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Protein

Peripheral plasma membrane protein CASK

Gene

CASK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Note: Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity.1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

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

  1. KM=563 µM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411ATPPROSITE-ProRule annotation
    Active sitei141 – 1411By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • guanylate kinase activity Source: ProtInc
    • protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    • calcium ion import Source: Ensembl
    • cell adhesion Source: ProtInc
    • extracellular matrix organization Source: Reactome
    • negative regulation of cell-matrix adhesion Source: BHF-UCL
    • negative regulation of cellular response to growth factor stimulus Source: BHF-UCL
    • negative regulation of keratinocyte proliferation Source: CACAO
    • negative regulation of wound healing Source: BHF-UCL
    • neurotransmitter secretion Source: Reactome
    • nucleotide phosphorylation Source: GOC
    • positive regulation of calcium ion import Source: Ensembl
    • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    • synaptic transmission Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    2.7.4.8. 2681.
    ReactomeiREACT_15293. Dopamine Neurotransmitter Release Cycle.
    REACT_163942. Syndecan interactions.
    REACT_23832. Nephrin interactions.
    SignaLinkiO14936.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peripheral plasma membrane protein CASK (EC:2.7.11.1)
    Short name:
    hCASK
    Alternative name(s):
    Calcium/calmodulin-dependent serine protein kinase
    Protein lin-2 homolog
    Gene namesi
    Name:CASK
    Synonyms:LIN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:1497. CASK.

    Subcellular locationi

    GO - Cellular componenti

    • actin cytoskeleton Source: ProtInc
    • basement membrane Source: CACAO
    • basolateral plasma membrane Source: Ensembl
    • cell-cell junction Source: BHF-UCL
    • ciliary membrane Source: BHF-UCL
    • cytoplasm Source: BHF-UCL
    • cytosol Source: Reactome
    • focal adhesion Source: UniProtKB
    • nuclear lamina Source: BHF-UCL
    • nuclear matrix Source: BHF-UCL
    • nucleolus Source: BHF-UCL
    • plasma membrane Source: ProtInc
    • presynaptic membrane Source: BHF-UCL
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation and microcephaly with pontine and cerebellar hypoplasia (MICPCH)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:300749
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti268 – 2681Y → H in MICPCH. 1 Publication
    VAR_062996
    Natural varianti396 – 3961P → S in MICPCH. 1 Publication
    VAR_062997
    Natural varianti710 – 7101D → G in MICPCH. 1 Publication
    VAR_062998
    FG syndrome 4 (FGS4)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionFG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.

    See also OMIM:300422
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281R → L in FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein. 1 Publication
    VAR_058719

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300422. phenotype.
    300749. phenotype.
    Orphaneti1934. Early infantile epileptic encephalopathy.
    323. FG syndrome.
    163937. X-linked intellectual disability, Najm type.
    PharmGKBiPA26081.

    Polymorphism and mutation databases

    BioMutaiCASK.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 926926Peripheral plasma membrane protein CASKPRO_0000094568Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei151 – 1511Phosphoserine; by autocatalysis1 Publication
    Modified residuei155 – 1551Phosphoserine; by autocatalysis1 Publication
    Modified residuei313 – 3131Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO14936.
    PaxDbiO14936.
    PRIDEiO14936.

    PTM databases

    PhosphoSiteiO14936.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expression is significantly greater in brain relative to kidney, lung, and liver and in fetal brain and kidney relative to lung and liver.1 Publication

    Gene expression databases

    BgeeiO14936.
    CleanExiHS_CASK.
    ExpressionAtlasiO14936. baseline and differential.
    GenevestigatoriO14936.

    Organism-specific databases

    HPAiCAB001949.
    HPA023857.

    Interactioni

    Subunit structurei

    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.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASKIN1Q8WXD94EBI-1215506,EBI-970261
    EPS8Q129293EBI-1215506,EBI-375576
    ID1P411343EBI-1215506,EBI-1215527
    LIN7AO149106EBI-1215506,EBI-2513988
    Nrxn1Q633733EBI-1215506,EBI-1780696From a different organism.
    RPH3AQ9Y2J03EBI-1215506,EBI-1216802
    SDC2P347412EBI-1215506,EBI-1172957
    SH2D4AQ9H7883EBI-1215506,EBI-747035
    SNTB2Q134252EBI-1215506,EBI-80411

    Protein-protein interaction databases

    BioGridi114141. 58 interactions.
    DIPiDIP-38727N.
    IntActiO14936. 36 interactions.
    MINTiMINT-102444.

    Structurei

    Secondary structure

    1
    926
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114Combined sources
    Beta strandi12 – 209Combined sources
    Beta strandi22 – 3110Combined sources
    Turni32 – 343Combined sources
    Beta strandi37 – 448Combined sources
    Helixi45 – 495Combined sources
    Beta strandi51 – 533Combined sources
    Helixi56 – 6813Combined sources
    Beta strandi77 – 837Combined sources
    Beta strandi86 – 927Combined sources
    Helixi99 – 10810Combined sources
    Helixi115 – 13420Combined sources
    Helixi144 – 1463Combined sources
    Beta strandi147 – 1493Combined sources
    Beta strandi151 – 1533Combined sources
    Beta strandi158 – 1603Combined sources
    Helixi163 – 1653Combined sources
    Beta strandi171 – 1733Combined sources
    Helixi183 – 1853Combined sources
    Helixi188 – 1914Combined sources
    Helixi199 – 21416Combined sources
    Helixi223 – 23210Combined sources
    Helixi239 – 2424Combined sources
    Helixi247 – 25610Combined sources
    Turni261 – 2633Combined sources
    Helixi267 – 2715Combined sources
    Helixi274 – 2774Combined sources
    Helixi279 – 2824Combined sources
    Helixi289 – 30214Combined sources
    Turni304 – 3063Combined sources
    Helixi309 – 3124Combined sources
    Helixi404 – 41613Combined sources
    Helixi423 – 4319Combined sources
    Helixi437 – 45014Combined sources
    Beta strandi489 – 4957Combined sources
    Beta strandi497 – 4993Combined sources
    Beta strandi503 – 5064Combined sources
    Helixi510 – 5123Combined sources
    Beta strandi513 – 5186Combined sources
    Helixi523 – 5275Combined sources
    Beta strandi535 – 5395Combined sources
    Helixi544 – 5463Combined sources
    Helixi549 – 55810Combined sources
    Beta strandi561 – 5688Combined sources
    Beta strandi741 – 7455Combined sources
    Helixi752 – 76211Combined sources
    Turni764 – 7663Combined sources
    Turni784 – 7863Combined sources
    Helixi793 – 8019Combined sources
    Beta strandi805 – 8117Combined sources
    Beta strandi814 – 8196Combined sources
    Helixi820 – 8289Combined sources
    Beta strandi832 – 8365Combined sources
    Helixi839 – 8413Combined sources
    Helixi842 – 8454Combined sources
    Turni848 – 8503Combined sources
    Beta strandi852 – 8587Combined sources
    Helixi870 – 88617Combined sources
    Helixi887 – 8893Combined sources
    Beta strandi891 – 8955Combined sources
    Helixi899 – 91315Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliO14936.
    SMRiO14936. Positions 5-394, 403-456, 487-925.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14936.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 276265Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini343 – 39856L27 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini402 – 45554L27 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 56476PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 68268SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini739 – 911173Guanylate kinase-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni305 – 31511Calmodulin-bindingAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    In the N-terminal section; belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.Curated
    Belongs to the MAGUK family.Curated
    Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
    Contains 2 L27 domains.PROSITE-ProRule annotation
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00760000118866.
    HOVERGENiHBG001858.
    InParanoidiO14936.
    KOiK06103.
    OMAiRCINRET.
    OrthoDBiEOG79CXZ5.
    PhylomeDBiO14936.
    TreeFamiTF314263.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR008145. 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.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    PF02828. L27. 2 hits.
    PF00595. PDZ. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    SMARTiSM00072. GuKc. 1 hit.
    SM00569. L27. 2 hits.
    SM00228. PDZ. 1 hit.
    SM00220. S_TKc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00856. 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]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: O14936-1) [UniParc]FASTAAdd to basket

    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.

    « Hide

            10         20         30         40         50
    MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS
    60 70 80 90 100
    SPGLSTEDLK REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC
    110 120 130 140 150
    FEIVKRADAG FVYSEAVASH YMRQILEALR YCHDNNIIHR DVKPHCVLLA
    160 170 180 190 200
    SKENSAPVKL GGFGVAIQLG ESGLVAGGRV GTPHFMAPEV VKREPYGKPV
    210 220 230 240 250
    DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR QWSHISESAK
    260 270 280 290 300
    DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA
    310 320 330 340 350
    RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV
    360 370 380 390 400
    LDSLEEIHAL TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN
    410 420 430 440 450
    PPSDAVQRAK EVLEEISCYP ENNDAKELKR ILTQPHFMAL LQTHDVVAHE
    460 470 480 490 500
    VYSDEALRVT PPPTSPYLNG DSPESANGDM DMENVTRVRL VQFQKNTDEP
    510 520 530 540 550
    MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN GISVANQTVE
    560 570 580 590 600
    QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS
    610 620 630 640 650
    VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS
    660 670 680 690 700
    KDDHNWWQGK LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW
    710 720 730 740 750
    FGKKKKQYKD KYLAKHNAVF DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV
    760 770 780 790 800
    GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK DEENGKNYYF VSHDQMMQDI
    810 820 830 840 850
    SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ ALKVLRTAEF
    860 870 880 890 900
    APFVVFIAAP TITPGLNEDE SLQRLQKESD ILQRTYAHYF DLTIINNEID
    910 920
    ETIRHLEEAV ELVCTAPQWV PVSWVY
    Length:926
    Mass (Da):105,123
    Last modified:April 17, 2007 - v3
    Checksum:i6C02008CE52728BA
    GO
    Isoform 2 (identifier: O14936-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         719-723: Missing.

    Show »
    Length:921
    Mass (Da):104,520
    Checksum:iC3C9FAE8D051AA27
    GO
    Isoform 3 (identifier: O14936-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         340-345: Missing.
         580-602: Missing.

    Note: Contains a phosphoserine at position 571.1 Publication

    Show »
    Length:897
    Mass (Da):102,114
    Checksum:i8B3BC03D2EF717CA
    GO
    Isoform 4 (identifier: O14936-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         580-602: Missing.
         719-723: Missing.

    Note: Contains a phosphoserine at position 577.1 Publication

    Show »
    Length:898
    Mass (Da):102,165
    Checksum:iB7BC96EB46CCD791
    GO
    Isoform 5 (identifier: O14936-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-385: Missing.
         386-386: L → M
         580-602: Missing.

    Note: Contains a phosphoserine at position 192.1 Publication

    Show »
    Length:518
    Mass (Da):59,383
    Checksum:i855EE0A1FC92D5B0
    GO
    Isoform 6 (identifier: O14936-6) [UniParc]FASTAAdd to basket

    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.

    Show »
    Length:909
    Mass (Da):103,211
    Checksum:iB0B98E6A73E36142
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti401 – 4011P → L in AAB88198 (Ref. 2) Curated
    Sequence conflicti479 – 4791D → G in AAB88125 (PubMed:9660868).Curated
    Sequence conflicti479 – 4791D → G in BAB12252 (Ref. 3) Curated
    Sequence conflicti479 – 4791D → G in AAU10527 (Ref. 4) Curated
    Sequence conflicti479 – 4791D → G in AAF72666 (PubMed:11003712).Curated
    Sequence conflicti479 – 4791D → G in AAF72667 (PubMed:11003712).Curated
    Sequence conflicti675 – 6751P → S in AAB88125 (PubMed:9660868).Curated
    Sequence conflicti675 – 6751P → S in AAU10527 (Ref. 4) Curated
    Sequence conflicti780 – 7801K → R in AAB88125 (PubMed:9660868).Curated
    Sequence conflicti780 – 7801K → R in AAU10527 (Ref. 4) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281R → L in FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein. 1 Publication
    VAR_058719
    Natural varianti96 – 961G → V in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041956
    Natural varianti268 – 2681Y → H in MICPCH. 1 Publication
    VAR_062996
    Natural varianti396 – 3961P → S in MICPCH. 1 Publication
    VAR_062997
    Natural varianti710 – 7101D → G in MICPCH. 1 Publication
    VAR_062998

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 385385Missing in isoform 5. 1 PublicationVSP_024421Add
    BLAST
    Alternative sequencei340 – 3456Missing in isoform 3. 2 PublicationsVSP_024422
    Alternative sequencei386 – 3861L → M in isoform 5. 1 PublicationVSP_024423
    Alternative sequencei580 – 60223Missing in isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_024424Add
    BLAST
    Alternative sequencei603 – 61412Missing in isoform 6. CuratedVSP_024425Add
    BLAST
    Alternative sequencei719 – 7235Missing in isoform 2, isoform 4 and isoform 6. 4 PublicationsVSP_024426

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF032119 mRNA. Translation: AAB88125.1.
    AF035582 mRNA. Translation: AAB88198.1.
    AB039327 mRNA. Translation: BAB12252.2.
    AY705392 mRNA. Translation: AAU10527.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71237.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71238.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71239.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71240.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41092.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41093.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41094.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41095.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41634.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41635.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41636.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41637.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42244.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42245.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42246.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42247.1.
    AL158144
    , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42762.1.
    AL158144
    , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42763.1.
    AL158144
    , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42764.1.
    AL158144
    , 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.
    CCDSiCCDS14257.1. [O14936-2]
    CCDS48094.1. [O14936-3]
    CCDS48095.1. [O14936-4]
    RefSeqiNP_001119526.1. NM_001126054.2. [O14936-4]
    NP_001119527.1. NM_001126055.2. [O14936-3]
    NP_003679.2. NM_003688.3. [O14936-2]
    UniGeneiHs.495984.

    Genome annotation databases

    EnsembliENST00000378158; ENSP00000367400; ENSG00000147044. [O14936-6]
    ENST00000378163; ENSP00000367405; ENSG00000147044. [O14936-1]
    ENST00000378166; ENSP00000367408; ENSG00000147044. [O14936-2]
    ENST00000421587; ENSP00000400526; ENSG00000147044. [O14936-3]
    ENST00000442742; ENSP00000398007; ENSG00000147044. [O14936-4]
    GeneIDi8573.
    KEGGihsa:8573.
    UCSCiuc004dfk.4. human. [O14936-1]
    uc004dfl.4. human. [O14936-2]
    uc004dfm.4. human. [O14936-4]
    uc004dfn.4. human. [O14936-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF032119 mRNA. Translation: AAB88125.1.
    AF035582 mRNA. Translation: AAB88198.1.
    AB039327 mRNA. Translation: BAB12252.2.
    AY705392 mRNA. Translation: AAU10527.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71237.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71238.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71239.1.
    AL627402
    , AL158144, AL353691, AL445239, AL603754 Genomic DNA. Translation: CAH71240.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41092.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41093.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41094.1.
    AL445239
    , AL158144, AL353691, AL603754, AL627402 Genomic DNA. Translation: CAI41095.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41634.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41635.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41636.1.
    AL603754
    , AL158144, AL353691, AL445239, AL627402 Genomic DNA. Translation: CAI41637.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42244.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42245.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42246.1.
    AL353691
    , AL158144, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42247.1.
    AL158144
    , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42762.1.
    AL158144
    , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42763.1.
    AL158144
    , AL353691, AL445239, AL603754, AL627402 Genomic DNA. Translation: CAI42764.1.
    AL158144
    , 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.
    CCDSiCCDS14257.1. [O14936-2]
    CCDS48094.1. [O14936-3]
    CCDS48095.1. [O14936-4]
    RefSeqiNP_001119526.1. NM_001126054.2. [O14936-4]
    NP_001119527.1. NM_001126055.2. [O14936-3]
    NP_003679.2. NM_003688.3. [O14936-2]
    UniGeneiHs.495984.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliO14936.
    SMRiO14936. Positions 5-394, 403-456, 487-925.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114141. 58 interactions.
    DIPiDIP-38727N.
    IntActiO14936. 36 interactions.
    MINTiMINT-102444.

    Chemistry

    BindingDBiO14936.
    ChEMBLiCHEMBL1908381.
    GuidetoPHARMACOLOGYi1959.

    PTM databases

    PhosphoSiteiO14936.

    Polymorphism and mutation databases

    BioMutaiCASK.

    Proteomic databases

    MaxQBiO14936.
    PaxDbiO14936.
    PRIDEiO14936.

    Protocols and materials databases

    DNASUi8573.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000378158; ENSP00000367400; ENSG00000147044. [O14936-6]
    ENST00000378163; ENSP00000367405; ENSG00000147044. [O14936-1]
    ENST00000378166; ENSP00000367408; ENSG00000147044. [O14936-2]
    ENST00000421587; ENSP00000400526; ENSG00000147044. [O14936-3]
    ENST00000442742; ENSP00000398007; ENSG00000147044. [O14936-4]
    GeneIDi8573.
    KEGGihsa:8573.
    UCSCiuc004dfk.4. human. [O14936-1]
    uc004dfl.4. human. [O14936-2]
    uc004dfm.4. human. [O14936-4]
    uc004dfn.4. human. [O14936-3]

    Organism-specific databases

    CTDi8573.
    GeneCardsiGC0XM041374.
    GeneReviewsiCASK.
    HGNCiHGNC:1497. CASK.
    HPAiCAB001949.
    HPA023857.
    MIMi300172. gene.
    300422. phenotype.
    300749. phenotype.
    neXtProtiNX_O14936.
    Orphaneti1934. Early infantile epileptic encephalopathy.
    323. FG syndrome.
    163937. X-linked intellectual disability, Najm type.
    PharmGKBiPA26081.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00760000118866.
    HOVERGENiHBG001858.
    InParanoidiO14936.
    KOiK06103.
    OMAiRCINRET.
    OrthoDBiEOG79CXZ5.
    PhylomeDBiO14936.
    TreeFamiTF314263.

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    2.7.4.8. 2681.
    ReactomeiREACT_15293. Dopamine Neurotransmitter Release Cycle.
    REACT_163942. Syndecan interactions.
    REACT_23832. Nephrin interactions.
    SignaLinkiO14936.

    Miscellaneous databases

    ChiTaRSiCASK. human.
    EvolutionaryTraceiO14936.
    GeneWikiiCASK.
    GenomeRNAii8573.
    NextBioi32157.
    PROiO14936.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO14936.
    CleanExiHS_CASK.
    ExpressionAtlasiO14936. baseline and differential.
    GenevestigatoriO14936.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR008145. 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.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    PF02828. L27. 2 hits.
    PF00595. PDZ. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    SMARTiSM00072. GuKc. 1 hit.
    SM00569. L27. 2 hits.
    SM00228. PDZ. 1 hit.
    SM00220. S_TKc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00856. 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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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. Cited for: INTERACTION WITH KIRREL3.
    10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "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.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-337 IN COMPLEX WITH AMP, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION OF NRXN1, PHOSPHORYLATION AT SER-151 AND SER-155.
    13. "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.
      , 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.
    14. "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.
    15. 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.
      , 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.

    Entry informationi

    Entry nameiCSKP_HUMAN
    AccessioniPrimary (citable) accession number: O14936
    Secondary accession number(s): A6NES1
    , B7ZKY0, O43215, Q17RI4, Q59HA0, Q5VT16, Q5VT17, Q5VT18, Q5VT19, Q66T42, Q9BYH6, Q9NYB2, Q9NYB3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: April 17, 2007
    Last modified: May 27, 2015
    This is version 174 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.