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O94921

- CDK14_HUMAN

UniProt

O94921 - CDK14_HUMAN

Protein

Cyclin-dependent kinase 14

Gene

CDK14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (18 Apr 2006)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Serine/threonine-protein kinase activity is promoted by associated cyclins CCDN3 and CCNY and repressed by CDKN1A.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei164 – 1641ATPCurated
    Active sitei256 – 2561Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi141 – 1499ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell division Source: UniProtKB-KW
    2. G2/M transition of mitotic cell cycle Source: UniProtKB
    3. regulation of canonical Wnt signaling pathway Source: UniProtKB
    4. regulation of cell cycle Source: GOC
    5. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiO94921.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase 14 (EC:2.7.11.22)
    Alternative name(s):
    Cell division protein kinase 14
    Serine/threonine-protein kinase PFTAIRE-1
    Short name:
    hPFTAIRE1
    Gene namesi
    Name:CDK14
    Synonyms:KIAA0834, PFTK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:8883. CDK14.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein. Cytoplasm. Nucleus
    Note: Recruited to the cell membrane by CCNY.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
    3. cytosol Source: Ensembl
    4. nucleus Source: HPA
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1641K → R: Abolishes protein kinase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA33221.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469Cyclin-dependent kinase 14PRO_0000086506Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei95 – 951Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO94921.
    PaxDbiO94921.
    PRIDEiO94921.

    PTM databases

    PhosphoSiteiO94921.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, pancreas, kidney, heart, testis and ovary. Also detected at lower levels in other tissues except in spleen and thymus where expression is barely detected.1 Publication

    Gene expression databases

    ArrayExpressiO94921.
    BgeeiO94921.
    CleanExiHS_PFTK1.
    GenevestigatoriO94921.

    Organism-specific databases

    HPAiHPA015267.

    Interactioni

    Subunit structurei

    Interacts with CCNY; CCNY mediates its recruitment to the plasma membrane and promotes phosphorylation of LRP6. Interacts with CCDN3 and CDKN1A. Interacts with SEPT8. Interacts with 14-3-3 proteina YWHAB, YWHAE, YWHAH and YWHAQ.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCND3P302815EBI-1043945,EBI-375013
    CCNYQ8ND7611EBI-1043945,EBI-1049189
    CDKN1AP389368EBI-1043945,EBI-375077
    HSP90AB1P082382EBI-1043945,EBI-352572
    YWHABP319465EBI-1043945,EBI-359815
    YWHAEP622583EBI-1043945,EBI-356498
    YWHAHQ049173EBI-1043945,EBI-306940
    YWHAQP273483EBI-1043945,EBI-359854

    Protein-protein interaction databases

    BioGridi111239. 11 interactions.
    DIPiDIP-39618N.
    IntActiO94921. 13 interactions.
    MINTiMINT-7147554.
    STRINGi9606.ENSP00000265741.

    Structurei

    3D structure databases

    ProteinModelPortaliO94921.
    SMRiO94921. Positions 98-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 419285Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG014652.
    InParanoidiO94921.
    KOiK08821.
    OMAiKKLRQAW.
    PhylomeDBiO94921.
    TreeFamiTF106508.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94921-1) [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

    MCDLIEPQPA EKIGKMKKLR RTLSESFSRI ALKKDDTTFD EICVTKMSTR    50
    NCQGMDSVIK PLDTIPEDKK VRVQRTQSTF DPFEKPANQV KRVHSENNAC 100
    INFKTSSTGK ESPKVRRHSS PSSPTSPKFG KADSYEKLEK LGEGSYATVY 150
    KGKSKVNGKL VALKVIRLQE EEGTPFTAIR EASLLKGLKH ANIVLLHDII 200
    HTKETLTLVF EYVHTDLCQY MDKHPGGLHP DNVKLFLFQL LRGLSYIHQR 250
    YILHRDLKPQ NLLISDTGEL KLADFGLARA KSVPSHTYSN EVVTLWYRPP 300
    DVLLGSTEYS TCLDMWGVGC IFVEMIQGVA AFPGMKDIQD QLERIFLVLG 350
    TPNEDTWPGV HSLPHFKPER FTLYSSKNLR QAWNKLSYVN HAEDLASKLL 400
    QCSPKNRLSA QAALSHEYFS DLPPRLWELT DMSSIFTVPN VRLQPEAGES 450
    MRAFGKNNSY GKSLSNSKH 469
    Length:469
    Mass (Da):53,057
    Last modified:April 18, 2006 - v3
    Checksum:i32CF9B9B7BD9CE0E
    GO
    Isoform 2 (identifier: O94921-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDE → MHGYFGCNAAAEPGYSAFVGTPQ

    Show »
    Length:451
    Mass (Da):50,662
    Checksum:i68210FCBC0D44031
    GO
    Isoform 3 (identifier: O94921-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-46: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:423
    Mass (Da):47,760
    Checksum:i5F5D5B2C611243FA
    GO

    Sequence cautioni

    The sequence BAA74857.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81Q → R in BAG60284. (PubMed:14702039)Curated
    Sequence conflicti158 – 1581G → W in AAG43234. (PubMed:11313143)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti432 – 4321M → I in an ovarian mucinous carcinoma; somatic mutation. 1 Publication
    VAR_046765
    Natural varianti463 – 4631S → R.1 Publication
    VAR_046766

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4646Missing in isoform 3. 1 PublicationVSP_038762Add
    BLAST
    Alternative sequencei1 – 4141MCDLI…TTFDE → MHGYFGCNAAAEPGYSAFVG TPQ in isoform 2. 2 PublicationsVSP_004803Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119833 mRNA. Translation: AAG43234.1.
    AB020641 mRNA. Translation: BAA74857.2. Different initiation.
    AK289782 mRNA. Translation: BAF82471.1.
    AK295086 mRNA. Translation: BAG58127.1.
    AK297974 mRNA. Translation: BAG60284.1.
    AK316026 mRNA. Translation: BAH14397.1.
    AC000057 Genomic DNA. Translation: AAS07411.1.
    AC000059 Genomic DNA. No translation available.
    AC002065 Genomic DNA. Translation: AAM48566.1.
    AC002456 Genomic DNA. No translation available.
    AC002458 Genomic DNA. Translation: AAS07412.1.
    AC006036 Genomic DNA. Translation: AAF19245.1.
    CH236949 Genomic DNA. Translation: EAL24162.1.
    CH471091 Genomic DNA. Translation: EAW76873.1.
    CH471091 Genomic DNA. Translation: EAW76874.1.
    BC136476 mRNA. Translation: AAI36477.1.
    BC136477 mRNA. Translation: AAI36478.1.
    BC152388 mRNA. Translation: AAI52389.1.
    BC152436 mRNA. Translation: AAI52437.1.
    BC167152 mRNA. Translation: AAI67152.1.
    BC167156 mRNA. Translation: AAI67156.1.
    CCDSiCCDS5619.1. [O94921-2]
    RefSeqiNP_001274064.1. NM_001287135.1. [O94921-1]
    NP_001274065.1. NM_001287136.1. [O94921-3]
    NP_001274066.1. NM_001287137.1.
    NP_036527.1. NM_012395.3. [O94921-2]
    XP_005250495.1. XM_005250438.1. [O94921-3]
    XP_005250496.1. XM_005250439.1. [O94921-3]
    XP_006716089.1. XM_006716026.1. [O94921-3]
    UniGeneiHs.258576.
    Hs.430742.

    Genome annotation databases

    EnsembliENST00000265741; ENSP00000265741; ENSG00000058091. [O94921-2]
    ENST00000380050; ENSP00000369390; ENSG00000058091. [O94921-1]
    ENST00000406263; ENSP00000385034; ENSG00000058091. [O94921-3]
    GeneIDi5218.
    KEGGihsa:5218.
    UCSCiuc003uky.2. human. [O94921-1]
    uc003ukz.1. human. [O94921-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119833 mRNA. Translation: AAG43234.1 .
    AB020641 mRNA. Translation: BAA74857.2 . Different initiation.
    AK289782 mRNA. Translation: BAF82471.1 .
    AK295086 mRNA. Translation: BAG58127.1 .
    AK297974 mRNA. Translation: BAG60284.1 .
    AK316026 mRNA. Translation: BAH14397.1 .
    AC000057 Genomic DNA. Translation: AAS07411.1 .
    AC000059 Genomic DNA. No translation available.
    AC002065 Genomic DNA. Translation: AAM48566.1 .
    AC002456 Genomic DNA. No translation available.
    AC002458 Genomic DNA. Translation: AAS07412.1 .
    AC006036 Genomic DNA. Translation: AAF19245.1 .
    CH236949 Genomic DNA. Translation: EAL24162.1 .
    CH471091 Genomic DNA. Translation: EAW76873.1 .
    CH471091 Genomic DNA. Translation: EAW76874.1 .
    BC136476 mRNA. Translation: AAI36477.1 .
    BC136477 mRNA. Translation: AAI36478.1 .
    BC152388 mRNA. Translation: AAI52389.1 .
    BC152436 mRNA. Translation: AAI52437.1 .
    BC167152 mRNA. Translation: AAI67152.1 .
    BC167156 mRNA. Translation: AAI67156.1 .
    CCDSi CCDS5619.1. [O94921-2 ]
    RefSeqi NP_001274064.1. NM_001287135.1. [O94921-1 ]
    NP_001274065.1. NM_001287136.1. [O94921-3 ]
    NP_001274066.1. NM_001287137.1.
    NP_036527.1. NM_012395.3. [O94921-2 ]
    XP_005250495.1. XM_005250438.1. [O94921-3 ]
    XP_005250496.1. XM_005250439.1. [O94921-3 ]
    XP_006716089.1. XM_006716026.1. [O94921-3 ]
    UniGenei Hs.258576.
    Hs.430742.

    3D structure databases

    ProteinModelPortali O94921.
    SMRi O94921. Positions 98-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111239. 11 interactions.
    DIPi DIP-39618N.
    IntActi O94921. 13 interactions.
    MINTi MINT-7147554.
    STRINGi 9606.ENSP00000265741.

    Chemistry

    BindingDBi O94921.
    ChEMBLi CHEMBL6162.
    GuidetoPHARMACOLOGYi 1967.

    PTM databases

    PhosphoSitei O94921.

    Proteomic databases

    MaxQBi O94921.
    PaxDbi O94921.
    PRIDEi O94921.

    Protocols and materials databases

    DNASUi 5218.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265741 ; ENSP00000265741 ; ENSG00000058091 . [O94921-2 ]
    ENST00000380050 ; ENSP00000369390 ; ENSG00000058091 . [O94921-1 ]
    ENST00000406263 ; ENSP00000385034 ; ENSG00000058091 . [O94921-3 ]
    GeneIDi 5218.
    KEGGi hsa:5218.
    UCSCi uc003uky.2. human. [O94921-1 ]
    uc003ukz.1. human. [O94921-2 ]

    Organism-specific databases

    CTDi 5218.
    GeneCardsi GC07P090095.
    HGNCi HGNC:8883. CDK14.
    HPAi HPA015267.
    MIMi 610679. gene.
    neXtProti NX_O94921.
    PharmGKBi PA33221.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG014652.
    InParanoidi O94921.
    KOi K08821.
    OMAi KKLRQAW.
    PhylomeDBi O94921.
    TreeFami TF106508.

    Enzyme and pathway databases

    SignaLinki O94921.

    Miscellaneous databases

    ChiTaRSi CDK14. human.
    GeneWikii PFTK1.
    GenomeRNAii 5218.
    NextBioi 20182.
    PROi O94921.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94921.
    Bgeei O94921.
    CleanExi HS_PFTK1.
    Genevestigatori O94921.

    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 cellular localization of human PFTAIRE1."
      Yang T., Chen J.-Y.
      Gene 267:165-172(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 2).
      Tissue: Brain and Testis.
    8. "KIAA0202, a human septin family member, interacting with hPFTAIRE1."
      Yang T., Gao Y.K., Chen J.Y.
      Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:520-525(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT8.
    9. "A Cdc2-related protein kinase hPFTAIRE1 from human brain interacting with 14-3-3 proteins."
      Gao Y., Jiang M., Yang T., Ni J., Chen J.
      Cell Res. 16:539-547(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YWHAB; YWHAE; YWHAH AND YWHAQ.
    10. "An RNA interference-based screen identifies MAP4K4/NIK as a negative regulator of PPARgamma, adipogenesis, and insulin-responsive hexose transport."
      Tang X., Guilherme A., Chakladar A., Powelka A.M., Konda S., Virbasius J.V., Nicoloro S.M., Straubhaar J., Czech M.P.
      Proc. Natl. Acad. Sci. U.S.A. 103:2087-2092(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Functional characterization of human PFTK1 as a cyclin-dependent kinase."
      Shu F., Lv S., Qin Y., Ma X., Wang X., Peng X., Luo Y., Xu B.E., Sun X., Wu J.
      Proc. Natl. Acad. Sci. U.S.A. 104:9248-9253(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCDN3 AND CDKN1A, MUTAGENESIS OF LYS-164.
    12. "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-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CCNY.
    14. "Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1."
      Jiang M., Gao Y., Yang T., Zhu X., Chen J.
      FEBS Lett. 583:2171-2178(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCNY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-164.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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] ILE-432 AND ARG-463.

    Entry informationi

    Entry nameiCDK14_HUMAN
    AccessioniPrimary (citable) accession number: O94921
    Secondary accession number(s): A4D1E6
    , A6NK51, A8WFP6, B4DHG5, B4DNM2, Q75N06, Q75N22, Q8N764, Q9H3D7, Q9UDR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: April 18, 2006
    Last modified: October 1, 2014
    This is version 142 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3