wanglab/gogpt-training-data huggingface dataset:
Protein: Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF) (Q64364)
Organism: Mus musculus (Mouse)
Function: Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression (By similarity). Binds to TOP1/TOPOI and stimulates its activity (By similarity). This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation (By similarity). Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing (By similarity). Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1. Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination (By similarity). Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1 (By similarity). Binds to HUWE1 and represses its ubiquitin ligase activity (By similarity). May play a role in controlling cell proliferation and apoptosis during mammary gland development (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8N726, ECO:0000269|PubMed:10359817, ECO:0000269|PubMed:15567177, ECO:0000269|PubMed:15601844, ECO:0000269|PubMed:8521522, ECO:0000305|PubMed:20513429}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8N726, ECO:0000305|PubMed:20513429}.; SUBCELLULAR LOCATION: [Isoform smARF]: Mitochondrion {ECO:0000269|PubMed:16713577}.
Interaction partners:
- E3 ubiquitin-protein ligase Mdm2
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- Nucleophosmin
- Cellular tumor antigen p53
- Cyclin-dependent kinase 4 inhibitor B
- CDKN2A-interacting protein
- Bcl-2-like protein 1
- Myc proto-oncogene protein
- Epidermal growth factor receptor
Sequence:
MGRRFLVTVRIQRAGRPLQERVFLVKFVRSRRPRTASCALAFVNMLLRLERILRRGPHRNPGPGDDDGQRSRSSSSAQLRCRFELRGPHYLLPPGARRSAGRLPGHAGGAARVRGSAGCARCLGSPAARLGPRAGTSRHRAIFAFRWVLFVFRWVVFVYRWERRPDRRA
Protein: VIM-26 (E5BDC6)
Organism: Klebsiella pneumoniae
Interaction partners:
Sequence:
MLKVISSLLVYMTASVMAVASPLAHSGEPSGEYPTVNEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHSTDNLVVYVPSANVLYGGCAVLELSSTSAGNVADADLAEWPTSVERIQKHYPEAEVVIPGHGLPGGLDLLQHTANVVKAHKNRSVAE
Protein: Probable indole-3-pyruvate monooxygenase YUCCA7 (EC 1.14.13.168) (Flavin-containing monooxygenase YUCCA7) (O49312)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in auxin biosynthesis. Belongs to the set of redundant YUCCA genes probably responsible for auxin biosynthesis in roots.
Interaction partners:
- L-tryptophan--pyruvate aminotransferase 1
- Tryptophan aminotransferase-related protein 1
- Tryptophan aminotransferase-related protein 2
- Aromatic aminotransferase ISS1
- Indole-3-acetaldehyde oxidase
- Amidase 1
- Indole-3-acetaldehyde oxidase
- Tryptophan aminotransferase-related protein 3
- Tryptophan aminotransferase-related protein 4
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
Sequence:
MCNNNNTSCVNISSMLQPEDIFSRRCIWVNGPVIVGAGPSGLAVAADLKRQEVPFVILERANCIASLWQNRTYDRLKLHLPKQFCQLPNLPFPEDIPEYPTKYQFIEYLESYATHFDLRPKFNETVQSAKYDKRFGLWRVQTVLRSELLGYCEFEYICRWLVVATGENAEKVVPEFEGLEDFGGDVLHAGDYKSGERYRGKRVLVVGCGNSGMEVSLDLCNHDASPSMVVRSSVHVLPREVLGKSTFELSVTMMKWMPVWLVDKTLLVLTRLLLGNTDKYGLKRPEIGPLELKNTAGKTPVLDIGAISMIKSGKIKIVAGIAKFGPGKVELVDGRVLQIDSVILATGYRSNVPSWLKENDLGEIGIEKNPFPKGWKGKAGLYAVGFTGRGLSGASFDAMSVAHDIANSWKEETKQQIKTVATRHRRCISHF
Protein: THO complex subunit tho5 (Q9USR5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- THO complex subunit tho7
- Uncharacterized protein P25A2.03
- THO complex subunit Tho3
- ATP-dependent RNA helicase uap56
- Pre-mRNA-splicing factor cwf28
- mRNA export protein mlo3
- Uncharacterized RNA-binding protein C106.12c
- THO complex subunit 2
- PCI domain-containing protein C1105.07c
- Ribosomal protein arginine N-methyltransferase rmt3
Sequence:
MTENAISDCLNVLDSTRTLCLRIHELKQHSRDADDQNPEQIKRQLMSKLLILREANRKSYEQLVQAKTITAEHKSELDNARIRLQALQYKKLHLKTIIKNYEEKEHIYTALPLVSKEEFLKEHPEFKSSNDHDLMLAILEDELKERQRLSTLKQELLKRKAALISENKAKRNALQKGDEKLQTFLRSSVPVQEYYNITSM
Protein: Caspase-3 (EC 3.4.22.56) (Q98UI8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNGDCVDAKRVDTTDASKDGASASQPMQVDAKPQSHAFRYSLNYPNIGHCIIINNKNFDRRTGMNPRNGTDVDAGNVMNVFRKLGYIVKVYNDQTVAQIMQVLTTVAHDDHSRCASLVCVLLSHGDEGVFFGTDTSVDLKSLTSLFRGDRCPSLVGKPKLFFIQACRGTELDPGVETDHTDHPDIPDGRERIPVEADFLYAYSTVPGYYSWRNTMTGSWFIQSLCEMMTKYGSELELLQIMTRVNHKVALDFESTSNMPGFDAKKQIPCIVSMLTKEMYFTP
Protein: RNA binding protein fox-1 homolog 2 (Fox-1 homolog B) (RNA-binding motif protein 9) (RNA-binding protein 9) (Q6NV06)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFGQFGKILDVEIIFNERGSKGFGFVTFESSGDAEKARERLHGTIVEGRKIEVNNATARVMTNKKMVSPYANGDSLSTLPYAGWKLSPMMGAMYGPEFYAVPGFPYPTTAAAAAAASTAASFRGAHLRGRGRPVYGAVRAAVPQPAIPAYPGVVYQDGFYGATELYSGYTAYRYTQLTAVASPTAAAAAAAAAYSDSYGRVYAADPYAAALATPAAAAAAAYGVGAMATLYRGGYSRFSPY
Protein: Prenylcysteine oxidase 1 (EC 1.8.3.5) (Chloride ion pump-associated 55 kDa protein) (Q99ML5)
Organism: Rattus norvegicus (Rat)
Function: Prenylcysteine oxidase that cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine (By similarity). Only active against free prenylcysteines and not prenylcysteine residues within prenylated proteins or peptides (By similarity). Involved in the final step in the degradation of prenylated proteins, by degrading prenylcysteines after the protein has been degraded (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q9UHG3}.
Interaction partners:
- Serum paraoxonase/arylesterase 1
- Apolipoprotein B-100
- Platelet-activating factor acetylhydrolase.
- Clusterin
- Apolipoprotein C-I
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein C-IV
- Apolipoprotein A-II
- Phospholipid transfer protein
Sequence:
MGRFAATLVGSLFGLGLLLCGLGRLASAEPRAPPEKIAIVGAGIGGTSSAYYLRKKFGKDVKIDVFEREEIGGRLATLKVQGHDYEAGGSVIHPLNLHMKRFVKELGLSSVPASGGLVGVYNGKSLVFEESSWFIINVIKLVWRYGFQSLRMHMWVEDLLDKFMRIYRYQSHDYAFSSVEKLMYAIGGDDYVRLLNQTLRENLKKAGFSETFLNEMIAPVMKVNFGQSTDLNAFVGAVSMTAADSNLWAVEGGNKVVCSGLLQASNSNLISGSVMSIEKTRTKQTGTPPKMYEVVYKTGSEIHSDFYDIVLVAAPLNRKMSNITFRNFDPPIEEFNDPYQQLVTTLIKGELNSTLFSSRHKDQFGLSAILVTDDSDMFINSLSIVASVSHKEGPPPAVDGMHVWKTFSKDILTKEQISKLFLSYDYAVRKPWLSYPYYNPPQKCPSIILHDRLYYLNGIEFAASCMEMSAIAGYNAALLAYHRWNGNEDMIDQDDLYEKLKTEL
Protein: Phosphoenolpyruvate synthase (PEP synthase) (EC 2.7.9.2) (Pyruvate, water dikinase) (P23538)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
Interaction partners:
- Phosphoenolpyruvate carboxykinase
- Pyruvate kinase I
- Phosphoenolpyruvate carboxylase
- NADP-dependent malic enzyme
- Pyruvate kinase II
- Transketolase 1
- NAD-dependent malic enzyme
- Pyruvate dehydrogenase
- Phosphoenolpyruvate synthase regulatory protein
- Enolase
Sequence:
MSNNGSSPLVLWYNQLGMNDVDRVGGKNASLGEMITNLSGMGVSVPNGFATTADAFNQFLDQSGVNQRIYELLDKTDIDDVTQLAKAGAQIRQWIIDTPFQPELENAIREAYAQLSADDENASFAVRSSATAEDMPDASFAGQQETFLNVQGFDAVLVAVKHVFASLFNDRAISYRVHQGYDHRGVALSAGVQRMVRSDLASSGVMFSIDTESGFDQVVFITSAWGLGEMVVQGAVNPDEFYVHKPTLAANRPAIVRRTMGSKKIRMVYAPTQEHGKQVKIEDVPQEQRDIFSLTNEEVQELAKQAVQIEKHYGRPMDIEWAKDGHTGKLFIVQARPETVRSRGQVMERYTLHSQGKIIAEGRAIGHRIGAGPVKVIHDISEMNRIEPGDVLVTDMTDPDWEPIMKKASAIVTNRGGRTCHAAIIARELGIPAVVGCGDATERMKDGENVTVSCAEGDTGYVYAELLEFSVKSSSVETMPDLPLKVMMNVGNPDRAFDFACLPNEGVGLARLEFIINRMIGVHPRALLEFDDQEPQLQNEIREMMKGFDSPREFYVGRLTEGIATLGAAFYPKRVIVRLSDFKSNEYANLVGGERYEPDEENPMLGFRGAGRYVSDSFRDCFALECEAVKRVRNDMGLTNVEIMIPFVRTVDQAKAVVEELARQGLKRGENGLKIIMMCEIPSNALLAEQFLEYFDGFSIGSNDMTQLALGLDRDSGVVSELFDERNDAVKALLSMAIRAAKKQGKYVGICGQGPSDHEDFAAWLMEEGIDSLSLNPDTVVQTWLSLAELKK
Protein: L-ornithine N(5)-monooxygenase (OMO) (EC 1.14.13.196) (L-ornithine N(5)-oxygenase) (Siderophore biosynthesis protein A) (G5EB76)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as the secreted triacetylfusarinine C (TAFC) involved in iron uptake and the intracellular iron storage compound desferriferricrocin (DFFC).
Interaction partners:
- GATA-type transcription factor sreA
Sequence:
MEPLQRKSELDFQSYRKMPLAQQRTQRLKPTSPEELHDLICVGFGPASLAIAIALHDALDPCLNKCAPTSGWQPKVAFLERQKQFAWHSGMLVPGSRMQISFIKDLATLRDPRSSFTFLNYLHQKDRLIHFTNLSTFLPARMEFEDYMRWCANQFSDVVTYGEEVIEVLPGKSSPDSPVVDYFTVLSRNVETGEISSRSARKVVLALGGTAKLPAELPQDPRIMHSSKYCTALPNLLKDNNEPYNIAVLGSGQSAAEIFHDLQKRYPNSRTSLIMRDTAMRPSDDSPFVNEVFNPERTDKFYNLSAAERERSLKADKATNYSVVRLELIEEIYHDMYLQRVKNPDETQWQHRILPSRKITRVEHYGPNKRMRVHVRAVKDGKDSLIGDGKEVLEVDALMVATGYNRNAHEQLLSKVQYLRPATQDRWTPSRDYRVDLDRSKVSAGAGIWLQGSNEQTHGLSDSLLSVLATRGGEMVESIFGEQLESAAVPDTRFRAML
Protein: Fatty acid-binding protein, adipocyte (Adipocyte lipid-binding protein) (ALBP) (Adipocyte-type fatty acid-binding protein) (A-FABP) (AFABP) (Fatty acid-binding protein 4) (P70623)
Organism: Rattus norvegicus (Rat)
Function: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04117}. Nucleus {ECO:0000250|UniProtKB:P04117}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Subject to constitutive nuclear export. {ECO:0000250|UniProtKB:P04117}.
Interaction partners:
- Hormone-sensitive lipase
- Gastrotropin
- Fatty acid-binding protein, liver
- Fatty acid-binding protein, heart
- Peroxisome proliferator-activated receptor gamma
- Fatty acid-binding protein 5
- Fatty acid-binding protein, brain
- 30 kDa adipocyte complement-related protein
- Platelet glycoprotein 4
- Lipoprotein lipase
Sequence:
MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNLIISVEGDLVVIRSESTFKNTEISFKLGVEFDEITPDDRKVKSIITLDGGVLVHVQKWDGKSTTIKKRRDGDKLVVECVMKGVTSTRVYERA
Protein: Zinc finger protein 386 (Kruppel-like) (F1MAL7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
FQEQLTFRDVAVDFSPDEWECLDPPQQRLYRDVMVENYRNLVSVALSHHCTQNFSPEQILKYSFTKGTNGSCGLKSLYLREDCIYIDESKAHHGRDMQCLITSNTKDVIDSRDQEHKTALTITPVRPDTLDEPSIYNCKYPQESFQHDLTLKESLEDLIDGLMFHPNSSIDKELRSRGLISTSDQIETFYTERSLLFSQQIAISYDPKHNSIDYGLPAIDPLSHSPNGDTDVWESPFMYKETSKDFSSESLLNNCNDIILEKSSQYNKICNDFDHCSSPNKYQYTLPKKPFNCDNFFTQCSKLSIHQYVQDNCYKSIDCDTMFNKTLNVITHKIQHSQKSYKCNECGKAFKYCSSYRKHRIIHTGEKPFKCKVCGKSFTQCASLKKHQRIHTGEKPYKCEECGRSFNHYSILGQHQRIHTGEKPYKCKQCGKSFTQCSSLQKHQVIHTGEKPFRCAECGKSFTQNSTLSQHQRIHTGEKPYKCEQCGKAFTQCSSLRKHQRIHTGEKPYKCEECGRAFNCRSSFTKHREFTQERNLTNVKTVTKLSSTAQTLLNTGESIQERNHTNVMNVENPLVSVPTLENMREFIHE
Protein: Candida glabrata strain CBS138 chromosome I complete sequence (Q6FQL9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
Sequence:
MFGAQHGIENQESIQNKRMKTMNTMKRKSSDMQESEQISADNQQDTDNNSILDATAAAVAANNAFNMNLLMNMHMNNLHSLNNVNTNPSFMAYQQRKQERREKESQKILQQQREQQQKQQQQQQQLQLQQSQQQQQQQQQQQQQREIQQQQQNIDDQMRASNEQLGNRSTSSSQQQLHQQLHQQYFGDMIIRSGILGNNDAGMMMSQMNMGSFGAENGNQNGMNDTLGSGIDNSNVVGNRNSSAIGQNMQNMIGENQGGIGLGQSSANGDYQKEIGVNNVFIKQEDSNSNLYQSSMSQAIKNSAMNQGHISPGNKDIDDDSMNNKYKNMRDSINNNPHLIHDKNIQQNLSPFYSPFGVDVSHLPMTSPPIFQNVGYGGDVHPRRRISISNGQISQLGEDIETVENLYNTQPPPMPQNRFQQAANNGIGEKPKKIRTDSTIDTEKQAQMNMYLGRNSGFPPESNNFNDYMMSTDSISSSNEQMMAHSQPPETNLSVSFNADNLRSNTTDVVGGDTHKAIGQVIKSPPSLSASPLSSVMKNDSGTQRHSTDSFTRGVNPGTQMQNGNINQKQGQYEQQQVRQNYNQNTYSNDEPLPGTTAWKKARLLERNRIAASKCRQRKKVAQMQLQKEYDELHKENSIIKRKLQYYEKLVSKFKKFSEAHISKCDKHDKESLRMIEEMLMIDSDINEVNESGLIVSMSER
Protein: LiPocalin-related protein variant 1a (Lipocln_cytosolic_FA-bd_dom domain-containing protein) (G5EEP5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRNLLIIVCIHLILLLVHFTDAFAGTVRPFFTTLPVPGRNVPIMRLFENYAASCRPKSKKDFNVDQLANLLQSLQMDEVATKAYNSLFFSMADMQIEKFMGKWYTVVDSKEVHKEDCSIFYFDMVLQTPYTATFTSKQYGVINNDVVTNEGYGSMVGPEPGAVLITTGSERDQCPFFPVRIGGLSDEGEYQYMILSTPLKYPTMVLTRDLTLFETKWKREVYDFVEKNGFMSPMAALNTRLHFTDVDVCRKVNKLYENGNV
Protein: Fin bud initiation factor (A1IGX5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Essential for the initiation of pectoral fin bud formation. Potentially acts downstream of retinoic acid and Wnt signaling and is required for tbx5 expression in the lateral plate mesoderm of presumptive pectoral fin bud regions.
Subcellular location: Endoplasmic reticulum {ECO:0000250}. Secreted {ECO:0000269|PubMed:17196583}. Golgi apparatus {ECO:0000269|PubMed:17196583}.
Interaction partners:
- Anoctamin
- Plakophilin 3b
- Zinc finger protein 536
- Unique cartilage matrix-associated protein
- Copine 8.
- Transmembrane protein 204
- Copine-8
- Transmembrane protein 19.
Sequence:
MGTMASPLFILIACLLSMRVGGAFFAGPLYPEMSNGTFHHYFVPDGYYEENDDPEKCQMLFKMMDNRKCTLDEDQDSVIRDDFTIIKRHIEDAARVLEGIGKSISFDLDGEDSYGKYLRRETTQISEAFSNSEKSLLELEVKFKQSQENELKEEHKISDDFLNMIVHTRDVLKETLDISLGLKDKHELLSLIIRSHGTRLSRLKNDYMKV
Protein: Cathepsin B (EC 3.4.22.1) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain] (A1E295)
Organism: Sus scrofa (Pig)
Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P07858}. Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space {ECO:0000269|PubMed:22261194}. Apical cell membrane {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10605}; Extracellular side {ECO:0000250|UniProtKB:P10605}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000250|UniProtKB:P10605}.
Interaction partners:
- Cathepsin D
- NACHT, LRR and PYD domains-containing protein 3
- BH3-interacting domain death agonist
- Bcl-2-like protein 1
- Legumain
- Lysosome-associated membrane glycoprotein 1
- Transmembrane serine protease 2
- Cathepsin S
- Collagen alpha-1
- Caspase-1
Sequence:
MWRLLATLSCLVLLTSARESLHFQPLSDELVNFINKQNTTWTAGHNFYNVDLSYVKKLCGTFLGGPKLPQRAAFAADMILPKSFDAREQWPNCPTIKEIRDQGSCGSCWAFGAVEAISDRICIRSNGRVNVEVSAEDMLTCCGDECGDGCNGGFPSGAWNFWTKKGLVSGGLYDSHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYTPSYKEDKHFGCSSYSISRNEKEIMAEIYKNGPVEGAFTVYSDFLQYKSGVYQHVTGDLMGGHAIRILGWGVENGTPYWLVGNSWNTDWGDNGFFKILRGQDHCGIESEIVAGIPCTPHF
Protein: adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q387N6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
- Phosphodiesterase
- Phosphodiesterase
Sequence:
MYGAGFPHNVVDSLNAGLSASIATREEKLHTLVKVSLIQPSSYEESVEQLLTTNVEKAGDELLVIVGPLGNQNVLWVRDKLEEHDLVAFAPLSYSDEVRGWNPHFYYPSVEPKAELLALIRYAVVFLRLRRVGFMYLKGTNFGDSSYTFTEQVMSMMGYKLCGTFAIDGNVNERIGDDVFDKEWEKFVKTRPQAVLLFGSPHDITKKFIHYLLREDHHTADAFVLTTSSSQTFLLNTWKEALEETNTELKPGQLIITGTGPLAGDTRYKIIQRFREEMTKYLNTNENWGGFAKPEHFDTNHNSGELMVLGWLAGEMLMRALVDTISLTNRTLFRLSLYNQRRYLIDDMVIGDFGGECGSAAQLQGAVCRCNQGGSVVYMKEVVGKYHLEAVEEGLLTWGTTRCFSTGIRVYAPLSGLVILISDNHVVQRANSLYFSGAVTLTGNDHIGDNDRLFFHSLNSSYSGAAKDLNDTLDERIVSAVFGVVTNEVLTTPGVIFFDPMVVFPQVSTFKRNVIHFFPTLTQELYVLAQYFSRLTNHIAHTIIRSDEAAEVAEVLSMSLMTFGASLGSRVLLNEHVSDIHMEHLKHGGDVFILGLTTPDVKTISKYLDTHPQARVFITFTDLLLYYEELKLEFSVTANAKAQRLLFATSLPHWADNSSTSETIIAYHEAVPDPSQWSPMSLRGFAIARVMQTLLLPMKKVSSSLLSDEIFWQTSFVIDDMRYGPFSDSDCIANGVQLSGNCVWNYGATDISVWSFGRVLDPTFPVMQEPVTPSIVYKKIRVQLSSSQVAGIIIGLVFALLLFVTLGVALYCTISNKRDNELAPRQSTDPVTLIFTDIESSTAQWATYPDIMTEAVAAHHRMIRQLVLKHDCYEVKTIGDSFMIACQDPFKAVQLAADLQLMFLHNDWGTDALDNFYREFEEANAKEDNEYTSPTACLDSEVYCRLWSGLRVRIGIHTGLCDIRHDEVTKGYDYYGPTTNMAARTESVANGGQVLLTHATYMSLSESQRHQVDVTALGPVQLRGVPQPVQLYQLNAVPGRTFVALRLDHDYYFEDGNETTNSTSENSSSRVELSESAQMIMSSLQMLLATFKGQQREKLLMPYCERWRVPLPRTNTEEWNDEYCREVIHRIAAKVGRVADHYAGTHSNHSISTLSSTSVVIISDNKILLDE
Protein: Uncharacterized proline-rich protein C70.10 (P78797)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MFFIVAAGFVIAALIAAIGMAINRFFVRRRQARAGQTKPATTRPMAEARARPGATAVPRRSPTSPQSAYVPATVYTSPIGSPRRGSVRYTHVMAHPNTTTTVSENLPEEVPPPYSPAATASNTPQNEASPAATEAVNHERPASPPPVYRPPEEMV
Protein: Cytochrome b559 subunit beta (PSII reaction center subunit VI) (P0C401)
Organism: Oryza sativa subsp. japonica (Rice)
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00643}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00643}.
Interaction partners:
- Photosystem II D2 protein
- Photosystem II reaction center protein L
- Photosystem II CP43 reaction center protein
- Cytochrome b559 subunit alpha
- Photosystem II protein D1
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein J
- 33 kDa subunit of oxygen evolving system of photosystem II
- Photosystem II reaction center protein H
- Photosystem II reaction center protein K
Sequence:
MTIDRTYPIFTVRWLAVHGLAVPTVFFLGSISAMQFIQR
Protein: Ubiquitin thioesterase zranb1-B (EC 3.4.19.12) (Zinc finger Ran-binding domain-containing protein 1-B) (A0JMQ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates apc protein, a negative regulator of Wnt-mediated transcription (By similarity). Acts as a regulator of autophagy by mediating deubiquitination of pik3c3/vps34, thereby promoting autophagosome maturation (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the stress fiber dynamics and cell migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UGI0}. Nucleus {ECO:0000250|UniProtKB:Q9UGI0}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000250|UniProtKB:Q9UGI0}.
Interaction partners:
- APC regulator of WNT-signaling pathway
- UBX domain protein 7.
- Inner nuclear membrane protein Man1
- Ubiquitin-ribosomal protein eS31 fusion protein
- TNF receptor-associated factor 6
- Histone H2A deubiquitinase MYSM1
- Ubiquitin carboxyl-terminal hydrolase.
- OTU deubiquitinase 4.
- Inhibin subunit beta Ab.
- Valosin-containing protein
Sequence:
MTDLGLKWSCEYCTYENWPSAIKCTMCRAQRHNAPIITEEPFKSSSSLDPSLCTTQGGSTLLICPDSSARPRVRIADELPETSSKWSCHMCTYLNWPRAIRCTQCLSQRQQGSQQHSPLSPSETPQTSGSRPSPVTSDPCEEYNDRNRLNMHAQRWPCSACTYENWPKSLRCVVCDHPKPSGSPETPQQDSEAESATSPSIVNEQERENVRTAGGGGGGSRGRLRKLSPPMCKGQAEVKIELASGAVGSDNEQEADFKKLKQIRNRMRRSDWLFLNACAGVVEGDLAAVEAYKSSGGDIARQLTADEVRILNRPSAFDAGFTLVHLAIRFQRQDMLAVLLTEVSQQTAKCIPALVCPELTEQIRREVAAALHRRKGEFPCYFFTDLVTFTLPADIEDLPPNVQEKLFDEVLDRDVQKELEEESPIINWSLELGTRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKSLNDSLHDCSHWFYTRWKEWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHVFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYDNRGAGANLNTDDDVTVTFLPLVDSERKLLHIHFLSAQEMGTEEQQERMLRQWMDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDGYRQLAACPTLSDGEEEEEDEDE
Protein: G-protein coupled receptor-associated sorting protein 1 (GASP-1) (Q5U4C1)
Organism: Mus musculus (Mouse)
Function: Modulates lysosomal sorting and functional down-regulation of a variety of G-protein coupled receptors. Targets receptors for degradation in lysosomes via its interaction with BECN2.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Beclin-2
Sequence:
MTRAEVEPGAQAKAENKPGDENANAAEVEPEAPLVVRPKVRTQIMTGARPKVKPKGTPGARPKGETSTPGGAYAKCKPKAIPIARSKHDAQVWAPNKFRGESMSKMGKQCQISAADPPLLSNDSGMVAQAKCLPVDRELANMDTESIPKKANSPAGFQPSYGSEEGTNMGSWYRARPVPKGEAYENSDFKWADKPSGSPSFWNRDEASTRFRPRKSMKANNRFRHMAKQEANTMPRHKNKQEFYNISSSDSEDESGKTPWFWPKDKTKVWSKPKEEPNSRSWFRSKKEVRVESTSGSECENPTKSLFWSGEEAKSRSKPRARKGVNMRARQQAKREACSDAMSGAIDTNKKESWFLPEEKANVFSKSKTKKEPRTRAVPKEEVKTKARASTKQEARPEEEVLVGAWFWDTQESTMADRISIKTTFVEEEPIVGDWFWSEEEASVDSETCHTSRPRAKEEQVSSFCLGSGKKSSMESGPKATSKSMPVAKEDEVVIGSWFWADDEEINLQADDESIFGSWFWGTGENSLRSVGVNCEKMPKAGEKEVTDSWFWAGDVNTEAEVEEQARSASTKATIFVPWFWSEKQPNMDLGSEPCSDIMAGAEEEPIIGPWFWAKVDNSVEAEVNSKSSLEDEEEPIRSPWFGAREQTDMKYAAGIRYKPMAEAEDANKKSCVWAKEPCLYPTNRECLKSTLGEKEDTVDPWLWSNNYPRTKTITGSWLWAAEEGNIDDETGEKIKLPTLEDNAFNSWFWKENEESIVEAPKREEFRPEAEEEDIIGSWFWAGDEDRFEPAAKINEENKIASEDEDTVGSWFWGNEEASLEAVRRGTFESAPGIKEEKVTGSWFWTDKAKVGAGSQTVETGSETEEEAIFESLIWAAKKDSIQAGVKRVSKPKDDGNIAVGSWLWSSDKATKEAKTLIVSEASPENGKESVVKFGSRAKDEVINKTGSGDNCKHSTEAETIVGAWFWEGDEASFESNPVPVCKAVCEPESSAEHEPDPSRRPQSWDEVTVQFKAGPWGKAGFPPMNPFRFPKEAASLFAEMFGGKPKLVEVGPEREPEPQFPFQYDPSYRSVREIREHLKARESAQPENWSCNCIQCELRIGSEEFEELLLLMDRNRDPFIHEISKIAMGMRGASQFTRDFIRNSGVVSLIEALLNYPSSRVRTRFLENMVRMAPPYPDLNMIETYVCQICEDTFDYDLDSPDQLSGLTMITHLTATSDYHKVVVNYLAGFFYLLNSGNTKTRFHVLKLLLNLSENLVMTKRLLVTDSVSEFMDLINREESDENIQIVLAIFETISKHIQKEALFSDDDDDDEEEDAVNLEPFISAFREAEKIAKELKRKPGNQKAP
Protein: Inner membrane protein YtfF (P39314)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Leucine efflux protein
- L-alanine exporter AlaE
- Aromatic amino acid exporter YddG
Sequence:
MISGVLYALLAGLMWGLIFVGPLIVPEYPAMLQSMGRYLALGLIALPIAWLGRVRLRQLARRDWLTALMLTMMGNLIYYFCLASAIQRTGAPVSTMIIGTLPVVIPVFANLLYSQRDGKLAWGKLAPALICIGIGLACVNIAELNHGLPDFDWARYTSGIVLALVSVVCWAWYALRNARWLRENPDKHPMMWATAQALVTLPVSLIGYLVACYWLNTQTPDFSLPFGPRPLVFISLMVAIAVLCSWVGALCWNVASQLLPTVILGPLIVFETLAGLLYTFLLRQQMPPLMTLSGIALLVIGVVIAVRAKPEKPLTESVSES