ID G7NSN5_MACMU Unreviewed; 1034 AA.
AC G7NSN5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Connector enhancer of kinase suppressor of ras 2 {ECO:0000313|EMBL:EHH30584.1};
GN ORFNames=EGK_20319 {ECO:0000313|EMBL:EHH30584.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH30584.1};
RN [1] {ECO:0000313|EMBL:EHH30584.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH30584.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- SIMILARITY: Belongs to the CNKSR family.
CC {ECO:0000256|ARBA:ARBA00009498}.
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DR EMBL; CM001273; EHH30584.1; -; Genomic_DNA.
DR Proteomes; UP000013456; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01260; PH_CNK_mammalian-like; 1.
DR CDD; cd09511; SAM_CNK1_2_3-suppressor; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR049628; CNK1-3_SAM.
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 PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR PANTHER; PTHR12844:SF21; CONNECTOR ENHANCER OF KINASE SUPPRESSOR OF RAS 2; 1.
DR Pfam; PF06663; CNK2_3_dom; 1.
DR Pfam; PF10534; CRIC_ras_sig; 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; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51290; CRIC; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EHH30584.1};
KW Transferase {ECO:0000313|EMBL:EHH30584.1}.
FT DOMAIN 11..76
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 84..178
FT /note="CRIC"
FT /evidence="ECO:0000259|PROSITE:PS51290"
FT DOMAIN 215..297
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 570..669
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 324..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..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..761
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 COMPBIAS 891..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 117467 MW; 364D84F3D09C80E0 CRC64;
MALIMEPVSK WSPSQVVDWM KGLDDCLQQY IKNFEREKIS GDQLLRITHQ ELEDLGVSRI
GHQELILEAV DLLCALNYGL ETENLKTLSH KLNASAKNLQ NFITGRRRSG HYDGRTSRKL
PNDFLTSVVD LIGAAKSLLA WLDRSPFAAV TDYSVTRNNV IQLCLELTTI VQQNTYLLQL
FFFLCYQCKT LSGVCDHIIS LSSDPLVSQS AHLEVIQLAN IKPSEGLSVC ILNTYDGLHV
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 DKSNSPTHYS LLPSLQMDAL RQDIMGTPVP ETTLYHTFQQ
SSLQHKSKKK NKGPIAGKSK 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 SGFNHCCLNA PVSACDPQDD VQPPEVEEEE EEEEEEGEAA GENIGEKSES
REEKLGDSLQ DLYRALEQAS LSPLGEHRIS TKKEYXXXXX XXXXXXXXXX XXXXXXXXXX
XFKAREGEVA IIDKVLDNPD LTSKEFQQWK QMYLDLFLDI CQNTTSNDPL SISSEVDVIT
SSLTHTHSYI ETHV
//
