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O94921 (CDK14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
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 names
Name:CDK14
Synonyms:KIAA0834, PFTK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11 Ref.13 Ref.14

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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

Subunit structure

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. Ref.8 Ref.9 Ref.11 Ref.13 Ref.14

Subcellular location

Cell membrane; Peripheral membrane protein. Cytoplasm. Nucleus. Note: Recruited to the cell membrane by CCNY. Ref.1 Ref.13 Ref.14

Tissue specificity

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. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O94921-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O94921-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDE → MHGYFGCNAAAEPGYSAFVGTPQ
Isoform 3 (identifier: O94921-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Cyclin-dependent kinase 14
PRO_0000086506

Regions

Domain135 – 419285Protein kinase
Nucleotide binding141 – 1499ATP By similarity

Sites

Active site2561Proton acceptor By similarity
Binding site1641ATP Probable

Amino acid modifications

Modified residue951Phosphoserine Ref.12 Ref.15

Natural variations

Alternative sequence1 – 4646Missing in isoform 3.
VSP_038762
Alternative sequence1 – 4141MCDLI…TTFDE → MHGYFGCNAAAEPGYSAFVG TPQ in isoform 2.
VSP_004803
Natural variant4321M → I in an ovarian mucinous carcinoma; somatic mutation. Ref.16
VAR_046765
Natural variant4631S → R. Ref.16
VAR_046766

Experimental info

Mutagenesis1641K → R: Abolishes protein kinase activity. Ref.11 Ref.14
Sequence conflict81Q → R in BAG60284. Ref.3
Sequence conflict1581G → W in AAG43234. Ref.1

Sequences

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

Last modified April 18, 2006. Version 3.
Checksum: 32CF9B9B7BD9CE0E

FASTA46953,057
        10         20         30         40         50         60 
MCDLIEPQPA EKIGKMKKLR RTLSESFSRI ALKKDDTTFD EICVTKMSTR NCQGMDSVIK 

        70         80         90        100        110        120 
PLDTIPEDKK VRVQRTQSTF DPFEKPANQV KRVHSENNAC INFKTSSTGK ESPKVRRHSS 

       130        140        150        160        170        180 
PSSPTSPKFG KADSYEKLEK LGEGSYATVY KGKSKVNGKL VALKVIRLQE EEGTPFTAIR 

       190        200        210        220        230        240 
EASLLKGLKH ANIVLLHDII HTKETLTLVF EYVHTDLCQY MDKHPGGLHP DNVKLFLFQL 

       250        260        270        280        290        300 
LRGLSYIHQR YILHRDLKPQ NLLISDTGEL KLADFGLARA KSVPSHTYSN EVVTLWYRPP 

       310        320        330        340        350        360 
DVLLGSTEYS TCLDMWGVGC IFVEMIQGVA AFPGMKDIQD QLERIFLVLG TPNEDTWPGV 

       370        380        390        400        410        420 
HSLPHFKPER FTLYSSKNLR QAWNKLSYVN HAEDLASKLL QCSPKNRLSA QAALSHEYFS 

       430        440        450        460 
DLPPRLWELT DMSSIFTVPN VRLQPEAGES MRAFGKNNSY GKSLSNSKH 

« Hide

Isoform 2 [UniParc].

Checksum: 68210FCBC0D44031
Show »

FASTA45150,662
Isoform 3 [UniParc].

Checksum: 5F5D5B2C611243FA
Show »

FASTA42347,760

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Cell cycle control of wnt receptor activation."
Davidson G., Shen J., Huang Y.L., Su Y., Karaulanov E., Bartscherer K., Hassler C., Stannek P., Boutros M., Niehrs C.
Dev. Cell 17:788-799(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-432 AND ARG-463.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001274064.1. NM_001287135.1.
NP_001274065.1. NM_001287136.1.
NP_001274066.1. NM_001287137.1.
NP_036527.1. NM_012395.3.
XP_005250495.1. XM_005250438.1.
XP_005250496.1. XM_005250439.1.
UniGeneHs.258576.
Hs.430742.

3D structure databases

ProteinModelPortalO94921.
SMRO94921. Positions 98-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111239. 11 interactions.
IntActO94921. 13 interactions.
MINTMINT-7147554.
STRING9606.ENSP00000265741.

Chemistry

BindingDBO94921.
ChEMBLCHEMBL6162.
GuidetoPHARMACOLOGY1967.

PTM databases

PhosphoSiteO94921.

Proteomic databases

PaxDbO94921.
PRIDEO94921.

Protocols and materials databases

DNASU5218.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265741; ENSP00000265741; ENSG00000058091. [O94921-2]
ENST00000380050; ENSP00000369390; ENSG00000058091. [O94921-1]
ENST00000406263; ENSP00000385034; ENSG00000058091. [O94921-3]
GeneID5218.
KEGGhsa:5218.
UCSCuc003uky.2. human. [O94921-1]
uc003ukz.1. human. [O94921-2]

Organism-specific databases

CTD5218.
GeneCardsGC07P090095.
HGNCHGNC:8883. CDK14.
HPAHPA015267.
MIM610679. gene.
neXtProtNX_O94921.
PharmGKBPA33221.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG014652.
InParanoidO94921.
KOK08821.
OMAKKLRQAW.
PhylomeDBO94921.
TreeFamTF106508.

Enzyme and pathway databases

SignaLinkO94921.

Gene expression databases

ArrayExpressO94921.
BgeeO94921.
CleanExHS_PFTK1.
GenevestigatorO94921.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDK14. human.
GeneWikiPFTK1.
GenomeRNAi5218.
NextBio20182.
PROO94921.
SOURCESearch...

Entry information

Entry nameCDK14_HUMAN
AccessionPrimary (citable) accession number: O94921
Secondary accession number(s): A4D1E6 expand/collapse secondary AC list , A6NK51, A8WFP6, B4DHG5, B4DNM2, Q75N06, Q75N22, Q8N764, Q9H3D7, Q9UDR0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: April 18, 2006
Last modified: March 19, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM