wanglab/gogpt-training-data huggingface dataset:
Protein: Pyruvate, phosphate dikinase (EC 2.7.9.1) (O76283)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MVAKKWVYYFGGGNADGNKNMKELLGGKGANLAEMVNLGIPVPPGFTITTEACKTYQETETIPQEVADQVRENVSRVEKEMGAKFGDPANPLLFSVRSGAAASMPGMMDTVLNLGLNKVTVDAWVRRAPRLERFVYDSYRRFITMYADIVMQVGREDFEEALSRMKERRGTKFDTDLTASDLKELCDGYLELFELKTGCSFPQDPVMQLFAAIKAVFRSWGNPRATIYRRMNNITGLLGTAVNVQAMVFGNINDRSATGVAFSRSPSTGENFFFGEYLVNAQGEDVVAGIRTPQQINHSLSLRWAKAHGVGEEERRKRYPSMEEAMPENYRLLCDVRKRLENHYRDMQDLEFTVQDGRLWLLQCRNGKRTIHAAVRIAIDMVNEGLISREEAVLRIDPYQVDHLMHPNLEPGAEKANKPIGRGLAASPGAAVGQVVFDAESAKEWSGRGKKVIMVRLETSPEDLAGMDAACGILTARGGMTSHAAVVARGMGKCCVSGCGDMVIRGKSFKLNGSVFREGDYITIDGSKGLIYAGKLKLRSPDLKGSFQTILQWCQEMKRLGVRTNADTPADAAKARSFGAEGVGLCRTEHMFFEGSRINFIREMILADSASGRKAALDKLLPIQRADFVGILRAMRGLPVTIRLLDPPLHEFVPHDAAAQFELAQKLGMPAEKVRNRVNALHELNPMLGHRGCRLGITYPEIYNMQVRAIIEAAIAVSEEGSSVIPEIMVPLVGKKEELSLIREEVVKTAEAVITKSGKRVHYTVGTMIEVPRAAVTADSIAQKADFFSFGTNDLTQMGCGFSRDDAGPFLRHYGNLGIYAQDPFQSIDQEGIGELVRIAVTKGRRVKPMLKMGICGEHGGDPATIGFCHKVGLDYVSCSPFRVPVAIVAAAHASIKDRRAAMKARKGFAAKL
Protein: Ceramide kinase-like isoform 7 (G0XYF5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFRGRRRSRVGALEEAPPENPKAAAEPERVLLRGIFEIRRESCDVALGERALRWRRIQPELPAGGTRHDLLSKEESLELEDIFSVKLKRRCWAKHPGRDTLLGITLFICLKEQRNKLKDSTLDLINFSEDHCDIWFRQFKKILDGFTSRPKALKILLNPQSHRKESVHVYYEKVEPLLKLAGIETDVTITEYEGHALSLLDECELRGFDGIY
Protein: Selenoprotein F (Q8GWP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MKQREMAKMVVLSAMMILILASTISAKEQLSTKECEDLGFSGLALCSDCHSLSEYVKDQELVSDCLKCCADDSEDSMSKVTYSGAILEVCMRKLVFYPEIVGFIEEEKEKFPSVKVQYIFNSPPKLIMLDEDGEHKESIRIDNWKREHLLQYMREKVKPTAAS
Protein: Aspartic proteinase sxa1 (EC 3.4.23.-) (P32834)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in degradation or processing of the mating pheromones. Its loss may cause a persistent response to the pheromones. It may cleave the mating pheromone M-factor. May be involved in processing of zymogens that are required for zygote formation.
Interaction partners:
- Carboxypeptidase sxa2
Sequence:
MKASFFVFAISALQALQASVASAYSEVPGKRSVVLNLQHSQYDHVARKLERTKVLNKRDSSGYPVLDLEYTDAGGYFANLTLGSNERVYSLTLDTGSPYTWVTAKNITALSASEIWSDTDGVDAGRSTSDIRTNACTNYTCFDYSSTTARRTNSSTIGFLASYGDNTTVLGYNMVDNAYFAGLTLPGFEFGLATREYDSSQISVTPGIIGLSVAMTITGISSDDKVVAFTPPTIVDQLVSANVIDTPAFGIYLNEDVGELIFGGYDKAKINGSVHWVNISSSDDSTFYSVNLESITVTNSTSSNNVQSSKRSSKDIEVNTTVTLDTGTVYIYLPEDTVESIADQYQGIVSEYGYVVIYCDSFSDSDYISFNFGSDADFHVSVNDLVIYRQESTSGDICYLALFEGDTSSYLLGQYFLQYVYSIYDWDAQKIGLAALNSNATSTANHQILNINSALRSVTSGQSVSATPTVSMSIAATSFGSSLVLTASASPSSTSVDGSSSSDSSEASGAASVGVSISAIVLCASTLISLLFA
Protein: Toucan, isoform B (Q9VQL8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGLNEFVSLLYGSSQSLNAHKDASTSTYPLPSVADWKEFQQMLKNHKNVQVKRYGFQDYHHSQDFKYGKIYSGIGSAAEAAGNGGGGGVGGGVTKRNASNGAGQNKLLNNNSSTHNNNMAKTSRIPTTTSKSMTSSASSSGSSELDILRSYTKNTIKSSLTSSTPSSSFLWNSFRMPRKQKSSLAEKKQSGESLRSGVDQTELQELNNGQSATGCPTPPMARDSKRTSIGNELPCETEAKLKRCEDQQDPQASTTASPLPMINPQEQEASGQVKEATITTANEPNALSLPDEISNSVSSTTMLATPRVDIAAQYPVLKPFTENGELDCARLAKFFQDTQFERKEEQRQILGLSVMVQFMSKELDAVACKENKHQCARTKGTLEKTILLLQHTQKDCERLREDLEDKGLEWIQRQQEKEYLHRTELKQAEEKLMEVQLRAKLKFCELESQLRAKDEESKQAQEAYRMEVSHKLALKQEHLRTAEQKIQELQTRLQQVETEEQGHREELIRKENIHTARLAEANQREQDLIDRVKSLTKELNTLKANKEHNERDLRDRLALSQDEISVLRTSSQRRSPCTSLPDNASAELNRLTSEADSLRCVLELKQAEISALSKAKADLIHESEERLKLSNRVALLEAQNEMLRTELEAKTEKEKEIQQKMEELQKAYKYESIKRTRLTYDKEELQYHLKQRSLQLQSAESKLQDLSTGSHDNSLSSHSRCSLGRSGLEIAVTTSSPTSPVMKGMIERNDSVSWTLEIEDESFKGNTSKIVRRAGSLRSNNERCPIQRRQTLTSNGHSNGSATNGGSSPAHPNPLSQSMSATALLRSSSNSGESEGRPLSRARSKSMCIKASATSSAVCESSGQRKKPQDELSLADWPEDIPLCSSSPQAPGIEMRPRSSTMKLMSSEAKKFQEIQESAGEAMVSGANSEDESCSASSEDIMRSSSASSTASGGSLSKRPKQPPSRMSIEEALPCTPMEVSWSEDAADANGLA
Protein: Down syndrome cell adhesion molecule 1, isoform D (A1Z6X1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQFYITEAENEYVIKGNAAVVKCKIPSFVADFVQVEAWVDEEGMELWRNNATDAYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVSSSPPKINALTYKPNIVESMASTAILCPAQGYPAPSFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPQVLPFSFGESAADVGDIASANCVVPKGDLPLEIRWSLNSAPIVNGENGFTLVRLNKRTSLLNIDSLNAFHRGVYKCIATNPAGTSEYVAELQVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Protein kinase C-like 2 (EC 2.7.11.13) (P36583)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the control of the cell shape. Target of the inhibitor staurosporine.
Interaction partners:
- GTP-binding protein rho1
- GTP-binding protein rho2
- Protein kinase C-like 1
- Cell wall integrity and stress response component 1
- Serine/threonine-protein kinase ksg1
- Cell division control protein 42 homolog
- Actin
- MAP kinase kinase kinase mkh1
- Small ribosomal subunit protein RACK1
- Rho1 guanine nucleotide exchange factor 1
Sequence:
MDMIDEAITEVVRKIERERSVIHGALSMKRLTQNQTVHQQLHSNIEESKKSIIYLEERLEKLKLRKNGVRKSNSEKPSVGIEKNPSFSTTKSAKSFSSTSSNIDSNLDLLNYDTPLTISKISFLLQQLEFKLSVEEQYRKGIEKMAKLYEREHDRRSIAEAEKKYVESAQKITLLKQALKRYHDLHIEIDEEDVPSTESRGNLNARRPQSGLLKITVGSLRNVTHSAGISKQTEMIVAIRAEDLERARTRPSRTDRFNETFEIDLEKTNEVEIVVYEKKNEKLLLPVGLLWIRLSDLVEKQRRKKVEQEVSDKGWVSADKMINQRLSIFLPSALNNISKPESTDRPNTASGNQSVSAWFSLEPMGQINLTMNFTKHNTRKRPMDAGLGRQGAIRQRKESVHEVYGHKFLQHQFYQIMRCALCGEFLKNAAGMQCIDCHYTCHKKCYPKVVTKCISKSSDSASSEYEKINHRIPHHFESHTNIGANWCCHCGYILPLGRKTARKCTECGITAHAQCVHLVPDFCGMSMEMANRVISEIRTTKIYKAQQHKQKSSHHKHHHHKKSKSSSSKHKENDKASVSITTTTTPSITPADPVPTSPKPLAIEPVKRKPVHAGNLEVTSVSDNKLGATVQVVEQKVDDKADALTKPPSLDAVKEPIPVPSVETSVVAQDLTHKAKRIGLEDFTFLSVLGKGNFGKVMLAELKSEKQLYAIKVLKKEFILENDEVESTKSEKRVFLVANRERHPFLVNLHSCFQTETRIYFVMDFVSGGDLMLHIQQEQFSRRRAQFYAAEVCLALKYFHDNGIIYRDLKLDNILLSPDGHVKVADYGLCKEDMWHDNTTATFCGTPEFMAPEILLEQQYTRSVDWWAFGVLIYQMLLGQSPFRGEDEEEIFDAILSDEPLYPIHMPRDSVSILQQLLTRDPKKRLGSGPNDAEDVMTHPFFSNINWDDIYHKRTQPPYIPSLNSPTDTKYFDEEFTRELPVLTPVNSILTKEMQQHFEGFSYSCEDDKPSTTDNA
Protein: N-acetyltransferase 8 (EC 2.3.1.-) (Acetyltransferase 2) (ATase2) (Camello-like protein 4) (Cysteinyl-conjugate N-acetyltransferase) (CCNAT) (EC 2.3.1.80) (Q9JIY7)
Organism: Mus musculus (Mouse)
Function: Acetylates the free alpha-amino group of cysteine S-conjugates to form mercapturic acids. This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S-conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6-acetylation of various proteins. Thereby, may regulate apoptosis through the acetylation and the regulation of the expression of PROM1. May also regulate amyloid beta-peptide secretion through acetylation of BACE1 and the regulation of its expression in neurons (By similarity).
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Cytosol aminopeptidase
- Aminopeptidase N
- Probable N-acetyltransferase family 8 member 5
Sequence:
MASFRIRQFQERDYKQVVDVFSRGMEEHIPTAFRHLLTLPRTLLLLAVVPLAIVLVSGSWFLAVVCIFFLFLFLWFLASKPWKNYVSKCLHTDMADITKSYLSVRGSGFWVAESGGQVVGTVAARPVKDPPLGRKQLQLFRLSVSSQHRGQGIAKALTRTVLQFARDQGYSDVVLVTGLLQQGAVTLYYSMGFQKTGESFVDILTWLVDVSLIHFIYPLPSAQKYEL
Protein: Protein orai-2 (CAP-binding protein complex-interacting protein 2) (Transmembrane protein 142B) (Q96SN7)
Organism: Homo sapiens (Human)
Function: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, STIM1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17452328}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with STIM1 upon store depletion. {ECO:0000269|PubMed:19706554}.
Interaction partners:
- Stromal interaction molecule 1
- Stromal interaction molecule 2
- Protein orai-3
- Calcium release-activated calcium channel protein 1
- Short transient receptor potential channel 6
- Short transient receptor potential channel 1
- Short transient receptor potential channel 3
- Short transient receptor potential channel 4
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MSAELNVPIDPSAPACPEPGHKGMDYRDWVRRSYLELVTSNHHSVQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLETQYQYPRPLLIAFSACTTVLVAVHLFALLISTCILPNVEAVSNIHNLNSISESPHERMHPYIELAWGFSTVLGILLFLAEVVLLCWIKFLPVDARRQPGPPPGPGSHTGWQAALVSTIIMVPVGLIFVVFTIHFYRSLVRHKTERHNREIEELHKLKVQLDGHERSLQVL
Protein: Lipase/esterase, putative (Q4WB49)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
Sequence:
MASPILRSPITSDLANVTPDLVDVSTPEKLKSYRESLEPIFTLENIIRGKENIISYEELDIPGPAGPMRATIFRPKHQTHPIDEIPGILHIHGGGLATGNRFLGFTMLDWVESLGAVCLTAEYRLAPEHHQPAQLEDSYAALQWMSDHAAELGFNPRKLVVCGSSAGGNLTAGVTLLARDRSGPQIRGQVLIYPWVDDGMDYVSMRQYADIAPVRDVDAAVLANYAFGERREHADMYTVPMRATNFAGLPPTFIDVGEADVFRDQDIAYASALWKDGVSTELHLWPGSWHGFDVFVPDAPISRRARAARLEWLRKLLSVPDGI
Protein: GM09415p (Q95S44)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDEDILNAVESLFGKDVKIVDCETSSSLQQEEVLLVNGVPVKLDGLPADDASAIKAALLEGQMPSVEHLNQLLFRAGLAQQPIEVETSLTVKSSLTTTEEVLVSRNGQILDERTVETKENFNHQSHQKEIWHPVKQQSALARATPENALKYRTTSNSMFASQATDSDERPVDPLGRQLNQTFSNASLMSSSSAITGSDQVIGSVSSTTIGDKSSNISSCDSGHDGLFHSVSMSAPWSHPRDTLTDSLYCDIPSSADESDAVSILNTHLKITEPFDCQTAPVYAKDIPKKGNLDSVVNLLINNNTKDLRFAFLTTSRLFSPPHQLLSKIIAKIDNEEENVLRLLNEWLDTCPGDFSHELLLQELENKRNVKGLAAFLDGIPQALAQKDENGRSQLNNLLTKQSSASSLGRQSSIKSLKRFAANVYKTDNVLNNCSSAFELAHQLYAIEYAYLSQIRLEEFVEILEKDELKTCISQTKAGTLGSNCISQVTIDSYVQWFNQLSYLTATEILKLGKKSQRAQMIDFWVETALECFNTGNFNSLMAILTALNLTAIARLKKTWAKVQTTKFEGLEHQMDPSSNFLNYRSTMKAAVWRSEREMANEIERAIIPFFSLFLKDLHAINESHETKLANGYINFEKCLHLGTQLRNFGKWQRLDCPYEQLPSVVSYLLKAEVLSEDLLMKASYESEPPETGEEKDHYKTLKAARKSNT
Protein: Peroxisomal bifunctional enzyme (PBE) (PBFE) (Multifunctional enzyme 1) (MFE1) (Multifunctional protein 1) (MFP1) [Includes: Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC 4.2.1.17) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] (P07896)
Organism: Rattus norvegicus (Rat)
Function: Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway. Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (Probable). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species. Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:11781327}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- 3-ketoacyl-CoA thiolase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAEYLRLPHSLAMIRLCNPPVNAVSPTVIREVRNGLQKAGSDHTVKAIVICGANGNFCAGADIHGFSAFTPGLALGSLVDEIQRYQKPVLAAIQGVALGGGLELALGCHYRIANAKARVGLPEVTLGILPGARGTQLLPRVVGVPVALDLITSGKYLSADEALRLGILDAVVKSDPVEEAIKFAQKIIDKPIEPRRIFNKPVPSLPNMDSVFAEAIAKVRKQYPGVLAPETCVRSIQASVKHPYEVGIKEEEKLFMYLRASGQAKALQYAFFAEKSANKWSTPSGASWKTASAQPVSSVGVLGLGTMGRGIAISFARVGISVVAVESDPKQLDAAKKIITFTLEKEASRAHQNGQASAKPKLRFSSSTKELSTVDLVVEAVFEDMNLKKKVFAELSALCKPGAFLCTNTSALNVDDIASSTDRPQLVIGTHFFSPAHVMRLLEVIPSRYSSPTTIATVMSLSKKIGKIGVVVGNCYGFVGNRMLAPYYNQGFFLLEEGSKPEDVDGVLEEFGFKMGPFRVSDLAGLDVGWKIRKGQGLTGPSLPPGTPVRKRGNSRYSPLGDMLCEAGRFGQKTGKGWYQYDKPLGRIHKPDPWLSTFLSQYREVHHIEQRTISKEEILERCLYSLINEAFRILEEGMAARPEHIDVIYLHGYGWPRHKGGPMFYAASVGLPTVLEKLQKYYRQNPDIPQLEPSDYLRRLVAQGSPPLKEWQSLAGPHGSKL
Protein: DOT1 like histone lysine methyltransferase (F6SJX8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
SGSPLNLNSMVSNINQPLEITAISSPESSLKSSPTPYQDHDQPPVLRKERPLGLTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLVGRKSAPSSEPINSSKWKSTFSPISDLGLAKAVDSPLQAGSALSHSPLFSFRPSLEEPAAEAKLPTHPRKSFAGSLGAAEGPSPGTNPPNGLAFSGGLAADLGLHSFNDGASLSHKGPDVTGLSASLSFPSQRGKDSTTEANPFLSRRQPEGLGGLKGEGNANKESGESLPLCGPSDKASLPHGSRASKGRDRELDFKGGHNLFISAAAVPPGGLLGGPGLVTVASSAGSATPTAQAPRPFLSTFAPGPQFTLGPMSLQANLGSVAGSSVLQSLFSTVPAAAGLVHVSSTATRLTNSHTMGSFSSGVAGGTVGEDHGALN
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FNC9)
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 K complete sequence
- Serine/threonine-protein kinase
- Candida glabrata strain CBS138 chromosome L complete sequence
- Serine/threonine-protein kinase RAD53
Sequence:
MSRSIANIQYLEAKNLAHWMKSADAPLFQVIDVRGSDYVGGHIKGCWNYPYRRLKVDDGYMEEMYKALNKKLEDTGSDRSLNAIFHCAQSQQRGPAAAMKLLRFLPDDKLSNFKIWVLRGGFNHWQDQYGEDQELTEDYEPDIWSW
Protein: TBC1 domain family member 3F (A6NER0)
Organism: Homo sapiens (Human)
Function: Acts as a GTPase activating protein for RAB5. Does not act on RAB4 or RAB11 (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associated with lipid rafts. {ECO:0000250}.
Interaction partners:
Sequence:
MDVVEVAGSWWAQEREDIIMKYEKGHRAGLPEDKGPKPFRSYNNNVDHLGIVHETELPPLTAREAKQIRREISRKSKWVDMLGDWEKYKSSRKLIDRAYKGMPMNIRGPMWSVLLNIEEMKLKNPGRYQIMKEKGKRSSEHIQRIDRDVSGTLRKHIFFRDRYGTKQRELLHILLAYEEYNPEVGYCRDLSHIAALFLLYLPEEDAFWALVQLLASERHSLQGFHSPNGGTVQGLQDQQEHVVATSQPKTMGHQDKKDLCGQCSPLGCLIRILIDGISLGLTLRLWDVYLVEGEQALMPITRIAFKVQQKRLTKTSRCGPWARFCNRFVDTWARDEDTVLKHLRASMKKLTRKKGDVPPPAKPEQGSSASRPVPASRGGKTLCKGDRQAPPGPPARFPRPIWSASPPRAPRSSTPCPGGAVREDTYPVGTQGVPSPALAQGGPQGSWRFLQWNSMPRLPTDLDVEGPWFRHYDFRQSCWVRAISQEDQLAPCWQAEHPAERVRSAFAAPSTDSDQGTPFRARDEQQCAPTSGPCLCGLHLESSQFPPGF
Protein: Renin (EC 3.4.23.15) (Angiotensinogenase) (P00797)
Organism: Homo sapiens (Human)
Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Subcellular location: Secreted {ECO:0000269|PubMed:12045255}. Membrane {ECO:0000269|PubMed:12045255}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000269|PubMed:12045255}.
Interaction partners:
- Angiotensinogen
- Renin receptor
- Angiotensin-converting enzyme
- Type-1 angiotensin II receptor
- Angiotensin-converting enzyme 2
- Kininogen-1
- Mineralocorticoid receptor
- Natriuretic peptides A
- Type-2 angiotensin II receptor
- Pro-opiomelanocortin
Sequence:
MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
Protein: Collagen alpha-3(IV) chain [Cleaved into: Tumstatin] (Q9QZS0)
Organism: Mus musculus (Mouse)
Function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736, ECO:0000269|PubMed:7962065}. Note=Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL). {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:7962065}.
Interaction partners:
- Collagen alpha-4
- Collagen, type IV, alpha 6
- Col4a5 protein
- Collagen alpha-2
- CD44 antigen
- Collagen alpha-1
- Platelet glycoprotein VI
- Integrin alpha-1
- Integrin alpha-3
- Integrin alpha-V
Sequence:
MHSKTAPRFLVFLLLTLLLLLAASPVASKGCVCKGKGQCLCAGTKGEKGEKGVPGSPGFPGQKGFPGPEGLPGPQGPKGSPGLPGLTGPKGIRGITGLPGFAGPPGLPGLPGHPGPRGLAGLPGCNGSKGEQGFPGFPGTPGYAGLPGPDGLKGQKGEPAQGEDRGFNGKGDPGPPGVPGFQGFPGLPGFPGPAGPPGPPGFFGLPGAMGPRGPKGHMGDSVIGQKGERGMKGLTGPPGPPGTVIFTLTQPYNKSDFKGEKGDEGERGEPGPPGPSGPPGDSYGSEKGAPGEPGPRGKPGKDGAPGFPGTEGAKGNRGFPGLRGEAGIKGRKGDIGPPGFPGPTEYYDAYLEKGERGMPGLPGPKGARGPQGPSGPPGVPGSPGLSRPGLRGPIGWPGLKGSKGERGPPGKDTVGPPGPLGCPGSPGPPGPPGPPGCPGDIVFKCSPGEHGMPGDTGPPGVPGLDGPKGEPGSPCTECHCFPGPPGVPGFPGLDGIKGIPGGRGVPGLKGNPGSPGSAGLPGFAGFPGDQGHPGLKGDKGDTPLPWGQVGNPGDPGLRGLPGRKGFDGTPGGPGAKGPPGPQGEPALSGRKGDQGPPGPPGFPGPPGPAGPAGPPGYGPQGEPGPKGAQGVPGVLGPPGEAGLKGEPSTSTPDLGPPGPPGPPGQAGPRGLPGLPGPVGKCDPGLPGPDGEPGIPEAGCPGPPGPKGNQGFPGTKGSPGCPGEMGKPGRPGEPGIPGAKGEPSVGRPGKPGKPGFPGERGNAGENGDIGLPGLPGLPGTPGRGGLDGPPGDPGQPGSPGAKGSPGRCIPGPRGTQGLPGLNGLKGQPGRRGDTGPKGDPGIPGMDRSGVPGDPGPPGTPGCPGEMGPPGQKGYPGAPGFPGPPGEKGEVGMMGYPGTTGPPGLPGKPGSQGQRGSLGIPGMKGEKGRPGAKGERGEKGKPGPSQTTLLKGDKGEPGLKGFVGNPGEKGNRGNPGLPGPKGLEGLPGLPGPPGPRGDTGSRGNPGRPGPHGMPGSMGIMGVPGPKGRKGTSGLPGLAGRPGLTGIHGPQGDKGEPGYSEGARPGPPGPKGDPGLPGDKGKKGERGVPGPPGQSGPAGPDGAPGSPGSPGHPGKPGPAGDLGLKGQKGFPGPPGSTGPPGPPGLPGLPGPMGMRGDQGRDGIPGPPGEKGETGLLGAYPGPKGSPGVPGAKGDRGVPGLSGLPGRKGVMGDVGPQGPPGTAGLPGPPGLPGAIIPGPKGDRGLPGLRGNPGEPGPPGPPGPIGKGIKGDKGFMGPPGPKGLPGTVGDMGPPGFPGAPGTPGLPGVRGDPGFPGFPGIKGEKGNPGFLGPIGHPGPVGPKGPPGPRGKPGTLKVISLPGSPGPPGVPGQPGMKGDPGPLGLPGIPGPCGPRGKPGKDGKPGTPGPAGTKGNKGLKGQQGPPGLDGLPGLKGNPGDRGTPATGTRMRGFIFTRHSQTTAIPSCPEGTQPLYSGFSLLFVQGNKRAHGQDLGTLGSCLQRFTTMPFLFCNINNVCNFASRNDYSYWLSTPALMPMDMAPISGRALEPYISRCTVCEGPAMAIAVHSQTTAIPPCPQDWVSLWKGFSFIMFTSAGSEGAGQALASPGSCLEEFRASPFIECHGRGTCNYYSNSYSFWLASLNPERMFRKPIPSTVKAGDLEKIISRCQVCMKKRH
Protein: PCI domain-containing protein 2 (CSN12-like protein) (Q5JVF3)
Organism: Homo sapiens (Human)
Function: Required for B-cell survival through the regulation of the expression of cell-cycle checkpoint MAD2L1 protein during B cell differentiation (By similarity). As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. Binds and stabilizes BRCA2 and is thus involved in the control of R-loop-associated DNA damage and transcription-associated genomic instability. Blocks the activity of the SRCAP chromatin remodeling complex by interacting with SRCAP complex member ZNHIT1 and inhibiting its interaction with the complex (By similarity). This prevents the deposition of histone variant H2AZ1/H2A.Z at the nucleosomes of key lymphoid fate regulator genes which suppresses their expression and restricts lymphoid lineage commitment (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}.
Interaction partners:
- Germinal-center associated nuclear protein
- Centrin-2
- Transcription and mRNA export factor ENY2
- Putative protein SEM1, isoform 2
- Centrin-3
- Mitotic spindle assembly checkpoint protein MAD1
- Mitotic spindle assembly checkpoint protein MAD2A
- Leukocyte receptor cluster member 8
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MAHITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFAAHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKINKLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHRSSQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHEAFFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQCILANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
Protein: V-type proton ATPase subunit a (Q86P41)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
RFIVRKFVGCWSLWTNLYLIFKHLLNPDVNAFQRKFVNEVRRCDEMERKLRYLEKEIKKDGIPMLDTGESPEAPQPREMIDLEATFEKLENELREVNQNAEALKRNFLELTELKHILRKTQVFFDEMADNQNEDEQAQLLGEEGVRASQPGQNLKLGFVAGVILRERLPAFERMLWRACKGNVFLRQAMIETPLEDPTNGDQVHKSVFIIFFQGDQLKTRVKKICEGFRATLYPCPEAPADRREMAMGVMTRIEDLNTVLGQTQDHRHRVLVAAAKNLKNWFVKVRKIKAIYHTLNLFNLDVTQKCLIAECWVPLLDIETIQLALRRGTERSGSSVPPILNRMQTFENPPTYNRTNKFTKAFQALIDAYGVASYREMNPAPYTIITFPFLFAVMFGDLGHGAIMALFGLWMIRKEKGLAAQKTDNEIWNIFFGGRYIIFLMGVFSMYTGLIYNDIFSKSLNIFGSHWHLSYNKSTVMENKFLQLSPKGDYEGAPYPFGMDPIWQVAGANKIIFHNAYKMKISIIFGVIHMIFGVVMSWHNHTYFRNRISLLYEFIPQLVFLLLLFFYMVLLMFIKWIKFAATNDKPYSEACAPSILITFIDMVLFNTPKPPPENCETYMFMGQHFIQVLFVLVAVGCIPVMLLAKPLLIMQARKQANVQPIAGATSDAEAGGVSNSGSHGGGGGHEEEEELSEIFIHQSIHTIEYVLGSVSHTASYLRLWALSLAHAQLAEVLWTMVLSIGLKQEGPVGGIVLTCVFAFWAILTVGILVLMEGLSAFLHTLRLHWVEFQSKFYKGQGYAFQPFSFDAIIENGAAAAEE