wanglab/gogpt-training-data huggingface dataset:
Protein: Kinesin-associated protein (G5EEE6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNQVSIDAHPSDQAIIVRFEQSPSSSAGISIKKRASSANVESLGHQKIIHLKEMSLDVDIRALSNVILQKCLFIPATSRSQLEQVLFYIQKRGNQRISARSRSSSAVSFDRRPIHSPTISAELGKIDEYIECFYGETSVEKNKGAVALYELSKNPQNLTQLVNNETLMMALARVFREDWKKHFEVGTNIMNLFVNISKFSCLHGILLHHKACMIGTLCVNAMEHETKRYDFWIAEMKKTDQETLRKLKTAIRKQAMLLAACVTFLTNLATDISVELKMVRRNLVALLVKCLQMSSESTSSLTTATIKFLLKLSIFDENKIVMEQNGTIEKLLKLFPIQDPELRKAVIMLLFNFSFDSKNLPKMVNGGLVPHMASLLDSDTKALNMMYLLSCNDDAKAMLAYTDAIKLLMKDVLSGTGSEVTKAVLLNICLEKRNAQLVCGQRGQGLDLLMEMSINSRDLMLIKVVRAISSHEGATQNMFLKWIETLIGIAKNEGADNSESKSSFGLECMGTVAELKVAPWAKIIQSENLVPWMKTQLQEGIDESEEVTVLRDIKPLQLQIVIACGTMARQLDAARLLAPLIDTFVQLLQSCQIDDEFVVQLLYVFLQFLKHKELSARLMTQDSALGAHMIDLMHDANAVVREVCDNALLIMGEHSKEWAKRIAGERFKWHNAQWLEMVERDDSEFVDYDDEDFGADLKFDHYDDGFDMNEPLF
Protein: Ascorbate-specific PTS system EIIA component (Ascorbate-specific phosphotransferase enzyme IIA component) (A0A0H2URW0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNLKQALIDNDSIRLGLEANNWKEAVKVAVDPLIESGAILPEYYDAIIESTEEYGPYYILMPGMAMPHARPEAGVQSDAFSLITLQNPVVFSDGKEVSVLLALAATSSKIHTSVAIPQIIALFELEDSIARLQACQTKEDVLAMIEESKDSPYLEGLDLES
Protein: Contig An11c0050, genomic contig (A2QVE5)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MSLGKKVTLNSGAQIPQLGFGTWQSAPGQVGDAVYEALKAGYRHLDLATIYQNQREVAEGIKRAYKDVPGLKREDIFITSKLWNSQHDPAVVEKALDECLAELELDYLDLYLVHWPVSFTTGSELFPLVKDSSVEGGDVVINDDISIVDTWKAMTQLPKSKARTVGVSNHMIPHLEAIINATGVVPAVNQIERHPVLQSNELIEYCQKKGIHVTAYSAFGNNGFGVPLLVTRPEVKEVAESASKRLGTTVTPAQVILAWSQVGGHSVIPKSVTPSRIHENFKEVELTPEEIAKVSELGKDRRRYNTPYVANTPRWDIDIFGEEEEKPAGHKIWSPVLFAAGYSSSAWVGRGKVSWDTVHLVGNHTPLLRQQTTPRFARLSF
Protein: Presenilin (EC 3.4.23.-) (A0A0S2Z4D2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MTELPAPLSYFQNAQMSEDNHLSNTNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI
Protein: Myo-inositol transporter 1 (Q10286)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transporter for myo-inositol.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- SPRY domain-containing protein C285.10c
- Putative E3 ubiquitin-protein ligase C36B7.05c
- Probable N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Inositol polyphosphate multikinase
- D-arabinono-1,4-lactone oxidase
- Phosphatidylethanolamine N-methyltransferase
Sequence:
MSISSKDFQNVTSAGFADDTFAADTFAADKKSPFESSVFENKTQVLPVDSVSRLSNGARSRSNSNISLSEPHALNDTVEDQPVSKWVWVLAFAAGIGGLLFGYDTGVISGALVVIGTSLGGHELTNGGKEFITSATSLGALLGGIIAGALADFFGRKPVIAIASIIIIVGSIVQVTAHHLWHMIVGRFVIGWGVGIASLIIPLYLSEIAPSKIRGRLVIIYVLLITAGQVIAYGIDTAFEHVHNGWRWMVGLAMVPAAFQLFILIWLPESPRLLVKKERSQEAYNTLARIYPTAHPYEIKTKLYLIQEGVRDPFSGSRWQKIVKTFKELYFNPSNFRALILACGLQAMQQLSGFNSLMYFSSTIFEVVGFNNPTATGLIIAATNFVFTIVAFGVIDFFGRRILLLLTVWGMIAALIVCAVAFHFLPKDENGNYTSGQSNAWAIVVLISMIVYVASYASGLGNLPWQQSELFPMSVRGLGTGMSTAVNWAGNLGIGASFLTLMSEITPTGTFALYGGLCFLGWLGALFCYPDLTDYTIEEIGELLKHGFGVRESMRHLKRVRQERAWSREDKEQNN
Protein: Transportin 3 (E9PFH4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGDLRTLELLLICAGHPQYEVVEISFNFWYRLGEHLYKTNDEVIHGIFKAYIQRLLHALARHCQLEPDHEGVPEETDDFGEFRMRVSDLVKDLIFLIGSMECFAQLYSTLKEGNPPWEVTEAVLFIMAAIAKSVDPENNPTLVEVLEGVVRLPETVHTAVRYTSIELVGEMSEVVDRNPQFLDPVLGYLMKGLCEKPLASAAAKAIHNICSVCRDHMAQHFNGLLEIARSLDSFLLSPEAAVGLLKGTALVLARLPLDKITECLSELCSVQVMALKKLLSQEPSNGISSDPTVFLDRLAVIFRHTNPIVENGQTHPCQKVIQEIWPVLSETLNKHRADNRIVERCCRCLRFAVRCVGKGSAALLQPLVTQMVNVYHVHQHSCFLYLGSILVDEYGMEEGCRQGLLDMLQALCIPTFQLLEQQNGLQNHPDTVDDLFRLATRFIQRSPVTLLRSQVVIPILQWAIASTTLDHRDANCSVMRFLRDLIHTGVANDHEEDFELRKELIGQVMNQLGQQLVSQLLHTCCFCLPPYTLPDVAEVLWEIMQVDRPTFCRWLENSLKGLPKETTVGAVTVTHKQLTDFHKQVTSAEECKQVCWALRDFTRLFR
Protein: Alpha/beta-Hydrolases superfamily protein (At2g24280/F27D4.19) (Q93Z34)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Vacuolar protein sorting-associated protein 41 homolog
- Probable glutamyl endopeptidase, chloroplastic
- At4g33625
- Signal peptidase complex catalytic subunit SEC11
- signal peptidase I
- Dipeptidyl peptidase IV-like protein
Sequence:
MSACLCLVFLFFSIVAEATYSPGGFHHLSSLRLKKKVSKSKHELPFETRYFPQNLDHFSFTPDSYKVFHQKYLINNRFWRKGGPIFVYTGNEGDIDWFASNTGFMLDIAPKFRALLVFIEHRFYGESTPFGKKSHKSAETLGYLNSQQALADYAILIRSLKQNLSSEASPVVVFGGSYGGMLAAWFRLKYPHITIGALASSAPILHFDNIVPLTSFYDAISQDFKDASINCFKVIKRSWEELEAVSTMKNGLQELSKKFRTCKGLHSQYSARDWLSGAFVYTAMVNYPTAANFMAPLPGYPVEQMCKIIDGFPRGSSNLDRAFAAASLYYNYSGSEKCFEMEQQTDDHGLDGWQYQACTEMVMPMSCSNQSMLPPYENDSEAFQEQCMTRYGVKPRPHWITTEFGGMRIETVLKRFGSNIIFSNGMQDPWSRGGVLKNISSSIVALVTKKGAHHADLRAATKDDPEWLKEQRRQEVAIIEKWISEYYRDLREEQ
Protein: Unconventional myosin-VI (Unconventional myosin-6) (A0A8I5ZYN7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004632}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}.
Interaction partners:
Sequence:
MEDGKPVWAPHPTDGFQMGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNVKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDTIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIREKLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYVKAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSAPSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANSARDALAKTVYSHLFDHVVDRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEVKLVGILDILDEENRLPQPSDQHFTSVVHQKHKDHFRLTIPRKSKLAVHRNLRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRALFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPEKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNLWLVCSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKPEVNRQIKDLEISIDALMAKIKSTMMTREQIQKEYDALVKSSEDLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEMEVKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLAQECRDRELALRIAQNESELISDEAQGDTALRRTNGTRPQMTPEQMAKEMSDILSRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYDFAPFLNNSPQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK
Protein: Protein sak1 (P48383)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Positively regulates cyclic AMP-dependent protein kinase-mediated exit from the mitotic cell cycle.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase cds1
- Protein kinase rad3
- Serine/threonine-protein kinase ssp1
- Fork head protein homolog 2
Sequence:
MNPSDLPGQIPLSRSDMNVQDQLDPVQRFDTHFMLPQEENFLNRPSITSESAHPRGSDLEQETELKRLALEHEHYSLESLAEKLRMDHVSANSEKFRQVFGICWLKRACEEQQDAAVQRNQIYAHYVEICNSLHIKPLNSASFGKLVRLLFPSIKTRRLGMRGHSKYHYCGIKLRGQDSFRRLRTFSDSSLSPVSCSSFPKPIPNHFENDVSSIQNTNQRVESSPASVNAAAIVRKSAVTPSSDPYNSPPPSIPLLGSQTNLQLAPSFAAPQAHPLPSHLSQSNVPPQLSHSSVPSPAPPRSVSQPTYFSQPMPQFSSSFVPGTSSIVPTLHPASAQEDFNLQHSLFFKLKLKFLPPHKLPWIPSLDVSSFSLPPIDYYLNGPYDNVEAKSALMNIYSSHCITLIESVRYMHLKQFLSEISNFPNSLSPSLLALLSSPYFTKWIERSDTVMYREILKLLFPMTLQVVPPPVLVLLRHLAENLVNHISSIYASHSSCLLQVKSETAAIFSNLLSRLLRVNDTAHAAARFLANPADRHLICNDWERFVSTRFIVHRELMCNDKEAVAALDEWYSILSTCSNPSELLDPLKDKHEASDTSMNRVELRQIDGVLDRMADFFLELPSRFPSCSPRMFLLCLGALQTSVLREITVSGGEAFGALWVIRCWVDEYMTWVAEIGGYLDDSYDELEQHHANFHNKAGISQSNIPPHLQEHRQSQQHFQQDIEALQSQQQQQATKNSLMEAAYQNAQKQKEDDYISIVFDTNGACS
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC 2.7.11.2) (Pyruvate dehydrogenase kinase isoform 4) (O70571)
Organism: Mus musculus (Mouse)
Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Stress-70 protein, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Pyruvate dehydrogenase protein X component, mitochondrial
- Angiopoietin-related protein 4
- Solute carrier family 2, facilitated glucose transporter member 4
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Peroxisome proliferator-activated receptor alpha
Sequence:
MKAARFVMRSASSLSSASLVPREVELFSRYSPSPLSMKQLLDFGSENACERTSFAFLRQELPVRLANILKEIDILPDRLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQKALSEFVDTLVKVRNRHHNVVPTMAQGILEYKDTCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSKTGNPSHIGSIDPNCDVVAVVQDAFECAKMLCDQYYLTSPELNLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPSLTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSESVEKLPVFNKSAFKHYQMSSEADDWCIPSREPKNLAKEKLAV
Protein: Protein interacting with Hsp90 1 (Nucleolar protein 17) (P38768)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-rRNA processing and required for the NOP58-snoRNA interaction.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- RuvB-like protein 2
- TPR repeat-containing protein associated with Hsp90
- RuvB-like protein 1
- Nucleolar protein 58
- ATP-dependent molecular chaperone HSP82
- ATP-dependent molecular chaperone HSC82
- Ribosome assembly 1 protein
- TEL2-interacting protein 1
- Nucleolar protein 56
- 13 kDa ribonucleoprotein-associated protein
Sequence:
MADFLLRPIKQRHRNEDKYVSVDAADGSVSKIEPIADFVIKTKLLSANGPEKLQDGRKVFINVCHSPLVPKPEVDFNARIVFPLIIQNEWEIPIITSCYRMDHDKKGQECYVWDCCINSDCSRWICDDIQLREILVEWCLESCEIRDSVVLCRDRIAFPKMKKKGAELPALEVLNDELHQDYKAKMHKIIEEEAGDPMSILRGRNDDGDDNNDPDDGTLPPLFPIENKISGAKIEEIDKNEIAHRNLKQAPAPAPAPHEQQEDVPEYEVKMKRFKGAAYKLRILIENKAPNSKPDRFSPSYNFAENILYINGKLSIPLPRDIVVNAADIKIFHIRKERTLYIYI
Protein: Hormone-sensitive lipase (HSL) (EC 3.1.1.79) (Monoacylglycerol lipase LIPE) (EC 3.1.1.23) (Retinyl ester hydrolase) (REH) (P54310)
Organism: Mus musculus (Mouse)
Function: Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters. Shows a preferential hydrolysis of DAGs over TAGs and MAGs and of the fatty acid (FA) esters at the sn-1 and sn-2 positions of the glycerol backbone in TAGs (By similarity). Preferentially hydrolyzes FA esters at the sn-3 position of the glycerol backbone in DAGs. Catalyzes the hydrolysis of 2-arachidonoylglycerol, an endocannabinoid and of 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:15550674}. Membrane, caveola {ECO:0000250|UniProtKB:Q05469}. Cytoplasm, cytosol {ECO:0000269|PubMed:15550674}. Lipid droplet {ECO:0000269|PubMed:15878856}. Note=Found in the high-density caveolae (By similarity). Translocates to the cytoplasm from the caveolae upon insulin stimulation (By similarity). Phosphorylation by AMPK reduces its translocation towards the lipid droplets. {ECO:0000250|UniProtKB:Q05469, ECO:0000269|PubMed:15878856}.
Interaction partners:
- Perilipin-1
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Fatty acid-binding protein, adipocyte
- Patatin-like phospholipase domain-containing protein 2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit gamma-2
- cAMP-dependent protein kinase type II-beta regulatory subunit
- 5'-AMP-activated protein kinase subunit gamma-1
Sequence:
MDLRTMTQSLVTLAEDNMAFFSSQGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAHLLHKSRYVASNRKSIFFRASHNLAELEAYLAALTQLRAMAYYAQRLLTINRPGVLFFEGDEGLTADFLQEYVTLHKGCFYGRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNITEIEVLSSLANMASTTVRVSRLLSLPPEAFEMPLTSDPRLTVTISPPLAHTGPAPVLARLISYDLREGQDSKVLNSLAKSEGPRLELRPRPHQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIFSIDYSLAPEAPFPRALEECFFAYCWAVKHCDLLGSTGERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLQSSASPSRLLSLMDPLLPLSVLSKCVSAYSGTEAEDHFDSDQKALGVMGLVQRDTSLFLRDLRLGASSWLNSFLELSGRKPQKTTSPTAESVRPTESMRRSVSEAALAQPEGLLGTDTLKKLTIKDLSNSEPSDSPEMSQSMETLGPSTPSDVNFFLRPGNSQEEAEAKDEVRPMDGVPRVRAAFPEGFHPRRSSQGVLHMPLYTSPIVKNPFMSPLLAPDSMLKTLPPVHLVACALDPMLDDSVMFARRLRDLGQPVTLKVVEDLPHGFLSLAALCRETRQATEFCVQRIRLILTPPAAPLN
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (A0A8I6G3R2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAGNVKKSSGAGGSGSGGSGAGGLIGLMKDAFQPHHHHHHHLSPHPPCTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDSLFMMKELAGAKVERPSSPFSMAPQASLPPVPPRLDLLQQRAPVPASTSVLGTASKASSSSLHKDKPLPIPPTLRDLPPPPPPDRPYSVGTETRPQRRPLPCTPGDCPSRDKLPPVPSSRPGDSWLSRPIPKVPVATPNPGDPWNGRELTNRHSLPFSLPSQMEPRADVPRLGSTFSLDTSTTMNSSPVAGPESEHPKIKPSSSANAIYSLAARPLPVPKLPPGEQGDSEEDTEYMTPTSRPVGVQKPEPKRPAETAQSSRACDCDQQIDSCTYEAMYNIQSQALSVAENSACGEGNLATAHTSTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGEPTNFNEGSQVPERPPKPFPRRINSERKASSYQQGGGAMANPAAAAPSPQLSSEIERLMSQGYSYQDIQKALVIAHNNIEMAKNILREFVSISSPAHVAT
Protein: N-formyl peptide receptor 3 (FMLP-related receptor II) (FMLP-R-II) (Formyl peptide receptor-like 2) (P25089)
Organism: Homo sapiens (Human)
Function: Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Acts as a receptor for humanin.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Heme-binding protein 1
- Annexin A1
- fMet-Leu-Phe receptor
- N-formyl peptide receptor 2
- Cathelicidin antimicrobial peptide
Sequence:
METNFSIPLNETEEVLPEPAGHTVLWIFSLLVHGVTFVFGVLGNGLVIWVAGFRMTRTVNTICYLNLALADFSFSAILPFRMVSVAMREKWPFGSFLCKLVHVMIDINLFVSVYLITIIALDRCICVLHPAWAQNHRTMSLAKRVMTGLWIFTIVLTLPNFIFWTTISTTNGDTYCIFNFAFWGDTAVERLNVFITMAKVFLILHFIIGFSVPMSIITVCYGIIAAKIHRNHMIKSSRPLRVFAAVVASFFICWFPYELIGILMAVWLKEMLLNGKYKIILVLINPTSSLAFFNSCLNPILYVFMGRNFQERLIRSLPTSLERALTEVPDSAQTSNTDTTSASPPEETELQAM
Protein: Chloride anion exchanger (Down-regulated in adenoma) (Protein DRA) (Solute carrier family 26 member 3) (Q9WVC8)
Organism: Mus musculus (Mouse)
Function: Mediates chloride-bicarbonate exchange with a chloride bicarbonate stoichiometry of 2:1 in the intestinal epithelia. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P40879}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:21976599}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P40879}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in sperm membranes. Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of sperm tail. {ECO:0000269|PubMed:21976599}.
Interaction partners:
- Na
- Cystic fibrosis transmembrane conductance regulator
- Sodium/hydrogen exchanger 3
- Na
- Na
- Sodium/hydrogen exchanger 2
- Myelin basic protein
- Carbonic anhydrase 2
Sequence:
MIEAIGNQYVVARPVYSTKTFGEEFKKTHRHHKTFLDHLKGCCSCSSQKAKKIALSLFPIASWLPAYKIKEWLLSDIVSGISTGLVAVLQGLAFALLVNIPPAYGLYAAFFPVITYFFLGTSRHISVGPFPVLSMMVGVVVTRVVSDPNASSELSSSSTENDSFIEEKVMVAASVTVLSGIIQLLLGVLQVGFVVIYLSESLISGFTTAAAIHVLVSQLKFMLQLPVPAYSDPFSIFKVLESVFTQIQKTNIADLVTSVIILVVVFVFKEINQRYRSKLPVPIPIELIMTVIATGVSYGCNFEDRFGVAVVGNMSLGFQPPITPSVEVFQDTIGDSFGIAIVGFAVAFSVASVYSLKYDYPIDGNQELIALGVSNIFTGAFKGFAGSTALSRSGVQESTGGKTQVAGLLSAVIVLIVIVAIGFLLQPLQKSVLAALALGNLKGMLMQFAEIGRLWKKDKYDCLIWIMTFIFAIVLGLGLGLAASVAFQLLTIVFRTQFPKCSTLANVGRSNIYKNKKNYAEVYEPEGVKIFRCPSPIYFANIGFFKQKLIDAVGFSPLRILRKRNKALKKIRKLQKRGLIQMTPKGFICTSDGFKDSDEELDNNQIEELDQPINTTDLPFDIDWNGDLPLNITIPKISLHSLILDFSAVSFLDVSSMRGLRTILQEFIRIKVDVYIVGTDDDFIDKLARCEFFDDEVTDSIFFLTIHDAILHILMKKDYSTSKFNSSQEKERKFDFTINTNGGLRNRECQVPVETKF
Protein: Chemotaxis protein CheV (P37599)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Chemotaxis involves both a phosphorylation-dependent excitation and a methylation-dependent adaptation. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis. Moreover, CheA-dependent phosphorylation of CheV is required for adaptation to attractants during B.subtilis chemotaxis.
Interaction partners:
- Chemotaxis protein CheA
- Flagellar motor switch phosphatase FliY
- Methyl-accepting chemotaxis protein McpC
- Methyl-accepting chemotaxis protein McpB
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Chemotaxis protein CheW
- Methyl-accepting chemotaxis protein McpA
- Methyl-accepting chemotaxis protein TlpC
- Methyl-accepting chemotaxis protein TlpB
- Chemotaxis protein methyltransferase
Sequence:
MSLQQYEILLDSGTNELEIVKFGVGENAFGINVMKVREIIQPVEVTSVPHSHQHVEGMIKLRGEILPVISLFSFFGVEPEGSKDEKYIVTEFNKRKIVFHVGSVSQIHRVSWEAIEKPTSLNQGMERHLTGIIKLEDLMIFLPDYEKIIYDIESDSGVDTYNMHTEGFDERRTDKKLIIVEDSPLLMRLLQDELKEAGYNNIASFENGKEAYEYIMNLAENETDLSKQIDMIITDIEMPKMDGHRLTKLLKENPKSSDVPVMIFSSLITDDLRHRGEVVGADEQISKPEISDLIKKVDTYVIE
Protein: AT19802p (Q8T971)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKITALLVLANLGFVLSESLAEMDRLATWRLHNISNKYKYLSTGNPEFYQWIERVNTVADEFNHYNKHRQRLEDQITERLITIRSIIAIRNASKRCLRFYLNQEAELESAYKSSNERKQQVLYQNSVRCPHGLDDGRLGDPYFVDYL
Protein: L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit monoheme) (Protein SoxA) (SoxAX cytochrome complex subunit A) (Sulfur oxidizing protein A) (Thiosulfate-oxidizing multienzyme system protein SoxA) (TOMES protein SoxA) (Q8KDM7)
Organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c and which then may be used for reductive CO(2) fixation.
Subcellular location: Periplasm {ECO:0000269|PubMed:18641134}.
Interaction partners:
- Sulfur oxidation protein SoxX
- Sulfur oxidation protein SoxB
- Sulfur oxidation protein SoxZ
- Sulfur oxidation protein SoxY
- DoxX family protein
- Sulfate adenylyltransferase
- SoxXA-binding protein SoxK
- Sulfide dehydrogenase, flavoprotein subunit
- Cytochrome subunit of sulfide dehydrogenase
Sequence:
MKKTIQRGLFTGALVLMTAMTAKPANAEVNYQALVDADVKAFQGFFRKEFPDVKLEDFGNGVYALDEDARKQWKEMEEFPPYELDVEAGKALFNKPFANGKSLASCFPNGGAVRGMYPYFDEKRKEVVTLEMAINECRVANGEKPYAWEKGDIARVSAYIASISRGQKVDVKVKSKAAYDAYMKGKKFFYAKRGQLNMSCSGCHMEYAGRHLRAEIISPALGHTTHFPVFRSKWGEIGTLHRRYAGCSNNIGAKPFAPQSEEYRDLEFFQTVMSNGLKYNGPASRK
Protein: Metal response element-binding transcription Factor-1, isoform F (X2JCQ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNDQEKQHQQQQQHYFHSEWKTTANSHGNSLSDSRDYDTNSSRNSLSGSPPVTSNCSSSGSLDFDRPLAQLLEPKLEADGLGIIHGDNYSIYGSQTAESTSGEQQVLNLGLTLDTGDAQATYGDLFGAQDQLTASQTHGHSQVVVSAAADNAFSLADQLTPLPITVIPITYHHTTENLSSSHSEVPLIASLSDITAQVFNLDDICFTLEYQFENQRLVQVQPPTVVSLSMVSSPNEAANPPINCDNDQGTGNSISRDSTSNSPAYFTIETSYVDEYDPNEPDEDEQLAHCIQPGVLHQDVDEEEVERQDENDQLMALAYESSDEALSRYRCNYENCYRSYSTIGNLRTHLKTHTGDYSFKCPEDGCHKAFLTSYSLKIHVRVHTKVKPYECEVSGCDKAFNTRYRLHAHLRLHNGETFNCELCQKCFTTLSDLKKHMRTHTQERPYKCPEDDCGKAFTASHHLKTHRRTHTGEKPYPCQEDSCQKSFSTSHSLKSHKKTHQRQLQNKGRKKRPLKTQQTKCSDQEQKDPQQEEQEEEEFIKEDQPEMTLLNPGSHCSETTSTDSGVVLQTLTPQDHLSNVFILQGNEPLILPETSQAYQLSYAAEEEIPSPWIDAGVLVSKPIIPMAPLTDACVALPTEMPSFVNLKPTFGNAVSGNMGDPQPETMDVDPTVETSLPTPTLELNQPNIEELLKQDSFENEEDMETESLLNDILMTIDNNSALLQATLQQASQVPSDASGLVELDIRDNKPTLKQITADAGICNCTNCKCDQTKSCHGGDCGAAAAQQTTRTGAPTTTTTTTTMNSSGGKRICGSVVPTKKLV
Protein: Deoxycytidine kinase (GgdCK) (EC 2.7.1.74) (Deoxyadenosine kinase) (EC 2.7.1.76) (Deoxyguanosine kinase) (EC 2.7.1.113) (Q5ZMF3)
Organism: Gallus gallus (Chicken)
Function: Phosphorylates the deoxyribonucleosides deoxycytidine, deoxyguanosine and deoxyadenosine. Displays highest activity against deoxycytidine followed by deoxyadenosine and then deoxyguanosine. Shows only very minor activity against deoxyuridine and deoxythymidine.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27707}.
Interaction partners:
Sequence:
MATPPKRGRLEGRVKKIAVEGNIAAGKSTFVNILKQADEGWEVVPEPVARWCNVQQNSEEDCEELTTSQKSGGNVLQMMYEKPERWSFTFQMYACLSRIRAQLKSIDGKLREAENPVVFFERSVYSDRYIFAANLYESDCMNETEWTIYQDWHDWMNKQFGQSLALDGIIYLRATPEKCLNRIYLRGRDEEQEIPIEYLEKLHYKHESWLQHKTLRTDFEYLQEIPILTLDVNEDFKGKKDRYDHMTEKVKEFLSTL