O94921 (CDK14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CDK14
Synonyms:	KIAA0834, PFTK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Wnt signaling pathway
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Inferred from direct assay Ref.13. Source: UniProtKB Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW regulation of canonical Wnt receptor signaling pathway Inferred from direct assay Ref.13. Source: UniProtKB
Cellular_component	cytoplasmic cyclin-dependent protein kinase holoenzyme complex Inferred from direct assay Ref.14Ref.13. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay Ref.14Ref.13. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein serine/threonine kinase activity Inferred from mutant phenotype Ref.14Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCND3	P30281	5	EBI-1043945,EBI-375013
CDKN1A	P38936	7	EBI-1043945,EBI-375077
HSP90AB1	P08238	2	EBI-1043945,EBI-352572
YWHAB	P31946	5	EBI-1043945,EBI-359815
YWHAE	P62258	3	EBI-1043945,EBI-356498
YWHAH	Q04917	3	EBI-1043945,EBI-306940
YWHAQ	P27348	3	EBI-1043945,EBI-359854

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 469	469	Cyclin-dependent kinase 14		PRO_0000086506
Regions
	Domain	135 – 419	285	Protein kinase
	Nucleotide binding	141 – 149	9	ATP By similarity
Sites
	Active site	256	1	Proton acceptor By similarity
	Binding site	164	1	ATP Probable
Amino acid modifications
	Modified residue	95	1	Phosphoserine Ref.12 Ref.15
Natural variations
	Alternative sequence	1 – 46	46	Missing in isoform 3.		VSP_038762
	Alternative sequence	1 – 41	41	MCDLI…TTFDE → MHGYFGCNAAAEPGYSAFVG TPQ in isoform 2.		VSP_004803
	Natural variant	432	1	M → I in an ovarian mucinous carcinoma; somatic mutation. Ref.16		VAR_046765
	Natural variant	463	1	S → R. Ref.16		VAR_046766
Experimental info
	Mutagenesis	164	1	K → R: Abolishes protein kinase activity. Ref.11 Ref.14
	Sequence conflict	8	1	Q → R in BAG60284. Ref.3
	Sequence conflict	158	1	G → W in AAG43234. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 18, 2006. Version 3. Checksum: 32CF9B9B7BD9CE0E	FASTA	469	53,057
	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
	Isoform 2 [UniParc]. Checksum: 68210FCBC0D44031	FASTA	451	50,662
	10 20 30 40 50 60 MHGYFGCNAA AEPGYSAFVG TPQICVTKMS TRNCQGMDSV IKPLDTIPED KKVRVQRTQS 70 80 90 100 110 120 TFDPFEKPAN QVKRVHSENN ACINFKTSST GKESPKVRRH SSPSSPTSPK FGKADSYEKL 130 140 150 160 170 180 EKLGEGSYAT VYKGKSKVNG KLVALKVIRL QEEEGTPFTA IREASLLKGL KHANIVLLHD 190 200 210 220 230 240 IIHTKETLTL VFEYVHTDLC QYMDKHPGGL HPDNVKLFLF QLLRGLSYIH QRYILHRDLK 250 260 270 280 290 300 PQNLLISDTG ELKLADFGLA RAKSVPSHTY SNEVVTLWYR PPDVLLGSTE YSTCLDMWGV 310 320 330 340 350 360 GCIFVEMIQG VAAFPGMKDI QDQLERIFLV LGTPNEDTWP GVHSLPHFKP ERFTLYSSKN 370 380 390 400 410 420 LRQAWNKLSY VNHAEDLASK LLQCSPKNRL SAQAALSHEY FSDLPPRLWE LTDMSSIFTV 430 440 450 PNVRLQPEAG ESMRAFGKNN SYGKSLSNSK H
	Isoform 3 [UniParc]. Checksum: 5F5D5B2C611243FA	FASTA	423	47,760
	10 20 30 40 50 60 MSTRNCQGMD SVIKPLDTIP EDKKVRVQRT QSTFDPFEKP ANQVKRVHSE NNACINFKTS 70 80 90 100 110 120 STGKESPKVR RHSSPSSPTS PKFGKADSYE KLEKLGEGSY ATVYKGKSKV NGKLVALKVI 130 140 150 160 170 180 RLQEEEGTPF TAIREASLLK GLKHANIVLL HDIIHTKETL TLVFEYVHTD LCQYMDKHPG 190 200 210 220 230 240 GLHPDNVKLF LFQLLRGLSY IHQRYILHRD LKPQNLLISD TGELKLADFG LARAKSVPSH 250 260 270 280 290 300 TYSNEVVTLW YRPPDVLLGS TEYSTCLDMW GVGCIFVEMI QGVAAFPGMK DIQDQLERIF 310 320 330 340 350 360 LVLGTPNEDT WPGVHSLPHF KPERFTLYSS KNLRQAWNKL SYVNHAEDLA SKLLQCSPKN 370 380 390 400 410 420 RLSAQAALSH EYFSDLPPRL WELTDMSSIF TVPNVRLQPE AGESMRAFGK NNSYGKSLSN SKH

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.
+	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.
IPI	IPI00165249. IPI00742856. IPI00877696.
RefSeq	NP_036527.1. NM_012395.2.
UniGene	Hs.258576.
3D structure databases
ProteinModelPortal	O94921.
ModBase	Search...
Protein-protein interaction databases
IntAct	O94921. 8 interactions.
MINT	MINT-7147554.
STRING	9606.ENSP00000265741.
PTM databases
PhosphoSite	O94921.
Proteomic databases
PaxDb	O94921.
PRIDE	O94921.
Protocols and materials databases
DNASU	5218.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265741; ENSP00000265741; ENSG00000058091. ENST00000380050; ENSP00000369390; ENSG00000058091. ENST00000406263; ENSP00000385034; ENSG00000058091.
GeneID	5218.
KEGG	hsa:5218.
UCSC	uc003uky.2. human. uc003ukz.1. human.
Organism-specific databases
CTD	5218.
GeneCards	GC07P090095.
HGNC	HGNC:8883. CDK14.
HPA	HPA015267.
MIM	610679. gene.
neXtProt	NX_O94921.
PharmGKB	PA33221.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG014652.
InParanoid	O94921.
KO	K08821.
OMA	KPERFTQ.
PhylomeDB	O94921.
Gene expression databases
ArrayExpress	O94921.
Bgee	O94921.
CleanEx	HS_PFTK1.
Genevestigator	O94921.
GermOnline	ENSG00000058091. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O94921.
ChEMBL	CHEMBL6162.
ChiTaRS	CDK14. human.
GenomeRNAi	5218.
NextBio	20182.
SOURCE	Search...

Entry information

Entry name

CDK14_HUMAN

Accession

Primary (citable) accession number: O94921
Secondary accession number(s): A4D1E6 , 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:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.