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CNKR2_MOUSE
ID   CNKR2_MOUSE             Reviewed;        1032 AA.
AC   Q80YA9; Q80TP2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Connector enhancer of kinase suppressor of ras 2;
DE            Short=Connector enhancer of KSR 2;
DE   AltName: Full=CNK homolog protein 2;
DE            Short=CNK2;
GN   Name=Cnksr2; Synonyms=Kiaa0902;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-338; SER-390;
RP   TYR-683; SER-685; SER-687 AND SER-906, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May function as an adapter protein or regulator of Ras
CC       signaling pathways.
CC   -!- SUBUNIT: Interacts with RAF1, RAB2L and RAL GTPase proteins.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q80YA9; Q9D415: Dlgap1; NbExp=3; IntAct=EBI-771429, EBI-400152;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80YA9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80YA9-2; Sequence=VSP_010890;
CC   -!- PTM: Phosphorylated on tyrosine. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CNKSR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65681.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK122399; BAC65681.1; ALT_INIT; mRNA.
DR   EMBL; BC043093; AAH43093.1; -; mRNA.
DR   EMBL; BC060716; AAH60716.1; -; mRNA.
DR   CCDS; CCDS30501.1; -. [Q80YA9-1]
DR   RefSeq; NP_001297648.1; NM_001310719.1. [Q80YA9-2]
DR   RefSeq; NP_808419.1; NM_177751.3. [Q80YA9-1]
DR   AlphaFoldDB; Q80YA9; -.
DR   SMR; Q80YA9; -.
DR   BioGRID; 232826; 48.
DR   IntAct; Q80YA9; 46.
DR   MINT; Q80YA9; -.
DR   STRING; 10090.ENSMUSP00000026750; -.
DR   iPTMnet; Q80YA9; -.
DR   PhosphoSitePlus; Q80YA9; -.
DR   MaxQB; Q80YA9; -.
DR   PaxDb; Q80YA9; -.
DR   PeptideAtlas; Q80YA9; -.
DR   PRIDE; Q80YA9; -.
DR   ProteomicsDB; 283451; -. [Q80YA9-1]
DR   ProteomicsDB; 283452; -. [Q80YA9-2]
DR   Antibodypedia; 456; 116 antibodies from 18 providers.
DR   DNASU; 245684; -.
DR   Ensembl; ENSMUST00000026750; ENSMUSP00000026750; ENSMUSG00000025658. [Q80YA9-1]
DR   GeneID; 245684; -.
DR   KEGG; mmu:245684; -.
DR   UCSC; uc009ush.1; mouse. [Q80YA9-1]
DR   UCSC; uc009usi.1; mouse. [Q80YA9-2]
DR   CTD; 22866; -.
DR   MGI; MGI:2661175; Cnksr2.
DR   VEuPathDB; HostDB:ENSMUSG00000025658; -.
DR   eggNOG; KOG1738; Eukaryota.
DR   GeneTree; ENSGT00940000156709; -.
DR   InParanoid; Q80YA9; -.
DR   OMA; EDMEMPP; -.
DR   OrthoDB; 1121556at2759; -.
DR   PhylomeDB; Q80YA9; -.
DR   TreeFam; TF326495; -.
DR   Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR   BioGRID-ORCS; 245684; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Cnksr2; mouse.
DR   PRO; PR:Q80YA9; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q80YA9; protein.
DR   Bgee; ENSMUSG00000025658; Expressed in primary visual cortex and 124 other tissues.
DR   ExpressionAtlas; Q80YA9; baseline and differential.
DR   Genevisible; Q80YA9; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR   GO; GO:0099173; P:postsynapse organization; ISO:MGI.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR010599; CNK2/3_dom.
DR   InterPro; IPR017874; CRIC_domain.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   Pfam; PF10534; CRIC_ras_sig; 1.
DR   Pfam; PF06663; DUF1170; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS51290; CRIC; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1032
FT                   /note="Connector enhancer of kinase suppressor of ras 2"
FT                   /id="PRO_0000089971"
FT   DOMAIN          11..76
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          84..178
FT                   /note="CRIC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00621"
FT   DOMAIN          215..297
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          302..515
FT                   /note="DUF1170"
FT   DOMAIN          570..669
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          324..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          538..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          864..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          874..917
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        324..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..558
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..696
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..712
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..766
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..890
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         338
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         683
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         685
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         687
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         756
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1T4"
FT   MOD_RES         767
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1T4"
FT   MOD_RES         906
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         271..319
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_010890"
SQ   SEQUENCE   1032 AA;  117396 MW;  FE97ED5E3CDB75BF CRC64;
     MALIMEPVSK WSPSQVVDWM KGLDDCLQQY IKNFEREKIS GDQLLRITHQ ELEDLGVSRI
     GHQELILEAV DLLCALNYGL ETENLKTLSH KLNASAKNLQ NFITGRRRSG HYDGRTSRKL
     PNDFLTSVVD LIGAAKSLLA WLDRSPFAAV TDYSVTRNNV IQLCLELTTI VQQDCTVYET
     ENKILHVCKT LSGVCDHIIS LSSDPLVSQS AHLEVIQLAN IKPSEGLGMY IKSTYDGLHV
     ITGTTENSPA DRCKKIHAGD EVIQVNHQTV VGWQLKNLVN ALREDPSGVI LTLKKRPQSM
     LTSAPALLKN MRWKPLALQP LIPRSPTSSV ATPSSTISTP TKRDSSALQD LYIPPPPAEP
     YIPRDEKGNL PCEDLRGHMV GKPVHKGSES PNSFLDQEYR KRFNIVEEDT VLYCYEYEKG
     RSSSQGRRES TPTYGKLRPI SMPVEYNWVG DYEDPNKMKR DSRRENSLLR YMSNEKIAQE
     EYMFQRNSKK DTGKKSKKKG DKSNSPAHYS LLPSLQMDAL RQDIMGTPVP ETTLYHTFQQ
     SSLQHKSKKK NKGAISGKSK RRISCKDLGR GDCEGWLWKK KDAKSYFSQK WKKYWFVLKD
     ASLYWYINEE DEKAEGFISL PEFKIDRASE CRKKYAFKAC HPKIKSFYFA AEHLDDMNRW
     LNRINMLTAG YAERERIKQE QDYWSESDKE EADTPSTPKQ DSPPPPYDTY PRPPSMSCAS
     PYVEAKHSRL SSTETSQSQS SHEEFRQEVT GSSAVSPIRK TASQRRSWQD LIETPLTSSG
     LHYLQTLPLE DSVFSDSAAI SPEHRRQSTL PTQKCHLQDH YGPYPLAESE RMQVLNGNGG
     KPRSFTLPRD SGFNHCCLNT PVSACDPQDD IQPPEVEEEE EEEEEEAAGE NVGEKNENRE
     EKLGDSLQDL YRALEEASLS PLGEHRISTK MEYKLSFIKR CNDPVMNEKL HRLRILKSTL
     KAREGEVAII DKVLDNPDLT SKEFQQWKQM YLDLFLDICQ STTSNDPLSI SSEVDVLTSS
     LTHTHSYIET HV
 
 
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