ID CSKP_HUMAN Reviewed; 926 AA. AC O14936; A6NES1; B7ZKY0; O43215; Q17RI4; Q59HA0; Q5VT16; Q5VT17; Q5VT18; AC Q5VT19; Q66T42; Q9BYH6; Q9NYB2; Q9NYB3; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 3. DT 12-OCT-2022, entry version 233. DE RecName: Full=Peripheral plasma membrane protein CASK {ECO:0000305}; DE Short=hCASK; DE EC=2.7.11.1 {ECO:0000269|PubMed:18423203}; DE AltName: Full=Calcium/calmodulin-dependent serine protein kinase; DE AltName: Full=Protein lin-2 homolog; GN Name=CASK {ECO:0000312|HGNC:HGNC:1497}; Synonyms=LIN2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH SDC2 AND RP EPB41. RC TISSUE=Brain, Liver, and Lung; RX PubMed=9660868; DOI=10.1083/jcb.142.1.129; RA Cohen A.R., Woods D.F., Marfatia S.M., Walther Z., Chishti A.H., RA Anderson J.M.; RT "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the RT basolateral membrane of epithelial cells."; RL J. Cell Biol. 142:129-138(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Zha D., Hu G.; RT "The human homolog of the rat CASK, Drosophila Camguk and C.elegans Lin-2 RT genes."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RC TISSUE=Kidney; RA Ding L., Saijo K., Kawai K., Akaza H., Ugai H., Yokoyama K.K., Ohno T.; RT "Putative alternative splicing form of human CASK mRNA (partial codes)."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Colon carcinoma; RA Yan Y., Merlin D.; RT "Caco2-BBE calcium/calmodulin-dependent serine protein kinase."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [5] 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., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., 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., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., 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., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., 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., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., 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., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-926 (ISOFORM 2). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 173-926 (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [MRNA] OF 27-926 (ISOFORM 3), AND TISSUE SPECIFICITY. RC TISSUE=Fetus; RX PubMed=11003712; DOI=10.1007/s003350010170; RA Stevenson D., Laverty H.G., Wenwieser S., Douglas M., Wilson J.B.; RT "Mapping and expression analysis of the human CASK gene."; RL Mamm. Genome 11:934-937(2000). RN [9] RP INTERACTION WITH KIRREL3. RX PubMed=19012874; DOI=10.1016/j.ajhg.2008.10.020; RA Bhalla K., Luo Y., Buchan T., Beachem M.A., Guzauskas G.F., Ladd S., RA Bratcher S.J., Schroer R.J., Balsamo J., DuPont B.R., Lilien J., RA Srivastava A.K.; RT "Alterations in CDH15 and KIRREL3 in patients with mild to severe RT intellectual disability."; RL Am. J. Hum. Genet. 83:703-713(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-571 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-577 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-192 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-572. RX PubMed=9546224; DOI=10.1038/nsb0498-317; RA Daniels D.L., Cohen A.R., Anderson J.M., Bruenger A.T.; RT "Crystal structure of the hCASK PDZ domain reveals the structural basis of RT class II PDZ domain target recognition."; RL Nat. Struct. Biol. 5:317-325(1998). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-337 IN COMPLEX WITH AMP, RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, PHOSPHORYLATION OF NRXN1, AND PHOSPHORYLATION AT SER-151 AND RP SER-155. RX PubMed=18423203; DOI=10.1016/j.cell.2008.02.036; RA Mukherjee K., Sharma M., Urlaub H., Bourenkov G.P., Jahn R., Suedhof T.C., RA Wahl M.C.; RT "CASK functions as a Mg2+-independent neurexin kinase."; RL Cell 133:328-339(2008). RN [14] RP VARIANT [LARGE SCALE ANALYSIS] VAL-96. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [15] RP INVOLVEMENT IN MICPCH SYNDROME. RX PubMed=19165920; DOI=10.1038/ng.194; RA Najm J., Horn D., Wimplinger I., Golden J.A., Chizhikov V.V., Sudi J., RA Christian S.L., Ullmann R., Kuechler A., Haas C.A., Flubacher A., RA Charnas L.R., Uyanik G., Frank U., Klopocki E., Dobyns W.B., Kutsche K.; RT "Mutations of CASK cause an X-linked brain malformation phenotype with RT microcephaly and hypoplasia of the brainstem and cerebellum."; RL Nat. Genet. 40:1065-1067(2008). RN [16] RP ERRATUM OF PUBMED:19165920. RA Najm J., Horn D., Wimplinger I., Golden J.A., Chizhikov V.V., Sudi J., RA Christian S.L., Ullmann R., Kuechler A., Haas C.A., Flubacher A., RA Charnas L.R., Uyanik G., Frank U., Klopocki E., Dobyns W.B., Kutsche K.; RL Nat. Genet. 40:1384-1384(2008). RN [17] RP VARIANT FGS4 LEU-28, AND CHARACTERIZATION OF VARIANT FGS4 LEU-28. RX PubMed=19200522; DOI=10.1016/j.ajhg.2008.12.018; RA Piluso G., D'Amico F., Saccone V., Bismuto E., Rotundo I.L., RA Di Domenico M., Aurino S., Schwartz C.E., Neri G., Nigro V.; RT "A missense mutation in CASK causes FG syndrome in an Italian family."; RL Am. J. Hum. Genet. 84:162-177(2009). RN [18] RP VARIANTS [LARGE SCALE ANALYSIS] MICPCH HIS-268; SER-396 AND GLY-710. RX PubMed=19377476; DOI=10.1038/ng.367; RA Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C., RA O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M., RA Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J., RA Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M., RA Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P., RA Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R., RA Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R., RA de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M., RA Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U., RA Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M., RA Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T., RA Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C., RA Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L., RA Futreal P.A., Stratton M.R.; RT "A systematic, large-scale resequencing screen of X-chromosome coding exons RT in mental retardation."; RL Nat. Genet. 41:535-543(2009). RN [19] RP VARIANT 19-GLY--TYR-926 DEL. RX PubMed=23662938; DOI=10.1111/epi.12203; RA Kodera H., Kato M., Nord A.S., Walsh T., Lee M., Yamanaka G., Tohyama J., RA Nakamura K., Nakagawa E., Ikeda T., Ben-Zeev B., Lev D., Lerman-Sagie T., RA Straussberg R., Tanabe S., Ueda K., Amamoto M., Ohta S., Nonoda Y., RA Nishiyama K., Tsurusaki Y., Nakashima M., Miyake N., Hayasaka K., RA King M.C., Matsumoto N., Saitsu H.; RT "Targeted capture and sequencing for detection of mutations causing early RT onset epileptic encephalopathy."; RL Epilepsia 54:1262-1269(2013). CC -!- FUNCTION: Multidomain scaffolding Mg(2+)-independent protein kinase CC that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, CC and plays a role in synaptic transmembrane protein anchoring and ion CC channel trafficking (PubMed:18423203). Contributes to neural CC development and regulation of gene expression via interaction with the CC transcription factor TBR1. Binds to cell-surface proteins, including CC amyloid precursor protein, neurexins and syndecans. May mediate a link CC between the extracellular matrix and the actin cytoskeleton via its CC interaction with syndecan and with the actin/spectrin-binding protein CC 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with CC the motor protein KIF17 to transport vesicles containing N-methyl-D- CC aspartate (NMDA) receptor subunit NR2B along microtubules (By CC similarity). {ECO:0000250|UniProtKB:O70589, CC ECO:0000269|PubMed:18423203}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:18423203}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000269|PubMed:18423203}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- COFACTOR: CC Note=Unlike other protein kinases, does not require a divalent cation CC such as magnesium for catalytic activity. CC {ECO:0000269|PubMed:18423203}; CC -!- ACTIVITY REGULATION: Differs from archetypal CaMK members in that the CC kinase domain exhibits a constitutively active conformation and the CC autoinhibitory region does not engage in direct contact with the ATP- CC binding cleft, although it still binds Ca(2+)/CAM. CC {ECO:0000269|PubMed:18423203}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=563 uM for ATP {ECO:0000269|PubMed:18423203}; CC KM=748.7 uM for ATP (when NRXN1 is phosphorylated) CC {ECO:0000269|PubMed:18423203}; CC Vmax=4.9 nmol/min/mmol enzyme {ECO:0000269|PubMed:18423203}; CC Note=Kinetics of autophosphorylation assay were measured, rather than CC phosphorylation of an exogenous substrate.; CC -!- SUBUNIT: CASK and LIN7 form two mutually exclusive tripartite complexes CC with APBA1 or CASKIN1 (By similarity). Component of the brain-specific CC heterotrimeric complex (LIN-10-LIN-2-LIN-7 complex) composed of at CC least APBA1, CASK, and LIN7, which associates with the motor protein CC KIF17 to transport vesicles along microtubules (By similarity). Forms a CC heterotrimeric complex with DLG1 and LIN7B via their L27 domains (By CC similarity). Identified in a complex with ACTN4, IQGAP1, MAGI2, NPHS1, CC SPTAN1 and SPTBN1 (By similarity). Part of a complex containing CASK, CC TBR1 and TSPYL2 (By similarity). Interacts with WHRN (By similarity). CC Interacts (via the PDZ, SH3 and guanylate kinase-like domains) with CC NRXN1 (via C-terminus) (By similarity). Interacts with CASKIN1, APBA1, CC LIN7(A/B/C) and L27 domain of DLG1 and isoform 2 of DLG4 (By CC similarity). Interacts with FCHSD2 (By similarity). Interacts with CC KIRREL3 (PubMed:19012874). Interacts with TBR1 (By similarity). CC Interacts with TSPYL2 (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:O70589, ECO:0000250|UniProtKB:Q62915, CC ECO:0000269|PubMed:18423203, ECO:0000269|PubMed:19012874, CC ECO:0000269|PubMed:9660868}. CC -!- INTERACTION: CC O14936; Q8WXD9: CASKIN1; NbExp=4; IntAct=EBI-1215506, EBI-970261; CC O14936; Q12929: EPS8; NbExp=3; IntAct=EBI-1215506, EBI-375576; CC O14936; P41134: ID1; NbExp=3; IntAct=EBI-1215506, EBI-1215527; CC O14936; O14910: LIN7A; NbExp=7; IntAct=EBI-1215506, EBI-2513988; CC O14936; Q9Y2J0: RPH3A; NbExp=3; IntAct=EBI-1215506, EBI-1216802; CC O14936; P34741: SDC2; NbExp=2; IntAct=EBI-1215506, EBI-1172957; CC O14936; Q9H788: SH2D4A; NbExp=4; IntAct=EBI-1215506, EBI-747035; CC O14936; Q13425: SNTB2; NbExp=3; IntAct=EBI-1215506, EBI-80411; CC O14936; Q13009: TIAM1; NbExp=2; IntAct=EBI-1215506, EBI-1050007; CC O14936; Q63373: Nrxn1; Xeno; NbExp=3; IntAct=EBI-1215506, EBI-1780696; CC O14936-2; Q8WXD9: CASKIN1; NbExp=2; IntAct=EBI-15957318, EBI-970261; CC O14936-4; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-12007726, EBI-12155483; CC O14936-4; O14910: LIN7A; NbExp=3; IntAct=EBI-12007726, EBI-2513988; CC O14936-4; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-12007726, EBI-821335; CC O14936-4; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-12007726, EBI-8852072; CC O14936-4; Q9HB63: NTN4; NbExp=3; IntAct=EBI-12007726, EBI-743459; CC O14936-4; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-12007726, EBI-747035; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62915}. Cytoplasm CC {ECO:0000250|UniProtKB:Q62915}. Cell membrane CC {ECO:0000250|UniProtKB:Q62915}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q62915}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=O14936-1; Sequence=Displayed; CC Name=2; CC IsoId=O14936-2; Sequence=VSP_024426; CC Name=3; CC IsoId=O14936-3; Sequence=VSP_024422, VSP_024424; CC Name=4; CC IsoId=O14936-4; Sequence=VSP_024424, VSP_024426; CC Name=5; CC IsoId=O14936-5; Sequence=VSP_024421, VSP_024423, VSP_024424; CC Name=6; CC IsoId=O14936-6; Sequence=VSP_024425, VSP_024426; CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression is significantly greater in CC brain relative to kidney, lung, and liver and in fetal brain and kidney CC relative to lung and liver. {ECO:0000269|PubMed:11003712}. CC -!- DOMAIN: The first L27 domain binds DLG1 and the second L27 domain CC probably binds LIN7. {ECO:0000250}. CC -!- DOMAIN: The protein kinase domain mediates the interaction with FCHSD2. CC -!- DISEASE: Intellectual developmental disorder with microcephaly and CC pontine and cerebellar hypoplasia (MICPCH) [MIM:300749]: 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. Affected individuals can CC manifest a severe phenotype consisting of severe intellectual deficit, CC congenital or postnatal microcephaly, disproportionate brainstem and CC cerebellar hypoplasia. A milder phenotype consists of intellectual CC disability alone or associated with nystagmus. CC {ECO:0000269|PubMed:19165920, ECO:0000269|PubMed:19377476}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: FG syndrome 4 (FGS4) [MIM:300422]: FG syndrome (FGS) is an X- CC linked disorder characterized by intellectual disability, relative CC macrocephaly, hypotonia and constipation. CC {ECO:0000269|PubMed:19200522}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: In the N-terminal section; belongs to the protein kinase CC superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MAGUK 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; AF032119; AAB88125.1; -; mRNA. DR EMBL; AF035582; AAB88198.1; -; mRNA. DR EMBL; AB039327; BAB12252.2; -; mRNA. DR EMBL; AY705392; AAU10527.1; -; mRNA. DR EMBL; AL158144; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL603754; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL627402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC117311; AAI17312.1; -; mRNA. DR EMBL; BC143454; AAI43455.1; -; mRNA. DR EMBL; AB208859; BAD92096.1; -; mRNA. DR EMBL; AF262404; AAF72666.1; -; mRNA. DR EMBL; AF262405; AAF72667.1; -; mRNA. DR CCDS; CCDS14257.1; -. [O14936-2] DR CCDS; CCDS48094.1; -. [O14936-3] DR CCDS; CCDS48095.1; -. [O14936-4] DR RefSeq; NP_001119526.1; NM_001126054.2. [O14936-4] DR RefSeq; NP_001119527.1; NM_001126055.2. [O14936-3] DR RefSeq; NP_003679.2; NM_003688.3. [O14936-2] DR PDB; 1KGD; X-ray; 1.31 A; A=739-914. DR PDB; 1KWA; X-ray; 1.93 A; A/B=487-572. DR PDB; 1ZL8; NMR; -; B=403-456. DR PDB; 3C0G; X-ray; 2.19 A; A/B=1-337. DR PDB; 3C0H; X-ray; 2.30 A; A/B=1-337. DR PDB; 3C0I; X-ray; 1.85 A; A=1-337. DR PDB; 3MFR; X-ray; 2.00 A; A=1-337. DR PDB; 3MFS; X-ray; 2.10 A; A=1-337. DR PDB; 3MFT; X-ray; 2.20 A; A=1-337. DR PDB; 3MFU; X-ray; 2.30 A; A=1-337. DR PDB; 3TAC; X-ray; 2.20 A; A=1-345. DR PDB; 6KMH; X-ray; 2.40 A; A/B=1-319. DR PDB; 7OAI; X-ray; 2.30 A; A/B/C/D=1-337. DR PDB; 7OAJ; X-ray; 1.93 A; A/B/C/D=1-337. DR PDB; 7OAK; X-ray; 2.23 A; A/B/C/D=1-337. DR PDB; 7OAL; X-ray; 2.17 A; A/B/C/D=1-337. DR PDBsum; 1KGD; -. DR PDBsum; 1KWA; -. DR PDBsum; 1ZL8; -. DR PDBsum; 3C0G; -. DR PDBsum; 3C0H; -. DR PDBsum; 3C0I; -. DR PDBsum; 3MFR; -. DR PDBsum; 3MFS; -. DR PDBsum; 3MFT; -. DR PDBsum; 3MFU; -. DR PDBsum; 3TAC; -. DR PDBsum; 6KMH; -. DR PDBsum; 7OAI; -. DR PDBsum; 7OAJ; -. DR PDBsum; 7OAK; -. DR PDBsum; 7OAL; -. DR AlphaFoldDB; O14936; -. DR SMR; O14936; -. DR BioGRID; 114141; 171. DR CORUM; O14936; -. DR DIP; DIP-38727N; -. DR ELM; O14936; -. DR IntAct; O14936; 93. DR MINT; O14936; -. DR STRING; 9606.ENSP00000367408; -. DR BindingDB; O14936; -. DR ChEMBL; CHEMBL1908381; -. DR DrugBank; DB01942; Formic acid. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; O14936; -. DR GlyGen; O14936; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O14936; -. DR PhosphoSitePlus; O14936; -. DR SwissPalm; O14936; -. DR BioMuta; CASK; -. DR EPD; O14936; -. DR jPOST; O14936; -. DR MassIVE; O14936; -. DR MaxQB; O14936; -. DR PaxDb; O14936; -. DR PeptideAtlas; O14936; -. DR PRIDE; O14936; -. DR ProteomicsDB; 48318; -. [O14936-1] DR ProteomicsDB; 48319; -. [O14936-2] DR ProteomicsDB; 48320; -. [O14936-3] DR ProteomicsDB; 48321; -. [O14936-4] DR ProteomicsDB; 48322; -. [O14936-5] DR ProteomicsDB; 48323; -. [O14936-6] DR TopDownProteomics; O14936-5; -. [O14936-5] DR ABCD; O14936; 1 sequenced antibody. DR Antibodypedia; 4529; 310 antibodies from 38 providers. DR DNASU; 8573; -. DR Ensembl; ENST00000378154.3; ENSP00000367396.2; ENSG00000147044.23. [O14936-6] DR Ensembl; ENST00000378163.7; ENSP00000367405.1; ENSG00000147044.23. [O14936-1] DR Ensembl; ENST00000644347.1; ENSP00000494183.1; ENSG00000147044.23. [O14936-3] DR Ensembl; ENST00000645566.1; ENSP00000494788.1; ENSG00000147044.23. [O14936-2] DR Ensembl; ENST00000646120.2; ENSP00000495291.2; ENSG00000147044.23. [O14936-4] DR GeneID; 8573; -. DR KEGG; hsa:8573; -. DR MANE-Select; ENST00000378163.7; ENSP00000367405.1; NM_001367721.1; NP_001354650.1. DR UCSC; uc004dfl.5; human. [O14936-1] DR CTD; 8573; -. DR DisGeNET; 8573; -. DR GeneCards; CASK; -. DR GeneReviews; CASK; -. DR HGNC; HGNC:1497; CASK. DR HPA; ENSG00000147044; Low tissue specificity. DR MalaCards; CASK; -. DR MIM; 300172; gene. DR MIM; 300422; phenotype. DR MIM; 300749; phenotype. DR neXtProt; NX_O14936; -. DR OpenTargets; ENSG00000147044; -. DR Orphanet; 1934; Early infantile epileptic encephalopathy. DR Orphanet; 323; NON RARE IN EUROPE: FG syndrome phenotypic spectrum. DR Orphanet; 163937; X-linked intellectual disability, Najm type. DR PharmGKB; PA26081; -. DR VEuPathDB; HostDB:ENSG00000147044; -. DR eggNOG; KOG0033; Eukaryota. DR eggNOG; KOG0609; Eukaryota. DR GeneTree; ENSGT00940000155600; -. DR HOGENOM; CLU_001715_5_3_1; -. DR InParanoid; O14936; -. DR OrthoDB; 95102at2759; -. DR PhylomeDB; O14936; -. DR TreeFam; TF314263; -. DR BRENDA; 2.7.11.1; 2681. DR BRENDA; 2.7.4.8; 2681. DR PathwayCommons; O14936; -. DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-373753; Nephrin family interactions. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR SABIO-RK; O14936; -. DR SignaLink; O14936; -. DR SIGNOR; O14936; -. DR BioGRID-ORCS; 8573; 13 hits in 730 CRISPR screens. DR ChiTaRS; CASK; human. DR EvolutionaryTrace; O14936; -. DR GeneWiki; CASK; -. DR GenomeRNAi; 8573; -. DR Pharos; O14936; Tchem. DR PRO; PR:O14936; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; O14936; protein. DR Bgee; ENSG00000147044; Expressed in buccal mucosa cell and 209 other tissues. DR ExpressionAtlas; O14936; baseline and differential. DR Genevisible; O14936; HS. DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc. DR GO; GO:0005604; C:basement membrane; IDA:CACAO. DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central. DR GO; GO:0005911; C:cell-cell junction; IDA:BHF-UCL. DR GO; GO:0060170; C:ciliary membrane; ISS:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005652; C:nuclear lamina; IDA:BHF-UCL. DR GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL. DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0031982; C:vesicle; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0004385; F:guanylate kinase activity; TAS:ProtInc. DR GO; GO:0042043; F:neurexin family protein binding; IEA:Ensembl. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IMP:BHF-UCL. DR GO; GO:0090288; P:negative regulation of cellular response to growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IDA:CACAO. DR GO; GO:0061045; P:negative regulation of wound healing; IMP:BHF-UCL. DR GO; GO:0090280; P:positive regulation of calcium ion import; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl. DR CDD; cd12081; SH3_CASK; 1. DR DisProt; DP01438; -. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR035473; CASK_SH3. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR014775; L27_C. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR036892; L27_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 2. DR SMART; SM00228; PDZ; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF101288; SSF101288; 2. DR SUPFAM; SSF50044; SSF50044; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS51022; L27; 2. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding; KW Cell membrane; Cytoplasm; Disease variant; Intellectual disability; Kinase; KW Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Serine/threonine-protein kinase; SH3 domain; Transferase. FT CHAIN 1..926 FT /note="Peripheral plasma membrane protein CASK" FT /id="PRO_0000094568" FT DOMAIN 12..276 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 343..398 FT /note="L27 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 402..455 FT /note="L27 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 489..564 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 612..682 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 739..911 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT REGION 305..315 FT /note="Calmodulin-binding" FT REGION 482..909 FT /note="Required for interaction with NRXN1 (via C-terminal FT tail)" FT /evidence="ECO:0000250|UniProtKB:Q62915" FT REGION 574..610 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 141 FT /evidence="ECO:0000250" FT BINDING 18..26 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 41 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 51 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 151 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:18423203" FT MOD_RES 155 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:18423203" FT MOD_RES 182 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O70589" FT MOD_RES 313 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..385 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_024421" FT VAR_SEQ 340..345 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11003712, ECO:0000303|Ref.2" FT /id="VSP_024422" FT VAR_SEQ 386 FT /note="L -> M (in isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_024423" FT VAR_SEQ 580..602 FT /note="Missing (in isoform 3, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11003712, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2, FT ECO:0000303|Ref.3" FT /id="VSP_024424" FT VAR_SEQ 603..614 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_024425" FT VAR_SEQ 719..723 FT /note="Missing (in isoform 2, isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9660868, ECO:0000303|Ref.4, FT ECO:0000303|Ref.7" FT /id="VSP_024426" FT VARIANT 19..926 FT /note="Missing (probable disease-associated variant found FT in a patient with epilepsy and pontocerebellar hypoplasia)" FT /evidence="ECO:0000269|PubMed:23662938" FT /id="VAR_078710" FT VARIANT 28 FT /note="R -> L (in FGS4; does not reveal significant FT alterations induced by the mutation substitution; causes a FT partial skipping of exon 2 of the protein; FT dbSNP:rs137852816)" FT /evidence="ECO:0000269|PubMed:19200522" FT /id="VAR_058719" FT VARIANT 96 FT /note="G -> V (in a lung large cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041956" FT VARIANT 268 FT /note="Y -> H (in MICPCH; dbSNP:rs137852817)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062996" FT VARIANT 396 FT /note="P -> S (in MICPCH; dbSNP:rs137852820)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062997" FT VARIANT 710 FT /note="D -> G (in MICPCH; dbSNP:rs137852818)" FT /evidence="ECO:0000269|PubMed:19377476" FT /id="VAR_062998" FT CONFLICT 401 FT /note="P -> L (in Ref. 2; AAB88198)" FT /evidence="ECO:0000305" FT CONFLICT 479 FT /note="D -> G (in Ref. 1; AAB88125, 3; BAB12252, 4; FT AAU10527 and 8; AAF72666/AAF72667)" FT /evidence="ECO:0000305" FT CONFLICT 675 FT /note="P -> S (in Ref. 1; AAB88125 and 4; AAU10527)" FT /evidence="ECO:0000305" FT CONFLICT 780 FT /note="K -> R (in Ref. 1; AAB88125 and 4; AAU10527)" FT /evidence="ECO:0000305" FT HELIX 8..11 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 12..20 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 22..31 FT /evidence="ECO:0007829|PDB:3C0I" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 37..44 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 45..49 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 56..68 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 99..108 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 115..134 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:3C0I" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:3TAC" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:3MFS" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 188..191 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 199..214 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 223..232 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 239..242 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 247..256 FT /evidence="ECO:0007829|PDB:3C0I" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 267..271 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 274..277 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:3C0I" FT HELIX 289..302 FT /evidence="ECO:0007829|PDB:3C0I" FT TURN 304..306 FT /evidence="ECO:0007829|PDB:3TAC" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:3C0G" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:3C0G" FT HELIX 404..416 FT /evidence="ECO:0007829|PDB:1ZL8" FT HELIX 423..431 FT /evidence="ECO:0007829|PDB:1ZL8" FT HELIX 437..450 FT /evidence="ECO:0007829|PDB:1ZL8" FT STRAND 489..495 FT /evidence="ECO:0007829|PDB:1KWA" FT STRAND 497..499 FT /evidence="ECO:0007829|PDB:1KWA" FT STRAND 503..506 FT /evidence="ECO:0007829|PDB:1KWA" FT HELIX 510..512 FT /evidence="ECO:0007829|PDB:1KWA" FT STRAND 513..518 FT /evidence="ECO:0007829|PDB:1KWA" FT HELIX 523..527 FT /evidence="ECO:0007829|PDB:1KWA" FT STRAND 535..539 FT /evidence="ECO:0007829|PDB:1KWA" FT HELIX 544..546 FT /evidence="ECO:0007829|PDB:1KWA" FT HELIX 549..558 FT /evidence="ECO:0007829|PDB:1KWA" FT STRAND 561..568 FT /evidence="ECO:0007829|PDB:1KWA" FT STRAND 741..745 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 752..762 FT /evidence="ECO:0007829|PDB:1KGD" FT TURN 764..766 FT /evidence="ECO:0007829|PDB:1KGD" FT TURN 784..786 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 793..801 FT /evidence="ECO:0007829|PDB:1KGD" FT STRAND 805..811 FT /evidence="ECO:0007829|PDB:1KGD" FT STRAND 814..819 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 820..828 FT /evidence="ECO:0007829|PDB:1KGD" FT STRAND 832..836 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 839..841 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 842..845 FT /evidence="ECO:0007829|PDB:1KGD" FT TURN 848..850 FT /evidence="ECO:0007829|PDB:1KGD" FT STRAND 852..858 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 870..886 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 887..889 FT /evidence="ECO:0007829|PDB:1KGD" FT STRAND 891..895 FT /evidence="ECO:0007829|PDB:1KGD" FT HELIX 899..913 FT /evidence="ECO:0007829|PDB:1KGD" FT MOD_RES O14936-3:571 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES O14936-4:577 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES O14936-5:192 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" SQ SEQUENCE 926 AA; 105123 MW; 6C02008CE52728BA CRC64; MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNAVF DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK DEENGKNYYF VSHDQMMQDI SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ ALKVLRTAEF APFVVFIAAP TITPGLNEDE SLQRLQKESD ILQRTYAHYF DLTIINNEID ETIRHLEEAV ELVCTAPQWV PVSWVY //