wanglab/gogpt-training-data huggingface dataset:
Protein: UBX domain-containing protein 3 (H2L056)
Organism: Caenorhabditis elegans
Function: Ubiquitin-binding protein which acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity. Together with ubxn-1 and ubxn-2, plays a role in hermaphrodite spermatogenesis probably by promoting the degradation of sex determination terminal factor tra-1. During mitosis, ensures the degradation of DNA licensing factor cdt-1 and the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5.
Subcellular location: Nucleus {ECO:0000269|PubMed:26842564}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550}. Chromosome {ECO:0000269|PubMed:26842564}. Cytoplasm {ECO:0000269|PubMed:26842564}. Note=Colocalizes with cdc-48.1 to the perinuclear region in spermatocytes (PubMed:20977550). Localizes to the nucleus during S phase in a cdc-48 and npl-4-dependent manner (PubMed:26842564). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:26842564}.
Interaction partners:
- Ubiquitin fusion degradation protein 1 homolog
- Transitional endoplasmic reticulum ATPase homolog 1
- UBX domain-containing protein 2
- UBX domain-containing protein 1
- UBX domain-containing protein 6
- Nuclear protein localization protein 4 homolog 2
- Transitional endoplasmic reticulum ATPase homolog 2
- Ubiquitin-like protease 4
- Ubiquitin fusion degradation protein 3 homolog
- DNA replication licensing factor MCM7
Sequence:
MDLTASLEDDQREKLRQYTEFTHQQDYEVAIGTLASLNWNLEQAIEAHLMQEDKNDDEDPEILETIPAAASGRNAGASSSSRFEPEVINIEDDEMPATRGRRRGRAVTPDETTTVDNQVKRLRIDDGSSSSSNGAATHHRGAAIPRQKRGQATEPTPSSSGSSSASFSSRRGTRANPVPPPNQEPAHPESARQNGGILASRHNNHNNQQNNHHHHHQRIPINPRRVDVFNVDSDEDDDSMAIAYEDDDDGVHEVHHSEVVARGSGPPNGRIPMIPDGFSSVSDALRNFVAIFSDRFCSTPQTQAFMPPFYTEPLPAAVKEAFDHPNSEHRRPLLFYINHDRSIAANIFASQVLCSETVSTLIRHQYVLFPWDITSDSNLMLFLEYLQAANMGDVRTIIQRLAMSKIESFPLMAIVVKERNSYRLVDYCRGTDTSDQVMEKLLSGVSEYSDIRMNEQSERREREEREAIRNQQEAEYKASLAADKARMEAKQQEIEEQRLEEERKLREEEEECVRRQTVASTVPEEPPASAPLAEIINVKFRLPEGGQDMRRFRRLESIQTLINYLSSKGYSPDKFKYFNSDFPKKEITRHFDLSHNFADTKWPAREQIFVEEI
Protein: AT5g02160 (Transmembrane protein) (Q9FPH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- ATP-dependent zinc metalloprotease FTSH 5, chloroplastic
- At4g35750
- Plastocyanin major isoform, chloroplastic
- Thioredoxin H9
- Chaperonin CPN60-like 1, mitochondrial
Sequence:
MTIAPALQTTFVSSTNFLKHSSSWGSPSPNNVILPKNKRSSSSVVVAAVGDVSSDGTIYLIGGAIAVALVGTAFPILFKRKDTCPECDGAGFVRKGGVTLRANAARKDLPQIVCANCNGLGKLNQIDKS
Protein: SH2 domain-containing protein 1B (EWS/FLI1-activated transcript 2) (EAT-2) (O14796)
Organism: Homo sapiens (Human)
Function: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244. In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4 without effecting its tyrosine phosphorylation; downstream signaling involves PLCG1 and ERK activation. Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling (By similarity). In the context of NK cell-mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule-organizing center and cytotoxic granules toward the NK cell synapse. Negatively regulates CD40-induced cytokine production in dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation (By similarity).
Interaction partners:
- Natural killer cell receptor 2B4
- SLAM family member 5
- SLAM family member 6
- T-lymphocyte surface antigen Ly-9
- Signaling lymphocytic activation molecule
- SLAM family member 7
- Eukaryotic initiation factor 4A-I
- Tyrosine-protein phosphatase non-receptor type 11
- T-cell surface antigen CD2
Sequence:
MDLPYYHGRLTKQDCETLLLKEGVDGNFLLRDSESIPGVLCLCVSFKNIVYTYRIFREKHGYYRIQTAEGSPKQVFPSLKELISKFEKPNQGMVVHLLKPIKRTSPSLRWRGLKLELETFVNSNSDYVDVLP
Protein: alpha-glucosidase (EC 3.2.1.20) (G5EB03)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Alpha-glucosidase
- Glucoamylase
- Glucoamylase
- Alpha/beta-glucosidase agdC
- Probable alpha/beta-glucosidase agdC
- Phosphotransferase
- Phosphotransferase
- Hexokinase
- Alpha/beta-glucosidase agdC
- Glycosyl hydrolases family 32 superfamily
Sequence:
MVRFLHLAGTLPVLASGAVQDALRPVAESAATVTATATVAGQQAQFTLSDYVDVGADLIANVDDPEAVNAQSVCPGYKASDIQQTDLGFTASLRLAGEPCNVYGTDVESLTLEMQYQDTDRLNIQITPTYVDASNASWYILPEEFVPRPKPAAGASESHSDFAVTWSNEPTFNFQVTRKSTGEVLFDTAGSVLVFENQFIEFVTSLPEEYNLYGLGERINQLRLLRNATLTSYAADIGNPIDANIYGQHAFYVDTRYFSVDEAGKHTYVKSSEADPSATYTSYSHGVFLRNSHGHEVVLNPQGLTWRTIGGSIDLTLYSGPTVAEVTKQYQRSTVGLPAMQKYDTLGFHQCRWGYNNWSVFADVLANFEKFEIPLEYLWADIDYMHGYRNFENDEYRFPYNETKVFLDKLHAGGRHFVPIVDAALYIPNPQNASDSYETYTRGAARDVFLKNPDGSLYIGAVWPGYTVFPDWHHPDAADFWANELVTWYEKVKFDGVWYDMSEVSSFCVGSCGSRNRTLNPVHPPFRLPGEPGNVDYEYPEGFELSNATEAASASAASSSQAATTATETTTSTSSYLRTSPTPGVRNVNYPPYVINHVQTGHDLAVHAVSPNATHVDGYHEYDVHSLYGHMGIQATYRGLTQIAPRKRPFIIGRSTFAGSGKWAGHWGGDNYSRWSSMYFSISQALQFSLYGIPMFGVDTCGFSGNTAEELCNRWMQLSAFFPFYRNHNVLGTIPQEPYQWASVIDATKKAMRIRYALLPYFYTLMHDAHTTGSTVLRALAWEFPDDPSLAAIDNQFLVGPSILVTPVLEPQVSTVKGVFPGVGQGEVWYDWYTQTAVDAQPGVNTTIDAPLGHIPVYVRGGSILPMQEPALTTRDARKTPWALLVALGKDGTASGHLYLDDGESIHPKVSLNVKFRATQTALTVSSEGEWKEANPLANVTILGVLENPVSVTSNGQQVPAEYDAQSRILVITGLNQFTNNGAWGQDWTLRW
Protein: ADP-ribosylation factor-like protein 1 (Q20758)
Organism: Caenorhabditis elegans
Function: GTP-binding protein that may be involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Plays a role in male tail tip morphogenesis.
Subcellular location: Golgi apparatus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:21408209}. Cytoplasmic granule {ECO:0000269|PubMed:21408209}. Note=Localizes to cytoplasmic granules (puncta) during the later stage of male tail tip retraction. {ECO:0000269|PubMed:21408209}.
Interaction partners:
- SEC7 domain-containing protein
- Uncharacterized protein F54C8.7
- GRIP domain-containing protein
- Short coiled-coil protein homolog
- Ras-related protein rab-6.2
- Monensin-resistant homolog 2
- ADP-ribosylation factor GTPase-activating protein 1
- Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 homolog
- ABC transporter family G domain-containing protein
Sequence:
MGGVMSYFRGLFGAREMRILILGLDGAGKTTILYRLQVGEVVTTIPTIGFNVEQVEYKNLKFQVWDLGGQTSIRPYWRCYYANTDAIIYVVDSADRDRVGISRQELATMLQEDELQGAVLAVLANKQDIAGCLTETEVYKALGLDALRNRTIQIFKTSASKGEGLDPAMDWLANQLQQKK
Protein: Apical junction molecule (H2KYC5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDIENLQSSNNRSQKSRPPDGFNAILQTAFSAILAFVLSLRIIVFATARKRLTTTAANPDIQVEEASSSSSDTSSDTEIVEEGVFIQRQGEPTMSEKKPAQGMPSVMSLLQTDEILSSCSDDEPTTSGLIPLPSLIQSNMSVLPNFLHTINEEESDEIRSLTGSSLASPRTVVDRRLSNISLLSPTPDEDFGLEQQEQQPENSEEVRGRESRTSLEEERIVVGEPRTTRQIEITQSASEDDRLDLLKELAKIGKSNTSTSQMSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAESEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHKLADADRDQEEELVFNEERRKTVTMDDNASLRSASITFDANRDEQDLLNESFASNPTDETVLMQKTKDEMDATSERPRSPLDLPPPPASVVLHPSAPPPPPPPLSSTEVVGNTTTTTTTHYAPKTWNDPSITTAPKIPVSLLSGAQPLPSVLTQRTTTSSYSAPNYSASSMSGVPSDVAPPPPLPIPNQSSSSAASYQHHHASSISKSISSSREDLLSEHATSRSTVREIPVHRAPSTAPSHSSVFEYHMMPTTTSTYHHVETPSDEYYRREVMTRTIITRSTEALSQTPLGRPASPLDRYLPYPTTTTTTSGDGRTREEKTVDYKVTYHRDIEEQERRIREDQARRQQEEQDRRDREDNARRILAQREHQEMERLREQQNLSERALAERERADKERLQQERLLRQQREKKRREEWDRLESIRLAEEEAELARRRALEKERIDREKAEEERKTMERLERERARLERERLEEERRQKEKAETERIERERREHERIEIERIERIKRERIERERREREEKKAEEDRLLRERLELERIERERRELEARERQELELQRREAEDRERQRLEDEAREMRRREEERREAELVADVHRQAEERERLRKRQEREEAERLERIRLEQQKIDMERIDAERRERERKEEERREFELIEAARRKKEARDRDRLDEMERERVREEEERREKERREQERRIAAEKERKRRQEEEEEIARLNELQRAAAARQAQRNAELDRQRQRDELDRKAQELSEREMREKERRDRERANEEAQLADLLERERHNQLIRENERREAVERANNRRLEDRRSRDKLDHIVRERSEKEQFELEKRRLLAEKEAMNRKKNHLLSSETLAKLTQPMYYTTREPEVTTKVERQVIERIDRNVWVEDVPYAPSQSAMGYLDNDENNRDRLYNPNDLNRNGSSRSRYQRAKNEKARRDFYHSSQDSAGLA
Protein: Malate synthase 1 (EC 2.3.3.9) (P30952)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Malate synthase which takes part in the glyoxylate cycle. MLS1 activity is essential for cells to grow on oleic acid as a sole carbon source. Two steps of the glyoxylate cycle take place in the cytosol, the splitting of isocitrate into succinate and glyoxylate, and the dehydrogenation of malate to oxaloacetate. However, the formation of malate from glyoxylate and acetyl-CoA undertaken MLS1, occurs in the peroxisomes when cells are grown on oleic acid (Probable). The source of acetyl-CoA being either peroxisomal when breaking down fatty acids, or cytosolic when extra-cellular two-carbon substrates are used, therefore, although not strictly essential, the peroxisomal localization of MLS1 appears to be advantageous for cells growing on oleic acid, in that acetyl-CoA production and utilization are thereby intimately compartmentalized together to increase efficiency (Probable).
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:11846793, ECO:0000269|PubMed:27678487}. Note=Imported in peroxisome via recognition by the peroxisomal targeting signal receptor PEX9 in an oleate-dependent manner. {ECO:0000269|PubMed:27678487}.
Interaction partners:
- Mitochondrial 2-methylisocitrate lyase ICL2
- Isocitrate lyase
- Acetyl-coenzyme A synthetase 1
- Malate dehydrogenase, cytoplasmic
- Citrate synthase, peroxisomal
- Phosphoenolpyruvate carboxykinase
- Citrate synthase 3, mitochondrial
- Citrate synthase, mitochondrial
- Acetyl-coenzyme A synthetase 2
- Malate dehydrogenase, peroxisomal
Sequence:
MVKVSLDNVKLLVDVDKEPFFKPSSTTVGDILTKDALEFIVLLHRTFNNKRKQLLENRQVVQKKLDSGSYHLDFLPETANIRNDPTWQGPILAPGLINRSTEITGPPLRNMLINALNAPVNTYMTDFEDSASPTWNNMVYGQVNLYDAIRNQIDFDTPRKSYKLNGNVANLPTIIVRPRGWHMVEKHLYVDDEPISASIFDFGLYFYHNAKELIKLGKGPYFYLPKMEHHLEAKLWNDVFCVAQDYIGIPRGTIRATVLIETLPAAFQMEEIIYQLRQHSSGLNCGRWDYIFSTIKRLRNDPNHILPNRNQVTMTSPFMDAYVKRLINTCHRRGVHAMGGMAAQIPIKDDPAANEKAMTKVRNDKIRELTNGHDGSWVAHPALAPICNEVFINMGTPNQIYFIPENVVTAANLLETKIPNGEITTEGIVQNLDIGLQYMEAWLRGSGCVPINNLMEDAATAEVSRCQLYQWVKHGVTLKDTGEKVTPELTEKILKEQVERLSKASPLGDKNKFALAAKYFLPEIRGEKFSEFLTTLLYDEIVSTKATPTDLSKL
Protein: Pickpocket 29, isoform D (Pickpocket 29, isoform G) (A8DYP1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Amiloride-sensitive Na+ channel
- Pickpocket protein 11
- Gustatory and pheromone receptor 32a
Sequence:
MWRKSVMNFRGFIRSFVENKGLLWIFVIGISGWSTVSILVLLKTRYETDSTTIGVSTAYSRWINTFPSIGICLTKSRAFNEFKAMMREYFQEDFAFSFTRMIYEYAFLNPNNIFTKEPTKNTSYPYNFNILDIRRKMFPTNCTECFKEIYFRGELVTDCEEIFKFHVTEMGYCFLANNLLDYDSIEEMPLRYSSLDNNRSLRLYMRSSVMYKYEMYVNSPEDLPFFNSLTYTISTDPTTYAFNVEEIHNHEGVIDEPISQRKCKFPSESSIEGFPYSFSACMSIIRSEFEMKTCDCSLFNPKDRNESLYCGLQHADCLIKEGFATRVKEYVGSSTVCLPSCVEQQISLVGVITENGTLYNNNTQITEIQIASPPTVRYERKVTQTKLDLIVGIGSVAGLFFGASLLNLLEIISYFIKKLKTMIFG
Protein: Fibrinogen gamma chain (P02680)
Organism: Rattus norvegicus (Rat)
Function: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02679}.
Interaction partners:
- Fibrinogen beta chain
- Fibrinogen alpha chain
- Prothrombin
- Serpin family F member 2
- Integrin subunit alpha 2b
- Alpha-2-HS-glycoprotein
- Antithrombin-III
- Heparin cofactor 2
- Kininogen-1
- Coagulation factor XIII B chain
Sequence:
MNWSLQLRSFILCWALLLLSPTGLAQYTATRDNCCILDERFGSYCPTTCGISDFLNSYQTDVDTDLQTLENILQRAENRTTEAKELIKAIQVYYNPDQPPKPGMIEGATQKSKKMVEEILKYEALLLTHESSIRYLQDIYTSNKQKITNLKQKVAQLEAQCQEPCKDSVRIHDTTGKDCQDIANKGAKESGLYFIRPLKATQQFLVYCEIDGSGNGWTVLQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWSGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMHFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKSSTPNGYDNGIIWATWKTRWYSMKETTMKIIPFNRLSIGDGQQHHMGGSKQVSVEHEVDVEYP
Protein: Ankyrin 2, isoform Y (X2JGD3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVTENGAQGDGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRGKVRLPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDEVAAVLIENGAALDAATKKGFTPLHLTAKYGHIKVAQLLLQKEADVDAQGKNGVTPLHVACHYNNQQVALLLLEKGASPHATAKNGHTPLHIAARKNQMDIATTLLEYGALANAESKAGFTPLHLSSQEGHAEISNLLIEHKAAVNHPAKNGLTPMHLCAQEDNVNVAEILEKNGANIDMATKAGYTPLHVASHFGQANMVRFLLQNGANVDAATSIGYTPLHQTAQQGHCHIVNLLLEHKANANAQTVNGQTPLHIARKLGYISVLDSLKTITKEDETAAAPSQAEEKYRVVAPEAMHESFMSDSEEEGGEDNMLSDQPYRYLTVDEMKSLGDDSLPIDVTRDERMDSNRMTQSAEYASGVPPTIGEEVISPHKTQVYGSSPKATVDGVYIANGSGHDEPPHVGRKLSWKSFLVSFLVDARGGAMRGCRHSGVRMIIPSRSTCQPTRVTCRYVKPQRTMHPPQLMEGEALASRVLELGPCSTKFIGPVVMEVPHFASLRGKEREIIILRSDNGETWREHTIDNSEEIIHDVLQQCFEPEEIAQLEEQAGNHVCRFVTYDFPQYFAVVSRIRQEVHAIGPEGGMVSSTVVPQVQAVFPQGALTKKIKVGLQAQPVDPDLTAKLLGRGVAVSPIVTVEPRRRKFHKAITLSMPAPKAHSQGMINQYSGNTPTLRLLCSITGGPSRAQWEDVTGSTPLTFVNDCVSFTTTVSARFWLMDCRNISDATKMATELYKEVIHVPFIAKFVVFAKKVEPFEAKLRVFCMTDDREDKTLEKHELYTEVAKSRDVEVLEGKPQYIEMAGNLVPVTKSGDQLQVQFKAFRENRLPFTVRVKDQHADIVGRTLFMKEPKVAKGEPPQQPICILNIVLPEAVIPDSTTAFSDRVTSAYRTSMFSLSKHQNDHYIGDIRIVDLSNLLGKDWIQLAPEIGINGEEIDEIINQNTDSIARQAQSMIRLYKDKPNYDILSLETALKNIGRDDIMKKCKSGRLSHSREFDEADLMKNSESVEELVRRESKRIQQINEREEVKYSAEEKEVEESESDEEAAKRTVAERREKIVKRLSIERSIPASTQKKEITREITEIKRKSLIEDKKAHHESEILMQLPADNVIIKTTTVPDQVIKMKMGKMDSTEVSKSEFDKELTHKFKTSGRSSEEEDQPSYPDQTDKIVQDISAAEKKEKDGVTFSRVTTITRQEARDITEDFLEIEKRSQLPATSTTATVHEKFVEEIKEKTSPLASVPQETVKEVQQVISEVTEIASKKVENIISSFESSKSVDATTVLPTQPSVESTKVSETIKNLEDAKAVSAEQVKTVHVVESSSIEETIAEFEAKKVKYDFHGGEPKTQIPKFTRKPSDDSMKPTAAPRATVESETESVLETKAEKPISKIPVKTIPTEAQKVSEVDARKITQDFLQGEKLAAEPKPSPAASKIPKVEPRKSVDKQVDRESKILDDVVASTATIMTAGLGDEQLKDQLVDHSEIIAKSETVAEKVTELLDTFHKIEEKVTKSEKTSEISSKVEELVKIEEKPLSQVQPKEDKVAEKVAEVIETFHKIEEKITTADARELTRDFLSMEQQNQLPSMPQAAEKPLESSLTSTSASEPESIVTVKPSPPASKIPVVEPRKIVFDESTKPLIEPEPVKTTEKKPLNERQLTADFLSMEQQTQLVSEPAKSLVEEVMKSAEQMVEQPKQQKSLNERQLTEDFLLMEQQTQLPSDIVKPTDKLIDGIESAAPVGDEASPFHTPKLTTSVVTQEPQQLASEYDSDTFGKQATIPLGDSKIDQGLIAPVSMEPRKSLTDAEFCKSVGETITKKMSVGVIEISDELKKIESEIPHSQTPPPTPSDNKTDKQNEEPELISLERDYLADTVTTLHTTTESTLERVSAITKIETLHERKVELSNLDTEKISHEIGDVKVGGGDDDSDGDSGDFVARIREEANILVDRVLEESVEIIESQGHQANGHEIAKLDYNSESENYAITCDDIGGVDVIKSPTIESMSGKSFDDNMSFTDEHIHLPLHAQNTSTTMTTTITTQFQQQQSQSAVSSTSAAKDKALF
Protein: Polyphenol oxidase (EC 1.14.18.1) (D2CVT3)
Organism: Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus)
Interaction partners:
Sequence:
FSKASSHRFKVSCNAASGDTNHPETTPKLITSLDMTHNVDRRNLLLGLGGLYGAANFTSLPSAFATPIAAPDNIADCVTASSNLQNPTDVVRGLACCPPALSSKPEIYTLPVNPVTRIRPAAQRATPEYIEKYKAAIQEMRKLPDDHPHSFKQQAMIHCAYCNGAYNQEQSGHPELQLQIHNSWLFYPFHRWYLYFYERILGKLINDPTFAIPHWNWDHPTGMMLPAMFEDADPALKQNPIFDPYRDVTHLPPAILDAEYAGANTGADCVNQISSNLASMYRQMITNATDTTSFSGGEFVSGDDPLQAGTLIAGSIERGIHTAMHRWVGNPRMANNEDMGNFYSAGYDPVFYVHHANVDRMWKIWNNASYVFYDENEKLVRVFNKDSIDIGRMGYDYERSSVPWLQSRPVAHAKRSKAAAQSVGTVKKVEDVEFPVKLDQVVKVLVKRPATNRTKEDKEKAHEILLLNGIKFDGEKFVKFDVFVNDVDDGIETTAAESEFAGSFAQLPHGSHSEKMLMTSGARFGITELLEDIEAEDDEYVLVNLVPKIGCDDAIVSEIKIELVPIVQT
Protein: GH09761p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q7K025)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LP23833p
- IP12580p1
Sequence:
MSVSDLIGALDAIPKLTVPESLVPEETSVFLDAPEWLTESYLQDALRKYYKDQLIRINWVKVNPALGKGENYGGVLTRVKAQFTRSDGSSQLGHYIVKSTFEGNEFAQNAMKPYDIFNREMIIYEQVLPKQKALLREIGDAEQIFAETMAVDIDNSALIFEDLNARGFVMPDRLVGLDQKLARIVLRKLAKMHATSAVLNERENHILESYDRGFFNRYTDNYEPAFVGMLQAATRRVAQWPGYEKYAEKLKALVPIYMELGKRIFDISPGHINVLAHGDLWTNNVLVKYDKQTGEPIDVVIIDFQYTAWGSPALDLFYFMNSSLEFDLHQNHQEQLIAYYFRHFADTLKKLQYRSTIPSLHQFHQQLQQKKFYAAHTSISVFPVQRNVETADADFNALMENNQRAMNFKDACYRNPIAQRILRELLPDFEAEGLLDADQ
Protein: Inactive pancreatic lipase-related protein 1 (PL-RP1) (P06857)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters (in vitro).
Subcellular location: Secreted {ECO:0000269|PubMed:9726421}.
Interaction partners:
Sequence:
MVSIWTIALFLLGAAKAKEVCYEQIGCFSDAEPWAGTAIRPLKVLPWSPERIGTRFLLYTNKNPNNFQTLLPSDPSTIEASNFQTDKKTRFIIHGFIDKGEENWLLDMCKNMFKVEEVNCICVDWKKGSQTSYTQAANNVRVVGAQVAQMLSMLSANYSYSPSQVQLIGHSLGAHVAGEAGSRTPGLGRITGLDPVEASFQGTPEEVRLDPTDADFVDVIHTDAAPLIPFLGFGTSQQMGHLDFFPNGGEEMPGCKKNALSQIVDLDGIWEGTRDFVACNHLRSYKYYSESILNPDGFASYPCASYRAFESNKCFPCPDQGCPQMGHYADKFAVKTSDETQKYFLNTGDSSNFARWRYGVSITLSGKRATGQAKVALFGSKGNTHQFNIFKGILKPGSTHSNEFDAKLDVGTIEKVKFLWNNNVVNPTFPKVGAAKITVQKGEEKTVHSFCSESTVREDVLLTLTPC
Protein: Guanine nucleotide-binding protein G(q) subunit alpha (EC 3.6.5.-) (Guanine nucleotide-binding protein alpha-q) (P50148)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Required for platelet activation. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs). Together with GNA11, required for heart development (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19001095}; Lipid-anchor {ECO:0000269|PubMed:19001095}. Golgi apparatus {ECO:0000269|PubMed:19001095}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:P21279}.
Interaction partners:
- Sphingosine 1-phosphate receptor 3
- Histamine H1 receptor
- Metabotropic glutamate receptor 5
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
- Beta-adrenergic receptor kinase 1
- Sphingosine 1-phosphate receptor 2
- Metabotropic glutamate receptor 1
- Rho guanine nucleotide exchange factor 25
- Lysophosphatidic acid receptor 1
Sequence:
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Protein: Response regulator GacA (Q4KAR8)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
- histidine kinase
- LuxR family transcriptional regulatory protein PsoR
- Autoinducer-binding transcriptional regulator, LuxR family
- Two-component transcriptional regulator PedR2
- UvrABC system protein C
- histidine kinase
- Sensor histidine kinase
- Sensory box histidine kinase
- Two-component sensor histidine kinase PedS2
- histidine kinase
Sequence:
MIRVLVVDDHDLVRTGITRMLADIDGLQVVGQAESGEESLLKARELKPDVVLMDVKMPGIGGLEATRKLLRSHPDIKVVAVTVCEEDPFPTRLLQAGAAGYLTKGAGLNEMVQAIRLVFAGQRYISPQIAQQLVFKSFQPSSDSPFDALSEREIQIALMIVGCQKVQIISDKLCLSPKTVNTYRYRIFEKLSISSDVELTLLAVRHGMVDASL
Protein: Large ribosomal subunit protein bL33m (54S ribosomal protein L39, mitochondrial) (O74394)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein bS6m
Sequence:
MAKKNKARLLVKLLSTAGTGFFYVRSRPKAAPKLAFIKYDPKIHKRVLFEESKMK
Protein: histidine--tRNA ligase (EC 6.1.1.21) (Q8IQX8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tyrosine--tRNA ligase
- Lysine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Tyrosine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- threonine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, cytoplasmic
- Eukaryotic translation initiation factor 2 subunit 1
Sequence:
MSDTREQILEQIKVQGDLVRQLKAAKESKEKTAPSGGGRVSSSGVPAQRQQQQQPQKQQQAQVQQQQHEQLHQIDEEVARLLALKATLGGDAAPTNQKFTLKTPKGTRDYGPQQMTLRQGVLDKIVQVFKRHGGEAIDTPVFELKEVLTGKYGEDSKLIYDLKDQGGEILSMRYDLTVPLARYLAMNKISSIKRYHIAKVYRRDNPAMTKGRYREFYQCDFDIAGTYDPMLPDAECVKIVSEILDTLDIGDYVIKLNHRQLLDGMFQACGVPADSFRTICSAVDKLDKSPWADVRKEMVDEKGLDEAAADRIGEYVRLSGGAELVEQLLANEKLKAVPNAVKGLEGMKQLLKYCSIFGLDKRVSFDLSLARGLDYYTGVIYEGVLKGESATVASPAKTSQQNGEQANEPATVGSVAGGGRYDNLVGMFDPRGKAVPCVGVSIGVERIFSVLEARAAASGLKLRTSDVEVYVASAHKGLHEQRLKVLNLLWDAGVKAEHSYKLNPKLLVQLQHCEEHQIPLVVVLGDAELAQGLVKLREVTTREETNVKLEDLAAEIRRRQQASA
Protein: EHS-1 (Eps15 (Endocytosis protein) Homologous Sequence) (Q9BIF4)
Organism: Caenorhabditis elegans
Interaction partners:
- Intersectin-1
- ENTH domain-containing protein
- FCH domain only protein 2
- AP-2 complex subunit alpha
- Clathrin light chain
- Putative stoned B-like protein
- Receptor tyrosine-protein kinase let-23
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Phosphatidylinositol-binding clathrin assembly protein unc-11
- Probable clathrin heavy chain 1
Sequence:
MDDSYAIATPHNDVFNHAFAEMNPHGAPRIGAAEAATFLKKSNLAMPVLGQIWELSDSQKVGSLDKRGAFVAFKLVAAAQQGKPVANSSLYDSSLQPPRFAPPVPPANMQHHFQPSFPSVGRAPPVPPPPHPSHPYSISSQQSSPAHPSSAFPPQWPITPTDQAKYDSIFQSLNPVNGKLSGAHVRPVLMNSGLDAHALARIWELSDQDKDGNLDRIEMSVALHLVYRSLQSDPVPAQLPPNLIHPSKAMYAHSSPNFAAPPHPPRPMMGSRAGSVTSLDDVNMSQSYSATMPRAYPPQPGRAYSAQAHVNGSRTSGASTPISASHSIHSFPAGEWPINTGDYADQFAQTDTNKDGLVDGMDMRAPMMTTGLSAQILAHVWALADIKKCGQLNLEQFALTMHLLDMAKRGESIPSELPLHLIPPSFRPPTEPSALHHPAQSVSTPQLPEATSMEIKEALEGENEEMKQLAESIQSMLVERKTAEEAVLQLEADMTIKNSSIKNLQVELATLESTVKQLERQKGEATRRLADYDTQIEQLESACKAQKETKEDTEKRMQQIDEDAKNAEDCKANDEKEMEELKKEIEMLDNQFKTVRGEIVKETSQREQKVAELTTLERKEARDQIQMEKLDAAIENTTKLTEQVSDAVEKSEEEMVQILRSQQRLLSTVIDQSLLSDDTVYGETAGTSSQNHVQQPPDPFASARANPAADPFAQVDQFGSSGHFDAAFPTDPFAQGGFPSDSGFAQSAPAKPAPPRPAPPKSARETPVNDPFAPSQGQSTQPAGFADFADFGSAFN
Protein: maleylacetoacetate isomerase (EC 5.2.1.2) (X1WBU0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAAQTKPVLYGYYRSSCSWRVRIAFALKGIEYEQKPINLIKDGGQQLTDQFKAINPMQQVPAVSIDGITLSQSLAIIQYIEETRPEPRLLPADPMQRAHVRIICDIIASGIQPLQNLYVLQKIGEDKVQWAQHFINRGFQALEPVLKETAGKYCVGDEISMADICLVPQVYNADRFKVDMTQYPTIRRLNQTLVEIEAFKASHPSRQPDTPDDLRL