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O14936

- CSKP_HUMAN

UniProt

O14936 - CSKP_HUMAN

Protein

Peripheral plasma membrane protein CASK

Gene

CASK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 3 (17 Apr 2007)
      Previous versions | rss
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    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

    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

    1. ATP binding Source: UniProtKB-KW
    2. guanylate kinase activity Source: ProtInc
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. calcium ion import Source: Ensembl
    2. cell adhesion Source: ProtInc
    3. extracellular matrix organization Source: Reactome
    4. negative regulation of cell-matrix adhesion Source: BHF-UCL
    5. negative regulation of cellular response to growth factor stimulus Source: BHF-UCL
    6. negative regulation of keratinocyte proliferation Source: BHF-UCL
    7. negative regulation of wound healing Source: BHF-UCL
    8. nucleotide phosphorylation Source: GOC
    9. positive regulation of calcium ion import Source: Ensembl
    10. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl

    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.
    ReactomeiREACT_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: Chromosome X

    Organism-specific databases

    HGNCiHGNC:1497. CASK.

    Subcellular locationi

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

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. basement membrane Source: Ensembl
    3. basolateral plasma membrane Source: Ensembl
    4. cell-cell junction Source: BHF-UCL
    5. ciliary membrane Source: BHF-UCL
    6. cytoplasm Source: BHF-UCL
    7. cytosol Source: Ensembl
    8. nuclear lamina Source: BHF-UCL
    9. nuclear matrix Source: BHF-UCL
    10. nucleolus Source: BHF-UCL
    11. plasma membrane Source: ProtInc
    12. presynaptic membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:300422]: FG syndrome (FGS) is an X-linked disorder characterized by mental retardation, relative macrocephaly, hypotonia and constipation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.
    Orphaneti323. FG syndrome.
    163937. X-linked intellectual disability, Najm type.
    PharmGKBiPA26081.

    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

    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

    ArrayExpressiO14936.
    BgeeiO14936.
    CleanExiHS_CASK.
    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
    LIN7AO149103EBI-1215506,EBI-2513988
    Nrxn1Q633733EBI-1215506,EBI-1780696From a different organism.
    RPH3AQ9Y2J03EBI-1215506,EBI-1216802
    SDC2P347412EBI-1215506,EBI-1172957

    Protein-protein interaction databases

    BioGridi114141. 50 interactions.
    DIPiDIP-38727N.
    IntActiO14936. 34 interactions.
    MINTiMINT-102444.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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, 487-572, 615-921.
    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.
    HOVERGENiHBG001858.
    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_dom.
    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. Align

    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

    MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS    50
    SPGLSTEDLK REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC 100
    FEIVKRADAG FVYSEAVASH YMRQILEALR YCHDNNIIHR DVKPHCVLLA 150
    SKENSAPVKL GGFGVAIQLG ESGLVAGGRV GTPHFMAPEV VKREPYGKPV 200
    DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR QWSHISESAK 250
    DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA 300
    RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV 350
    LDSLEEIHAL TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN 400
    PPSDAVQRAK EVLEEISCYP ENNDAKELKR ILTQPHFMAL LQTHDVVAHE 450
    VYSDEALRVT PPPTSPYLNG DSPESANGDM DMENVTRVRL VQFQKNTDEP 500
    MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN GISVANQTVE 550
    QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS 600
    VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS 650
    KDDHNWWQGK LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW 700
    FGKKKKQYKD KYLAKHNAVF DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV 750
    GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK DEENGKNYYF VSHDQMMQDI 800
    SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ ALKVLRTAEF 850
    APFVVFIAAP TITPGLNEDE SLQRLQKESD ILQRTYAHYF DLTIINNEID 900
    ETIRHLEEAV ELVCTAPQWV PVSWVY 926
    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.

    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.

    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.

    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. 1 PublicationCurated
    Sequence conflicti479 – 4791D → G in AAB88125. (PubMed:9660868)Curated
    Sequence conflicti479 – 4791D → G in BAB12252. 1 PublicationCurated
    Sequence conflicti479 – 4791D → G in AAU10527. 1 PublicationCurated
    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. 1 PublicationCurated
    Sequence conflicti780 – 7801K → R in AAB88125. (PubMed:9660868)Curated
    Sequence conflicti780 – 7801K → R in AAU10527. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14257.1. [O14936-2 ]
    CCDS48094.1. [O14936-3 ]
    CCDS48095.1. [O14936-4 ]
    RefSeqi NP_001119526.1. NM_001126054.2. [O14936-4 ]
    NP_001119527.1. NM_001126055.2. [O14936-3 ]
    NP_003679.2. NM_003688.3. [O14936-2 ]
    UniGenei Hs.495984.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KGD X-ray 1.31 A 739-914 [» ]
    1KWA X-ray 1.93 A/B 487-572 [» ]
    1ZL8 NMR - B 403-456 [» ]
    3C0G X-ray 2.19 A/B 1-337 [» ]
    3C0H X-ray 2.30 A/B 1-337 [» ]
    3C0I X-ray 1.85 A 1-337 [» ]
    3MFR X-ray 2.00 A 1-337 [» ]
    3MFS X-ray 2.10 A 1-337 [» ]
    3MFT X-ray 2.20 A 1-337 [» ]
    3MFU X-ray 2.30 A 1-337 [» ]
    3TAC X-ray 2.20 A 1-345 [» ]
    ProteinModelPortali O14936.
    SMRi O14936. Positions 5-394, 403-456, 487-572, 615-921.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114141. 50 interactions.
    DIPi DIP-38727N.
    IntActi O14936. 34 interactions.
    MINTi MINT-102444.

    Chemistry

    BindingDBi O14936.
    ChEMBLi CHEMBL1908381.
    GuidetoPHARMACOLOGYi 1959.

    PTM databases

    PhosphoSitei O14936.

    Proteomic databases

    MaxQBi O14936.
    PaxDbi O14936.
    PRIDEi O14936.

    Protocols and materials databases

    DNASUi 8573.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378158 ; ENSP00000367400 ; ENSG00000147044 . [O14936-6 ]
    ENST00000378163 ; ENSP00000367405 ; ENSG00000147044 . [O14936-1 ]
    ENST00000378166 ; ENSP00000367408 ; ENSG00000147044 . [O14936-2 ]
    ENST00000421587 ; ENSP00000400526 ; ENSG00000147044 . [O14936-3 ]
    ENST00000442742 ; ENSP00000398007 ; ENSG00000147044 . [O14936-4 ]
    GeneIDi 8573.
    KEGGi hsa:8573.
    UCSCi uc004dfk.4. human. [O14936-1 ]
    uc004dfl.4. human. [O14936-2 ]
    uc004dfm.4. human. [O14936-4 ]
    uc004dfn.4. human. [O14936-3 ]

    Organism-specific databases

    CTDi 8573.
    GeneCardsi GC0XM041374.
    GeneReviewsi CASK.
    HGNCi HGNC:1497. CASK.
    HPAi CAB001949.
    HPA023857.
    MIMi 300172. gene.
    300422. phenotype.
    300749. phenotype.
    neXtProti NX_O14936.
    Orphaneti 323. FG syndrome.
    163937. X-linked intellectual disability, Najm type.
    PharmGKBi PA26081.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG001858.
    KOi K06103.
    OMAi RCINRET.
    OrthoDBi EOG79CXZ5.
    PhylomeDBi O14936.
    TreeFami TF314263.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_163942. Syndecan interactions.
    REACT_23832. Nephrin interactions.
    SignaLinki O14936.

    Miscellaneous databases

    ChiTaRSi CASK. human.
    EvolutionaryTracei O14936.
    GeneWikii CASK.
    GenomeRNAii 8573.
    NextBioi 32157.
    PROi O14936.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14936.
    Bgeei O14936.
    CleanExi HS_CASK.
    Genevestigatori O14936.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR008145. 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 ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    PF02828. L27. 2 hits.
    PF00595. PDZ. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    SMARTi SM00072. GuKc. 1 hit.
    SM00569. L27. 2 hits.
    SM00228. PDZ. 1 hit.
    SM00220. S_TKc. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00856. 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 ]
    ProtoNeti Search...

    Publicationsi

    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. "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. 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.
    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.
      , 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. Cited for: VARIANT FGS4 LEU-28, CHARACTERIZATION OF VARIANT FGS4 LEU-28.
    15. "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: October 1, 2014
    This is version 166 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