wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoporin NDC1 (Transmembrane protein 48) (Q8VCB1)
Organism: Mus musculus (Mouse)
Function: Component of the nuclear pore complex (NPC), which plays a key role in de novo assembly and insertion of NPC in the nuclear envelope. Required for NPC and nuclear envelope assembly, possibly by forming a link between the nuclear envelope membrane and soluble nucleoporins, thereby anchoring the NPC in the membrane (By similarity).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Central core structure of the nuclear pore complex. {ECO:0000250}.
Interaction partners:
- Nucleoporin NUP35
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup155
- Nucleoporin 205
- Aladin
- Nucleoporin NUP188
- Nuclear pore membrane glycoprotein 210
- Nuclear pore complex protein Nup85
- Nucleoporin Nup43
- Nucleoporin SEH1
Sequence:
MATAASGPCAGGSPRDILWRVLGWRIVTSIVWSVVLLPVCITAFIVLSSINLFHPIQWLSDSCNDFYSSQVIFHLLLLAVVIIIISIFNVEFYTVVPSISGSRLALIARILHPQQLTHSFIHAAMGMAVAWCAAIMTKGQYSSLVVPCTGTESLDSPAAQTCLNEYHLFFLLSGAFMGYSYSLLYFINNMNYLPFPIIQQYKFLRFRRSLLLLVKHSCVESLFMVRNFCIVYYFFGHIPKAWISTALDLHTDEQAHRPLDTIGGLLNVSLLYHVWLCGVFLLVTWYSSWILFKIYATEAHVFPVQPPFAEASDECLPKVLNSNPPRIVKYLALQDLMLLSQYSPSRRQEVFSLSQPGGHPHNWTAISRECLNLLNDMTQKLVLYQEAAATNGRMYSSYSVEPKKLSSAEETAFQTPKPSQTPSVPPLVKTSLFSPKLSTPNVSSPFGTPFGSSVVNRMAGILDVNPFSGSPQSPQLIRRGPRLWTHTSDQQVSAISNPSPCASVTAEGKTVRQPSVIYSWIQNKREQIKNFLSKRVLIMYFFSKHPEASIQAVFSDAQMHIWALEGLSHLVAASFTEDRFGVVQTTLPAILHTLLTLQEAVDKYFKLPHASSKPPRASGSLVDTSYKTLRFAFRASLKTAIYRITTTFGEHLNAVQASAEHQKRLQQFLEFKE
Protein: Probable cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome aa3 subunit 1) (Cytochrome c oxidase polypeptide I) (P9WP71)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protoheme IX farnesyltransferase
- Cytochrome c oxidase subunit 2
- Probable cytochrome c oxidase subunit 3
- Cytochrome bc1 complex cytochrome c subunit
- Cytochrome bc1 complex cytochrome b subunit
- Uncharacterized protein Rv2876
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Probable cytochrome c oxidase polypeptide 4
- Conserved protein
- Uncharacterized protein
Sequence:
MTAEAPPLGELEAIRPYPARTGPKGSLVYKLITTTDHKMIGIMYCVACISFFFIGGLLALLMRTELAAPGLQFLSNEQFNQLFTMHGTIMLLFYATPIVFGFANLVLPLQIGAPDVAFPRLNAFSFWLFVFGATIGAAGFITPGGAADFGWTAYTPLTDAIHSPGAGGDLWIMGLIVAGLGTILGAVNMITTVVCMRAPGMTMFRMPIFTWNIMVTSILILIAFPLLTAALFGLAADRHLGAHIYDAANGGVLLWQHLFWFFGHPEVYIIALPFFGIVSEIFPVFSRKPIFGYTTLVYATLSIAALSVAVWAHHMFATGAVLLPFFSFMTYLIAVPTGIKFFNWIGTMWKGQLTFETPMLFSVGFMVTFLLGGLTGVLLASPPLDFHVTDSYFVVAHFHYVLFGTIVFATFAGIYFWFPKMTGRLLDERLGKLHFWLTFIGFHTTFLVQHWLGDEGMPRRYADYLPTDGFQGLNVVSTIGAFILGASMFPFVWNVFKSWRYGEVVTVDDPWGYGNSLEWATSCPPPRHNFTELPRIRSERPAFELHYPHMVERLRAEAHVGRHHDEPAMVTSS
Protein: TNF superfamily member 10, like (Tumor necrosis factor (Ligand) superfamily, member 10 like) (Q7ZYX9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MATQNNQDYYRSVSSESTTYMMVPANSRGRDSPSKLWIAMVVIVVVVLQIASTTGLFVYLNMSLSQVKSQGVTEELRCLGLLNVLGKDQDIPEDLAQLFGEPCMKLAEGIKAYISKVTDSIISKQTLHAARTRTHSYNTTGSKFMTTVMQRPSAHLTLSSASDNSRPQSDMHQPQFDLHQSCRHPVHTWANKSFGAHLYNMTLTNGRLRVPQDGRYYLYSQVYFRYPSPSDSDQSSVSHQLVQCIYKKTSYLNPIQLLKGVGTKCWAPDAEYALHSVYQGGLFELRAGDEVFVSVSSPTMVYGEDSSSYFGAFRLDL
Protein: GABA(C) receptor (G1SEE5)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- GABA
- GABA
Sequence:
MVAAQNMKFSIFLLWWGWALATEGRMHWPGREVHEMSQKSRPQRQRREAHEDTHKQGSPILKRSPDITKSPLTKSEQLLRIDDHDFSMRPGFGGPAIPVGVDVQVESLDSISEVDMDFTMTLYLRHYWKDERLSFPSTNNLSMTFDGRLVKKIWVPDMFFVHSKRSFIHDTTTDNVMLRVQPDGRVLYSLRVTVTAMCNMDFSRFPLDTQTCSLEIESYAYTEDDLMLYWKKGNDSLKTDERISLSQFLIQEFHTTTKLAFYSSTGWYNRLYINFTLRRHIFFFLLQTYFPATLMVMLSWVSFWIDRRAVPARVPLGITTVLTMSTIITGVNASMPRVSYIKAVDIYLWVSFVFVFLSVLEYAAVNYLTTVQERKERKLREKLPCTCGLPQPRAVMLDGSYSDVEVNDLSSFVPDNGEKPDRMMVQLTLASERSSPQRKSQRSSYVSMRIDTHAIDKYSRIIFPAAYILFNLIYWSIFS
Protein: LD31742p (Withered, isoform A (EC 2.3.1.21)) (Withered, isoform B) (Q7JQH9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAEAHAAVAFSFAITHEGFDINYDHEVLNLVWNSGVRSWKKRLARARNGVRNGVYPAHIQSLWLISAIALGLHFAGYQAPFNLTNRILVHLPSNTINWQVTACFLAALVVWLSICFTMRYTLKLLLMYKGWMYESRAPGSRVSLPTMLWVAVVRVLSSWNKPGLYSFQGSLPRLPLPSVKDTMTRYLRSVRPLLDDENYTRMERLAKEFEQTIGKKLQWYLILKSWWSTNYVSDWWEEYVYLRGRSPLCVNSNFYGTDAIFMNLTDKQAARAANVISLLLNFRRLIEHQELQPIMVQGMIPLCSWQYERTFNTARVPGLETDRIIHYRDSNHIVVLHKGCYYKMLIYYKGRILRPCELQVQIEEILKGKATPVEGEEHLAALTAWNRSKWAEARNTFFSWGVNQTSLRTIESAAFVLSLDDEPFEFDLARPELLDNFGKKLLHGNGYNRWFDKCFTVCVGTNGRVGFNAEHTWADAPVLGHLWEYIFGDDIYGYDETGNTKGTPAFQPPTPTRLTWDLKPCLAQIEEATIDVTKLINEVNLRILVHQDYGKGFMKKCRISPDAYIQMALQLAYYRDAGRFSLTYEASMTRLFREGRTETVRPCTIESSAWVKAMQNPNTTNDERVKMMQAACDRHQLGYQDAMCGRGIDRHLFCLYVVSKYLEVDSPFLNEVLSEPWRLSTSQTPHGQTPKMDLKKHPNCISAGGGFGPVADDGYGVSYIIAGENLIFFHISAKTTCQQTDVHRFAQNISQALSDIRSMFEQHMKDHPKPAKSLTNGKST
Protein: DNA ligase 1 (EC 6.5.1.1) (DNA ligase I) (Polydeoxyribonucleotide synthase [ATP] 1) (P12000)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Subcellular location: Nucleus.
Interaction partners:
- Flap endonuclease 1
- Proliferating cell nuclear antigen
- Exodeoxyribonuclease 1
- DNA ligase 3
- DNA polymerase delta catalytic subunit
- Serine/threonine-protein kinase chk1
- DNA replication ATP-dependent helicase/nuclease dna2
- DNA polymerase epsilon catalytic subunit A
- Replication factor C subunit 2
- ATP-dependent DNA helicase II subunit 2
Sequence:
MRTVFSQIPRFKQVNQYIRMSTRQSDISNFFISSASHKSEHVEVSQSSSDSKNVDGRSTSEKRKVESVKLVDESKHNNHDDTGTQNVERENNIVSEAKKQKTLGSSSSSSDAVSSNNDSGASTPIPLPIKEPPLESNARNDKLKGHATFAEMVKAFTKIENTSKRLEIIDIMGTYFFGILRDHPSDLLACVYLSINKLGPDYSGLELGIGESIIMKAIGESTGQTLQQIKLSFHKVGDLGLVAQTSRQNQPTMFKPAALTIPFLFDSLKKIAQMSGNQSQNRKIGVIKRLLSSCEGAEPKYLIRALEGKLRLQLAEKTILVALANATAQYHADKNGEKLSQQDRIEGEQILRDVYCQLPSYDLIVPHLIEHGLGTLRETCKLTPGIPTKPMLAKPTKQISEVLNTFDQAAFTCEYKYDGERAQVHFTEDGKFYVFSRNSENMSVRYPDISVSVSKWKKPDARSFILDCEAVGWDRDENKILPFQKLATRKRKDVKIGDIKVRACLFAFDILYLNGQPLLETPLNERRKLLYSMFQPSTGDFTFAKHSDQKSIESIEEFLEESVKDSCEGLMVKMLEGPDSHYEPSKRSRHWLKVKKDYLSGVGDSLDLIVIGAYYGKGKRTSVYGAFLLGCYDPDTETVQSICKLGTGFSEEHLETFYNQLKDIVISKKKDFYAHSDVPAHQPDVWFEPKYLWEVLAADLSLSPVYKAAIGYVQEDKGISLRFPRFIRIREDKSWEDATTSEQVSEFYRSQVAYSQKEKEGSPAAEDY
Protein: T-cell defective protein 2 (Q9N428)
Organism: Caenorhabditis elegans
Function: May act synergistically with the Wnt pathways to control T-cell fate specification, gonad development, and P12 cell fate specification. Required for the distribution of pop-1 and tlp-1 proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:12679102}. Cytoplasm {ECO:0000269|PubMed:12679102}. Note=Cytoplasmic in neurons and nuclear in T-cells.
Interaction partners:
Sequence:
MFSPDTNSEFYDDFYTKYNTNMAPTTSTFNAQPRLSLDSGLGLTNDSFYSTDLNETHLMDISAGNASTSFQSQPPPQLESSPPTKWARIRTPPNRKKKISHEGPNQEALPPGFNLFSPPSRKKIKTAFSSPPPKSMKTPDSLRKSIRISSPSPFKVTFSKTPLKLSNNENVTGIHIGRSGTYYNKQVTGSASKRCLLPSKPDGFTFLGSPGNSDVLDFPLQTTFEGFGDLDTPAKINAALEVNNDDSMDYYQYAGMIETSSSLATYTNSTGPLVENHARNLKSVPISRTASRNLMKISRKSVEEPVPEPQAVHVEPVIEKPTKISAKKEKEQKKSAAKEAALKEAKEKEMRIWKLAPFETPKKEVPLYSGRWLVISTGRTLAQQELFSDAKSFFKANPPPAPRAPQAPELASGPRRIPTIQRVTLFKHRYRSPRD
Protein: Follicle-stimulating hormone receptor (FSH-R) (Follitropin receptor) (P23945)
Organism: Homo sapiens (Human)
Function: G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11847099, ECO:0000269|PubMed:24692546}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Follitropin subunit beta
- Glycoprotein hormones alpha chain
- Thyrotropin subunit beta
- Guanine nucleotide-binding protein G
- Bone morphogenetic protein 15
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
- Pro-glucagon
- Growth/differentiation factor 9
- Natriuretic peptides A
Sequence:
MALLLVSLLAFLSLGSGCHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFSGFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPNLQYLLISNTGIKHLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVGLSFESVILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLKKLPTLEKLVALMEASLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSSLAEDNESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILRVLIWFISILAITGNIIVLVILTTSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIHTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLTAITLERWHTITHAMQLDCKVQLRHAASVMVMGWIFAFAAALFPIFGISSYMKVSICLPMDIDSPLSQLYVMSLLVLNVLAFVVICGCYIHIYLTVRNPNIVSSSSDTRIAKRMAMLIFTDFLCMAPISFFAISASLKVPLITVSKAKILLVLFHPINSCANPFLYAIFTKNFRRDFFILLSKCGCYEMQAQIYRTETSSTVHNTHPRNGHCSSAPRVTSGSTYILVPLSHLAQN
Protein: Ubiquitin-conjugating enzyme E2 variant 1 (UEV-1) (CROC-1) (TRAF6-regulated IKK activator 1 beta Uev1A) (Q13404)
Organism: Homo sapiens (Human)
Function: Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UBE2N, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production. UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:11076860, ECO:0000269|PubMed:9305758}. Note=Excluded from the nucleolus.
Interaction partners:
Sequence:
MAATTGSGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTIYENRIYSLKIECGPKYPEAPPFVRFVTKINMNGVNSSNGVVDPRAISVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQCYSN
Protein: Succinate-semialdehyde dehydrogenase [NADP(+)] 1 (SSA dehydrogenase 1) (SSADH 1) (SSDH 1) (EC 1.2.1.16) (Q9US47)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 4-aminobutyrate aminotransferase
- Succinate-semialdehyde dehydrogenase [NADP
- Probable citrate synthase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
- Malate dehydrogenase, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- Probable ATP-citrate synthase subunit 2
- Probable ATP-citrate synthase subunit 1
Sequence:
MSTSSKLSTNIKDLSLFDLEEFPARSYIGGKWVTAASGKTFDVENPGLNETLAPVTDMSVEETRKAIKVAHEAFLSYRNSDIKERYAILRRWYDLIMENADDLATMMTLENGKALGDAKGEVVYAAKFIDWFAGEALRISGDSSMSSNPQNRIITIKQPVGVVGIITPWNFPAAMITRKVGAALAAGCTVVIRPAAETPFTALALAKLAERAGVPAGVLNMVTANSPSEHGIELTTNPLIRKVSFTGSTNVGKILAKQSSSTLKKLSLELGGNAPFIVFEDADLEKAADALMACKFRGSGQTCVCANRIYVHSSVYDAFVDLVTERVSKFKLGYGLDAGVTHGPLISEKAISKVKQHVEDAVQKGGVVVTGGKVASNLGPMYFEPTVIINAKQGMLISEEETFGPVGALFKFDTEDEVVAWANDSPVGLAGYLFSKDISRVFRVGEALQVGMVGCNTGLVSDVLSPFGGVKESGFGREGSKYGISEYLDIKSLTISTL
Protein: Electron transfer flavoprotein subunit alpha (Alpha-ETF) (H0YK49)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|PIRNR:PIRNR000089}.
Interaction partners:
Sequence:
MFRAAAPGQLRRANLLPRVAAKLEVAPISDIIAIKSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFDAAATSGGSASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLFKVVPEMTEILKKK
Protein: Uncharacterized protein (Q57TW1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYQMNDTKEQKQTATISLSTMEEKMTKIDTVIGSALFGANRPKETGTPYTSAGGGEVYFNPSNLLGYVWNYVKDERARGDSSGMGVSGPDLHMRPPQWMEDKNVSIDGTPLTEEELRAPNFWQTKYKRELDIGEAIQEVKRTRRTEATHDIVGSISWLGRKLGWSEPLDEQYARKKVEERYRLLGGQDTTGSVVDEATTGQKIGVATPWKVLLESVETGRPVAKVANERRLCVDFYGVDHFFDARLPLIWFTTKCGIAVGIIQGSLKAIQAVNVDVQFLKASGVGILSILNMSVFASVVKWGGNCALFSTAFCFGDSLATSLKYFLLPPHDARQRSILNYSLGFAMSGSTVGILPWWILSDMSLAFRLSVSGAFVGGILGLAVGTVMRRLVILNTTRLEATNRELRRYEALMRRQRCWVEEERLKATNQRLVWW
Protein: At2g29660 (Expressed protein) (Zinc finger (C2H2 type) family protein) (O82389)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAARKLGSLLRQYFFSLCFLFLGCFFFPKDADYKQKRRKKKLRRVSSSSGSSLSSSWTYLKRVFLSTTRISKSRNQTHPNVTLTSARSSQNSLVTLVQPDTTNQPDPETRIHQQTEFEISSSDEIFPCNSCGEIFPKINLLENHIAIKHAVSELIAGESSTNIVKIIFKSGWPEQGNYKSPVINRILKIHNSSKILTRFEEYREFVKAKAARSNGGGRRWDDERCVADGNELLRFYCSTFMCDLGQNGKSNLCGHQYCSICGIIGSGFSPKLDGIATLATGWRGHVAVPEEVEEEFGFMNVKRAMLVCRVVAGRVGCDLIDDDDVDKSDGGGYDSLVGQSGNKSGALLRIDDDELLVFNPRAVLPCFVIVYTV
Protein: Protein phosphatase (EC 3.1.3.16) (Q57Z96)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGGQSSVTTTPEQIPVNGKSLDWGPPPDDIPEEERDNEELVLQTWAFCKAKPSPAQNYRSDVEERKRRQSMLWRKRASFIELDCGEDSFFVSNTYKVIGVADGVGGWRDEGVDASHFANSLMENAKHFSETHRKELNPEVILQSAFDKVLHDKVVKAGSSTACVVALQKDSSGEHYLDVANVGDSGVLVVRNRQVQHRVHEKVHGFNAPFQLAVLPPHLQGRAFSDRVSDATREKIPVQRGDVVITGTDGLFDNRFNISLAADAGWIGHVQGSALERVPLVGLLLGPIFANDKVAYVDPQRVAQRIVQDAYKTSLDESAHTPWASMLRKFGVEDAKGGKVDDITLVLSRVTTREELNATSTW
Protein: Protein TANC1 (Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1) (Q0VGY8)
Organism: Mus musculus (Mouse)
Function: May be a scaffold component in the postsynaptic density.
Subcellular location: Postsynaptic density {ECO:0000250}.
Interaction partners:
- Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3
Sequence:
MLKAVLKKSREGGKGSKKEAGGDFGSETPALSSSGDSPVNSLSTTEDTYRVSLAKGVSMSLPSSPLLPRQSLLTQSRSNKKSPGPVRKPKYVESPRVPGDPVMIPFGEGSKPSEPSATEAKADNEPSCSPAAQELLTRLGFLLGEGIPSATHITIEDKNEAMCTALSQGISPCSTLTSSTASPSTDSPCSTLNSCVSKTAASKSPCETISSPSSTLESKDSGIIATITSSSENDDRSGSSLEWNRDGSLRLGVQKGVLHDRRADNCSPVAEEETTGSAESVLPKAEPSAGDGPVPYPQSSGSLIMPRPNSVAATSSTKLEDLSYLDGQRNAPLRTSIRLPWHNTAGGRAPEVKARFAPYKPQEILLKPLLFEVPSITTDSVFVGRDWLFHQIEENLRNTELAENRGAVVVGSVGFGKTAIISKLVALSCHGSRMRQIASSSPSLSPKSSDPTQDLPGTPLLSPSSSTSALSVTRTPAGPGTADSQRPREDAVKYLASKVVAYHYCQADNTYTCLVPEFVHSIAALLCRSHQLAAYRDLLIKEPQLQSMLSLRSCVQDPVAAFKRGVLEPLTSLRNEQKIPEEEYIILIDGLNEAEFHKPDYGDTLSSFITKIIPKFPTWLKLIVTVRANFQEIISALPFVKLSLDDFPDNKDIHSDLHAYVQHRVHSSQDILSNISLNGKADAALISKVSSHLVLRSLGSYLYLKLTLDLFQRGHLVIKSASYKVVPVSLSELYLLQCNMKFMTQSAFDRALPILNVALASLHPMTDEQIFQAINAGHIQGEQGWEDFQQRMEALSCFLIKRRDKTRMFCHPSFREWLVWRADGESTAFLCEPRNGHALLAFMFSRQESKLNRQQTMELGHHILKAHIFKGLSKKTGVSSSHLQALWIGYSTEGLSAALASLRNLYTPNVKVSRLLILGGANVNYRTEVLNNAPILCVQSHLGHEEVVTLLLEFGACLDGMSENGMNALCYAAAAGHMKLVCLLIKKGARVDHLDKKGQCALVHSALRGHSDILQYLLNCEWSAGPPQPGTLRKSQALQQALTAAASMGHSSVVQSLLGMAEEHEIEVNGTDTLWGETALTAAAGRGKVEICELLLERGAAVSRANRRGVPPLFCAARQGHWQVVRLLLDRGCDVNLSDKQGRTPLMVASCEGHLSTVEFLLSKGAALSSLDKEGLSALSWACLKGHRAVVQYLVEEGAEIDQTDKNGRTPLDLAAFYGDAETVLYLVEKGAVIEHVDHSGMRPLDRAIGCRNTAVVVTLLRKGAKLGNAAWAMATSKPDILIILLQKLVEEGNVMYKKGKMKEAAQRYQYALRKFPREGLGEDMRPFNELRVSLYLNLSRCRRKTNDFGLAEEFASKALELKPKSYEAFYARARAKRNSRQFLAALADLQEAVKLCPNNQEIKRLLARVEEECKQLQRNQQQKQQGPPPAPANDSDNEEDAPASSLKDHFPIEEAEEEDTSSQEESISPTPRSQPPPSVPSPYIRNLQEGLQSKGRSASPQSRAGISKSLRETVAQSGLVMQPTKQAQIVKTNQHLGSGQSSMRNSSTKIQVSSQNPPPSPMPGRVSAAPAVSRNQHLEGTGPFTAGTGCGHFGDRLGASQSLQLQRSESGTAYPLPSKVKAAERLLAHASVAVDMAPPNQGGPVSCSDVRHPASLSSSGSSGSPSSSIKMSSSTSSLTSSSSVSDGFKVQGPDSRIRDKGTTQVQGGTAEHRPRNTPFMGIMDKTARFQQQSNPPNRSWHCPVAEGLLTNTATAAGLQSNSEKPTLKPGGYCSQAKPCSVPPLSMGVHNGAQVKELEENKCQIPALCQDNRITKGVPHLYPEGVSKQPLHVSTEAHRSHLTSAKPKRSFIESNV
Protein: Transforming acidic coiled-coil containing protein 1 (E7EVI4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTEGSMGVTLEASAEADLKAGNSCPELVPSRRSKLRKPKPVPLRKKAIGGEFSDTNAAVEGTPLPKASYHFSPEELDENTSPLLGDARFQKSPPDLKETPGTLSSDTNDSGVELGEESRSSPLKLEFDFTEDTGNIEARKALPRKLGRKLGSTLTPKIQKDGISKSAGLEQPTDPVARDGPLSQTSSKPDPSQWESPSFNPFGSHSVLQNSPPLSSEGSYHFDPDNFDESMDPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLITSGCKVKKHETQSLALDACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSAGAEVKGIEKETCQKMEEDGSTVLGLLESSAEKAPVSVSCGGESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKTD
Protein: NADPH oxidase organizer 1 (NADPH oxidase regulatory protein) (Nox organizer 1) (Nox-organizing protein 1) (SH3 and PX domain-containing protein 5) (Q8NFA2)
Organism: Homo sapiens (Human)
Function: Constitutively potentiates the superoxide-generating activity of NOX1 and NOX3 and is required for the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity. Isoform 3 is more potent than isoform 1 in activating NOX3. Together with NOXA1, may also substitute to NCF1/p47phox and NCF2/p67phox in supporting the phagocyte NOX2/gp91phox superoxide-generating activity.
Subcellular location: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:12716910}; Peripheral membrane protein {ECO:0000269|PubMed:12716910}; Cytoplasmic side {ECO:0000269|PubMed:12716910}. Note=Isoform 3 associates with the plasma membrane in a lipid-dependent manner (PubMed:12716910).
Interaction partners:
- Cytochrome b-245 light chain
- NADPH oxidase 1
- Neutrophil cytosol factor 2
- NADPH oxidase activator 1
- Neutrophil cytosol factor 4
- Neutrophil cytosol factor 1
- NADPH oxidase 3
- NADPH oxidase 2
- Ras-related C3 botulinum toxin substrate 2
- Dual oxidase 1
Sequence:
MAGPRYPVSVQGAALVQIKRLQTFAFSVRWSDGSDTFVRRSWDEFRQLKKTLKETFPVEAGLLRRSDRVLPKLLGQASLDAPLLGRVGRTSRGLARLQLLETYSRRLLATAERVARSPTITGFFAPQPLDLEPALPPGSRVILPTPEEQPLSRAAGRLSIHSLEAQSLRCLQPFCTQDTRDRPFQAQAQESLDVLLRHPSGWWLVENEDRQTAWFPAPYLEEAAPGQGREGGPSLGSSGPQFCASRAYESSRADELSVPAGARVRVLETSDRGWWLCRYGDRAGLLPAVLLRPEGLGALLSGTGFRGGDDPAGEARGFPEPSQATAPPPTVPTRPSPGAIQSRCCTVTRRALERRPRRQGRPRGCVDSVPHPTTEQ
Protein: Serine/threonine-protein kinase 4 homolog A (EC 2.7.11.1) (Kinase responsive to stress A) (STE20-like kinase krsA) (O61125)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulates both cAMP signaling during early development and the stress response. Functions as an activator of adenylylcyclase.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16842885}.
Interaction partners:
Sequence:
MSTLNVPKETMSRKDPEKFFTIVEKLGEGSYGSVYKAINISTGIVVAIKKVSVDNDLEDMEKEISFMKQCKSPYIVTYYASFRKENEVWIVMEHCGAGSVCDAMKITDKTLSEDQIAVVSRDVLQGLAYLHSVRKIHRDIKAGNILMNHKGESKLADFGVSGQLSDTMAKRQTVIGTPFWMAPEVIQEIGYDYKADIWSYGITCIEMAESKPPLFNVHPMRVIFMIPNPSRPPPKLTEPEKWSPEFNDFLAKCLTRKPELRPSAEELLKHPFITKAKSHSLLVPLIDEQDIIINEKGREVALGIEQRDEEEEDEDEDSEDSDDNRGTMVRAKPRSMQNSGGEDNDEEYDTGTMVITDNKNSYDTVVFNNDDEDSGTMKLKNTMPSNKKNFVPDYMNQFKKSDDDVTNVPLSDKYSSYSLEELKKMLAELEIEREKEVQKTLEKFSINRQALLAVIDEKKSK
Protein: Trophinin (G5E9N2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRRNDYGYRVPLFQGPLPPPGSLGLPFPPDIQTETTEEDSVLLMHTLLAATKDSLAMDPPVVNRPKKSKTKKAPIKTITKAAPAAPPVPAANEIATNKPKITWQALNLPVITQISQALPTTEVTNTQASSVTAQPKKANKMKRVTAKAAQGSQSPTGHEGGTIQLKSPLQVLKLPVISQNIHAPIANESASSQALITSIKPKKASKAKKAANKAIASATEVSLAATATHTATTQGQITNETASIHTTAASIRTKKASKARKTIAKVINTDTEHIEALNVTDAATRQIEASVVAIRPKKSKGKKAASRGPNSVSEISEAPLATQIVTNQALAATLRVKRGSRARKAATKARATESQTPNADQGAQAKIASAQTNVSALETQVAAAVQALADDYLAQLSLEPTTRTRGKRNRKSKHLNGDERSGSNYRRIPWGRRPAPPRDVAILQERANKLVKYLLVKDQTKIPIKRSDMLRDVIQEYDEYFPEIIERASYTLEKMFRVNLKEIDKQSSLYILISTQESSAGILGTTKDTPKLGLLMVILSVIFMNGNKASEAVIWEVLRKLGLRPGVRHSLFGEVRKLITDEFVKQKYLEYKRVPNSRPPEYEFFWGLRSYHETSKMKVLKFACRVQKKDPKDWAVQYREAVEMEVQAAAVAVAEAEARAEWFQHQHWLYWRTQHQHGLQ
Protein: Copper transport protein ATOX1 (Metal transport protein ATX1) (O08997)
Organism: Mus musculus (Mouse)
Function: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense (By similarity).
Interaction partners:
- Copper-transporting ATPase 1
- Copper-transporting ATPase 2
- Extracellular superoxide dismutase
- High affinity copper uptake protein 1
- Cytochrome c oxidase copper chaperone
- Copper chaperone for superoxide dismutase
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- Cytochrome c oxidase assembly protein COX11
- Protein SLC31A2
- COMM domain-containing protein 1
Sequence:
MPKHEFSVDMTCEGCAEAVSRVLNKLGGVEFNIDLPNKKVCIDSEHSSDTLLATLNKTGKAVSYLGPK
Protein: Copper transport protein ATOX1 (Metal transport protein ATX1) (G5EE41)
Organism: Caenorhabditis elegans
Interaction partners:
- P-type Cu
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- Cytochrome c oxidase copper chaperone
- Copper homeostasis protein cutC homolog
- Cytochrome c oxidase assembly protein COX11
- MATH domain containing
- RNA polymerase I-specific transcription initiation factor tif-1A
- Ubiquitin-ribosomal protein eL40 fusion protein
- NTF2-related export protein
Sequence:
MTQYVFEMGMTCNGCANAARKVLGKLGEDKIKIDDINVETKKITVTTDLPASDVLEALKKTGKEIKQLQ
Protein: Arginine kinase (AK) (EC 2.7.3.3) (P51541)
Organism: Limulus polyphemus (Atlantic horseshoe crab)
Function: Catalyzes the reversible transfer of the terminal phosphoryl group of ATP to L-arginine.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MVDQATLDKLEAGFKKLQEASDCKSLLKKHLTKDVFDSIKNKKTGMGATLLDVIQSGVENLDSGVGIYAPDAESYRTFGPLFDPIIDDYHGGFKLTDKHPPKEWGDINTLVDLDPGGQFIISTRVRCGRSLQGYPFNPCLTAEQYKEMEEKVSSTLSSMEDELKGTYYPLTGMSKATQQQLIDDHFLFKEGDRFLQTANACRYWPTGRGIFHNDAKTFLVWVNEEDHLRIISMQKGGDLKTVYKRLVTAVDNIESKLPFSHDDRFGFLTFCPTNLGTTMRASVHIQLPKLAKDRKVLEDIASKFNLQVRGTRGEHTESEGGVYDISNKRRLGLTEYQAVREMQDGILEMIKMEKAAA
Protein: Sulfite oxidase, mitochondrial (EC 1.8.3.1) (Q07116)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidation of sulfite to sulfate, the terminal reaction in the oxidative degradation of sulfur-containing amino acids.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:6181785, ECO:0000269|PubMed:8276806}.
Interaction partners:
- Ethylmalonic encephalopathy 1
- Thiosulfate sulfurtransferase
- 3-mercaptopyruvate sulfurtransferase
- 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- NADH-cytochrome b5 reductase 3
- Molybdopterin synthase catalytic subunit
- NADH-cytochrome b5 reductase 1
- Cysteine dioxygenase type 1
- NADH-cytochrome b5 reductase 2
- Molybdenum cofactor biosynthesis protein 1
Sequence:
MLPRLYRSVAVGLPRAIRAKSTPLRLCIQACSSSDSLKPQHPSLTFSDDNSRTRGWKVMGTLIGLGAVLAYHDHRCRASQESPRIYSKEDVRSHNNLKTGVWVTLGSEVFDVTKFVDLHPGGQSKLMLAAGGPLEPFWALYAVHNQPHVRELLAEYKIGELNPEDRMSPPLEASDPYSNDPMRHPALRINSQRPFNAEPPPELLTESYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHRLRETEAHVCFEGLDSDPTGTAYGASIPLARAMDPQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTVDFDLAPSIQELPIQSAITQPQDGTTVESGEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQHPRKAWAWRIWQLKAHVPAEQKELNIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQVVP