wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma-tubulin complex component 4 homolog (Gamma-ring complex protein 75 kDa) (d75p) (dGrip75) (Q9VKU7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000305}.
Interaction partners:
- Gamma-tubulin complex component
- Grip163
- Gamma-tubulin complex component 2 homolog
- Tubulin gamma-1 chain
- Gamma-tubulin complex component 3
- Grip71
- Tubulin gamma-2 chain
- Testis-specific gamma-tubulin ring protein 91
- GEO02508p1
- Gamma-tubulin complex component
Sequence:
MIHDLLLACRSHNPEQLGIKAFNETTVIDQFIHPCEREIFMDIIKIIKVYQEVEQFTHSSGRKSDTHGELPDSLHGYYLLNLAKGIEMALEEYYAEIGRLEKYCLGNERNSLSYVYNALYAKFPLLVFMRNLITEIHVLNLRGCVLLHNLHQQCEHGDIQLEKAIKIIMKPVKNAFFSSLAHWLLFGVIDDVHSEFFIKFTPTDAVDGSSFSKSATCSLLSAEKNPEDYIWQYEVNMSQLPGFFSIVLAEKVLFVGQTVLVFKMGRNVKVKNKTDPLAAKLAELDSDDIYQLWSGRESEFFKMVVDLSNEDTINVFRLEKVIIDIKNYVSARLSEIAVNEVDLERQMGLIKDFFLLGRGEFYLEFCSQMVGTMETYREERFKNVTRSFELAATVTGITDDLDKFSLICQRSTSEPDDTSDFNFLQGLSLKYEYEWPLNLLFSPTTIERYNNIFRFLLIIRTYQYEIQRVWAKQTWRAKSAKDVPPNNKIITLRNYLMFFLNNMQYYIQVDVLESQFGILMNVIKSRSDFEVIQRAHTVFLANVLSHCFLLNESETQLNVTGSQNRNPIYGTLLKLFGICEKFAHMTQTKDPSDDLEDEVDQLNESFGVQIASLIQLLVDVKSASCLGPLSQLLLRLDFNCWFSASHNTSA
Protein: Non-structural maintenance of chromosomes element 1 homolog (Non-SMC element 1 homolog) (EC 2.3.2.27) (Q8WV22)
Organism: Homo sapiens (Human)
Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair. NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair. MAGEF1-NSMCE1 ubiquitin ligase promotes proteasomal degradation of MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19 impairs the activity of several DNA repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters as cofactors.
Subcellular location: Nucleus {ECO:0000269|PubMed:18086888}. Chromosome, telomere {ECO:0000305|PubMed:18086888}.
Interaction partners:
- Non-structural maintenance of chromosomes element 3 homolog
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosomes element 4 homolog A
- E3 SUMO-protein ligase NSE2
- Structural maintenance of chromosomes protein 5
- EP300-interacting inhibitor of differentiation 3
- SMC5-SMC6 complex localization factor protein 2
- Small ubiquitin-related modifier 4
- Melanoma-associated antigen F1
- Zinc finger protein 597
Sequence:
MQGSTRRMGVMTDVHRRFLQLLMTHGVLEEWDVKRLQTHCYKVHDRNATVDKLEDFINNINSVLESLYIEIKRGVTEDDGRPIYALVNLATTSISKMATDFAENELDLFRKALELIIDSETGFASSTNILNLVDQLKGKKMRKKEAEQVLQKFVQNKWLIEKEGEFTLHGRAILEMEQYIRETYPDAVKICNICHSLLIQGQSCETCGIRMHLPCVAKYFQSNAEPRCPHCNDYWPHEIPKVFDPEKERESGVLKSNKKSLRSRQH
Protein: UPF0098 protein YbcL (P77368)
Organism: Escherichia coli (strain K12)
Subcellular location: Periplasm {ECO:0000269|PubMed:11439028}.
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator YbcM
- Multidrug transporter EmrE
Sequence:
MKTLIVSTVLAFITFSAQAAAFQVTSNEIKTGEQLTTSHVFSGFGCEGGNTSPSLTWSGVPEGTKSFAVTVYDPDAPTGSGWWHWTVVNIPATVTYLPVDAGRRDGTKLPTGAVQGRNDFGYAGFGGACPPKGDKPHHYQFKVWALKTEKIPVDSNSSGALVGYMLNANKIATAEITPVYEIK
Protein: Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH3 (EC 2.1.1.367) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Protein SET DOMAIN GROUP 19) (Suppressor of variegation 3-9 homolog protein 3) (Su(var)3-9 homolog protein 3) (Q9C5P4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:11691919}. Chromosome, centromere {ECO:0000269|PubMed:11691919}. Note=Associates with centromeric constitutive heterochromatin.
Interaction partners:
- Calmodulin-lysine N-methyltransferase
- At5g64360
- Tetratricopeptide repeat
- Chaperone DnaJ-domain superfamily protein
Sequence:
MQGVPGFNTVPNPNHYDKSIVLDIKPLRSLKPVFPNGNQGPPFVGCPPFGPSSSEYSSFFPFGAQQPTHDTPDLNQTQNTPIPSFVPPLRSYRTPTKTNGPSSSSGTKRGVGRPKGTTSVKKKEKKTVANEPNLDVQVVKKFSSDFDSGISAAEREDGNAYLVSSVLMRFDAVRRRLSQVEFTKSATSKAAGTLMSNGVRTNMKKRVGTVPGIEVGDIFFSRIEMCLVGLHMQTMAGIDYIISKAGSDEESLATSIVSSGRYEGEAQDPESLIYSGQGGNADKNRQASDQKLERGNLALENSLRKGNGVRVVRGEEDAASKTGKIYIYDGLYSISESWVEKGKSGCNTFKYKLVRQPGQPPAFGFWKSVQKWKEGLTTRPGLILPDLTSGAESKPVSLVNDVDEDKGPAYFTYTSSLKYSETFKLTQPVIGCSCSGSCSPGNHNCSCIRKNDGDLPYLNGVILVSRRPVIYECGPTCPCHASCKNRVIQTGLKSRLEVFKTRNRGWGLRSWDSLRAGSFICEYAGEVKDNGNLRGNQEEDAYVFDTSRVFNSFKWNYEPELVDEDPSTEVPEEFNLPSPLLISAKKFGNVARFMNHSCSPNVFWQPVIREGNGESVIHIAFFAMRHIPPMAELTYDYGISPTSEARDESLLHGQRTCLCGSEQCRGSFG
Protein: 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase (EC 2.4.1.283) (Neomycin biosynthesis protein 8) (Neo-8) (Neomycin biosynthesis protein D) (Q53U18)
Organism: Streptomyces fradiae (Streptomyces roseoflavus)
Function: Glycosyltransferase involved in the biosynthesis of neomycin by mediating conversion of 2-deoxystreptamine (2-DOS) to 2'-N-acetylparomamine using UDP-alpha-D-glucosamine as sugar donor.
Interaction partners:
Sequence:
MRVLRLTPFFHHDCVTAWPAEFDAVGGMQVQILRLSRELADRGVEQLVMTVGFPGLPRERVDRPGLRVRVTRAPLPRLRSELTGLVGLNQAWLAAVLTACAPLRRTWRPDLVHVHADGQLWALLAGPLVSRLVGAPYCLTLHCSRLASYEPMSRFDRLQHRLVAAAERYALRRARRVSTLTSRTADTVARLLPLDRALVDVLPDSVGDVRPVARPEAEEYVRSLGVPAGRPVVGWVGRVAHEKGWRDFVAMAERWDAGSGAPGAVFAVVGDGPQRERMREAVEAAGLADRFVFTGFLPHDAVPSVMTALDVLVMPSAHEELGGSALEAMVCGTPVAGYAVGGLRDTVGSVTPSLLVPRGDVAALTRAAGDAVTDAERHRKTVAAAVPDLLGRYGADTVERALEHYRLAVGRASGGGAGWAP
Protein: Replication in mitochondria 2, isoform D (M9NDD0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MAISHCGISSTTPKSMSIVQCLRHIVQNEGPRALFKGLGPNLVGVAPSRAIYFCTYSQTKNTLNSLGFVERDSPLVHIMSAASAGFVSSTATNPIWFVKTRMQLDYNSKVQMTVRQCIERVYAQGGVAAFYKGITASYFGICETMVHFVIYEFIKSKLLEQRNQRHTDTKGSRDFLEFMMAGAVSKTIASCIAYPHEVARTRLREEGNKYNSFWQTLHTVWKEEGRAGLYRGLATQLVRQIPNTAIMMATYEAVVYVLTRRFNNKSNEFYDF
Protein: cAMP-dependent protein kinase (EC 2.7.11.11) (Q5AP71)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Adenylate cyclase
- Ras-like protein 1
- Ras2p
- Enhanced filamentous growth protein 1
- cAMP-dependent protein kinase
- Stress-responsive transcriptional activator
- Mitogen-activated protein kinase MKC1
- Phosphodiesterase
- Transcriptional regulator EFH1
Sequence:
MTSMEPADTSIRSLNDINLQELANKQHQRNIYAQGSPTLEDSITSNGNDINNPNNNINKTNNNSNSSLSLTKKTSRHINKDTTTKGKYTLNDFQILRTLGTGSFGRVHLTRSIHNGRFYAMKVLKKQRVVQMKQIEHTNDERRMLKLAQHPFIIRMWGTFQDCHNLFMIMDYIEGGELFSLLRKSQRFPTPVAKFYAAEVFLAIEYLHSLDIIYRDLKPENILLDKNGHIKLTDFGFAKEVQDVTYTLCGTPDYIAPEVVATKPYNKSVDWWSFGILIFEMLTGYTPFYDPTPMKTYENILNGSITYPDYLPPDILDLLQKLIVKDLTQRLGNLQGGSDDVKNHPWFKEVIWERLLSRDIETPYEPPITSGVGDTSQFDRYPEDKDLDYGISGVEDPYRDQFQDF
Protein: Adenosylhomocysteinase (AdoHcyase) (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase) (P10819)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Interaction partners:
- Methionine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine beta-synthase
- Cysteine synthase
- Cystathionine gamma-lyase
- Kynurenine--oxoglutarate transaminase
- Cobalamin-independent methionine synthase MetE C-terminal/archaeal domain-containing protein
- S-adenosylmethionine synthase
- L-serine dehydratase
- Threonine ammonia-lyase
Sequence:
MTKLHYKVKDISLAAWGRKEIEIAENEMPGLMTLRKKYGPAQILKGARIAGCLHMTIQTAVLIETLTALGAQVQWSSCNIFSTQDQAAAAIAATGVPVYAWKGETEEEYNWCVEQTIVFQDGQPLNMILDDGGDLTNLVHEKYPQFLAGIKGISEETTTGVHNLYKMFKEGKLKVPAINVNDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQSLSKMGARVLVTEIDPINALQACMDGYQIVTMETAAPLSNIFVTTTGCRDIVRGEHFAVMKEDAIVCNIGHFDCEIDVAWLNANAKKDTVKPQVDRYTLANGVHIILLAEGRLVNLGCGTGHPSFVMSNSFCNQTLAQIALWTKTEEYPLGVHFLPKILDEEVARLHLDQLGAKLTTLTEKQSEYLSVPVAGPYKVDHYRY
Protein: DNA replication complex GINS protein psf3 (Q9UTC3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The GINS complex plays an essential role in the initiation of DNA replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA replication complex GINS protein psf2
- DNA replication complex GINS protein sld5
- DNA replication licensing factor mcm6
- DNA replication complex GINS protein psf1
- DNA replication licensing factor mcm5
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm7
Sequence:
MDYYDIDSILSENQKVPCTSTVSIPGLGHEGRMVPTGSKVELPFWLAEVLAINSFVSIHMPAPFSSVVRNALKANPNSVSIRDITTHYYHFAEKMLHLISDDSLVQISLNTLRSRAMLIADASLNPQGALQQNSQFIEGLDDFEKHILRVSHNAHRSLINWQNSTS
Protein: Dim1p homolog (Thioredoxin like 4A) (Thioredoxin-like 4A, isoform CRA_a) (O14835)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFFFSYHRGW
Protein: Kallikrein-1 (EC 3.4.21.35) (Kidney/pancreas/salivary gland kallikrein) (Tissue kallikrein) (P06870)
Organism: Homo sapiens (Human)
Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
Interaction partners:
- Kallistatin
- Kininogen-1
- Kallikrein-2
- Plasma serine protease inhibitor
Sequence:
MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGGILVHRQWVLTAAHCISDNYQLWLGRHNLFDDENTAQFVHVSESFPHPGFNMSLLENHTRQADEDYSHDLMLLRLTEPADTITDAVKVVELPTEEPEVGSTCLASGWGSIEPENFSFPDDLQCVDLKILPNDECKKAHVQKVTDFMLCVGHLEGGKDTCVGDSGGPLMCDGVLQGVTSWGYVPCGTPNKPSVAVRVLSYVKWIEDTIAENS
Protein: Thioredoxin-like protein Clot (Thioredoxin Clot) (AtClot) (Q9FMN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 2
Sequence:
MTLKKVDANPSTLESSLQELKSDETSRSKINFILFLADNDPTTGQSWCPDCVRAEPVIYKTLEEFPEEVKLIRAYAGDRPTWRTPAHPWRVDSRFKLTGVPTLVRWDGDSVKGRLEDHQAHLPHLILPLLAPST
Protein: Brain-specific homeobox protein homolog (Q810B3)
Organism: Mus musculus (Mouse)
Function: DNA binding protein that function as transcriptional activator. Is essential for normal postnatal growth and nursing. Is an essential factor for neuronal neuropeptide Y and agouti-related peptide function and locomotory behavior in the control of energy balance.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:17353277}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17353277}.
Interaction partners:
Sequence:
MNLNFTSPLHPASSQRPTSFFIEDILLHKPKPLREVAPDHFASSLASRVPLLDYGYPLMPTPTLLTPHAHHPLHKGDHHHPYFLTTSGMPVPALFPHPQHAELPGKHCRRRKARTVFSDSQLSGLEKRFEIQRYLSTPERVELATALSLSETQVKTWFQNRRMKHKKQLRKSQDEPKAADGPESPEGSPRAPEGAPADARLSLPAGAFVLTEPEDEVDIGDEGELSSGPHVL
Protein: Four and a half LIM domains protein 3 (FHL-3) (Skeletal muscle LIM-protein 2) (SLIM-2) (Q9R059)
Organism: Mus musculus (Mouse)
Function: Recruited by SOX15 to FOXK1 promoters where it acts as a transcriptional coactivator of FOXK1.
Subcellular location: Nucleus {ECO:0000269|PubMed:17363903}. Cytoplasm {ECO:0000269|PubMed:17363903}.
Interaction partners:
- Krueppel-like factor 3
Sequence:
MSEAFDCAKCNESLYGRKYIQTDSGPYCVPCYDNTFANTCAECQQLIGHDSRELFYEDRHFHEGCFRCCRCQRSLADEPFTCQDSELLCNECYCTAFSSQCSACGETVMPGSRKLEYGGQTWHEHCFLCSGCEQPLGSRSFVPDKGAHYCVPCYENKFAPRCARCSKTLTQGGVTYRDQPWHRECLVCTGCKTPLAGQQFTSRDDDPYCVACFGELFAPKCSSCKRPITGGSGGGEGAGLGGGKYVSFEDRHWHHSCFSCARCSTSLVGQGFVPDGDQVLCQGCSQAGP
Protein: Olfactory receptor 3A1 (Olfactory receptor 17-40) (OR17-40) (Olfactory receptor OR17-15) (P47881)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MQPESGANGTVIAEFILLGLLEAPGLQPVVFVLFLFAYLVTVRGNLSILAAVLVEPKLHTPMYFFLGNLSVLDVGCISVTVPSMLSRLLSRKRAVPCGACLTQLFFFHLFVGVDCFLLTAMAYDRFLAICRPLTYSTRMSQTVQRMLVAASWACAFTNALTHTVAMSTLNFCGPNVINHFYCDLPQLFQLSCSSTQLNELLLFAVGFIMAGTPMALIVISYIHVAAAVLRIRSVEGRKKAFSTCGSHLTVVAIFYGSGIFNYMRLGSTKLSDKDKAVGIFNTVINPMLNPIIYSFRNPDVQSAIWRMLTGRRSLA
Protein: Splicing factor 3A subunit (Q9FMC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVVKMKQIMRWPPWPPLFAVKFDVIVVVHQMDGLLDSDGGGDDSTDQSQRGGGTTTRKRPVVEIKWKGPKSVTLKRSVVRNLTEEGGFRGDGVVEWNEEFKRVCEFSVYKEGSFLPWFVSLTVFSGLNQGSKEKVRSFGKASLNIAEYFSLMKEDDVQVKVPLKDCDSSSVRSPHVHISLQFSPKESLPERQRSALPVLWSPLSAEAEKAESVVKVGLRKMKTFNNCMSSTQASEKESEKDGSSGSGSDGKSPERNLDSDSSYPFDTDSLDEGDAADESEENKENESSLADPVNYKTLRSANWARGSFHTVTNPEDEDLIYYSHRSPLAETGHCSDEVSNDVVSLEQAKGQMSKKRMLSWKKRKLSFRSPKQKGEPLLKKDCLEEGGDDIDFDRRQLSSSDESNSDWYRSDDAIMKPLSQFGDDDFVVGSWETKEIISRDGLMKLTARVFLASIDQRSERAAGESACTALVAVMAHWLGSNRDIIPTRSEFDSLIREGSSEWRNMCENEEYRERFPDKHFDLETVLQAKVRPICVVPERSFIGFFHPEKSEEEEGKEDASLDFLKGVMSFDSIWEELMKQEPEESASEPVIYIVSWNDHFFVLLVNHDAYYIIDTLGERLYEGCNQAYVLKFDKDAEIKRLPSVIKDNKADMGNQKQGGKNKSEQPERSKESEEQEEEEVVCRGKESCREYIKSFLAAIPIQQVKADMKKGLVSSLHHRLQIELHYTKHLHHHQPNMFESSATEVTVSEAAVSVTVAWSLASQFSNSGGFSCEMAELLGVKV
Protein: L-ribulose-5-phosphate 4-epimerase AraD (EC 5.1.3.4) (Phosphoribulose isomerase) (P08203)
Organism: Escherichia coli (strain K12)
Function: Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction).
Interaction partners:
- L-arabinose isomerase
- Ribulokinase
- Xylulose kinase
- L-ribulose-5-phosphate 3-epimerase UlaE
- Putative L-ribulose-5-phosphate 3-epimerase SgbU
- L-Rhamnulokinase
- Rhamnulose-1-phosphate aldolase
- Arabinose-proton symporter
- Ribulose-phosphate 3-epimerase
- L-ribulose-5-phosphate 4-epimerase SgbE
Sequence:
MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIETGEVVEGTKKPSSDTPTHRLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDAAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ
Protein: Mannan-binding lectin serine protease 1 (EC 3.4.21.-) (Complement factor MASP-3) (Complement-activating component of Ra-reactive factor) (Mannose-binding lectin-associated serine protease 1) (MASP-1) (Mannose-binding protein-associated serine protease) (Ra-reactive factor serine protease p100) (RaRF) (Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain] (P98064)
Organism: Mus musculus (Mouse)
Function: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development.
Subcellular location: Secreted {ECO:0000269|PubMed:8133044}.
Interaction partners:
- Mannose-binding protein C
- Ficolin-1
- Ficolin-2
- Plasma protease C1 inhibitor
- Mannose-binding protein A
- Complement C4-B
- Mannan-binding lectin serine protease 2
- Collectin-11
- Complement C2
- Collectin-10
Sequence:
MRFLSFWRLLLYHALCLALPEVSAHTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVSLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQTHSVQILFRSDNSGENRGWRLSYRAAGNECPKLQPPVYGKIEPSQAVYSFKDQVLVSCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKIVDCGAPAGLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLPVCGVPKFSRKQISRIFNGRPAQKGTMPWIAMLSHLNGQPFCGGSLLGSNWVLTAAHCLHQSLDPEEPTLHSSYLLSPSDFKIIMGKHWRRRSDEDEQHLHVKRTTLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEQPSTEGTMVIVSGWGKQFLQRFPENLMEIEIPIVNSDTCQEAYTPLKKKVTKDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRITGVRN
Protein: 65 kDa phosphoprotein (pp65) (65 kDa matrix phosphoprotein) (Phosphoprotein UL83) (Tegument protein UL83) (P06725)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Counteracts the host antiviral immune response when activated and phosphorylated, by preventing host IRF3 from entering the nucleus. Inhibits also the type I interferon production by inactivating the enzymatic activity of DNA sensor CGAS without affecting STING1. Participates in the transactivation of viral major immediate-early genes by the recruitment of host IFI16 to the promoters pf these genes.
Subcellular location: Virion tegument {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:17715235, ECO:0000269|PubMed:29263269, ECO:0000269|PubMed:7815485}. Host cytoplasm {ECO:0000269|PubMed:17715235}. Note=As part of the incoming virion, pp65 is targeted to the nucleus immediately after infection (PubMed:7815485). The newly synthesized pp65 is observed in the nucleus until some time after 48 hours postinfection (PubMed:17715235). Thereafter, pp65 is probably exported and accumulates in the cytoplasm (PubMed:17715235). Also found in dense bodies (PubMed:7815485).
Interaction partners:
Sequence:
MESRGRRCPEMISVLGPISGHVLKAVFSRGDTPVLPHETRLLQTGIHVRVSQPSLILVSQYTPDSTPCHRGDNQLQVQHTYFTGSEVENVSVNVHNPTGRSICPSQEPMSIYVYALPLKMLNIPSINVHHYPSAAERKHRHLPVADAVIHASGKQMWQARLTVSGLAWTRQQNQWKEPDVYYTSAFVFPTKDVALRHVVCAHELVCSMENTRATKMQVIGDQYVKVYLESFCEDVPSGKLFMHVTLGSDVEEDLTMTRNPQPFMRPHERNGFTVLCPKNMIIKPGKISHIMLDVAFTSHEHFGLLCPKSIPGLSISGNLLMNGQQIFLEVQAIRETVELRQYDPVAALFFFDIDLLLQRGPQYSEHPTFTSQYRIQGKLEYRHTWDRHDEGAAQGDDDVWTSGSDSDEELVTTERKTPRVTGGGAMAGASTSAGRKRKSASSATACTSGVMTRGRLKAESTVAPEEDTDEDSDNEIHNPAVFTWPPWQAGILARNLVPMVATVQGQNLKYQEFFWDANDIYRIFAELEGVWQPAAQPKRRRHRQDALPGPCIASTPKKHRG
Protein: NPD009 (Q9HBH6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MENHHSPKGQRRFQRKGVIGAVFCRMSQSSPSRQGKEGCCREGTAYAKAYQFMASHLSLGKPVSTGSIPRFNKALFNKQAKCKPNHYSFIGLSMLSPENFSIGCKYSVWFSESKGF
Protein: G-protein-signaling modulator 1 (Activator of G-protein signaling 3) (Q6IR34)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide dissociation inhibitor (GDI) which functions as a receptor-independent activator of heterotrimeric G-protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form thus uncoupling heterotrimeric G-proteins signaling from G protein-coupled receptors. Controls spindle orientation and asymmetric cell fate of cerebral cortical progenitors. May also be involved in macroautophagy in intestinal cells. May play a role in drug addiction.
Subcellular location: Cytoplasm, cytosol. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Nuclear mitotic apparatus protein 1
- Protein inscuteable homolog
- Chaperone Ric-8A
- FERM and PDZ domain-containing protein 1
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MASPAPPVAEELPGPASRRLYSRMEASCLELALEGERLCKAGDFKAGVAFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLKEYARALQFHKHDLLLARTIGDRMGEAKASGNLGNTLKVLGRFDEAIVCCQRHLDIAQEQGDKVGEARALYNIGNVYHAKGKQLSWNAAQDPGHLPPDVRETLHRASEFYERNLSLVKELGDRAAQGRAYGNLGNTHYLLGNFTEATTFHKERLAIAKEFGDKAAERRAYSNLGNAHIFLGRFDVAAEHYKKTLQLSRQLRDQAVEAQACYSLGNTYTLLQDYERAAEYHLRHLVIAQELADRVGEGRACWSLGNAYVSMGSPAQALTFAKKHLQISQEIGDRNGELTARMNIAHLQLALGRLTSPAAAEKPDLAGYEAQGARPKRTQRLSAETWDLLRLPLDREQNGETHHTGDWRGPGRDSLPLPMRSRKYQEGPDAIERRPREGSHSPLDSADVRVQVPRTGIPRAPSSDEECFFDLLSKFQSSRMDDQRCPLEEGQAGAAEATAAPSVEDRAAQSSVTASPQTEEFFDLIASSQSRRLDDQRASVGSLPGLRITLNNVGHLRGDGDAQEPGDEFFNMLIKYQSSRIDDQRCPPPDVLPRGPTMPDEDFFSLIQRVQAKRMDEQRVDLAGSPEQEASGLPDPQQQCPPGAS
Protein: Matrix metalloproteinase-17 (MMP-17) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 4) (MT-MMP 4) (MTMMP4) (Membrane-type-4 matrix metalloproteinase) (MT4-MMP) (MT4MMP) (Q9ULZ9)
Organism: Homo sapiens (Human)
Function: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.
Subcellular location: [Isoform Long]: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Furin
- Matrix metalloproteinase-14
- Metalloproteinase inhibitor 1
Sequence:
MRRRAARGPGPPPPGPGLSRLPLPLLLLLALGTRGGCAAPAPAPRAEDLSLGVEWLSRFGYLPPADPTTGQLQTQEELSKAITAMQQFGGLEATGILDEATLALMKTPRCSLPDLPVLTQARRRRQAPAPTKWNKRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGHHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDPLRYGLPYEDKVRVWQLYGVRESVSPTAQPEEPPLLPEPPDNRSSAPPRKDVPHRCSTHFDAVAQIRGEAFFFKGKYFWRLTRDRHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDFSLPPGGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQSPLWRGVPSTLDDAMRWSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVCGDSQADGSVAAGVDAAEGPRAPPGQHDQSRSEDGYEVCSCTSGASSPPGAPGPLVAATMLLLLPPLSPGALWTAAQALTL
Protein: Recombination signal binding protein for immunoglobulin kappa J region (A0A8I5ZUF4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPSGFPQSPRTSPRARPKTRITGALPMDYTKGSSAEERPAHAPSSGKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFYIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEQNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPTNESNTNSEGNYTNASTNSTSVTSSTATVVS