGDAGYPGRDGNDGLPGLPGQRGDDGLPGLPGLIGERGDDGLPGYPGERGLRGIDGKRGPDGARGLPGPPGLDGYPGAPGERGMDGLPGFPGKDGIPGYPGERGEVGLPGLPGMRGEDGLPGLPGLAGQKGARGDDGLPGLPGLPGPVGARGRPGPPGIPGAYNALLHSPKGERGEAGPPGQKGYPGETGSPGLQGPPGPAGLPGLAGPPGNPGRPGPPGFKGAMGVNGPPGIAGRVGHPGPPGPPGYPGGIGGLAPPRGFTFARHSQTTDIPRCPPGSQMLWTGYSLLYVQGNGRTSGQDLGQAGSCLSKFSTMPFMFCNLNSVCHVSSRNDYSFWLSTAEPMTQMMNPVSGTAIRPYISRCAVCEIPTQIMAVHSQDSYIPECPRGWSPLYSGYSFVMHTAAGAEGTGQNLQSPGSCLEEFRAVPFIECHGRGTCNHYATNHGFWLAIVDRNKQWRKPMSQTLKAGGLKDRVSRCQVCLKNR
Protein: Uncharacterized protein Rv1995 (P9WLP3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1993c
- HTH-type transcriptional regulator CmtR
- Universal stress protein Rv1996
Sequence:
MVASGAATKGVTVMKQTPPAAVGRRHLLEISASAAGVIALSACSGSPPEPGKGRPDTTPEQEVPVTAPEDLMREHGVLKRILLIYREGIRRLQADDQSPAPALNESAQIIRRFIEDYHGQLEEQYVFPKLEQAGKLTDITSVLRTQHQRGRVLTDRVLAATTAAAAFDQPARDTLAQDMAAYIRMFEPHEAREDTVVFPALRDVMSAVEFRDMAETFEDEEHRRFGEAGFQSVVDKVADIEKSLGIYDLSQFTPS
Protein: tRNA selenocysteine 1-associated protein 1 (SECp43) (tRNA selenocysteine-associated protein 1) (Q80VC6)
Organism: Mus musculus (Mouse)
Function: Involved in the early steps of selenocysteine biosynthesis and tRNA(Sec) charging to the later steps resulting in the cotranslational incorporation of selenocysteine into selenoproteins. Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins synthesis.
Subcellular location: Nucleus. Cytoplasm. Note=Abundant in the nucleus. {ECO:0000250}.
Interaction partners:
- O-phosphoseryl-tRNA
- Pre-mRNA-processing factor 39
- L-seryl-tRNA
- Selenocysteine-specific elongation factor
- Selenocysteine insertion sequence-binding protein 2
- RNA-binding protein 25
- U1 small nuclear ribonucleoprotein C
- Selenide, water dikinase 2
- U2 small nuclear ribonucleoprotein A'
- Splicing factor U2AF 65 kDa subunit
Sequence:
MAASLWMGDLEPYMDENFISRAFATMGETVMSVKIIRNRLTGIPAGYCFVEFADLATAEKCLHKINGKPLPGATPAKRFKLNYATYGKQPDNSPEYSLFVGDLTPDVDDGMLYEFFVKVYPSCRGGKVVLDPTGVSKGYGFVKFTDELEQKRALTECQGAVGLGCKPVRLSVAIPKASRVKPVEYSQMYSYSYNQYYQQYQNYYAQWGYDQNTGSYSYSYPQYGYTQSTMQTYEEVGDDALEDPAPQLDVTEANKEFMEQSEELYDALMDCHWQPLDTVSSEIPAMM
Protein: Heme oxygenase 2 (HO-2) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 2 soluble form] (P30519)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
Subcellular location: Microsome membrane {ECO:0000305|PubMed:7890772}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
Interaction partners:
- Biliverdin reductase A
- Ferrochelatase, mitochondrial
- Flavin reductase
- Histidine--tRNA ligase, mitochondrial
- Frataxin, mitochondrial
- Ceruloplasmin
- Hephaestin
- Holocytochrome c-type synthase
- Protoheme IX farnesyltransferase, mitochondrial
- Heme oxygenase 1
Sequence:
MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFILAAGVALAAGLLAWYYM
Protein: Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) (Polypeptide GalNAc transferase 2) (GalNAc-T2) (pp-GaNTase 2) (Protein-UDP acetylgalactosaminyltransferase 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 2 soluble form] (Q6PB93)
Organism: Mus musculus (Mouse)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region (By similarity). Involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted {ECO:0000250|UniProtKB:Q10471}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
Sequence:
MRRRSRMLLCFALLWVLGIAYYMYSGGGSALAAGGGGAGRKGDWNDIDSIKKKDLHHSRGDEKAQGVETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLHMDRGIPDTRHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKRSPPHLIKEIILVDDYSNDPEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNERWLEPLLERVAEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAPIKTPMIAGGLFVMDKLYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHVFRKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKHFYYAAVPSARNVPYGNIQSRLELRKKLGCKPFKWYLDNVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGIYECHNAGGNQEWALTKEKSVKHMDLCLTVVDRSPGSLIRLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLDSRTAKSGGLSVEVCGPALSQQWKFSLNLQQ
Protein: inorganic diphosphatase (EC 3.6.1.1) (Q384W5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Plasma membrane ATPase
- Plasma membrane ATPase
- inorganic diphosphatase
- ATP synthase F1 subunit gamma protein, putative
- ATP synthase alpha chain
- ATP synthase subunit beta
- V-type ATPase, C subunit, putative
- Vacuolar ATP synthase subunit D, putative
- H
- Vacuolar proton pump subunit B
Sequence:
MNNTHGVDSRSDRTSPQDLASAEVAGLPFSASLGTNISTGRGSEADVAEPIQEAVDRKVSELDLAAYDKDDFTQPMIKKIMSRLFSAFDVTHLGYLTPDKVEEVCRYLGRNMSDGDVKAMKAEINAIDGHVTFEKFWAWWCSHPVHSRTKCFSMVSADFSMPYHQQQLVVHEKGEMYTPSYRVLYFFRDLETGRERQVSPWHDIPLYVRDLVRTKPEATPMNRYNFICEIPKWTRAKFEIATGESFNPIKQDIKNGVPRFYKHGDMMWNYGAFPQTWESTEVLFEAGVTGDNDPVDAVEIGMTQFKVGQVSAVKVLGVLGMIDEGKMDWKVVCISHNDPICRFMKDIHDVPKFLPGCLDAIREWFRVYKICQGGEASHFAFDGEFKDKEYAMKVIDESHNMWHNLLKVNKRGEL
Protein: NFAT activation molecule 1 (Calcineurin/NFAT-activating ITAM-containing protein) (NFAT-activating protein with ITAM motif 1) (Q8R4V1)
Organism: Mus musculus (Mouse)
Function: May function in immune system as a receptor which activates via the calcineurin/NFAT-signaling pathway the downstream cytokine gene promoters. Activates the transcription of IL-13 and TNF-alpha promoters (By similarity). May be involved in the regulation of B-cell, but not T-cell, development.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Partially recruited to lipid rafts upon BCR stimulation. {ECO:0000250}.
Interaction partners:
Sequence:
MESWLLRRGARVRCLHPPSWLPAWCFLCLLPVPQTLQLTGLVSLTHTSLPIMVSLANTDVFFSCRIEDFTRLQRDLPVKLFHTDIHGRRRWEKQINCQHRPGMENHTRDCMVKLSQANTSATGIYYFIVEGEETYQSDGVVILVRDTVYQPPAFKVQEALMLGFTSLMSVLGVLGTALLLWKKKQISVLGKHTAKTCSGLKSTVGTTKPPAESVYTSLQRRETEVYACMKEETGSPVFSQSPATKEKLNRFEDDNEFNLVYENL
Protein: Histidyl-tRNA synthetase (D6RJE6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPRLSQNKQALEGLGDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQAGEEPLNVGSVAAGGR
Protein: Transcription termination/antitermination protein NusG (P9WIU9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Participates in transcription elongation, termination and antitermination.
Interaction partners:
- Large ribosomal subunit protein uL11
- Protein translocase subunit SecE
- Large ribosomal subunit protein uL1
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL6
- Transcription termination factor Rho
Sequence:
MTTFDGDTSAGEAVDLTEANAFQDAAAPAEEVDPAAALKAELRSKPGDWYVVHSYAGYENKVKANLETRVQNLDVGDYIFQVEVPTEEVTEIKNGQRKQVNRKVLPGYILVRMDLTDDSWAAVRNTPGVTGFVGATSRPSALALDDVVKFLLPRGSTRKAAKGAASTAAAAEAGGLERPVVEVDYEVGESVTVMDGPFATLPATISEVNAEQQKLKVLVSIFGRETPVELTFGQVSKI
Protein: Mitochondrial inner membrane m-AAA protease component AFG3L1 (EC 3.4.24.-) (EC 3.6.-.-) (AFG3-like protein 1) (Q920A7)
Organism: Mus musculus (Mouse)
Function: Putative ATP-dependent protease. Required for the maturation of paraplegin (SPG7) after its cleavage by mitochondrial-processing peptidase (MPP), converting it into a proteolytically active mature form.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11549317, ECO:0000269|PubMed:19656850}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Mitochondrial inner membrane m-AAA protease component paraplegin
- ATP-dependent clpX-like chaperone, mitochondrial
- Metalloendopeptidase OMA1, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Dysbindin domain-containing protein 1
- Prohibitin 1
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS11m
Sequence:
MLLRLVGAAGSRALAWPFSKLWRCGGCAGSGGTVWSSVRACGIALQGHLGRCSQQLALQGKLTSFSPRLYSKPPRGFEKFFKNKKNRKSASPGNSVPPKKEPKNAGPGGDGGNRGGKGDDFPWWKRMQKGEFPWDDKDFRSLAVLGAGVAAGFLYFYFRDPGKEITWKHFVQYYLARGLVDRLEVVNKQFVRVIPVPGTTSERFVWFNIGSVDTFERNLESAQWELGIEPTNQAAVVYTTESDGSFLRSLVPTLVLVSILLYAMRRGPMGTGRGGRGGGLFSVGETTAKILKNNIDVRFADVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAMLTGPPGTGKTLLAKATAGEANVPFITVNGSEFLEMFVGVGPARVRDMFAMARKHAPCILFIDEIDAIGRKRGRGHLGGQSEQENTLNQMLVEMDGFNSSTNVVVLAGTNRPDILDPALTRPGRFDRQIYIGPPDIKGRSSIFKVHLRPLKLDGSLSKDALSRKLAALTPGFTGADISNVCNEAALIAARHLSPSVQERHFEQAIERVIGGLEKKTQVLQPSEKTTVAYHEAGHAVVGWFLEHADPLLKVSIIPRGKGLGYAQYLPREQFLYTREQLFDRMCMMLGGRVAEQLFFGQITTGAQDDLRKVTQSAYAQIVQFGMSEKLGQVSFDFPRQGETMVEKPYSEATAQLIDEEVRCLVRSAYNRTLELLTQCREQVEKVGRRLLEKEVLEKADMIELLGPRPFAEKSTYEEFVEGTGSLEEDTSLPEGLKDWNKGREEGGTERGLQESPV
Protein: Mediator of RNA polymerase II transcription subunit 27 (Cofactor required for Sp1 transcriptional activation subunit 8) (CRSP complex subunit 8) (Mediator complex subunit 27) (Q9DB40)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MADVLSVGVNLEAFSQAISAIQALRSSVSRVFDCLKDGMRNKETLEGREKAFIANFQDNLHSVNRDLNELERLSNLVGKPSENHPLHNSGLLSLDPVQDKTPLYSQLLQAYKWSNKLQYHAGLASGLLNQQSLKRSANQMGVSAKRRPKAQPTTLVLPPQYVDDVISRIDRMFPEMSIHLSRPNGTSAMLLVTLGKVLKVIVVMRSLFIDRTIVKGYNESVYTEDGKLDIWSKSSYQVFQKVTDHATTALLHYQLPQMPDVVVRSFMTWLRSYIKLFQAPCQRCGKFLQDGLPPTWRDFRTLEAFHDTCRQ