Q00537 (CDK17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 17
EC=2.7.11.22

Alternative name(s):
Cell division protein kinase 17
PCTAIRE-motif protein kinase 2
Serine/threonine-protein kinase PCTAIRE-2

Gene names

Name:	CDK17
Synonyms:	PCTAIRE2, PCTK2

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	523 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Found in a complex containing CABLES1, CDK16 and TDRD7. Interacts with TDRD7 By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
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	cell cycle Inferred from electronic annotation. Source: GOC
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein serine/threonine kinase activity Inferred from electronic annotation. Source: EC protein kinase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q00537-1)

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: Q00537-2)

The sequence of this isoform differs from the canonical sequence as follows:
     513-523: HGKNRRQSMLF → VFVINHFTCRS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 523	523	Cyclin-dependent kinase 17		PRO_0000086487
Regions
	Domain	192 – 473	282	Protein kinase
	Nucleotide binding	198 – 206	9	ATP By similarity
Sites
	Active site	313	1	Proton acceptor By similarity
	Binding site	221	1	ATP By similarity
Amino acid modifications
	Modified residue	9	1	Phosphoserine By similarity
	Modified residue	80	1	Phosphoserine Ref.8
	Modified residue	105	1	Phosphoserine Ref.8
	Modified residue	137	1	Phosphoserine Ref.6 Ref.8 Ref.10
	Modified residue	146	1	Phosphoserine Ref.6
	Modified residue	165	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9
	Modified residue	180	1	Phosphoserine Ref.7 Ref.9 Ref.10
	Modified residue	203	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	513 – 523	11	HGKNRRQSMLF → VFVINHFTCRS in isoform 2.		VSP_043295
	Natural variant	214	1	T → I Found in a renal cell carcinoma sample; somatic mutation. Ref.11		VAR_064743
Experimental info
	Sequence conflict	367	1	S → L in CAA47004. Ref.1
	Sequence conflict	433	1	Q → E in CAA47004. Ref.1
	Sequence conflict	451	1	T → R in CAA47004. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 15, 2005. Version 2. Checksum: 429ABD1DCBB5A082	FASTA	523	59,582
	10 20 30 40 50 60 MKKFKRRLSL TLRGSQTIDE SLSELAEQMT IEENSSKDNE PIVKNGRPPT SHSMHSFLHQ 70 80 90 100 110 120 YTGSFKKPPL RRPHSVIGGS LGSFMAMPRN GSRLDIVHEN LKMGSDGESD QASGTSSDEV 130 140 150 160 170 180 QSPTGVCLRN RIHRRISMED LNKRLSLPAD IRIPDGYLEK LQINSPPFDQ PMSRRSRRAS 190 200 210 220 230 240 LSEIGFGKME TYIKLEKLGE GTYATVYKGR SKLTENLVAL KEIRLEHEEG APCTAIREVS 250 260 270 280 290 300 LLKDLKHANI VTLHDIVHTD KSLTLVFEYL DKDLKQYMDD CGNIMSMHNV KLFLYQILRG 310 320 330 340 350 360 LAYCHRRKVL HRDLKPQNLL INEKGELKLA DFGLARAKSV PTKTYSNEVV TLWYRPPDVL 370 380 390 400 410 420 LGSSEYSTQI DMWGVGCIFF EMASGRPLFP GSTVEDELHL IFRLLGTPSQ ETWPGISSNE 430 440 450 460 470 480 EFKNYNFPKY KPQPLINHAP RLDSEGIELI TKFLQYESKK RVSAEEAMKH VYFRSLGPRI 490 500 510 520 HALPESVSIF SLKEIQLQKD PGFRNSSYPE TGHGKNRRQS MLF
	Isoform 2 [UniParc]. Checksum: 5FD1C9DFC4B050C6	FASTA	523	59,531
	10 20 30 40 50 60 MKKFKRRLSL TLRGSQTIDE SLSELAEQMT IEENSSKDNE PIVKNGRPPT SHSMHSFLHQ 70 80 90 100 110 120 YTGSFKKPPL RRPHSVIGGS LGSFMAMPRN GSRLDIVHEN LKMGSDGESD QASGTSSDEV 130 140 150 160 170 180 QSPTGVCLRN RIHRRISMED LNKRLSLPAD IRIPDGYLEK LQINSPPFDQ PMSRRSRRAS 190 200 210 220 230 240 LSEIGFGKME TYIKLEKLGE GTYATVYKGR SKLTENLVAL KEIRLEHEEG APCTAIREVS 250 260 270 280 290 300 LLKDLKHANI VTLHDIVHTD KSLTLVFEYL DKDLKQYMDD CGNIMSMHNV KLFLYQILRG 310 320 330 340 350 360 LAYCHRRKVL HRDLKPQNLL INEKGELKLA DFGLARAKSV PTKTYSNEVV TLWYRPPDVL 370 380 390 400 410 420 LGSSEYSTQI DMWGVGCIFF EMASGRPLFP GSTVEDELHL IFRLLGTPSQ ETWPGISSNE 430 440 450 460 470 480 EFKNYNFPKY KPQPLINHAP RLDSEGIELI TKFLQYESKK RVSAEEAMKH VYFRSLGPRI 490 500 510 520 HALPESVSIF SLKEIQLQKD PGFRNSSYPE TGVFVINHFT CRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A family of human cdc2-related protein kinases." Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C., Harlow E., Tsai L.-H. EMBO J. 11:2909-2917(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal brain.
[2]	"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] (ISOFORMS 1 AND 2). Tissue: Trachea.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 1). Tissue: Testis.
[6]	"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-137; SER-146 AND SER-165, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-180, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-80; SER-105; SER-137 AND SER-165, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-180, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-180, MASS SPECTROMETRY.
[11]	"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A. Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ILE-214.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X66360 mRNA. Translation: CAA47004.1. AK290011 mRNA. Translation: BAF82700.1. AK315214 mRNA. Translation: BAG37649.1. AC125612 Genomic DNA. No translation available. CH471054 Genomic DNA. Translation: EAW97566.1. CH471054 Genomic DNA. Translation: EAW97567.1. BC033005 mRNA. Translation: AAH33005.1.
IPI	IPI00376955.
PIR	S23384.
RefSeq	NP_001163935.1. NM_001170464.2. NP_002586.2. NM_002595.4.
UniGene	Hs.506415.
3D structure databases
ProteinModelPortal	Q00537.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q00537. 4 interactions.
MINT	MINT-1681036.
STRING	9606.ENSP00000261211.
PTM databases
PhosphoSite	Q00537.
Polymorphism databases
DMDM	59803097.
Proteomic databases
PaxDb	Q00537.
PRIDE	Q00537.
Protocols and materials databases
DNASU	5128.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261211; ENSP00000261211; ENSG00000059758. ENST00000543119; ENSP00000444459; ENSG00000059758.
GeneID	5128.
KEGG	hsa:5128.
UCSC	uc001tep.2. human.
Organism-specific databases
CTD	5128.
GeneCards	GC12M096673.
HGNC	HGNC:8750. CDK17.
HPA	HPA015325.
MIM	603440. gene.
neXtProt	NX_Q00537.
PharmGKB	PA33096.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233024.
HOVERGEN	HBG014652.
InParanoid	Q00537.
KO	K15595.
OMA	MKHAYFR.
OrthoDB	EOG44BB24.
PhylomeDB	Q00537.
Enzyme and pathway databases
BRENDA	2.7.11.22. 2681.
Gene expression databases
ArrayExpress	Q00537.
Bgee	Q00537.
CleanEx	HS_PCTK2.
Genevestigator	Q00537.
GermOnline	ENSG00000059758. 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	Q00537.
ChEMBL	CHEMBL5790.
ChiTaRS	CDK17. human.
GenomeRNAi	5128.
NextBio	19768.
SOURCE	Search...

Entry information

Entry name

CDK17_HUMAN

Accession

Primary (citable) accession number: Q00537
Secondary accession number(s): A8K1U6, B2RCQ2, Q8NEB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 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.