CSKP_HUMAN
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 03-AUG-2022, entry version 232.
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; 170.
DR CORUM; O14936; -.
DR DIP; DIP-38727N; -.
DR ELM; O14936; -.
DR IntAct; O14936; 90.
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; 309 antibodies from 39 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
