wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium homeostasis modulator protein 1 (D3Z291)
Organism: Mus musculus (Mouse)
Function: Pore-forming subunit of a voltage-gated ion channel, also permeable to larger molecules including ATP, required for sensory perception of sweet, bitter and umami tastes. Specifically present in type II taste bud cells, where it plays a central role in sweet, bitter and umami taste perception by inducing ATP release from the cell, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways. Together with CALHM3, forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells (TBCs). Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to changes in extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of Ca(2+), Na(+) and K(+), as well as permeation of monovalent anions. Acts as an activator of the ERK1 and ERK2 cascade (By similarity). Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum (By similarity). May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Basolateral cell membrane {ECO:0000269|PubMed:30804437}; Multi-pass membrane protein. Note=Localizes to the basolateral membrane of epithelial cells including taste cells (PubMed:30804437). Colocalizes with HSPA5 at the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q8IU99, ECO:0000269|PubMed:30804437}.
Interaction partners:
- Calcium homeostasis modulator protein 3
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Sodium channel protein type 9 subunit alpha
- Transient receptor potential cation channel subfamily M member 5
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Pannexin-1
- Taste receptor type 1 member 2
Sequence:
MDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNVVYSLGILLTPPLVLFLLGLVMNNNISMLAEEWKRPAGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVATLGNGSLVPGLPAPELARLLARVPCPEIYDGNWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQVAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGVLATATATATATEAVQSPSDRTEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQEAPLMSNGWAGGEPRPPRKEVATYFSKV
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 8 (A2AMZ4)
Organism: Mus musculus (Mouse)
Function: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1). Required to stabilize NDUFAF5.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:A1L188}.
Interaction partners:
- Arginine-hydroxylase NDUFAF5, mitochondrial
Sequence:
MSVNGAVWGRVRSRFRAFPEHLAACGAEASAYGKCVQASTAPGGRLSKDLCVREFEALRSCFAAAAKKTMMGGS
Protein: O-glycoside alpha-1,2-mannosyltransferase homolog 5 (EC 2.4.1.-) (Q96WW1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable mannosyltransferase involved in O-glycosylation of cell wall and secreted proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS15m
- Phospholipid-transporting ATPase accessory subunit ivn1
- Alpha-1,3/1,6-mannosyltransferase alg2
- Zinc finger SWIM domain-containing protein sws1
- Cell wall alpha-1,3-glucan synthase mok12
Sequence:
MKRYDTLHVWKLIKLLICKFLLFHDFGTALFTSLVKASMLGFHNWRRTYWLYLKKLRPINDTYDAPFAIGCKNVAYEASQYPRMNATFMVLARNSDLDGVLSSMNSIERRFNRHFKYPYVFLNDEPFTTEFKKAVKDATDSSIQFGVLDDELWNFPKDVDKDMIDESIAEQVGVVYANFPSYHKMCRFFSRNFYKHPLMQQYEWYWRLEPEVTFSCDISYDPFYYMDKHNKVYGYVIAIKELAKTVPNLFRYTVAHQKISNLPTTDLWSFFLDKRYETRIKKLKEEQKDQGYYVLPEPPLNRIDGQIYNLCHFWSNFEIARLDFYNSKEYNEYVDALENAGGFWTERWGDAPVHSLAVGLLLNRSQVHYFRDLGYQHSTIQHCGQEYGCNCDCPFNIPDYETKPGSCINEWASVMGGFLDE
Protein: GTPase-activating protein GYP5 (Q12344)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTPase-activating protein which accelerates the GTP hydrolysis rate of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis.
Subcellular location: Cytoplasm. Bud. Bud neck.
Interaction partners:
- Probable GTPase-activating protein GYL1
- Reduced viability upon starvation protein 167
- Reduced viability upon starvation protein 161
- GTPase-activating protein GYP8
- GTPase-activating protein GYP1
- GTPase-activating protein GYP7
- GTPase-activating protein GYP6
Sequence:
MSSDKSIEKNTDTIASEVHEGDNHSNNLGSMEEEIKSTPSDQYEEIAIIPTEPLHSDKELNDKQQSLGHEAPTNVSREEPIGISGDEDTQITEQNVNEQRQETREPSSEIDLNEPLDVEKDVTTDVQAPNGLNIEKEYDAVKENEKVYADTKEVVSSPENREVTGKNSGGEKSSSSKFLDDESGTTTAANANDISISSEVTPERSSENDNNQIHITNEVAAGINLNENKEQKAAIEDGPVTAENLSSETARKVPPIPTQIINEKGDNSSENEVSAIPTTSSPPLPPRQNVATSTSPKLPPRGKQREQPPKTKNAVPPPLEEEMKSEKFRKNFEETKRNSYHHVPLTGSKTAQLESTAEINLIASRYRKTSHHLNKEGEETRESLQEGQSFLKSTFTSFLENLSEYNEVENVNEEDREMFKIDWSFWTQVVNDYATVASNEPENLEAHVTNGIPPQIRGIIWQLMANSKSREMEDIYETLLDTECLHEATIRRDLRRTKFVAEDKMESLYKVIKVYSVYDPDVGYTQGMGFIAAPLLINCENEAESFGLLVGLMKNYGLRELFLPGMPGLMLMLYQFDRLLEEHSPSLYNRLIREGISSTMYATQWFLTFFAYKFPLEFVLRIFDIVFVEGIEVLLKFAVNLMLKNEETLVKLRFDELLDFLKDELFNYYLMGNQDDASVVQMGLSNGNSFKGNDDGTFSYNVDLFVHDAMTGVYITPLTLRRYRGEYVEIHEKEQKKEDHYESLRIQNHQLQREAQKLEHDYSILNKENISAANELIQNRLNMEMLLDEKNDLINTITDIKSQIEEEIRKQNLPNPDASLPKADLREDLERTISRNNEVMRENGQLEERITELQAEIDELININKEQVSTASLLERDSKAKGRKGWTGFKKVFK
Protein: Carboxypeptidase (EC 3.4.16.-) (Q6FIK7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome B complete sequence
- Aspartate protease
- RING-type E3 ubiquitin transferase
Sequence:
MKLAYLAGVAAVLSQVDAFSLSGAQDYFYNKSPVQNTLKNIFPAHLDDISFGTRRRSGIKKKKNWDAVVKMEGLEGHQLRVNKIVNPKKLGVDPHVKQLTGYLDNELEDKHFFFWFFESRNDPKNDPVILWLNGGPGCSSLTGLFFELGPSSIDGQKLKPVKNPFSWNSNASVIFLDQPVNVGFSYAGSNSNGGVSNTVAAGKDVYAFLQLFFKQFPQYADGQDFHIAGESYAGHYIPVFASEILAHPQKERHFNLTSVLIGNGLTDPLTQYRYYKPMACGEGSGADPVLSPEECSAMEDSLDRCLSLIDACYQSESVWACVPASIYCNNAQLAPYQRTGRNVYDVRKDCEGGSLCYPELQNIDDYLNMDYVREAVGAEVDHYESCNFDINRNFLFNGDWMKPYHKQVIEILEKGLPVLIYAGDKDFICNWMGNRAWTDELQWKYSSGFAQEPVRNWTASITGEVAGEVKSYENLTFLRLFDGGHMVPYDQPESSLSMLNEWIHKFHL
Protein: Late cornified envelope protein 1A (Late envelope protein 1) (Q5T7P2)
Organism: Homo sapiens (Human)
Function: Precursors of the cornified envelope of the stratum corneum.
Interaction partners:
- Late cornified envelope protein 2D
- Late cornified envelope protein 2B
- Late cornified envelope protein 2C
- Late cornified envelope protein 1D
- Late cornified envelope protein 1B
- Late cornified envelope protein 6A
- Late cornified envelope protein 5A
- Late cornified envelope protein 4A
- Late cornified envelope protein 1F
- Late cornified envelope protein 3C
Sequence:
MSCQQSQQQCQPPPKCTPKCPPKCPTPKCPPKCPPKCPPVSSCCSVSSGGCCGSSSGGGCSSGGGGCCLSHHRRHRSHRHRLQSSGCCSQPSGGSSCCGGDSGQHSGGCC
Protein: Transmembrane protein 139 (Q8IV31)
Organism: Homo sapiens (Human)
Function: May be involved in cellular trafficking of proteins such as SLC4A1.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVPMHLLGRLEKPLLLLCCASFLLGLALLGIKTDITPVAYFFLTLGGFFLFAYLLVRFLEWGLRSQLQSMQTESPGPSGNARDNEAFEVPVYEEAVVGLESQCRPQELDQPPPYSTVVIPPAPEEEQPSHPEGSRRAKLEQRRMASEGSMAQEGSPGRAPINLRLRGPRAVSTAPDLQSLAAVPTLEPLTPPPAYDVCFGHPDDDSVFYEDNWAPP
Protein: Exosome complex component 10 homolog (RRP6/EXOSC10) (EC 3.1.13.-) (Q9VFF3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:19225159, ECO:0000269|PubMed:21289297, ECO:0000269|PubMed:25632158}. Chromosome {ECO:0000269|PubMed:19225159, ECO:0000269|PubMed:26389589}. Cytoplasm {ECO:0000269|PubMed:19225159}. Cytoplasm, cell cortex {ECO:0000269|PubMed:19225159}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19225159}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19225159}. Midbody {ECO:0000269|PubMed:19225159}. Note=Relocates to the DNA double-strand breaks in response to irradiation, the relocalization is dependent on the activity of the DNA-damage response (DDR) kinases tefu/ATM and mei-41/ATR (PubMed:25632158). Associates with heterochromatic regions, e.g. telomeres and chromocenter, in polytene chromosomes (PubMed:26389589). Distribution during mitosis is dynamic. In prophase, protein is found either in the nucleus or it redistributes to the cytoplasm and separating centrosomes, accumulating on the pericentriolar material. At prometaphase, it is detected on the condensed chromosomes. In metaphase, it localizes to either the spindle and presumptive perichromosomal layer or to the condensing chromosomes. At anaphase, protein transitions exclusively to the chromosomes. During telophase, it associates with the spindle remnant or both the chromosomes and the spindle remnant. During cytokinesis, it is observed on the midbody, astral microtubules, the pericentriolar material and cell cortex, yet is not enriched in the nascently forming nuclei (PubMed:19225159). {ECO:0000269|PubMed:19225159, ECO:0000269|PubMed:25632158, ECO:0000269|PubMed:26389589}.
Interaction partners:
- Exosome complex exonuclease RRP44
- RNA helicase
- FI01414p
- FI07225p
- Ribosomal RNA-processing protein 42
- Exosome complex component RRP4
- Exosome complex component RRP45
- Csl4
- Nuclear nucleic acid-binding protein C1D
- FI06805p
Sequence:
MPRTPKRVHQEAKEESAQADQPPKKSASEDVEAFTNKGFKNAIAATKAANAFPQGTARALYLSYPGYARVMEDLTQRVVALIGNVLHSKDIKGDIKKRQPEEQFEMVQECNDVLFERITTNLDIKGGLRRNTQQVVEAQVDVMSSSTSIEPAVASPQTQGTPKAGSWNRTTGTPQRSMVSARLFTAKNIVRPQTQFREPVDNSAQNPFVPRLKEKPNSLKPLALLPEYDDAGNVQSYLHPYEFELLKFQPPEEQFQKQKPVLPALMAETELMVVDTVEKLKQALEELRQAPQIAIDVEHHSYRTFMGITCLVQMSTRSKDYIFDTLILRDDMHILNLVLTDPKKLKILHGADLDIEWLQRDLSLYIVNMFDTHRAAKALNMARLSLAYLLKHYLDLDVDKSLQLADWRMRPLPQQLVDYARQDTHFLIYVYGRMTNDLLQQHAEPGLLGSVYQQSTDVCKKRYNKPHIGPESHLDLVRKTKRSFDNRQLYALRGIFEWRDATARSEDESYGYVLPNHMMLQIAESLPREMQGILACCNPIPPLVRQQLHTLHQIVLKARDQPLVKPILEAHSSTQAALPPSTKDFSSKLYCPHDFSQLEEIRDDLPTLLKRNSTTGKLEVPNKEEVAKVDPTLAAPAMALFEKQSKPTQEEEQRWAHLRKESQTMRMPYKRYLAILPLMVQLKADQLARERSELQKRQLCPAAPTVEQNIKLEAHAIGKEDDDMYSVPLKEQLKRKHPQANVKTDPEQQPTASKRPRKDENSQTKPPVKIEPVEKVQQALGESDDEVVEVPIERQATEPPKPSPAQNNRKQKKNQFQRGFKAKNRGNHPQSSSQQVPQHKGTGNFDYKNVDFRQFKGGAQRARGTEIKQQIRGKNRPNNRNNKQFNKLFTFSNVRKEGKK
Protein: Misshapen, isoform F (M9PH19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAHQQQQQLAPSVNCSLDDIDLTALKDPAGIFELIEVVGNGTYGQVYKGRHTKTGQLAAIKVMDVTEDEEEEIKLEINVLKKYSNHRNIATYYGAFIKKSPPGKDDQLWLVMEYCGAGSVTDLVKSTKGQSLKEEWIAYICREILRGLSYLHSNKVIHRDIKGQNVLLTDNAEVKLVDFGVSAQLDRTIGRRNTFIGTPYWMAPEVIACDENPDATYDNRSDLWSLGITALEMAESQPPLCDLHPMRALFLIPRNSPPRLKSKKWSKKFHGFIDTVLVKDYHQRPYTENLLKHGFIKDQPTDRQVRIQLKDHIDRCKKRKQEKEREDYRYSGSDNDDDEPQLAGEHSSIVQAPGGDTLRRNFQQIQEGRLAAEQQQQHHLMAQAQAQAAAAHAAAQAQAQLQQQQQQAAAAAAAAAHAAQQAQQAAQQAQAQQPQANRQPKPPSRQQVEEPGPPARPPQRLIVVPDPPHANRPLPPTPKCGEPAGQTPQQQQRNSQNNFKPSLPPRRPEDHLDVLAAQLSELGVVFSQQPQPQTAAGGQGSQQQAQPEAPPRNNRQSSGLSSSGGSASGGGGSSKPAAALPQQSNNHLGQPVNPLDPLDSSDSDSEPDEPNDRARNDGTLLASDPPKPLPGLGPVSEDANTTTPLSHGSGGPPNRPLPPTPDDDDQAGDRTLIMKRKLEQNINRLQKSASTSQANVTPSRRGDESNLLRDWDFDRFFPKNANGPRGSGRGSPTTTASLSRSSQLSTLKVDTKLQRASVAEAITRPVPRGYQPLKAEPSASQSIAKEQGSASGSGSGSGSASGSGSGGSTNSPAHKRQDSDSRLPTNFERGFRRENSDFFPLAKRYSAVFSGASASGSTAGSPSAQALQRSSAVYQRNSIYSSSISSKSKENDVPGAPGAAAAGTATASAKPGPAAATTTATKGAAPKTSKSLANFHFLRPRREKTESVIVLQNAAVRAQRLQQLQQQQQQQQLQQQQQQQNRGGGGGGGGGGGGGGSSGVGADGTGLGTPGTRTSSVLPDLLSQASPATPPRHDKSSSEEKQRSFLTFGFGAGGSGPSRRESHVNVNVTPTSHEAANDTPEIRKYKKRFNSEILCAALWGVNLLIGTENGLMLLDRSGQGKVYQLISRRRFQQMEVLEGQNILVTISGKKNRVRVYYLSWLKSKILRTDGLSDQVERRNGWINVGDLQGAVHFKIVKYERIKFLVIALKDSIEIYAWAPKPYHKFMAFKNFGELEHRPLLVDLTIEDQSRLKVIYGSAEGFHAVDLDSAEVYDIYLPKHGAIIPHCIVALPNSNGMQLLLCYDNEGVYVNTVGRVSKNIVLQWGEMPTSVAYIGTGQIMGWGNKAIEIRSVESGHLDGVFMHKKAQRLKFLCERNDKVFFSSAKGASSCQIYFMTLNKPGMANW
Protein: Anillin (Q8K298)
Organism: Mus musculus (Mouse)
Function: Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis. May play a significant role in podocyte cell migration.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9NQW6}. Cell projection, bleb {ECO:0000250|UniProtKB:Q9NQW6}. Note=Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody. {ECO:0000250|UniProtKB:Q9NQW6}.
Interaction partners:
- Transforming protein RhoA
- Rac GTPase-activating protein 1
- Kinesin-like protein KIF23
- Kinesin-like protein KIF11
- Protein ECT2
- Protein diaphanous homolog 3
- Citron Rho-interacting kinase
- Disks large-associated protein 5
- Inner centromere protein
- Centrosomal protein of 55 kDa
Sequence:
MDPFTEKLLERTRARRENLQRKMAERPTAVARSAPHAKRGREPLSEASNQQQPLPGGEEKSCTKPSPSKKRCSDKIEVGAPDLENTEPIDVAKPCSPMPAPRQAKPPAPAAISESVAAPAALLSADRGLNSGSEASATSSVKTRMQRLAEQRRHWDSDLTDDVSESSYFAPVPTEDKAASPSKPPISNASATPVGRRGRLANLAATICSWEDDVSHSSAKQNSVQEQPGTACLSKSSSASGASASINSSSVQQEATCCSPRDGNASVRKDPSSNAAHGPLLSASVSSSVKASSPVTAATFITENREAQNPELLHKTASPLKTEARKPCEKPTLSQGAQPKEEANREVCLQSQSKDKLATPGGRGIKPFLERFGERCQEHSKESPSYRASHKTPNITPNTKAIQERLFKQNTCSSTTHLAQQLKQEREKELACLRGRLDKGNLWSAEKNEKSRSKHLETKQEVHCQNTPLKKHQTVASTPLTSVTDKVAENEPAVKLSSTEPAGSTESEMTKSSPLKITLFLEEEKSLKVASDLEVEQNTEAVREVEMSVDDEDINSSRVINDIFSDVLEEGELDVEKSQEEMDQVGAENSEEQEDALNISSMSLLAPLAQTVGVVSLENVISSPPSELRDSNLSAASPKPGKFQRTRVPRAESADSLGSEDRDLLYSIDAYRSQRFKETERPSIKQVIVRKEDVTSKLGEKKNVFSGQVNIKQKMQELNNDINLQQTVIYQASQALNCCVDEEHGKGSLEEAEAERLLLIATEKRALLIDELNKLKSEGPQRRNKTSVISQSEFAPSKGSVTLSEICLPLKADFVCSTAQKTDASNYYYLIMLKAGAEQMVATPLASTANSLSGDALTFPTTFTLHDVSNDFEINIEVYSLVQKKDSLGPDKKKKASKSKAITPKRLLTSITSKSSLHSSVMASPGGLGAVRTSNFTLVGSHTLSLSSVGDTKFALDKVPFLSPLEGHICLKISCQVNSAVEEKGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDERRKNPIGRINLANCISHQIEPANREFCARRNTLELITVRPQREDDRETLVSQCRDTLCVTKNWLSADTKEERDLWMQKLNQVIVDIRLWQPDACYKPVGKP
Protein: Nigrocin-2JDa (B3A0M6)
Organism: Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis)
Function: Has antibacterial activity against E.coli ATCC 25992 (MIC=16 uM), E.coli CIB 84492 (MIC=16 uM), S.aureus ATCC 25923 (MIC=16 uM) and S.aureus CIB 85462 (MIC=8 uM). Has antifungal activity against C.albicans (MIC=63 uM). Has hemolytic activity against rabbit erythrocytes.
Subcellular location: Secreted {ECO:0000305|PubMed:22917879}.
Interaction partners:
Sequence:
GIFGKILGAGKKVLCGLSGLC
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic (GPD-C) (GPDH-C) (EC 1.1.1.8) (P21695)
Organism: Homo sapiens (Human)
Function: Has glycerol-3-phosphate dehydrogenase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7772607}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Glycerol-3-phosphate acyltransferase 4
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Sequence:
MASKKVCIVGSGNWGSAIAKIVGGNAAQLAQFDPRVTMWVFEEDIGGKKLTEIINTQHENVKYLPGHKLPPNVVAVPDVVQAAEDADILIFVVPHQFIGKICDQLKGHLKANATGISLIKGVDEGPNGLKLISEVIGERLGIPMSVLMGANIASEVADEKFCETTIGCKDPAQGQLLKELMQTPNFRITVVQEVDTVEICGALKNVVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAKLFCSGPVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKELLNGQKLQGPETARELYSILQHKGLVDKFPLFMAVYKVCYEGQPVGEFIHCLQNHPEHM
Protein: Adenosine 3'-phospho 5'-phosphosulfate transporter 2 (Adenosine 3'-phosphate 5'-phosphosulfate transporter) (PAPS transporter 2) (Solute carrier family 35 member B3 homolog) (Q20787)
Organism: Caenorhabditis elegans
Function: Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein madd-4
- 5'-3' exoribonuclease 2 homolog
Sequence:
MTAAQIHSDCSVHMLPRHVKEDVEPIHLLGFNIARKPKWLQFVLLSLAIFILYIGYGYMQELIFKLPGMKPFGWTLTLIQFLIYSGCGYTECIIWHNTKRMIPWRIYGVIAFFTVATMGLSNASVGYLNYPTQVIFKCCKLIPVLIGGILIQGKRYGWIDIGAAMLMSLGIIMFTLADNKVSPNFDSRGYIMICGALLADAVIGNIQEKNMKKYGGSSNEMVLYSYGIGSVFIFAFVVLSGEVFSAIPFFLENSWKTFGYALILSCLGYLGVNVVLTHIKVFGALVAVTVTTLRKALTIILSFMLFSKPFTIEYVYAGSVVMLAIYLNLYSKNKTSWDNMIRRFVARAMGYHDVSVARKDPMTV
Protein: Cortexillin-1 (Cortexillin I) (Q54HG2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Actin-bundling protein. When linked to F-actin the actin filaments form preferentially anti-parallel bundles that associate into meshworks. Plays a major role in cytokinesis. Negatively regulates cortical localization of rapgap1.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8752217}.
Interaction partners:
- Ras GTPase-activating-like protein rgaA
- Myosin-2 heavy chain
- Dynacortin
- Ras GTPase-activating-like protein gapA
- Inner centromere protein A
- Fimbrin
- Actin binding protein
Sequence:
MAGKDWEIVQEKAFTAWVNSVLDKRGEKISDVGKDLSDGVKLIFFLELISSKKFNKKYDFEPKARINMIQNVALALKFLDEELKIKVQGIGSEDFVDNNKKMILGFLWTLYRKYRIAVISEGDKSSEEGLLLWCKNTTTGYDGVNITSFTKSFRDGLAFLALSHKFEPESFKFQEFEAMDPIARLNAAFDFAEKGLGVPKLLEAEEVMRGTTDERSLVLYTSLFFHAYRAKEEKARLESSKNEMANRLAGLENSLESEKVSREQLIKQKDQLNSLLASLESEGAEREKRLRELEAKLDETLKNLELEKLARMELEARLAKTEKDRAILELKLAEAIDEKSKLEQQIEATRIRGAAEAQGLGLLRKNLDTHVHDLLKWQKLTMENSSSSSIDDQIIVEVSGLPFGEQVKHLATKLEAENLAIMKLLNQKEDDLKAQKLKSSKSKK
Protein: Aspartate aminotransferase, mitochondrial (mAspAT) (EC 2.6.1.1) (EC 2.6.1.7) (Fatty acid-binding protein) (FABP-1) (Glutamate oxaloacetate transaminase 2) (Kynurenine aminotransferase 4) (Kynurenine aminotransferase IV) (Kynurenine--oxoglutarate transaminase 4) (Kynurenine--oxoglutarate transaminase IV) (Plasma membrane-associated fatty acid-binding protein) (FABPpm) (Transaminase A) (P00507)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11962739}. Cell membrane {ECO:0000269|PubMed:11962739}. Note=Located in the mitochondria of liver, pancreas, spleen, heart, pituitary gland and submandibular gland cells. In kidney, located in the mitochondria, on the cell surface of regions with protrusions in distal tubules, on the apical cell surface of protrusions along the microvilli in cortical collecting ducts, in condensing vacuoles, on the cell surface at cell boundaries of adjoining kidney cells and on the cell surface of endothelial cells lining capillaries in the glomerulus. Also located at the cell surface of endothelial cells lining arterioles and on the cell surface of lymphocytes.
Interaction partners:
- Malate dehydrogenase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Glutamate dehydrogenase 1, mitochondrial
- Malate dehydrogenase, cytoplasmic
- L-lactate dehydrogenase B chain
- Fumarate hydratase, mitochondrial
- L-lactate dehydrogenase C chain
- Alanine aminotransferase 1
- Asparagine synthetase
- L-lactate dehydrogenase A chain
Sequence:
MALLHSGRVLSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAGKNLDKEYLPIGGLADFCKASAELALGENSEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEMAAVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK
Protein: pH-response regulator protein palF/RIM8 (Q9UW13)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. Required for hyphal development.
Interaction partners:
- pH-response regulator protein palI/RIM9
- pH-response regulator protein palH/RIM21
- pH-response transcription factor pacC/RIM101
- Calpain-like protease palB/RIM13
- pH-response regulator protein palA/RIM20
- Ubiquitin-binding ESCRT-I subunit protein
- Vacuolar-sorting protein SNF7
- Dfg16p
Sequence:
MRRAVSKILPTPKLFNDSAHFHSNFRLEYNSVDDFYVQLDNPHKVWLPGEEISGQVVLISKKNLANIVITLSLVGFIKINASSHSKLRPLKHTLFDYTIKIYGKDEEEQTDSAEFSNGLLKGEHVFPFIVKLPNKRVYTSIDFGKGSINYILKAAIGNSSSYVIPASPDNASTSSLTKKKILQNPSHTSEKVISLVNPIDVSLLPRPKPKRLILKDPRTSSNKKLSRTQTSTSTINTMSSNEHDHSLPEGATPEDSDHKSLKSIPVPTIKAILEVPQRGYLRGESIPIKLSINHLRKIQDFNGIIITFVRVCRLDNGPDGVVESFRKDLQQLILPLYVDPVTFQSEINSSLRVPADAFPTILGCPLVSFQYFVEVLINLSGKSIALDSDVDARAKANPQATKSSSDKFKFNFDSTQTERSTYINTDSYKRSKKFLQLTTEIYIGTHRSSTQEEQAPQAEEVASRRSSSMASNSNSSPAVFSTSSPHSPVEHQYAGAINSIPESVAVSNFTPPYENVVPSYVPPEFVSHLQNQSELSEKERMRQHESSLLPSAPPDDEQPSPVNMTSNQQPFSFFTYQNTNTSPPVPLDDDLYQEPVDSAPNYLNVNNDRLIVPQDNNSNSET
Protein: FAST kinase domain-containing protein 4 (Protein TBRG4) (Transforming growth factor beta regulator 4) (B4DU42)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MEVSGGARCDIMAAHLVKRCTCLLREAARQAPAMAPVGRLRLAWVAHKTLTSSATSPISHLPGSLMEPVEKERASTPYIEKQVDHLIKKATRPEELLELLGGSHDLDSNQAAMVLIRLSHLLSEKPEDKGLLIQDAHFHQLLCLLNSQIASVWHGTLSKLLGSLYALGIPKASKELQSVEQEVRWRMRKLKYKHLAFLAESCATLSQEQHSQELLAELLTHLERRWTEIEDSHTLVTVMMKVGHLSEPLMNRLEDKCLELVEHFGPNELRKVLVMLAAQSRRSVPLLRAISYHLVQKPFSLTKDVLLDVAYAYGKLSFHQTQVSQRLATDLLSLMPSLTSGEVAHCAKSFALLKWLSLPLFEAFAQHVLNRAQDITLPHLCSVLLAFARLNFHPDQEDQFFSLVHEKLGSELPGLEPALQVDLVWALCVLQQAREAELQAVLHPEFHIQFLGGKSQKDQNTFQKLLHINATALLEYPEYSGPLLPASAVAPGPSALDRKVTPLQKELQETLKGLLGSADKGSLEVATQYGWVLDAEVLLDSDGEFLPVRDFVAPHLAQPTGSQSPPPGSKRLAFLRWEFPNFNSRSKDLLGRFVLARRHIVAAGFLIVDVPFYEWLELKSEWQKGAYLKDKMRKAVAEELAK
Protein: Anaerobic C4-dicarboxylate transporter DcuC (P0ABP3)
Organism: Escherichia coli (strain K12)
Function: Responsible for the transport of C4-dicarboxylates during anaerobic growth. Catalyzes the uptake of fumarate coupled to the export of succinate. Can also catalyze the uptake of fumarate and the efflux of succinate, without exchange. Shows low rates of transport, which are sufficient for succinate export during fermentation but not for fumarate-succinate exchange in fumarate respiration, indicating that it may function in vivo as the succinate efflux carrier for glucose fermentation, even if it is also able to operate as a fumarate-succinate antiporter.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Anaerobic C4-dicarboxylate transporter DcuB
- Citrate/succinate antiporter
- PTS system galactitol-specific EIIA component
- Probable succinate transporter subunit YjjB
- Probable succinate transporter subunit YjjP
- Inner membrane protein YcdZ
Sequence:
MLTFIELLIGVVVIVGVARYIIKGYSATGVLFVGGLLLLIISAIMGHKVLPSSQASTGYSATDIVEYVKILLMSRGGDLGMMIMMLCGFAAYMTHIGANDMVVKLASKPLQYINSPYLLMIAAYFVACLMSLAVSSATGLGVLLMATLFPVMVNVGISRGAAAAICASPAAIILAPTSGDVVLAAQASEMSLIDFAFKTTLPISIAAIIGMAIAHFFWQRYLDKKEHISHEMLDVSEITTTAPAFYAILPFTPIIGVLIFDGKWGPQLHIITILVICMLIASILEFLRSFNTQKVFSGLEVAYRGMADAFANVVMLLVAAGVFAQGLSTIGFIQSLISIATSFGSASIILMLVLVILTMLAAVTTGSGNAPFYAFVEMIPKLAHSSGINPAYLTIPMLQASNLGRTLSPVSGVVVAVAGMAKISPFEVVKRTSVPVLVGLVIVIVATELMVPGTAAAVTGK