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O76039

- CDKL5_HUMAN

UniProt

O76039 - CDKL5_HUMAN

Protein

Cyclin-dependent kinase-like 5

Gene

CDKL5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Mediates phosphorylation of MECP2.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421ATPPROSITE-ProRule annotation
    Active sitei135 – 1351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi19 – 279ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: HGNC
    2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    3. kinase activity Source: MGI
    4. protein kinase activity Source: HGNC
    5. protein serine/threonine kinase activity Source: ProtInc
    6. Rac GTPase binding Source: BHF-UCL

    GO - Biological processi

    1. neuron migration Source: BHF-UCL
    2. positive regulation of axon extension Source: BHF-UCL
    3. positive regulation of dendrite morphogenesis Source: BHF-UCL
    4. positive regulation of Rac GTPase activity Source: BHF-UCL
    5. protein autophosphorylation Source: HGNC
    6. protein phosphorylation Source: ProtInc
    7. regulation of dendrite development Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.22. 2681.
    SignaLinkiO76039.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase-like 5 (EC:2.7.11.22)
    Alternative name(s):
    Serine/threonine-protein kinase 9
    Gene namesi
    Name:CDKL5
    Synonyms:STK9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11411. CDKL5.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. dendrite cytoplasm Source: BHF-UCL
    3. dendritic growth cone Source: BHF-UCL
    4. nucleus Source: HGNC
    5. ruffle membrane Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Chromosomal aberrations involving CDKL5 are found in patients manifesting early-onset seizures and spams and psychomotor impairment. Translocation t(X;6)(p22.3;q14); translocation t(X;7)(p22.3;p15).
    Epileptic encephalopathy, early infantile, 2 (EIEE2) [MIM:300672]: A severe form of epilepsy characterized by seizures or spasms beginning in infancy. Patients with epileptic encephalopathy early infantile type 2 manifest features resembling Rett syndrome such as microcephaly, lack of speech development, stereotypic hand movements. However, EIEE2 and Rett syndrome are considered two distinct entities.13 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401A → V in EIEE2; causes mislocalization of the protein in the cytoplasm. 2 Publications
    VAR_058022
    Natural varianti72 – 721I → N in EIEE2. 1 Publication
    VAR_058023
    Natural varianti72 – 721I → T in EIEE2. 1 Publication
    VAR_058024
    Natural varianti127 – 1271H → R in EIEE2. 1 Publication
    VAR_058025
    Natural varianti152 – 1521C → F in EIEE2; affect activity; causes mislocalization of the protein in the cytoplasm. 1 Publication
    VAR_023560
    Natural varianti175 – 1751R → S in EIEE2; affect activity; does not affect the cellular distribution of the protein. 1 Publication
    VAR_023561
    Natural varianti178 – 1781R → P in EIEE2. 1 Publication
    VAR_058026
    Natural varianti178 – 1781R → Q in EIEE2. 1 Publication
    VAR_071103
    Natural varianti180 – 1801P → L in EIEE2. 1 Publication
    VAR_037635
    Natural varianti220 – 2201L → P in EIEE2; causes mislocalization of the protein in the cytoplasm. 2 Publications
    VAR_058027
    Natural varianti288 – 2881T → I in EIEE2. 1 Publication
    VAR_058028
    Natural varianti291 – 2911C → Y in EIEE2. 1 Publication
    VAR_058029
    Natural varianti399 – 3991N → T in EIEE2. 1 Publication
    VAR_058030
    Natural varianti718 – 7181V → M in EIEE2. 1 Publication
    VAR_058032
    Natural varianti793 – 7931V → A in EIEE2; unknown pathological significance. 1 Publication
    VAR_037636

    Keywords - Diseasei

    Disease mutation, Epilepsy, Mental retardation

    Organism-specific databases

    MIMi300672. phenotype.
    PharmGKBiPA36218.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10301030Cyclin-dependent kinase-like 5PRO_0000085826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei407 – 4071Phosphoserine4 Publications
    Modified residuei720 – 7201Phosphoserine1 Publication
    Modified residuei761 – 7611Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylated.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO76039.
    PaxDbiO76039.
    PRIDEiO76039.

    PTM databases

    PhosphoSiteiO76039.

    Expressioni

    Tissue specificityi

    Expressed in brain, lung, kidney, prostate, ovary, placenta, pancreas and testis.

    Gene expression databases

    BgeeiO76039.
    CleanExiHS_CDKL5.
    GenevestigatoriO76039.

    Organism-specific databases

    HPAiCAB011577.
    HPA002847.

    Interactioni

    Subunit structurei

    Interacts with MECP2.1 Publication

    Protein-protein interaction databases

    BioGridi112668. 6 interactions.
    IntActiO76039. 6 interactions.
    MINTiMINT-7241055.
    STRINGi9606.ENSP00000369325.

    Structurei

    Secondary structure

    1
    1030
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 123
    Beta strandi13 – 2412
    Beta strandi26 – 327
    Turni33 – 353
    Beta strandi38 – 436
    Helixi55 – 6612
    Beta strandi75 – 817
    Beta strandi84 – 907
    Beta strandi93 – 953
    Helixi96 – 1027
    Helixi109 – 12820
    Helixi138 – 1403
    Beta strandi141 – 1433
    Beta strandi149 – 1513
    Helixi180 – 1834
    Helixi191 – 20616
    Helixi216 – 22712
    Helixi232 – 2409
    Helixi242 – 2443
    Helixi258 – 2625
    Turni263 – 2653
    Helixi268 – 27710
    Helixi282 – 2843
    Helixi288 – 2925
    Helixi295 – 2984

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BGQX-ray2.00A1-303[»]
    ProteinModelPortaliO76039.
    SMRiO76039. Positions 9-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 297285Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi784 – 7896Poly-Lys

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000049181.
    HOVERGENiHBG050863.
    InParanoidiO76039.
    KOiK08824.
    OMAiQPGSTSK.
    OrthoDBiEOG7992PS.
    PhylomeDBiO76039.
    TreeFamiTF101032.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O76039-1) [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

    MKIPNIGNVM NKFEILGVVG EGAYGVVLKC RHKETHEIVA IKKFKDSEEN     50
    EEVKETTLRE LKMLRTLKQE NIVELKEAFR RRGKLYLVFE YVEKNMLELL 100
    EEMPNGVPPE KVKSYIYQLI KAIHWCHKND IVHRDIKPEN LLISHNDVLK 150
    LCDFGFARNL SEGNNANYTE YVATRWYRSP ELLLGAPYGK SVDMWSVGCI 200
    LGELSDGQPL FPGESEIDQL FTIQKVLGPL PSEQMKLFYS NPRFHGLRFP 250
    AVNHPQSLER RYLGILNSVL LDLMKNLLKL DPADRYLTEQ CLNHPTFQTQ 300
    RLLDRSPSRS AKRKPYHVES STLSNRNQAG KSTALQSHHR SNSKDIQNLS 350
    VGLPRADEGL PANESFLNGN LAGASLSPLH TKTYQASSQP GSTSKDLTNN 400
    NIPHLLSPKE AKSKTEFDFN IDPKPSEGPG TKYLKSNSRS QQNRHSFMES 450
    SQSKAGTLQP NEKQSRHSYI DTIPQSSRSP SYRTKAKSHG ALSDSKSVSN 500
    LSEARAQIAE PSTSRYFPSS CLDLNSPTSP TPTRHSDTRT LLSPSGRNNR 550
    NEGTLDSRRT TTRHSKTMEE LKLPEHMDSS HSHSLSAPHE SFSYGLGYTS 600
    PFSSQQRPHR HSMYVTRDKV RAKGLDGSLS IGQGMAARAN SLQLLSPQPG 650
    EQLPPEMTVA RSSVKETSRE GTSSFHTRQK SEGGVYHDPH SDDGTAPKEN 700
    RHLYNDPVPR RVGSFYRVPS PRPDNSFHEN NVSTRVSSLP SESSSGTNHS 750
    KRQPAFDPWK SPENISHSEQ LKEKEKQGFF RSMKKKKKKS QTVPNSDSPD 800
    LLTLQKSIHS ASTPSSRPKE WRPEKISDLQ TQSQPLKSLR KLLHLSSASN 850
    HPASSDPRFQ PLTAQQTKNS FSEIRIHPLS QASGGSSNIR QEPAPKGRPA 900
    LQLPDGGCDG RRQRHHSGPQ DRRFMLRTTE QQGEYFCCGD PKKPHTPCVP 950
    NRALHRPISS PAPYPVLQVR GTSMCPTLQV RGTDAFSCPT QQSGFSFFVR 1000
    HVMREALIHR AQVNQAALLT YHENAALTGK 1030
    Length:1,030
    Mass (Da):115,538
    Last modified:November 1, 1998 - v1
    Checksum:i8A1C9C438610EF08
    GO
    Isoform 2 (identifier: O76039-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         905-1030: DGGCDGRRQR...YHENAALTGK → GQMDPGWHVS...NLNDLKETAL

    Note: Predominant transcript in brain.

    Show »
    Length:960
    Mass (Da):107,519
    Checksum:i6E955E0B40DBC1B8
    GO

    Sequence cautioni

    The sequence CAA61445.1 differs from that shown. Reason: Frameshift at position 415.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti339 – 3402HR → GT in CAA61445. (PubMed:8864140)Curated
    Sequence conflicti541 – 5411L → W in CAA61445. (PubMed:8864140)Curated
    Sequence conflicti731 – 76434Missing in CAA61445. (PubMed:8864140)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401A → V in EIEE2; causes mislocalization of the protein in the cytoplasm. 2 Publications
    VAR_058022
    Natural varianti72 – 721I → N in EIEE2. 1 Publication
    VAR_058023
    Natural varianti72 – 721I → T in EIEE2. 1 Publication
    VAR_058024
    Natural varianti127 – 1271H → R in EIEE2. 1 Publication
    VAR_058025
    Natural varianti152 – 1521C → F in EIEE2; affect activity; causes mislocalization of the protein in the cytoplasm. 1 Publication
    VAR_023560
    Natural varianti175 – 1751R → S in EIEE2; affect activity; does not affect the cellular distribution of the protein. 1 Publication
    VAR_023561
    Natural varianti178 – 1781R → P in EIEE2. 1 Publication
    VAR_058026
    Natural varianti178 – 1781R → Q in EIEE2. 1 Publication
    VAR_071103
    Natural varianti180 – 1801P → L in EIEE2. 1 Publication
    VAR_037635
    Natural varianti220 – 2201L → P in EIEE2; causes mislocalization of the protein in the cytoplasm. 2 Publications
    VAR_058027
    Natural varianti288 – 2881T → I in EIEE2. 1 Publication
    VAR_058028
    Natural varianti291 – 2911C → Y in EIEE2. 1 Publication
    VAR_058029
    Natural varianti368 – 3681N → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036578
    Natural varianti374 – 3741A → T in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041997
    Natural varianti399 – 3991N → T in EIEE2. 1 Publication
    VAR_058030
    Natural varianti444 – 4441R → C.1 Publication
    VAR_058031
    Natural varianti574 – 5741P → Q in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_041998
    Natural varianti718 – 7181V → M in EIEE2. 1 Publication
    VAR_058032
    Natural varianti734 – 7341T → A.1 Publication
    Corresponds to variant rs55803460 [ dbSNP | Ensembl ].
    VAR_041999
    Natural varianti791 – 7911Q → P.4 Publications
    Corresponds to variant rs35478150 [ dbSNP | Ensembl ].
    VAR_023562
    Natural varianti793 – 7931V → A in EIEE2; unknown pathological significance. 1 Publication
    VAR_037636
    Natural varianti923 – 9231R → C.1 Publication
    VAR_058033
    Natural varianti999 – 9991V → M.
    Corresponds to variant rs35693326 [ dbSNP | Ensembl ].
    VAR_037637
    Natural varianti1023 – 10231E → G.1 Publication
    Corresponds to variant rs34166184 [ dbSNP | Ensembl ].
    VAR_042000

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei905 – 1030126DGGCD…ALTGK → GQMDPGWHVSSVTRSATEGP SYSEQLGAKSGPNGHPYNRT NRSRMPNLNDLKETAL in isoform 2. 1 PublicationVSP_044082Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15057 mRNA. Translation: CAA75342.1.
    AY217744 mRNA. Translation: AAO64440.1.
    HQ171445 mRNA. Translation: ADN38258.1.
    Z92542, AL109798 Genomic DNA. Translation: CAI42485.1.
    AL109798, Z92542 Genomic DNA. Translation: CAI41159.1.
    X89059 mRNA. Translation: CAA61445.1. Frameshift.
    CCDSiCCDS14186.1. [O76039-1]
    PIRiS58296.
    RefSeqiNP_001032420.1. NM_001037343.1. [O76039-1]
    NP_003150.1. NM_003159.2. [O76039-1]
    XP_006724574.1. XM_006724511.1. [O76039-1]
    UniGeneiHs.659851.

    Genome annotation databases

    EnsembliENST00000379989; ENSP00000369325; ENSG00000008086. [O76039-1]
    ENST00000379996; ENSP00000369332; ENSG00000008086. [O76039-1]
    GeneIDi6792.
    KEGGihsa:6792.
    UCSCiuc004cym.3. human. [O76039-1]
    uc022btn.1. human. [O76039-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15057 mRNA. Translation: CAA75342.1 .
    AY217744 mRNA. Translation: AAO64440.1 .
    HQ171445 mRNA. Translation: ADN38258.1 .
    Z92542 , AL109798 Genomic DNA. Translation: CAI42485.1 .
    AL109798 , Z92542 Genomic DNA. Translation: CAI41159.1 .
    X89059 mRNA. Translation: CAA61445.1 . Frameshift.
    CCDSi CCDS14186.1. [O76039-1 ]
    PIRi S58296.
    RefSeqi NP_001032420.1. NM_001037343.1. [O76039-1 ]
    NP_003150.1. NM_003159.2. [O76039-1 ]
    XP_006724574.1. XM_006724511.1. [O76039-1 ]
    UniGenei Hs.659851.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BGQ X-ray 2.00 A 1-303 [» ]
    ProteinModelPortali O76039.
    SMRi O76039. Positions 9-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112668. 6 interactions.
    IntActi O76039. 6 interactions.
    MINTi MINT-7241055.
    STRINGi 9606.ENSP00000369325.

    Chemistry

    BindingDBi O76039.
    ChEMBLi CHEMBL1163112.

    PTM databases

    PhosphoSitei O76039.

    Proteomic databases

    MaxQBi O76039.
    PaxDbi O76039.
    PRIDEi O76039.

    Protocols and materials databases

    DNASUi 6792.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379989 ; ENSP00000369325 ; ENSG00000008086 . [O76039-1 ]
    ENST00000379996 ; ENSP00000369332 ; ENSG00000008086 . [O76039-1 ]
    GeneIDi 6792.
    KEGGi hsa:6792.
    UCSCi uc004cym.3. human. [O76039-1 ]
    uc022btn.1. human. [O76039-2 ]

    Organism-specific databases

    CTDi 6792.
    GeneCardsi GC0XP018443.
    HGNCi HGNC:11411. CDKL5.
    HPAi CAB011577.
    HPA002847.
    MIMi 300203. gene.
    300672. phenotype.
    neXtProti NX_O76039.
    PharmGKBi PA36218.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000049181.
    HOVERGENi HBG050863.
    InParanoidi O76039.
    KOi K08824.
    OMAi QPGSTSK.
    OrthoDBi EOG7992PS.
    PhylomeDBi O76039.
    TreeFami TF101032.

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 2681.
    SignaLinki O76039.

    Miscellaneous databases

    ChiTaRSi CDKL5. human.
    GeneWikii CDKL5.
    GenomeRNAii 6792.
    NextBioi 26529.
    PROi O76039.
    SOURCEi Search...

    Gene expression databases

    Bgeei O76039.
    CleanExi HS_CDKL5.
    Genevestigatori O76039.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a novel serine-threonine kinase gene from the Xp22 region."
      Montini E., Andolfi G., Caruso A., Buchner G., Walpole S.M., Mariani M., Consalez G.G., Trump D., Ballabio A., Franco B.
      Genomics 51:427-433(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Disruption of the serine/threonine kinase 9 gene causes severe X-linked infantile spasms and mental retardation."
      Kalscheuer V.M., Tao J., Donnelly A., Hollway G., Schwinger E., Kuebart S., Menzel C., Hoeltzenbein M., Tommerup N., Eyre H., Harbord M., Haan E., Sutherland G.R., Ropers H.-H., Gecz J.
      Am. J. Hum. Genet. 72:1401-1411(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN EIEE2, CHROMOSOMAL TRANSLOCATION, VARIANT PRO-791.
    3. "A novel transcript of cyclin-dependent kinase-like 5 (CDKL5) has an alternative C-terminus and is the predominant transcript in brain."
      Williamson S.L., Giudici L., Kilstrup-Nielsen C., Gold W., Pelka G.J., Tam P.P., Grimm A., Prodi D., Landsberger N., Christodoulou J.
      Hum. Genet. 131:187-200(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    4. "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].
    5. "Differential screening leads to novel genetic markers of monocyte to macrophage maturation."
      Krause S.W., Rehli M., Kreutz M., Schwarzfischer L., Paulauskis J.D., Andreesen J.D.
      J. Leukoc. Biol. 60:540-545(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 339-789.
    6. Cited for: INVOLVEMENT IN EIEE2.
    7. Cited for: INTERACTION WITH MECP2, FUNCTION, AUTOPHOSPHORYLATION, INVOLVEMENT IN EIEE2.
    8. "Functional consequences of mutations in CDKL5, an X-linked gene involved in infantile spasms and mental retardation."
      Bertani I., Rusconi L., Bolognese F., Forlani G., Conca B., De Monte L., Badaracco G., Landsberger N., Kilstrup-Nielsen C.
      J. Biol. Chem. 281:32048-32056(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS EIEE2 PHE-152 AND SER-175.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-720, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Mutations in the X-linked cyclin-dependent kinase-like 5 (CDKL5/STK9) gene are associated with severe neurodevelopmental retardation."
      Tao J., Van Esch H., Hagedorn-Greiwe M., Hoffmann K., Moser B., Raynaud M., Sperner J., Fryns J.-P., Schwinger E., Gecz J., Ropers H.-H., Kalscheuer V.M.
      Am. J. Hum. Genet. 75:1149-1154(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EIEE2 PHE-152 AND SER-175, VARIANT PRO-791.
    14. Cited for: INVOLVEMENT IN EIEE2.
    15. Cited for: VARIANT EIEE2 ASN-72, VARIANT CYS-444.
    16. "CDKL5 mutations cause infantile spasms, early onset seizures, and severe mental retardation in female patients."
      Archer H.L., Evans J., Edwards S., Colley J., Newbury-Ecob R., O'Callaghan F., Huyton M., O'Regan M., Tolmie J., Sampson J., Clarke A., Osborne J.
      J. Med. Genet. 43:729-734(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EIEE2 LEU-180 AND ALA-793.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-368.
    18. "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: VARIANTS [LARGE SCALE ANALYSIS] THR-374; GLN-574; ALA-734; PRO-791 AND GLY-1023.
    19. Cited for: VARIANTS EIEE2 VAL-40; PRO-220 AND MET-718.
    20. Cited for: VARIANTS EIEE2 VAL-40 AND PRO-220, CHARACTERIZATION OF VARIANTS EIEE2 VAL-40 AND PRO-220.
    21. "CDKL5 mutations in boys with severe encephalopathy and early-onset intractable epilepsy."
      Elia M., Falco M., Ferri R., Spalletta A., Bottitta M., Calabrese G., Carotenuto M., Musumeci S.A., Lo Giudice M., Fichera M.
      Neurology 71:997-999(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EIEE2 PRO-178; ILE-288 AND TYR-291.
    22. "A novel mutation in the X-linked cyclin-dependent kinase-like 5 (CDKL5) gene associated with a severe Rett phenotype."
      Sprovieri T., Conforti F.L., Fiumara A., Mazzei R., Ungaro C., Citrigno L., Muglia M., Arena A., Quattrone A.
      Am. J. Med. Genet. A 149:722-725(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EIEE2 THR-399.
    23. "Novel mutations in the CDKL5 gene, predicted effects and associated phenotypes."
      Russo S., Marchi M., Cogliati F., Bonati M.T., Pintaudi M., Veneselli E., Saletti V., Balestrini M., Ben-Zeev B., Larizza L.
      Neurogenetics 10:241-250(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EIEE2 THR-72 AND ARG-127, VARIANTS PRO-791 AND CYS-923.
    24. "Clinical features and gene mutational spectrum of CDKL5-related diseases in a cohort of Chinese patients."
      Zhao Y., Zhang X., Bao X., Zhang Q., Zhang J., Cao G., Zhang J., Li J., Wei L., Pan H., Wu X.
      BMC Med. Genet. 15:24-24(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EIEE2 GLN-178.

    Entry informationi

    Entry nameiCDKL5_HUMAN
    AccessioniPrimary (citable) accession number: O76039
    Secondary accession number(s): G9B9X4
    , Q14198, Q5H985, Q8IYC7, Q9UJL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 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