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Q00536 (CDK16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence 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.14 Ref.15 Ref.16

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.14 Ref.15 Ref.16

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.14 Ref.15 Ref.16

Subcellular location

Cytoplasm. Cytoplasmic vesiclesecretory vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionsynapsesynaptosome By similarity. Note: Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY. Ref.15 Ref.16

Tissue specificity

Detected in pancreas islets (at protein level). Detected in brain and pancreas. Ref.15

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 processDifferentiation
Spermatogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoplasmic vesicle
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processexocytosis

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

protein phosphorylation

Traceable author statement PubMed 1437147. Source: ProtInc

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype Ref.15. Source: UniProtKB

spermatogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

extrinsic component of cytoplasmic side of plasma membrane

Inferred from direct assay Ref.16. Source: UniProtKB

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 16091426. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay Ref.16Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SEC23AQ154363EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Cyclin-dependent kinase 16
PRO_0000086484

Regions

Domain165 – 446282Protein kinase
Nucleotide binding171 – 1799ATP By similarity

Sites

Active site2861Proton acceptor By similarity
Binding site1941ATP Probable

Amino acid modifications

Modified residue121Phosphoserine; by BRSK2 Ref.15
Modified residue421Phosphoserine Ref.11
Modified residue781Phosphoserine Ref.8 Ref.11
Modified residue821Phosphoserine Ref.8 Ref.11
Modified residue951Phosphoserine; by CDK5 Ref.8 Ref.11
Modified residue1191Phosphoserine Ref.8 Ref.11 Ref.13
Modified residue1381Phosphoserine Ref.8 Ref.9 Ref.11
Modified residue1531Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue1551Phosphoserine Ref.9

Natural variations

Alternative sequence11M → MPLYGRARDHVTHPSILGTR PGRPMAGPITAAVPEKICNG AFCSCSGAFPLDPNNPSLGP LPSISHLNLRTQIAM in isoform 2.
VSP_046134
Alternative sequence11M → MQSEIAM in isoform 3.
VSP_046342

Experimental info

Mutagenesis121S → A: Abolishes phosphorylation by BRSK2. Abolishes effect on insulin secretion. Ref.15
Mutagenesis1191S → A: Strongly reduces interaction with CCNY. Ref.16
Mutagenesis1531S → A: Constitutively activated, due to loss of an inhibitory phosphorylation site. Increases interaction with CCNY. Ref.15 Ref.16
Mutagenesis1531S → D: Abolishes interaction with CCNY. Ref.15 Ref.16
Mutagenesis1941K → A: Loss of kinase activity. Abolishes effect on insulin secretion. Ref.15 Ref.16
Mutagenesis1941K → R: Loss of kinase activity. Ref.15 Ref.16
Sequence conflict251N → D in BAH13564. Ref.3

Secondary structure

......................................................... 496
Helix Strand Turn

Details...

Sequences

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

Last modified April 1, 1993. Version 1.
Checksum: 9A5DDD34A5E5CBBB

FASTA49655,716
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 9D3020F5CADD1899
Show »

FASTA57063,458
Isoform 3 [UniParc].

Checksum: AC4B7353DFF4D005
Show »

FASTA50256,375

References

« Hide '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. 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] (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. expand/collapse author list , 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. 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 (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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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.
[16]"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.
[17]"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.
CCDSCCDS14276.1. [Q00536-1]
CCDS48101.1. [Q00536-3]
CCDS55408.1. [Q00536-2]
PIRS23385.
RefSeqNP_001163931.1. NM_001170460.1. [Q00536-2]
NP_006192.1. NM_006201.4. [Q00536-1]
NP_148978.2. NM_033018.3. [Q00536-3]
XP_005272672.1. XM_005272615.1. [Q00536-1]
XP_006724597.1. XM_006724534.1. [Q00536-1]
XP_006724598.1. XM_006724535.1. [Q00536-1]
UniGeneHs.496068.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTLX-ray2.40A163-478[»]
ProteinModelPortalQ00536.
SMRQ00536. Positions 71-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111154. 20 interactions.
IntActQ00536. 9 interactions.
STRING9606.ENSP00000405798.

Chemistry

BindingDBQ00536.
ChEMBLCHEMBL4597.
GuidetoPHARMACOLOGY1969.

PTM databases

PhosphoSiteQ00536.

Polymorphism databases

DMDM266425.

Proteomic databases

MaxQBQ00536.
PaxDbQ00536.
PRIDEQ00536.

Protocols and materials databases

DNASU5127.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000276052; ENSP00000276052; ENSG00000102225. [Q00536-2]
ENST00000357227; ENSP00000349762; ENSG00000102225. [Q00536-1]
ENST00000457458; ENSP00000405798; ENSG00000102225. [Q00536-3]
ENST00000518022; ENSP00000429751; ENSG00000102225. [Q00536-1]
ENST00000603165; ENSP00000474587; ENSG00000270633. [Q00536-2]
ENST00000604531; ENSP00000474779; ENSG00000270633. [Q00536-3]
ENST00000605184; ENSP00000474747; ENSG00000270633. [Q00536-1]
ENST00000605853; ENSP00000475112; ENSG00000270633. [Q00536-1]
GeneID5127.
KEGGhsa:5127.
UCSCuc004dho.3. human. [Q00536-1]
uc011mli.2. human.

Organism-specific databases

CTD5127.
GeneCardsGC0XP047078.
HGNCHGNC:8749. CDK16.
HPACAB016535.
HPA000974.
HPA001366.
MIM311550. gene.
neXtProtNX_Q00536.
PharmGKBPA33095.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidQ00536.
KOK08820.
OMAVAMDRMK.
OrthoDBEOG7966H8.
PhylomeDBQ00536.
TreeFamTF106508.

Enzyme and pathway databases

BRENDA2.7.11.22. 2681.
SignaLinkQ00536.

Gene expression databases

ArrayExpressQ00536.
BgeeQ00536.
CleanExHS_PCTK1.
GenevestigatorQ00536.

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

ChiTaRSCDK16. human.
GeneWikiPCTK1.
GenomeRNAi5127.
NextBio19762.
PROQ00536.
SOURCESearch...

Entry information

Entry nameCDK16_HUMAN
AccessionPrimary (citable) accession number: Q00536
Secondary accession number(s): A8K280 expand/collapse secondary AC list , B7Z7C8, J3KN74, J3KQP7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 150 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome X

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