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O14936 (CSKP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peripheral plasma membrane protein CASK

Short name=hCASK
EC=2.7.11.1
Alternative name(s):
Calcium/calmodulin-dependent serine protein kinase
Protein lin-2 homolog
Gene names
Name:CASK
Synonyms:LIN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length926 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity. Ref.11

Enzyme regulation

Differs from archetypal CaMK members in that the kinase domain exhibits a constitutively active conformation and the autoinhibitory region does not engage in direct contact with the ATP-binding cleft, although it still binds Ca2+/CAM. Ref.11

Subunit structure

Binds WHRN and NRXN1 cytosolic tail. Interacts with CASKIN1, APBA1, LIN7(A/B/C) and L27 domain of DLG1 and isoform 2 of DLG4 By similarity. CASK and LIN7 form two mutually exclusive tripartite complexes with APBA1 or CASKIN1 By similarity. Interacts with FCHSD2. Interacts with TSPYL2. Part of a complex containing CASK, TBR1 and TSPYL2 By similarity. Identified in a complex with ACTN4, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 By similarity. Interacts with KIRREL3. Ref.1 Ref.9

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cell membrane; Peripheral membrane protein By similarity.

Tissue specificity

Ubiquitous. Expression is significantly greater in brain relative to kidney, lung, and liver and in fetal brain and kidney relative to lung and liver. Ref.8

Domain

The first L27 domain binds DLG1 and the second L27 domain probably binds LIN7 By similarity.

The protein kinase domain mediates the interaction with FCHSD2.

Involvement in disease

Mental retardation and microcephaly with pontine and cerebellar hypoplasia (MICPCH) [MIM:300749]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Affected individuals can manifest a severe phenotype consisting of severe intellectual deficit, congenital or postnatal microcephaly, disproportionate brainstem and cerebellar hypoplasia. A milder phenotype consists of mental retardation alone or associated with nystagmus.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

FG syndrome 4 (FGS4) [MIM:300422]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Sequence similarities

In the N-terminal section; belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 2 L27 domains.

Contains 1 PDZ (DHR) domain.

Contains 1 protein kinase domain.

Contains 1 SH3 domain.

Biophysicochemical properties

Kinetic parameters:

Kinetics of autophosphorylation assay were measured, rather than phosphorylation of an exogenous substrate.

KM=563 µM for ATP Ref.11

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainRepeat
SH3 domain
   LigandATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion import

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

extracellular matrix organization

Traceable author statement. Source: Reactome

negative regulation of cell-matrix adhesion

Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL

negative regulation of cellular response to growth factor stimulus

Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL

negative regulation of keratinocyte proliferation

Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL

negative regulation of wound healing

Inferred from mutant phenotype PubMed 18664494. Source: BHF-UCL

nucleotide phosphorylation

Traceable author statement Ref.1. Source: GOC

positive regulation of calcium ion import

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

basement membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

ciliary membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

cytosol

Inferred from electronic annotation. Source: Ensembl

nuclear lamina

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

nuclear matrix

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

nucleolus

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

presynaptic membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

guanylate kinase activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 11377421PubMed 15694377PubMed 16688213Ref.11PubMed 21763699PubMed 24366813Ref.1. Source: IntAct

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14936-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O14936-2)

The sequence of this isoform differs from the canonical sequence as follows:
     719-723: Missing.
Isoform 3 (identifier: O14936-3)

The sequence of this isoform differs from the canonical sequence as follows:
     340-345: Missing.
     580-602: Missing.
Isoform 4 (identifier: O14936-4)

The sequence of this isoform differs from the canonical sequence as follows:
     580-602: Missing.
     719-723: Missing.
Isoform 5 (identifier: O14936-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-385: Missing.
     386-386: L → M
     580-602: Missing.
Isoform 6 (identifier: O14936-6)

The sequence of this isoform differs from the canonical sequence as follows:
     603-614: Missing.
     719-723: Missing.
Note: Gene prediction confirmed by EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 926926Peripheral plasma membrane protein CASK
PRO_0000094568

Regions

Domain12 – 276265Protein kinase
Domain343 – 39856L27 1
Domain402 – 45554L27 2
Domain489 – 56476PDZ
Domain615 – 68268SH3
Domain739 – 911173Guanylate kinase-like
Nucleotide binding18 – 269ATP By similarity
Region305 – 31511Calmodulin-binding

Sites

Active site1411 By similarity
Binding site411ATP By similarity

Amino acid modifications

Modified residue1511Phosphoserine; by autocatalysis Ref.11
Modified residue1551Phosphoserine; by autocatalysis Ref.11

Natural variations

Alternative sequence1 – 385385Missing in isoform 5.
VSP_024421
Alternative sequence340 – 3456Missing in isoform 3.
VSP_024422
Alternative sequence3861L → M in isoform 5.
VSP_024423
Alternative sequence580 – 60223Missing in isoform 3, isoform 4 and isoform 5.
VSP_024424
Alternative sequence603 – 61412Missing in isoform 6.
VSP_024425
Alternative sequence719 – 7235Missing in isoform 2, isoform 4 and isoform 6.
VSP_024426
Natural variant281R → L in FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein. Ref.15
VAR_058719
Natural variant961G → V in a lung large cell carcinoma sample; somatic mutation. Ref.12
VAR_041956
Natural variant2681Y → H in MICPCH. Ref.16
VAR_062996
Natural variant3961P → S in MICPCH. Ref.16
VAR_062997
Natural variant7101D → G in MICPCH. Ref.16
VAR_062998

Experimental info

Sequence conflict4011P → L in AAB88198. Ref.2
Sequence conflict4791D → G in AAB88125. Ref.1
Sequence conflict4791D → G in BAB12252. Ref.3
Sequence conflict4791D → G in AAU10527. Ref.4
Sequence conflict4791D → G in AAF72666. Ref.8
Sequence conflict4791D → G in AAF72667. Ref.8
Sequence conflict6751P → S in AAB88125. Ref.1
Sequence conflict6751P → S in AAU10527. Ref.4
Sequence conflict7801K → R in AAB88125. Ref.1
Sequence conflict7801K → R in AAU10527. Ref.4

Secondary structure

................................................................................................................... 926
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 17, 2007. Version 3.
Checksum: 6C02008CE52728BA

FASTA926105,123
        10         20         30         40         50         60 
MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK 

        70         80         90        100        110        120 
REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH 

       130        140        150        160        170        180 
YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV 

       190        200        210        220        230        240 
GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR 

       250        260        270        280        290        300 
QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA 

       310        320        330        340        350        360 
RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL 

       370        380        390        400        410        420 
TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP 

       430        440        450        460        470        480 
ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM 

       490        500        510        520        530        540 
DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN 

       550        560        570        580        590        600 
GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS 

       610        620        630        640        650        660 
VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK 

       670        680        690        700        710        720 
LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNAVF 

       730        740        750        760        770        780 
DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK 

       790        800        810        820        830        840 
DEENGKNYYF VSHDQMMQDI SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ 

       850        860        870        880        890        900 
ALKVLRTAEF APFVVFIAAP TITPGLNEDE SLQRLQKESD ILQRTYAHYF DLTIINNEID 

       910        920 
ETIRHLEEAV ELVCTAPQWV PVSWVY 

« Hide

Isoform 2 [UniParc].

Checksum: C3C9FAE8D051AA27
Show »

FASTA921104,520
Isoform 3 [UniParc].

Checksum: 8B3BC03D2EF717CA
Show »

FASTA897102,114
Isoform 4 [UniParc].

Checksum: B7BC96EB46CCD791
Show »

FASTA898102,165
Isoform 5 [UniParc].

Checksum: 855EE0A1FC92D5B0
Show »

FASTA51859,383
Isoform 6 [UniParc].

Checksum: B0B98E6A73E36142
Show »

FASTA909103,211

References

« Hide 'large scale' references
[1]"Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells."
Cohen A.R., Woods D.F., Marfatia S.M., Walther Z., Chishti A.H., Anderson J.M.
J. Cell Biol. 142:129-138(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SDC2 AND EPB41.
Tissue: Brain, Liver and Lung.
[2]"The human homolog of the rat CASK, Drosophila Camguk and C.elegans Lin-2 genes."
Zha D., Hu G.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]"Putative alternative splicing form of human CASK mRNA (partial codes)."
Ding L., Saijo K., Kawai K., Akaza H., Ugai H., Yokoyama K.K., Ohno T.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Tissue: Kidney.
[4]"Caco2-BBE calcium/calmodulin-dependent serine protein kinase."
Yan Y., Merlin D.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Colon carcinoma.
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[7]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-926 (ISOFORM 2).
Tissue: Brain.
[8]"Mapping and expression analysis of the human CASK gene."
Stevenson D., Laverty H.G., Wenwieser S., Douglas M., Wilson J.B.
Mamm. Genome 11:934-937(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 173-926 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 27-926 (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Fetus.
[9]"Alterations in CDH15 and KIRREL3 in patients with mild to severe intellectual disability."
Bhalla K., Luo Y., Buchan T., Beachem M.A., Guzauskas G.F., Ladd S., Bratcher S.J., Schroer R.J., Balsamo J., DuPont B.R., Lilien J., Srivastava A.K.
Am. J. Hum. Genet. 83:703-713(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIRREL3.
[10]"Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition."
Daniels D.L., Cohen A.R., Anderson J.M., Bruenger A.T.
Nat. Struct. Biol. 5:317-325(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-572.
[11]"CASK functions as a Mg2+-independent neurexin kinase."
Mukherjee K., Sharma M., Urlaub H., Bourenkov G.P., Jahn R., Suedhof T.C., Wahl M.C.
Cell 133:328-339(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-337 IN COMPLEX WITH AMP, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION OF NRXN1, AUTOPHOSPHORYLATION AT SER-151 AND SER-155.
[12]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-96.
[13]"Mutations of CASK cause an X-linked brain malformation phenotype with microcephaly and hypoplasia of the brainstem and cerebellum."
Najm J., Horn D., Wimplinger I., Golden J.A., Chizhikov V.V., Sudi J., Christian S.L., Ullmann R., Kuechler A., Haas C.A., Flubacher A., Charnas L.R., Uyanik G., Frank U., Klopocki E., Dobyns W.B., Kutsche K.
Nat. Genet. 40:1065-1067(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MICPCH SYNDROME.
[14]Erratum
Najm J., Horn D., Wimplinger I., Golden J.A., Chizhikov V.V., Sudi J., Christian S.L., Ullmann R., Kuechler A., Haas C.A., Flubacher A., Charnas L.R., Uyanik G., Frank U., Klopocki E., Dobyns W.B., Kutsche K.
Nat. Genet. 40:1384-1384(2008)
[15]"A missense mutation in CASK causes FG syndrome in an Italian family."
Piluso G., D'Amico F., Saccone V., Bismuto E., Rotundo I.L., Di Domenico M., Aurino S., Schwartz C.E., Neri G., Nigro V.
Am. J. Hum. Genet. 84:162-177(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FGS4 LEU-28, CHARACTERIZATION OF VARIANT FGS4 LEU-28.
[16]"A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation."
Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C., O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M., Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J. expand/collapse author list , Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M., Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P., Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R., Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R., de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M., Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U., Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M., Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T., Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C., Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L., Futreal P.A., Stratton M.R.
Nat. Genet. 41:535-543(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] MICPCH HIS-268; SER-396 AND GLY-710.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF032119 mRNA. Translation: AAB88125.1.
AF035582 mRNA. Translation: AAB88198.1.
AB039327 mRNA. Translation: BAB12252.2.
AY705392 mRNA. Translation: AAU10527.1.
AL627402 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71237.1.
AL627402 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71238.1.
AL627402 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71239.1.
AL627402 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71240.1.
AL445239 expand/collapse EMBL AC list , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41092.1.
AL445239 expand/collapse EMBL AC list , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41093.1.
AL445239 expand/collapse EMBL AC list , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41094.1.
AL445239 expand/collapse EMBL AC list , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41095.1.
AL603754 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41634.1.
AL603754 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41635.1.
AL603754 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41636.1.
AL603754 expand/collapse EMBL AC list , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41637.1.
AL353691 expand/collapse EMBL AC list , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42244.1.
AL353691 expand/collapse EMBL AC list , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42245.1.
AL353691 expand/collapse EMBL AC list , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42246.1.
AL353691 expand/collapse EMBL AC list , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42247.1.
AL158144 expand/collapse EMBL AC list , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42762.1.
AL158144 expand/collapse EMBL AC list , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42763.1.
AL158144 expand/collapse EMBL AC list , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42764.1.
AL158144 expand/collapse EMBL AC list , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42765.1.
BC117311 mRNA. Translation: AAI17312.1.
BC143454 mRNA. Translation: AAI43455.1.
AB208859 mRNA. Translation: BAD92096.1.
AF262404 mRNA. Translation: AAF72666.1.
AF262405 mRNA. Translation: AAF72667.1.
CCDSCCDS14257.1. [O14936-2]
CCDS48094.1. [O14936-3]
CCDS48095.1. [O14936-4]
RefSeqNP_001119526.1. NM_001126054.2. [O14936-4]
NP_001119527.1. NM_001126055.2. [O14936-3]
NP_003679.2. NM_003688.3. [O14936-2]
UniGeneHs.495984.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KGDX-ray1.31A739-914[»]
1KWAX-ray1.93A/B487-572[»]
1ZL8NMR-B403-456[»]
3C0GX-ray2.19A/B1-337[»]
3C0HX-ray2.30A/B1-337[»]
3C0IX-ray1.85A1-337[»]
3MFRX-ray2.00A1-337[»]
3MFSX-ray2.10A1-337[»]
3MFTX-ray2.20A1-337[»]
3MFUX-ray2.30A1-337[»]
3TACX-ray2.20A1-345[»]
ProteinModelPortalO14936.
SMRO14936. Positions 5-394, 403-456, 487-572, 615-921.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114141. 50 interactions.
DIPDIP-38727N.
IntActO14936. 34 interactions.
MINTMINT-102444.

Chemistry

BindingDBO14936.
ChEMBLCHEMBL1908381.
GuidetoPHARMACOLOGY1959.

PTM databases

PhosphoSiteO14936.

Proteomic databases

MaxQBO14936.
PaxDbO14936.
PRIDEO14936.

Protocols and materials databases

DNASU8573.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378158; ENSP00000367400; ENSG00000147044. [O14936-6]
ENST00000378163; ENSP00000367405; ENSG00000147044. [O14936-1]
ENST00000378166; ENSP00000367408; ENSG00000147044. [O14936-2]
ENST00000421587; ENSP00000400526; ENSG00000147044. [O14936-3]
ENST00000442742; ENSP00000398007; ENSG00000147044. [O14936-4]
GeneID8573.
KEGGhsa:8573.
UCSCuc004dfk.4. human. [O14936-1]
uc004dfl.4. human. [O14936-2]
uc004dfm.4. human. [O14936-4]
uc004dfn.4. human. [O14936-3]

Organism-specific databases

CTD8573.
GeneCardsGC0XM041374.
GeneReviewsCASK.
HGNCHGNC:1497. CASK.
HPACAB001949.
HPA023857.
MIM300172. gene.
300422. phenotype.
300749. phenotype.
neXtProtNX_O14936.
Orphanet323. FG syndrome.
163937. X-linked intellectual disability, Najm type.
PharmGKBPA26081.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG001858.
KOK06103.
OMARCINRET.
OrthoDBEOG79CXZ5.
PhylomeDBO14936.
TreeFamTF314263.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.
SignaLinkO14936.

Gene expression databases

ArrayExpressO14936.
BgeeO14936.
CleanExHS_CASK.
GenevestigatorO14936.

Family and domain databases

Gene3D2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR011009. Kinase-like_dom.
IPR004172. L27.
IPR014775. L27_C.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR000719. Prot_kinase_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
PF02828. L27. 2 hits.
PF00595. PDZ. 1 hit.
PF00069. Pkinase. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
SM00569. L27. 2 hits.
SM00228. PDZ. 1 hit.
SM00220. S_TKc. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 2 hits.
PS50106. PDZ. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCASK. human.
EvolutionaryTraceO14936.
GeneWikiCASK.
GenomeRNAi8573.
NextBio32157.
PROO14936.
SOURCESearch...

Entry information

Entry nameCSKP_HUMAN
AccessionPrimary (citable) accession number: O14936
Secondary accession number(s): A6NES1 expand/collapse secondary AC list , B7ZKY0, O43215, Q17RI4, Q59HA0, Q5VT16, Q5VT17, Q5VT18, Q5VT19, Q66T42, Q9BYH6, Q9NYB2, Q9NYB3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM