wanglab/gogpt-training-data huggingface dataset:
Protein: Sox100B (Q9VA17)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein hedgehog
- Protein Wnt-4
- FI18025p1
- Fibroblast growth factor
- Protein snail
- Scalloped, isoform Q
- Protein Wnt-5
Sequence:
MSDSSSSNCSKDRAKPVETLVLANYALKAEQKKAQGQGGRKEDERITTAVMKVLEGYDWNLVQASAKAPTDRKKEHIKRPMNAFMVWAQAARRVMSKQYPHLQNSELSKSLGKLWKNLKDSDKKPFMEFAEKLRMTHKQEHPDYKYQPRRKKARVLPSQQSGEGGSPGPEMTLSATMGSSGKPRSSNSNGQRRAGKGNAAADLGSCASTISHANVGSNSSDVFSNEAFMKSLNSACAASLMEQSLIETGLDSPCSTASSMSSLTPPATPYNVAPSNAKASAANNPSLLLRQLSEPVANAGDGYGVLLEAGREYVAIGEVNYQGQSAGVQSGAEGGGAGQEMDFLENINGYGGYTGSRVSYPAYSYPANGGHFATEEQQQQQALQASEALNYKPAAADIDPKEIDQYFMDQMLPMTQHHHPHHTHPLHHPLHHSPPLNSSASLSSACSSASSQQPVAEYYEHLGYSPAASSASQNPNFGPQQPYANGAASMTPTLGDPAPQQELQSQQQEQQHQNPSQHHLWGTYTYVNP
Protein: VQ domain-containing protein (A0A178VL61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEATSQPCFSHNSSLHSTRKQPAKPWKKPVTGLPQRMHPKVYRVEPVNFKELVQRLTGAEDVEQEVHQVEAKPVKISDDTTTAKDNPFAFDLSPSSSRFWEAFPLLSPANLSRW
Protein: Protein NLP7 (AtNLP7) (NIN-like protein 7) (Nodule inception protein-like protein 7) (Q84TH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in regulation of nitrate assimilation and in transduction of the nitrate signal.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00852, ECO:0000269|PubMed:18826430, ECO:0000269|PubMed:26744214}.
Interaction partners:
- LOB domain-containing protein 37
- Protein NRT1/ PTR FAMILY 6.3
- Nitrate regulatory gene2 protein
- High-affinity nitrate transporter 2.1
- Transcription factor TCP20
- Nitrate reductase 1
- MADS-box transcription factor ANR1
- Nitrate reductase 2
- Calcium-dependent protein kinase 30
- CBL-interacting serine/threonine-protein kinase 8
Sequence:
MCEPDDNSARNGVTTQPSRSRELLMDVDDLDLDGSWPLDQIPYLSSSNRMISPIFVSSSSEQPCSPLWAFSDGGGNGFHHATSGGDDEKISSVSGVPSFRLAEYPLFLPYSSPSAAENTTEKHNSFQFPSPLMSLVPPENTDNYCVIKERMTQALRYFKESTEQHVLAQVWAPVRKNGRDLLTTLGQPFVLNPNGNGLNQYRMISLTYMFSVDSESDVELGLPGRVFRQKLPEWTPNVQYYSSKEFSRLDHALHYNVRGTLALPVFNPSGQSCIGVVELIMTSEKIHYAPEVDKVCKALEAVNLKSSEILDHQTTQICNESRQNALAEILEVLTVVCETHNLPLAQTWVPCQHGSVLANGGGLKKNCTSFDGSCMGQICMSTTDMACYVVDAHVWGFRDACLEHHLQKGQGVAGRAFLNGGSCFCRDITKFCKTQYPLVHYALMFKLTTCFAISLQSSYTGDDSYILEFFLPSSITDDQEQDLLLGSILVTMKEHFQSLRVASGVDFGEDDDKLSFEIIQALPDKKVHSKIESIRVPFSGFKSNATETMLIPQPVVQSSDPVNEKINVATVNGVVKEKKKTEKKRGKTEKTISLDVLQQYFTGSLKDAAKSLGVCPTTMKRICRQHGISRWPSRKIKKVNRSITKLKRVIESVQGTDGGLDLTSMAVSSIPWTHGQTSAQPLNSPNGSKPPELPNTNNSPNHWSSDHSPNEPNGSPELPPSNGHKRSRTVDESAGTPTSHGSCDGNQLDEPKVPNQDPLFTVGGSPGLLFPPYSRDHDVSAASFAMPNRLLGSIDHFRGMLIEDAGSSKDLRNLCPTAAFDDKFQDTNWMNNDNNSNNNLYAPPKEEAIANVACEPSGSEMRTVTIKASYKDDIIRFRISSGSGIMELKDEVAKRLKVDAGTFDIKYLDDDNEWVLIACDADLQECLEIPRSSRTKIVRLLVHDVTTNLGSSCESTGEL
Protein: Elicitor peptide 4 (Q9FIA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Elicitor of plant defense.
Interaction partners:
- Elicitor peptide 5
- Staphylococcal-like nuclease CAN1
- Phospholipase A1-Igamma1, chloroplastic
- Elicitor peptide 6
- KH domain-containing protein HEN4
- Elicitor peptide 3
- RNA-binding KH domain-containing protein PEPPER
- Precursor of elicitor peptide 1
- Elicitor peptide 7
- Armadillo repeat only 3
Sequence:
MERGVSYYLWIPFKFIHQTFGSLLLKLLGLRSPSDHSFPEDGEEEVKVVEVSSRGLPGKKNVLKKSRESSGKPGGTNKKPF
Protein: Metabotropic glutamate receptor (DmGluRA) (P91685)
Organism: Drosophila melanogaster (Fruit fly)
Function: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8824309}; Multi-pass membrane protein {ECO:0000269|PubMed:8824309}.
Interaction partners:
- Fragile X messenger ribonucleoprotein 1 homolog
- Inositol 1,4,5-trisphosphate receptor
- IP03705p
- Gamma-aminobutyric acid type B receptor subunit 2
- NMDA receptor 2, isoform C
- G protein beta subunit 5
- G protein alpha i subunit subunit alpha 65A)
- Calmodulin
Sequence:
MKQKNNNGTILVVVMVLSWSRVVDLKSPSNTHTQDSVSVSLPGDIILGGLFPVHEKGEGAPCGPKVYNRGVQRLEAMLYAIDRVNNDPNILPGITIGVHILDTCSRDTYALNQSLQFVRASLNNLDTSGYECADGSSPQLRKNASSGPVFGVIGGSYSSVSLQVANLLRLFHIPQVSPASTAKTLSDKTRFDLFARTVPPDTFQSVALVDILKNFNWSYVSTIHSEGSYGEYGIEALHKEATERNVCIAVAEKVPSAADDKVFDSIISKLQKKPNARGVVLFTRAEDARRILQAAKRANLSQPFHWIASDGWGKQQKLLEGLEDIAEGAITVELQSEIIADFDRYMMQLTPETNQRNPWFAEYWEDTFNCVLTSLSVKPDTSNSANSTDNKIGVKAKTECDDSYRLSEKVGYEQESKTQFVVDAVYAFAYALHNLHNDRCNTQSDQTTETRKHLQSESVWYRKISTDTKSQACPDMANYDGKEFYNNYLLNVSFIDLAGSEVKFDRQGDGLARYDILNYQRQENSSGYQYKVIGKWFNGLQLNSETVVWNKETEQPTSACSLPCEVGMIKKQQGDTCCWICDSCESFEYVYDEFTCKDCGPGLWPYADKLSCYALDIQYMKWNSLFALIPMAIAIFGIALTSIVIVLFAKNHDTPLVRASGRELSYTLLFGILVCYCNTFALIAKPTIGSCVLQRFGIGVGFSIIYSALLTKTNRISRIFHSASKSAQRLKYISPQSQVVITTSLIAIQVLITMIWMVVEPPGTRFYYPDRREVILKCKIQDMSFLFSQLYNMILITICTIYAIKTRKIPENFNESKFIGFTMYTTCIIWLAFVPIYFGTGNSYEVQTTTLCISISLSASVALVCLYSPKVYILVFHPDKNVRKLTMNSTVYRRSAAAVAQGAPTSSGYSRTHAPGTSALTGGAVGTNASSSTLPTQNSPHLDEASAQTNVAHKTNGEFLPEVGERVEPICHIVNK
Protein: Copal-8-ol diphosphate hydratase TPSSA9, chloroplastic (EC 4.2.1.133) (13-labden-8,15-diol pyrophosphate synthase TPSSA9) (SsLPS) (Diterpene synthase Sa9) (SsTpsSa9) (Labd-13-en-8-ol diphosphate synthase) (SsLPPS) (G8GJ96)
Organism: Salvia sclarea (Clary sage)
Function: Involved in the biosynthesis of labdane-type diterpenoid including sclareol, a diterpene-diol that is used as fragrance and flavoring, and has anticancer effects (able to kill leukemic and colon cancer cells by apoptosis) (Probable). Sclareol can also be used as synthesis precursor of ambergris substitution fragance products such as ambrox (Probable). Terpene synthase that produces 8-hydroxycopalyl diphosphate from geranylgeranyl diphosphate (GGPP).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:22834731}.
Interaction partners:
Sequence:
MTSVNLSRAPAAIIRRRLQLQPEFHAECSWLKSSSKHAPFTLSCQIRPKQLSQIAELRVTSLDASQASEKDISLVQTPHKVEVNEKIEESIEYVQNLLMTSGDGRISVSPYDTAVIALIKDLKGRDAPQFPSCLEWIAHHQLADGSWGDEFFCIYDRILNTLACVVALKSWNLQSDIIEKGVTYIKENVHKLKGANVEHRTAGFELVVPTFMQMATDLGIQGLPYDHPLIKEIADTKQQRLKEIPKDLVYQMPTNLLYSLEGLGDLEWERLLKLQSGNGSFLTSPSSTAAVLMHTKDEKCLKYIENALKNCDGGAPHTYPVDIFSRLWAIDRLQRLGISRFFQHEIKYFLDHIESVWEETGVFSGRYTKFSDIDDTSMGVRLLKMHGYDVDPNVLKHFKQQDGKFSCYIGQSVESASPMYNLYRAAQLRFPGEEVLEEATKFAFNFLQEMLVKDRLQERWVISDHLFDEIKLGLKMPWYATLPRVEAAYYLDHYAGSGDVWIGKSFYRMPEISNDTYKELAILDFNRCQTQHQLEWIQMQEWYDRCSLSEFGISKRELLRSYFLAAATIFEPERTQERLLWAKTRILSKMITSFVNISGTTLSLDYNFNGLDEIISANEDQGLAGTLLATFHQLLDGFDIYTLHQLKHVWSQWFMKVQQGEGSGGEDAVLLANTLNICAGLNEDVLSNNEYTALSTLTNKICNRLAQIQDNKILQVVDGSIKDKELEQDMQALVKLVLQENGGAVDRNIRHTFLSVSKTFYYDAYHDDETTDLHIFKVLFRPVV
Protein: Rifin (Q8IHM3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKYNYTNILLFSLSLNILFLSSGVYNQGNHNLTLYKPTTTSRLLCECELYAPSNYDNDPEMKAVIHDFDHQTSERYKEYDKRTIKNRKKCKDQCDKEIQKIILKDKIEKELTEKLATLETNITTKDIPTCVCEKSLADKTEKFCLNCGFGLGSGVLQSLGLFGGSGIYAWTIGAPAAAIAAAKEAGAAAGIKAGHAVGATKVVELVNSKFGVETLGGQTLNDFFTATNYMNETLIFEAVHKEFYKTCVYSGTNASDRICIIFNSLSTGQGGTVTANEFIGTTAKEIVTQAQYTSNATASNVTTVKTAALKAKNMAVVEAGFDSYITAVNASIAAIFIIVLVMVIIYLILRYRRKKKMKKKLQYIKLLKE
Protein: Brevinin-1OKd (C0HL11)
Organism: Nidirana okinavana (Kampira Falls frog) (Babina okinavana)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000250|UniProtKB:A7WNV4}.
Interaction partners:
Sequence:
FLGSIIGALAKGLPSLIALIKK
Protein: Extraembryonic, spermatogenesis, homeobox 1 (A2AG22)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MENSLFNSMFLEEANYQEPEGFEPSRGEAAAPVAEAPQAWNGNENLGGGFLESNAQLGEADAAPVRQSLMRPLMQPVAQSSPQPLPANPLQAPQQPEEQEEEEEEQPGEEQPQQEPKPRRYRICFTPIQLQELEAFFQRVQYPDLFARVELARRLGLPEPRVQVWFQNRRAKWRRLRRAQAFRNMVPVAMSPPVGVYLDDHYGPIPIVEVIWKCYPMVPRPMHPQMMPLPPRPPPGFRMPPPFRPPPLPPFPWPPVPPDAHIPNAAREYNPFPFPFPFPFPFPNPFPNPNPNPNPNPNPNPNPNQNFAGPRYRY
Protein: Flotillin (Q6P2A7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU366054}. Endosome {ECO:0000256|RuleBase:RU366054}.
Interaction partners:
Sequence:
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILSRLPESVERLTGVSISQVNHNKPLRTA
Protein: Serine/arginine-rich splicing factor RS41 (At-RSp41) (AtRS41) (P92966)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for constitutive and alternative pre-mRNA splicing (Probable). Involved in primary miRNA processing and pri-miRNA biogenesis. Binds both intronless and intron-containing pri-miRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:24146632, ECO:0000269|PubMed:26227967}. Nucleus speckle {ECO:0000269|PubMed:24146632, ECO:0000269|PubMed:26227967}.
Interaction partners:
- Serine/arginine-rich splicing factor SC35
- Serine/arginine-rich SC35-like splicing factor SCL30A
- Nuclear protein-like
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
- Splicing factor U2af large subunit A
- RNA-binding motif protein 25
- Serine/arginine-rich splicing factor SR45
- Protein BTR1
- RNA-binding KH domain-containing protein RCF3
Sequence:
MKPVFCGNFEYDARESDLERLFRKYGKVERVDMKAGFAFVYMEDERDAEDAIRALDRFEYGRTGRRLRVEWTKNDRGGAGRSGGSRRSSSGLRPSKTLFVINFDAQNTRTRDLERHFEPYGKIVNVRIRRNFAFIQYEAQEDATRALDATNSSKLMDKVISVEYAVKDDDSRGNGYSPERRRDRSPDRRRRSPSPYRRERGSPDYGRGASPVAHKRERTSPDYGRGRRSPSPYKRARLSPDYKRDDRRRERVASPENGAVRNRSPRKGRGESRSPPPYEKRRESRSPPPYEKRRESRSPPPYEKRRERSRSRSKSSPENGQVESPGQIMEVEAGRGYDGADSPIRESPSRSPPAEE
Protein: Interleukin (C7AL04)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDRRYRISFLTLFLTGCLQGNPIPRLLAGIDYLEENITCPDSVFYTPTDVEDSCIVAALACSIKELDTVKVECLDNAVHLESMQHHISMTATDLQKTIDKENSTTDTSECICEDKRLEKSFKDFIQNIRHLTQAHAAKRLSS
Protein: Glutaredoxin-2, mitochondrial (Q923X4)
Organism: Mus musculus (Mouse)
Function: Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.
Subcellular location: [Isoform 1]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Mitochondrial peptide methionine sulfoxide reductase
- Thioredoxin
- Glutaredoxin-3
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin, mitochondrial
- Peroxiredoxin-2
Sequence:
MSWRRAASVGRRLVASGRILAGRRGAAGAAGSGMGNSTSSFWGKSTTTPVNQIQETISNNCVVIFSKTSCSYCSMAKKIFHDMNVNYKAVELDMLEYGNQFQDALHKMTGERTVPRIFVNGRFIGGAADTHRLHKEGKLLPLVHQCYLKKKQEERH
Protein: choloylglycine hydrolase (EC 3.5.1.24) (Bile salt hydrolase) (Choloylglycine hydrolase) (G4XR37)
Organism: Bifidobacterium breve
Interaction partners:
Sequence:
MDIMNVQANQSDGRKSVMCTGFRFSDDEGNTYFGRNLDWSFSYGETILVTPRGYHYDTVFGAGGKAKPNAVIGVGVVMADRPMYFDCANEHGLAIAGLNFPGYASFVHEPVEGTENVATFEYPLWVARNFDSVDEVEEALRNVTLVSQIVPGQQESLLHWFIGDGKRSIVVEQMADGMHVHHDDVDVLTNQPTFDFHMENLRNYMCVSNEMAEPTSWGKASLTAWGAGVGMHGIPGDVSSPSRSVRVAYTNAHYPQQNDEAANVSRLFHTLGSVQMVDGMAKMGNGQFERTLYTSGYSSKTNTYYMNTYDDPAIRSYAMADYDMDSSELISVAR
Protein: Leishmanolysin-like peptidase (EC 3.4.24.-) (Q384F7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTFPPVVYCTADATVSPSPAVCLLTAGCRRPCCSWRIALKVSFSQTPIAQCFSYNLLSFALCLRLCVAMRLRTQVVGIGQLRTSFTSRICMGRRSNSVFFHLWLSFASLCLGNSDSSEGSPPVSNGTSPVVLSDQSVANMEANDSQWKPIRIVVSAKDLDDSLKYCVVAGVPRPDFMGGTLRCKTGDVLTNEKRLILTEHALPSAIHLHAERLLVGMEIDNIVVPEFDSPACKSFTVPIHHRSVGVPQADIILYVASGPAPHDGPAYATTCASLLSGRPIAGAINFSPSAITESYLYIRTVAHEIAHVLGFNFEAMKQLNMVGTKNIRGKSSVKVVKTPNVVKVARQYYGCGKITGMELEDNGDDSVRNSHWKRRIARDDLMTAIMGVSHYSELTLAFFLDTGFYRVNWEKGERMRWGHGAGCSFIEGKCMENNETNFPDMFCNDSAETLSCTHDRQALGRCTVHSYAVPIEESVRYFTMSWVGGSDNNLMDYCPVVEPYTDSYCRDGRRELLPGSRIGESSRCVKGEGLVAFTTHVGDICVEIHCGKRRGVSIRYSGDDSWHVCPEGGHVTPDKTFSEGRIVCPKWEEVCDDNAMTLSCLAAVFAIFVSALSLVV
Protein: Leader peptide SpeFL (Arrest peptide SpeFL) (P0DTV7)
Organism: Escherichia coli (strain K12)
Function: A small protein (arrest peptide) encoded upstream of inducible ornithine carboxylase gene (speF) that controls expression of downstream genes (speF and patE) by nascent chain-translational arrest and transcriptional attenuation. In the presence of ornithine a toeprint due to ribosomal arrest can be seen on the speFL transcript. Only L-ornithine (not other tested amino acids) has this effect. It is thought that in the presence of ornithine, ribosomal stalling on speFL prevents binding of Rho transcription termination factor to a downstream rut site allowing transcription of the operon. In the absence of ornithine, ribosomes terminate translation and are recycled, exposing the rut site allowing Rho to bind and prematurely terminate transcription. The presence of a pair of rare Arg codons could slow down translation to prevent polysome accumulation and to expose the rut site to Rho (Probable).
Interaction partners:
Sequence:
MENNSRTMPHIRRTTHIMKFAHRNSFDFHFFNAR
Protein: D-allose transport system permease protein AlsC (P32720)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system AlsBAC for D-allose; probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- D-allose-binding periplasmic protein
- D-allose import ATP-binding protein AlsA
- D-allulose-6-phosphate 3-epimerase
- D-allose kinase
- Ribose import binding protein RbsB
- Galactofuranose-binding protein YtfQ
- HTH-type transcriptional regulator RpiR
- Arabinose import ATP-binding protein AraG
- Ribose import ATP-binding protein RbsA
- Xylose import ATP-binding protein XylG
Sequence:
MGFTTRVKSEASEKKPFNFALFWDKYGTFFILAIIVAIFGSLSPEYFLTTNNITQIFVQSSVTVLIGMGEFFAILVAGIDLSVGAILALSGMVTAKLMLAGVDPFLAAMIGGVLVGGALGAINGCLVNWTGLHPFIITLGTNAIFRGITLVISDANSVYGFSFDFVNFFAASVIGIPVPVIFSLIVALILWFLTTRMRLGRNIYALGGNKNSAFYSGIDVKFHILVVFIISGVCAGLAGVVSTARLGAAEPLAGMGFETYAIASAIIGGTSFFGGKGRIFSVVIGGLIIGTINNGLNILQVQTYYQLVVMGGLIIAAVALDRLISK
Protein: Methanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase (MDO) (EC 1.1.99.37) (Methanol dehydrogenase (nicotinoprotein)) (Methanol:NDMA oxidoreductase) (C5MRT8)
Organism: Mycobacterium sp. (strain DSM 3803 / JC1)
Function: Catalyzes the oxidation of methanol to yield formaldehyde. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA) can serve this function in vitro and is reduced to 4-(hydroxylamino)-N,N-dimethylaniline. It is also able to use ethanol and formaldehyde with an activity comparable to methanol, and has a weak activity with methylamine as substrate.
Interaction partners:
Sequence:
MAIELNQIWDFPIKEFHPFPRALLGVGAHDIIGVEAKNLGFKRTLLMTTGLRGSGIIEELTGKIEYQGVEVVLYDKVESNPKDYNVMEAAALYQQERCDSIISIGGGSSHDAAKGARVVIAHDGRNINEFEGFAKSTNKQNPPHIAVSTTAGTGSETSWAYVITDTSDMEHPHKWVGFDEATIVTLAIDDPLLYYTCPQHFTAYCGFDVLAHGSEPYVSRLDFAPSLGNALYSVELVAKHLREAVFEPRNLKAREGMMNAQYIAGQAFNSGGLGIVHSISHAVSAFFDSHHGLNNAIALPRVWEYNLPSRYERYAQLATAMGVDTRNMTTVQAADAAVEAAIRLSQDVGIPDNFSQVRVDSYDKNRMNTGKYAGKGEVIKGDDKSVLAISEHIQGDWCTPGNPREVTVDSMIPVVGHAINGTY
Protein: Protocadherin 7 (A0A0A6YWD5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XNISIGSDHCSEYSCQTSNKYSKQPFRRVTFSVVSQPQDPHQGSLQSCYDSGLEESETPSSKSSSGPRLGALPLPEDNYERTTPDGSVGEAEHMENGVAVITTFPFLPFPHGKTHGRRVLLRPLH
Protein: Selenocysteine lyase (EC 4.4.1.16) (A0A0A0MQU4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MPGSSGAGMEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGNPSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTSKGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDILAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCNFSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGRSTTRAEVDLVVQDLKQAVAQLEDQA
Protein: Calretinin (CR) (Q08331)
Organism: Mus musculus (Mouse)
Function: Calretinin is a calcium-binding protein which is abundant in auditory neurons.
Subcellular location: Synapse {ECO:0000269|PubMed:35165172}. Cell projection, dendrite {ECO:0000269|PubMed:33488348}. Note=Located in dendrioles, small dendrites that makes up a brush structure found as the terminal specialization of a dendrite of a unipolar brush cell. {ECO:0000269|PubMed:33488348}.
Interaction partners:
- Parvalbumin alpha
- Somatostatin
- Pro-neuropeptide Y
- Glutamate decarboxylase 1
- RNA binding protein fox-1 homolog 3
- 45 kDa calcium-binding protein
- T-box brain protein 1
- Glutamate decarboxylase 2
- LIM/homeobox protein Lhx6
- Vesicular glutamate transporter 2
Sequence:
MAGPQQQPPYLHLAELTASQFLEIWKHFDADGNGYIEGKELENFFQELEKARKGSGMMSKSDNFGEKMKEFMQKYDKNSDGKIEMAELAQILPTEENFLLCFRQHVGSSAEFMEAWRKYDTDRSGYIEANELKGFLSDLLKKANRPYDEPKLQEYTQTILRMFDLNGDGKLGLSEMSRLLPVQENFLLKFQGMKLTSEEFNAIFTFYDKDGSGYIDENELDALLKDLYEKNKKEMNIQQLTTYRKSVMSLAEAGKLYRKDLEIVLCSEPPV
Protein: ATPase GET3A (AtGET3A) (EC 3.6.-.-) (Arsenical pump-driving ATPase) (Arsenite-stimulated ATPase) (Guided entry of tail-anchored proteins 3 homolog A) (Q949M9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (By similarity). Involved in the control of root hair growth through the regulation of syntaxin SYP123 expression.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28096354}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}.
Interaction partners:
- Protein GET4
- AT3g13440/MRP15_7
- Outer arm dynein light chain 1 protein
- Trafficking protein particle complex subunit
- Conserved oligomeric Golgi complex subunit 1
- Trafficking protein particle complex II-specific subunit 130 homolog
- acid phosphatase
- Tetratricopeptide repeat
- Vacuolar protein sorting-associated protein 32 homolog 2
- At1g77230
Sequence:
MAADLPEATVQNILDQESLKWVFVGGKGGVGKTTCSSILAICLASVRSSVLIISTDPAHNLSDAFQQRFTKSPTLVQGFSNLFAMEVDPTVETDDMAGTDGMDGLFSDLANAIPGIDEAMSFAEMLKLVQTMDYATIVFDTAPTGHTLRLLQFPATLEKGLSKLMSLKSRFGGLMTQMSRMFGMEDEFGEDALLGRLEGLKDVIEQVNRQFKDPDMTTFVCVCIPEFLSLYETERLVQELAKFEIDTHNIIINQVLYDDEDVESKLLRARMRMQQKYLDQFYMLYDDFNITKLPLLPEEVTGVEALKAFSHKFLTPYHPTTSRSNVEELERKVHTLRLQLKTAEEELERVKSG
Protein: DNA-binding protein RAP1 (A0A1D8PIK2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367107}. Chromosome, telomere {ECO:0000256|RuleBase:RU367107}.
Interaction partners:
- Taf145p
- Origin recognition complex subunit 1
- Transcription factor TBF1
Sequence:
MNYPYSSFEDDGQYQTDLSEVASRNADEEAAGHQQQQLQYHRRVQIEEATRQRQQQQQHHQQQSSPSSSDDFNFESQQIKPNRPKNSPPKPIFVDKDGKSMLFYIPEDEPNRNKYRDLIIRYGGVIVEKGFPTVILLSNNEDLYGFSKLKFIDDCIAKNQLLSVFDYGTYGTYNNPEDAAFDTTSIINELNDDLSSNISSSFSTIEGTSSMVEVPVAAPAAIPLPPPPHQQQRSIDAFPNPNINNARRGSSGHRFTIEQDEFILEHIRRKPRFRQSQKFYAQLALLEPLRGHTGNSIRSRFRKHLESRLNYIYKTDDQDQLIRDEAGNLIKIGLDEMPGTLKNKFTPEDDYLLCCVALEYMASNNIDSIGLRYSFFDGMYRKYRNHTLQSWRDRFRKYIRDKSDLVDYKEYYENCEKVGMAPRCLTRIAP
Protein: Conserved oligomeric Golgi complex subunit 8 (COG complex subunit 8) (Component of oligomeric Golgi complex 8) (Q04632)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 5
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 2
- t-SNARE affecting a late Golgi compartment protein 2
- Vacuolar protein sorting-associated protein 53
- Vacuolar protein sorting-associated protein 52
Sequence:
MELILNSLISDDLTEEQKRLSLDFLQDILQSNTKDYESYFSSRAVPGSITEDIAEIDAELSALDRKIRKTLLDNTSQIIGNILENDDRAQLDDIAKSLEQLWELDTNINKAADRNVTNDDINNESVSIDDFLEDDKEDNDTGRIMTTESNNLARKKKEDEFHKALSRLRNRISTKEDDKDDIRSDTLVTVLENLDSITDLMELPFLARTCIRTGHYQEAVMLYTHTTSLRSRFPGSTIVDEVCEKVLNEISTTMLSGLVKLLSTNVSVNSLKKILQYLNSIPPFDGKTNKSLLSVFLAMRYKFITDEIASYPLDVESSNESLIEMMVKRKIEVLREHVYMSLNVFLKSFLYDTNDLEIPFPEELESTVLRINGTNEEKEIEEKEKETKKEEYQKQDSVANNEEDVTENKSIEDVQEEVQGKVEGEDDGAERKTENEIENETVNKTEDKAEKEKEEEVNTKDNKAEKEEEEINKVEVTPEEPSKSIDNKAEKEEEEINKVEVTPEEPSKKIRTSKRENKIPTNAVMLQFVDKCITYVLKDLTRGLNSIKLSDSVCLQLVYCSFRLCDLNRNYHHLFLKKINDTSLFTTEQLARAIDKRAELASKYIYS
Protein: Alpha-hemolysin (Alpha-HL) (Alpha-toxin) (P09616)
Organism: Staphylococcus aureus
Function: Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis. Human RBCs bind much less alpha-toxin than do rabbit RBCs. Heptamer oligomerization and pore formation is required for lytic activity.
Subcellular location: Secreted {ECO:0000269|PubMed:8943190}. Note=Secreted as a monomer (PubMed:8943190). After oligomerization and pore formation, the complex is translocated across the bilayer, probably via the Gly-rich domain of each strand. {ECO:0000269|PubMed:8943190}.
Interaction partners:
Sequence:
MKTRIVSSVTTTLLLGSILMNPVAGAADSDINIKTGTTDIGSNTTVKTGDLVTYDKENGMHKKVFYSFIDDKNHNKKLLVIRTKGTIAGQYRVYSEEGANKSGLAWPSAFKVQLQLPDNEVAQISDYYPRNSIDTKEYMSTLTYGFNGNVTGDDTGKIGGLIGANVSIGHTLKYVQPDFKTILESPTDKKVGWKVIFNNMVNQNWGPYDRDSWNPVYGNQLFMKTRNGSMKAADNFLDPNKASSLLSSGFSPDFATVITMDRKASKQQTNIDVIYERVRDDYQLHWTSTNWKGTNTKDKWTDRSSERYKIDWEKEEMTN