Q00536 (CDK16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 16
EC=2.7.11.22

Alternative name(s):
Cell division protein kinase 16
PCTAIRE-motif protein kinase 1
Serine/threonine-protein kinase PCTAIRE-1

Gene names

Name:	CDK16
Synonyms:	PCTAIRE1, PCTK1

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

General annotation (Comments)

Function	Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development By similarity. Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Can phosphorylate CCNY at 'Ser-336' (in vitro). Ref.13 Ref.14 Ref.15
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.13 Ref.14 Ref.15
Subunit structure	Found in a complex containing CABLES1, CDK17 and TDRD7. Interacts with YWHAH, YWHAQ and YWHAZ. Interacts with NSF. Identified in a complex with NSF, syntaxin-1, synaptotagmin, SYN1, SYP and CDK5R1 By similarity. Interacts with BRSK2. Interacts with CCNY; this increases the CDK16 kinase activity. Ref.13 Ref.14 Ref.15
Subcellular location	Cytoplasm. Cytoplasmic vesicle › secretory vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction › synapse › synaptosome By similarity. Note: Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY. Ref.14 Ref.15
Tissue specificity	Detected in pancreas islets (at protein level). Detected in brain and pancreas. Ref.14
Post-translational modification	Phosphorylation at Ser-153 inhibits kinase activity.
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 AAH01048.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAH15607.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis
Cellular component	Cell junction Cell membrane Cytoplasm Cytoplasmic vesicle Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: GOC exocytosis Inferred from sequence or structural similarity. Source: UniProtKB growth hormone secretion Inferred from sequence or structural similarity. Source: UniProtKB neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB regulation of insulin secretion involved in cellular response to glucose stimulus Inferred from mutant phenotype Ref.14. Source: UniProtKB spermatogenesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from direct assay Ref.14. Source: UniProtKB extrinsic to internal side of plasma membrane Inferred from direct assay Ref.15. Source: UniProtKB neuron projection Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-KW transport vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
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 serine/threonine kinase activity Inferred from direct assay Ref.15Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SEC23A	Q15436	3	EBI-726261,EBI-81088

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q00536-1)

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: Q00536-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPLYGRARDH...HLNLRTQIAM

Note: No experimental confirmation available.

Isoform 3 (identifier: Q00536-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQSEIAM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 496

496

Cyclin-dependent kinase 16

PRO_0000086484

Regions

Domain

165 – 446

282

Protein kinase

Nucleotide binding

171 – 179

9

ATP By similarity

Sites

Active site

286

1

Proton acceptor By similarity

Binding site

194

1

ATP Probable

Amino acid modifications

Modified residue

12

1

Phosphoserine; by BRSK2 Ref.14

Modified residue

42

1

Phosphoserine Ref.10

Modified residue

78

1

Phosphoserine Ref.8 Ref.10

Modified residue

82

1

Phosphoserine Ref.8 Ref.10

Modified residue

95

1

Phosphoserine; by CDK5 Ref.8 Ref.10

Modified residue

110

1

Phosphoserine By similarity

Modified residue

119

1

Phosphoserine Ref.8 Ref.10 Ref.12

Modified residue

138

1

Phosphoserine Ref.8 Ref.9 Ref.10

Modified residue

153

1

Phosphoserine Ref.9 Ref.11 Ref.12

Modified residue

155

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

1

1

M → MPLYGRARDHVTHPSILGTR PGRPMAGPITAAVPEKICNG AFCSCSGAFPLDPNNPSLGP LPSISHLNLRTQIAM in isoform 2.

VSP_046134

Alternative sequence

1

1

M → MQSEIAM in isoform 3.

VSP_046342

Experimental info

Mutagenesis

12

1

S → A: Abolishes phosphorylation by BRSK2. Abolishes effect on insulin secretion. Ref.14

Mutagenesis

119

1

S → A: Strongly reduces interaction with CCNY. Ref.15

Mutagenesis

153

1

S → A: Constitutively activated, due to loss of an inhibitory phosphorylation site. Increases interaction with CCNY. Ref.14 Ref.15

Mutagenesis

153

1

S → D: Abolishes interaction with CCNY. Ref.14 Ref.15

Mutagenesis

194

1

K → A: Loss of kinase activity. Abolishes effect on insulin secretion. Ref.14 Ref.15

Mutagenesis

194

1

K → R: Loss of kinase activity. Ref.14 Ref.15

Sequence conflict

25

1

N → D in BAH13564. Ref.3

Secondary structure

1

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496

Helix Strand Turn

Details...

Beta strand

164 – 173

10

Beta strand

175 – 184

10

Turn

185 – 187

3

Beta strand

190 – 196

7

Helix

212 – 215

4

Beta strand

226 – 231

6

Beta strand

236 – 241

6

Beta strand

244 – 246

3

Helix

247 – 253

7

Turn

254 – 256

3

Helix

260 – 279

20

Beta strand

282 – 286

5

Helix

289 – 291

3

Beta strand

292 – 294

3

Beta strand

300 – 302

3

Beta strand

304 – 309

6

Helix

325 – 327

3

Helix

330 – 333

4

Helix

342 – 357

16

Helix

367 – 378

12

Turn

383 – 385

3

Helix

389 – 391

3

Helix

393 – 397

5

Helix

408 – 411

4

Helix

417 – 426

10

Helix

431 – 433

3

Helix

437 – 440

4

Helix

444 – 449

6

Beta strand

454 – 456

3

Helix

462 – 464

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 9A5DDD34A5E5CBBB	FASTA	496	55,716
	10 20 30 40 50 60 MDRMKKIKRQ LSMTLRGGRG IDKTNGAPEQ IGLDESGGGG GSDPGEAPTR AAPGELRSAR 70 80 90 100 110 120 GPLSSAPEIV HEDLKMGSDG ESDQASATSS DEVQSPVRVR MRNHPPRKIS TEDINKRLSL 130 140 150 160 170 180 PADIRLPEGY LEKLTLNSPI FDKPLSRRLR RVSLSEIGFG KLETYIKLDK LGEGTYATVY 190 200 210 220 230 240 KGKSKLTDNL VALKEIRLEH EEGAPCTAIR EVSLLKDLKH ANIVTLHDII HTEKSLTLVF 250 260 270 280 290 300 EYLDKDLKQY LDDCGNIINM HNVKLFLFQL LRGLAYCHRQ KVLHRDLKPQ NLLINERGEL 310 320 330 340 350 360 KLADFGLARA KSIPTKTYSN EVVTLWYRPP DILLGSTDYS TQIDMWGVGC IFYEMATGRP 370 380 390 400 410 420 LFPGSTVEEQ LHFIFRILGT PTEETWPGIL SNEEFKTYNY PKYRAEALLS HAPRLDSDGA 430 440 450 460 470 480 DLLTKLLQFE GRNRISAEDA MKHPFFLSLG ERIHKLPDTT SIFALKEIQL QKEASLRSSS 490 MPDSGRPAFR VVDTEF
	Isoform 2 [UniParc]. Checksum: 9D3020F5CADD1899	FASTA	570	63,458
	10 20 30 40 50 60 MPLYGRARDH VTHPSILGTR PGRPMAGPIT AAVPEKICNG AFCSCSGAFP LDPNNPSLGP 70 80 90 100 110 120 LPSISHLNLR TQIAMDRMKK IKRQLSMTLR GGRGIDKTNG APEQIGLDES GGGGGSDPGE 130 140 150 160 170 180 APTRAAPGEL RSARGPLSSA PEIVHEDLKM GSDGESDQAS ATSSDEVQSP VRVRMRNHPP 190 200 210 220 230 240 RKISTEDINK RLSLPADIRL PEGYLEKLTL NSPIFDKPLS RRLRRVSLSE IGFGKLETYI 250 260 270 280 290 300 KLDKLGEGTY ATVYKGKSKL TDNLVALKEI RLEHEEGAPC TAIREVSLLK DLKHANIVTL 310 320 330 340 350 360 HDIIHTEKSL TLVFEYLDKD LKQYLDDCGN IINMHNVKLF LFQLLRGLAY CHRQKVLHRD 370 380 390 400 410 420 LKPQNLLINE RGELKLADFG LARAKSIPTK TYSNEVVTLW YRPPDILLGS TDYSTQIDMW 430 440 450 460 470 480 GVGCIFYEMA TGRPLFPGST VEEQLHFIFR ILGTPTEETW PGILSNEEFK TYNYPKYRAE 490 500 510 520 530 540 ALLSHAPRLD SDGADLLTKL LQFEGRNRIS AEDAMKHPFF LSLGERIHKL PDTTSIFALK 550 560 570 EIQLQKEASL RSSSMPDSGR PAFRVVDTEF
	Isoform 3 [UniParc]. Checksum: AC4B7353DFF4D005	FASTA	502	56,375
	10 20 30 40 50 60 MQSEIAMDRM KKIKRQLSMT LRGGRGIDKT NGAPEQIGLD ESGGGGGSDP GEAPTRAAPG 70 80 90 100 110 120 ELRSARGPLS SAPEIVHEDL KMGSDGESDQ ASATSSDEVQ SPVRVRMRNH PPRKISTEDI 130 140 150 160 170 180 NKRLSLPADI RLPEGYLEKL TLNSPIFDKP LSRRLRRVSL SEIGFGKLET YIKLDKLGEG 190 200 210 220 230 240 TYATVYKGKS KLTDNLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV TLHDIIHTEK 250 260 270 280 290 300 SLTLVFEYLD KDLKQYLDDC GNIINMHNVK LFLFQLLRGL AYCHRQKVLH RDLKPQNLLI 310 320 330 340 350 360 NERGELKLAD FGLARAKSIP TKTYSNEVVT LWYRPPDILL GSTDYSTQID MWGVGCIFYE 370 380 390 400 410 420 MATGRPLFPG STVEEQLHFI FRILGTPTEE TWPGILSNEE FKTYNYPKYR AEALLSHAPR 430 440 450 460 470 480 LDSDGADLLT KLLQFEGRNR ISAEDAMKHP FFLSLGERIH KLPDTTSIFA LKEIQLQKEA 490 500 SLRSSSMPDS GRPAFRVVDT EF

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]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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] (ISOFORMS 1 AND 2). Tissue: Testis and Thalamus.
[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]	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].
[6]	"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 3). Tissue: Brain and Placenta.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"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-78; SER-82; SER-95; SER-119 AND SER-138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-138; SER-153 AND SER-155, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-42; SER-78; SER-82; SER-95; SER-119 AND SER-138, MASS SPECTROMETRY.
[11]	"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-153, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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-119 AND SER-153, MASS SPECTROMETRY.
[13]	"Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1 kinase." Shehata S.N., Hunter R.W., Ohta E., Peggie M.W., Lou H.J., Sicheri F., Zeqiraj E., Turk B.E., Sakamoto K. Cell. Signal. 24:2085-2094(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCNY.
[14]	"Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively regulates glucose-stimulated insulin secretion in pancreatic beta-cells." Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L., Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O., Yu L. J. Biol. Chem. 287:30368-30375(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, TISSUE SPECIFICITY.
[15]	"Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and is essential for spermatogenesis." Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M., Pelliniemi L.J., Boesl M., Geley S. Mol. Cell. Biol. 32:868-879(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CCNY, MUTAGENESIS OF SER-119; SER-153 AND LYS-194.
[16]	"Crystal structure of the PCTAIRE1 kinase in complex with indirubin e804." Structural genomics consortium (SGC) Submitted (JUN-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 163-478.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X66363 mRNA. Translation: CAA47006.1.
BT006827 mRNA. Translation: AAP35473.1.
AK290145 mRNA. Translation: BAF82834.1.
AK301832 mRNA. Translation: BAH13564.1.
AL096791 Genomic DNA. Translation: CAD20055.1.
AL513366 Genomic DNA. No translation available.
CH471164 Genomic DNA. Translation: EAW59295.1.
CH471164 Genomic DNA. Translation: EAW59297.1.
BC001048 mRNA. Translation: AAH01048.1. Different initiation.
BC015607 mRNA. Translation: AAH15607.1. Different initiation.

IPI

IPI00549858.
IPI00954838.

PIR

S23385.

RefSeq

NP_001163931.1. NM_001170460.1.
NP_006192.1. NM_006201.4.
NP_148978.2. NM_033018.3.

UniGene

Hs.496068.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MTL	X-ray	2.40	A	163-478	[»]

ProteinModelPortal

Q00536.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q00536. 3 interactions.

STRING

9606.ENSP00000405798.

PTM databases

PhosphoSite

Q00536.

Polymorphism databases

DMDM

266425.

Proteomic databases

PaxDb

Q00536.

PRIDE

Q00536.

Protocols and materials databases

DNASU

5127.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276052; ENSP00000276052; ENSG00000102225.
ENST00000357227; ENSP00000349762; ENSG00000102225.
ENST00000518022; ENSP00000429751; ENSG00000102225.

GeneID

5127.

KEGG

hsa:5127.

UCSC

uc004dho.3. human.

Organism-specific databases

CTD

5127.

GeneCards

GC0XP047078.

HGNC

HGNC:8749. CDK16.

HPA

CAB016535.
HPA001366.

MIM

311550. gene.

neXtProt

NX_Q00536.

PharmGKB

PA33095.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233024.

HOVERGEN

HBG014652.

InParanoid

Q00536.

KO

K08820.

OrthoDB

EOG44BB24.

PhylomeDB

Q00536.

Enzyme and pathway databases

BRENDA

2.7.11.22. 2681.

Gene expression databases

ArrayExpress

Q00536.

Bgee

Q00536.

CleanEx

HS_PCTK1.

Genevestigator

Q00536.

GermOnline

ENSG00000102225. 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

Q00536.

ChEMBL

CHEMBL4597.

ChiTaRS

CDK16. human.

GenomeRNAi

5127.

NextBio

19762.

SOURCE

Search...

Entry information

Entry name

CDK16_HUMAN

Accession

Primary (citable) accession number: Q00536
Secondary accession number(s): A8K280 , B7Z7C8, J3KN74, J3KQP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 136 of the entry and version 1 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.