ID CNKR2_HUMAN Reviewed; 1034 AA. AC Q8WXI2; B4DGR4; B7ZLJ1; B9EG83; E7ESA4; O94976; Q5JPK4; Q5JPN0; AC Q8WXI1; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 12-SEP-2018, entry version 149. 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=CNK2, KIAA0902, KSR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION RP WITH RAF1; RAB2L AND RAL GTPASE PROTEINS, AND PHOSPHORYLATION. RC TISSUE=Fetal brain; RX PubMed=14597674; DOI=10.1096/fj.02-1096com; RA Lanigan T.M., Liu A., Huang Y.Z., Mei L., Margolis B., Guan K.-L.; RT "Human homologue of Drosophila CNK interacts with Ras effector RT proteins Raf and Rlf."; RL FASEB J. 17:2048-2060(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Brain, and Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP STRUCTURE BY NMR OF 8-79. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the N-terminal SAM-domain of human KIAA0902 RT protein (connector enhancer of kinase suppressor of RAS 2)."; RL Submitted (JUL-2007) to the PDB data bank. RN [11] RP VARIANT [LARGE SCALE ANALYSIS] HIS-46. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [12] RP INVOLVEMENT IN MRXSHG. RX PubMed=25223753; DOI=10.1002/ana.24274; RA Vaags A.K., Bowdin S., Smith M.L., Gilbert-Dussardier B., RA Brocke-Holmefjord K.S., Sinopoli K., Gilles C., Haaland T.B., RA Vincent-Delorme C., Lagrue E., Harbuz R., Walker S., Marshall C.R., RA Houge G., Kalscheuer V.M., Scherer S.W., Minassian B.A.; RT "Absent CNKSR2 causes seizures and intellectual, attention, and RT language deficits."; RL Ann. Neurol. 76:758-764(2014). RN [13] RP INVOLVEMENT IN MRXSHG, AND VARIANT MRXSHG 712-ARG--VAL-1034 DEL. RX PubMed=28098945; DOI=10.1111/epi.13666; RA Damiano J.A., Burgess R., Kivity S., Lerman-Sagie T., Afawi Z., RA Scheffer I.E., Berkovic S.F., Hildebrand M.S.; RT "Frequency of CNKSR2 mutation in the X-linked epilepsy-aphasia RT spectrum."; RL Epilepsia 58:E40-E43(2017). CC -!- FUNCTION: May function as an adapter protein or regulator of Ras CC signaling pathways. {ECO:0000269|PubMed:14597674}. CC -!- SUBUNIT: Interacts with RAF1, RAB2L and RAL GTPase proteins. CC {ECO:0000269|PubMed:14597674}. CC -!- INTERACTION: CC Q8ML92:ave (xeno); NbExp=5; IntAct=EBI-1045119, EBI-2563975; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=CNK2A, KSR2A; CC IsoId=Q8WXI2-1; Sequence=Displayed; CC Name=2; Synonyms=CNK2B, KSR2B; CC IsoId=Q8WXI2-2; Sequence=VSP_010887; CC Note=Ref.2 (BAA74925) sequence differs from that shown due to CC frameshifts in positions 859, 929, 985 and 1019. {ECO:0000305}; CC Name=3; CC IsoId=Q8WXI2-4; Sequence=VSP_043168, VSP_010887; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=Q8WXI2-5; Sequence=VSP_043169; CC Note=No experimental confirmation available.; CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000269|PubMed:14597674}. CC -!- DISEASE: Mental retardation, X-linked, syndromic, Houge type CC (MRXSHG) [MIM:301008]: A form of mental retardation, a disorder CC characterized by significantly below average general intellectual CC functioning associated with impairments in adaptive behavior and CC manifested during the developmental period. MRXSHG is CC characterized by delayed development, intellectual disability, CC speech and language delay, and early-onset seizures. Carrier CC females may be mildly affected. {ECO:0000269|PubMed:25223753, CC ECO:0000269|PubMed:28098945}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the CNKSR family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF418269; AAL60502.1; -; mRNA. DR EMBL; AF418270; AAL60503.1; -; mRNA. DR EMBL; AB020709; BAA74925.2; ALT_FRAME; mRNA. DR EMBL; AK294728; BAG57875.1; -; mRNA. DR EMBL; AL928874; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL807781; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL772392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471074; EAW98977.1; -; Genomic_DNA. DR EMBL; BC126121; AAI26122.1; -; mRNA. DR EMBL; BC136289; AAI36290.1; -; mRNA. DR EMBL; BC143839; AAI43840.1; -; mRNA. DR CCDS; CCDS14198.1; -. [Q8WXI2-1] DR CCDS; CCDS55387.1; -. [Q8WXI2-2] DR CCDS; CCDS55388.1; -. [Q8WXI2-5] DR CCDS; CCDS55389.1; -. [Q8WXI2-4] DR RefSeq; NP_001162118.1; NM_001168647.2. [Q8WXI2-5] DR RefSeq; NP_001162119.1; NM_001168648.2. [Q8WXI2-2] DR RefSeq; NP_001162120.1; NM_001168649.2. [Q8WXI2-4] DR RefSeq; NP_055742.2; NM_014927.4. [Q8WXI2-1] DR UniGene; Hs.555917; -. DR PDB; 2EAN; NMR; -; A=8-77. DR PDB; 3BS5; X-ray; 2.00 A; B=5-84. DR PDBsum; 2EAN; -. DR PDBsum; 3BS5; -. DR ProteinModelPortal; Q8WXI2; -. DR SMR; Q8WXI2; -. DR BioGrid; 116534; 7. DR DIP; DIP-29736N; -. DR IntAct; Q8WXI2; 4. DR MINT; Q8WXI2; -. DR STRING; 9606.ENSP00000368824; -. DR iPTMnet; Q8WXI2; -. DR PhosphoSitePlus; Q8WXI2; -. DR BioMuta; CNKSR2; -. DR DMDM; 50400586; -. DR EPD; Q8WXI2; -. DR MaxQB; Q8WXI2; -. DR PaxDb; Q8WXI2; -. DR PeptideAtlas; Q8WXI2; -. DR PRIDE; Q8WXI2; -. DR ProteomicsDB; 75059; -. DR ProteomicsDB; 75060; -. [Q8WXI2-2] DR ProteomicsDB; 75061; -. [Q8WXI2-4] DR ProteomicsDB; 75062; -. [Q8WXI2-5] DR Ensembl; ENST00000379510; ENSP00000368824; ENSG00000149970. [Q8WXI2-1] DR Ensembl; ENST00000425654; ENSP00000397906; ENSG00000149970. [Q8WXI2-5] DR Ensembl; ENST00000543067; ENSP00000444633; ENSG00000149970. [Q8WXI2-4] DR Ensembl; ENST00000642359; ENSP00000496709; ENSG00000149970. [Q8WXI2-2] DR GeneID; 22866; -. DR KEGG; hsa:22866; -. DR UCSC; uc004czw.4; human. [Q8WXI2-1] DR CTD; 22866; -. DR DisGeNET; 22866; -. DR EuPathDB; HostDB:ENSG00000149970.14; -. DR GeneCards; CNKSR2; -. DR HGNC; HGNC:19701; CNKSR2. DR HPA; HPA001502; -. DR MalaCards; CNKSR2; -. DR MIM; 300724; gene. DR MIM; 301008; phenotype. DR neXtProt; NX_Q8WXI2; -. DR OpenTargets; ENSG00000149970; -. DR PharmGKB; PA134867759; -. DR eggNOG; KOG1738; Eukaryota. DR eggNOG; ENOG4110T89; LUCA. DR GeneTree; ENSGT00390000017199; -. DR HOGENOM; HOG000231501; -. DR HOVERGEN; HBG051040; -. DR InParanoid; Q8WXI2; -. DR KO; K17536; -. DR OMA; STKLEYK; -. DR OrthoDB; EOG091G037J; -. DR PhylomeDB; Q8WXI2; -. DR TreeFam; TF326495; -. DR Reactome; R-HSA-5674135; MAP2K and MAPK activation. DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants. DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants. DR Reactome; R-HSA-6802949; Signaling by RAS mutants. DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions. DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF. DR SignaLink; Q8WXI2; -. DR SIGNOR; Q8WXI2; -. DR ChiTaRS; CNKSR2; human. DR EvolutionaryTrace; Q8WXI2; -. DR GeneWiki; CNKSR2; -. DR GenomeRNAi; 22866; -. DR PRO; PR:Q8WXI2; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000149970; Expressed in 162 organ(s), highest expression level in primary visual cortex. DR CleanEx; HS_CNKSR2; -. DR CleanEx; HS_KSR2; -. DR Genevisible; Q8WXI2; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0043005; C:neuron projection; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR010599; CNKSR2. 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 3D-structure; Alternative splicing; Coiled coil; Complete proteome; KW Cytoplasm; Disease mutation; Membrane; Mental retardation; KW Phosphoprotein; Polymorphism; Reference proteome. FT CHAIN 1 1034 Connector enhancer of kinase suppressor FT of ras 2. FT /FTId=PRO_0000089970. FT DOMAIN 11 76 SAM. {ECO:0000255|PROSITE- FT ProRule:PRU00184}. FT DOMAIN 84 178 CRIC. {ECO:0000255|PROSITE- FT ProRule:PRU00621}. FT DOMAIN 215 297 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT DOMAIN 332 515 DUF1170. FT DOMAIN 570 669 PH. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT COILED 875 904 {ECO:0000255}. FT COMPBIAS 354 357 Poly-Pro. FT COMPBIAS 703 706 Poly-Pro. FT COMPBIAS 875 888 Poly-Glu. FT MOD_RES 12 12 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80YA9}. FT MOD_RES 338 338 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80YA9}. FT MOD_RES 390 390 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80YA9}. FT MOD_RES 683 683 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q80YA9}. FT MOD_RES 685 685 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80YA9}. FT MOD_RES 687 687 Phosphoserine. FT {ECO:0000250|UniProtKB:Q80YA9}. FT MOD_RES 756 756 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Z1T4}. FT MOD_RES 767 767 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Z1T4}. FT MOD_RES 908 908 Phosphoserine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT VAR_SEQ 271 319 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043168. FT VAR_SEQ 435 464 Missing (in isoform 4). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_043169. FT VAR_SEQ 899 1034 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:10048485, FT ECO:0000303|PubMed:14597674, FT ECO:0000303|PubMed:14702039}. FT /FTId=VSP_010887. FT VARIANT 46 46 R -> H (in a colorectal cancer sample; FT somatic mutation; dbSNP:rs771705122). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035681. FT VARIANT 712 1034 Missing (in MRXSHG). FT {ECO:0000269|PubMed:28098945}. FT /FTId=VAR_080600. FT HELIX 8 10 {ECO:0000244|PDB:3BS5}. FT HELIX 13 21 {ECO:0000244|PDB:3BS5}. FT HELIX 25 30 {ECO:0000244|PDB:3BS5}. FT HELIX 31 37 {ECO:0000244|PDB:3BS5}. FT HELIX 41 45 {ECO:0000244|PDB:3BS5}. FT HELIX 49 54 {ECO:0000244|PDB:3BS5}. FT HELIX 60 77 {ECO:0000244|PDB:3BS5}. SQ SEQUENCE 1034 AA; 117535 MW; E43DB0D8D72D954C 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 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 TKMEYKLSFI KRCNDPVMNE KLHRLRILKS TLKAREGEVA IIDKVLDNPD LTSKEFQQWK QMYLDLFLDI CQNTTSNDPL SISSEVDVIT SSLAHTHSYI ETHV //