CDK16_HUMAN
ID CDK16_HUMAN Reviewed; 496 AA.
AC Q00536; A8K280; B7Z7C8; J3KN74; J3KQP7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Cyclin-dependent kinase 16;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 16;
DE AltName: Full=PCTAIRE-motif protein kinase 1;
DE AltName: Full=Serine/threonine-protein kinase PCTAIRE-1;
GN Name=CDK16; Synonyms=PCTAIRE1, PCTK1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=1639063; DOI=10.1002/j.1460-2075.1992.tb05360.x;
RA Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C.,
RA Harlow E., Tsai L.-H.;
RT "A family of human cdc2-related protein kinases.";
RL EMBO J. 11:2909-2917(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-82; SER-95; SER-119
RP AND SER-138, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-153 AND SER-155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-78; SER-82; SER-95;
RP SER-119 AND SER-138, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-153, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH CCNY.
RX PubMed=22796189; DOI=10.1016/j.cellsig.2012.06.018;
RA Shehata S.N., Hunter R.W., Ohta E., Peggie M.W., Lou H.J., Sicheri F.,
RA Zeqiraj E., Turk B.E., Sakamoto K.;
RT "Analysis of substrate specificity and cyclin Y binding of PCTAIRE-1
RT kinase.";
RL Cell. Signal. 24:2085-2094(2012).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BRSK2, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF SER-12; SER-153 AND LYS-194, PHOSPHORYLATION AT SER-12, AND
RP TISSUE SPECIFICITY.
RX PubMed=22798068; DOI=10.1074/jbc.m112.375618;
RA Chen X.Y., Gu X.T., Saiyin H., Wan B., Zhang Y.J., Li J., Wang Y.L.,
RA Gao R., Wang Y.F., Dong W.P., Najjar S.M., Zhang C.Y., Ding H.F., Liu J.O.,
RA Yu L.;
RT "Brain-selective kinase 2 (BRSK2) phosphorylation on PCTAIRE1 negatively
RT regulates glucose-stimulated insulin secretion in pancreatic beta-cells.";
RL J. Biol. Chem. 287:30368-30375(2012).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH CCNY,
RP AND MUTAGENESIS OF SER-119; SER-153 AND LYS-194.
RX PubMed=22184064; DOI=10.1128/mcb.06261-11;
RA Mikolcevic P., Sigl R., Rauch V., Hess M.W., Pfaller K., Barisic M.,
RA Pelliniemi L.J., Boesl M., Geley S.;
RT "Cyclin-dependent kinase 16/PCTAIRE kinase 1 is activated by cyclin Y and
RT is essential for spermatogenesis.";
RL Mol. Cell. Biol. 32:868-879(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-65; SER-95; SER-138;
RP SER-153 AND SER-155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 163-478.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the PCTAIRE1 kinase in complex with indirubin e804.";
RL Submitted (JUN-2010) to the PDB data bank.
CC -!- FUNCTION: Protein kinase that plays a role in vesicle-mediated
CC transport processes and exocytosis. Regulates GH1 release by brain
CC neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization.
CC Required for normal spermatogenesis. Regulates neuron differentiation
CC and dendrite development (By similarity). Plays a role in the
CC regulation of insulin secretion in response to changes in blood glucose
CC levels. Can phosphorylate CCNY at 'Ser-336' (in vitro). {ECO:0000250,
CC ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189,
CC ECO:0000269|PubMed:22798068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC Evidence={ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189,
CC ECO:0000269|PubMed:22798068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.22; Evidence={ECO:0000269|PubMed:22184064,
CC ECO:0000269|PubMed:22796189, ECO:0000269|PubMed:22798068};
CC -!- SUBUNIT: Found in a complex containing CABLES1, CDK17 and TDRD7.
CC Interacts with YWHAH, YWHAQ and YWHAZ. Interacts with NSF. Identified
CC in a complex with NSF, syntaxin-1, synaptotagmin, SYN1, SYP and CDK5R1
CC (By similarity). Interacts with BRSK2. Interacts with CCNY; this
CC increases the CDK16 kinase activity. {ECO:0000250,
CC ECO:0000269|PubMed:22184064, ECO:0000269|PubMed:22796189,
CC ECO:0000269|PubMed:22798068}.
CC -!- INTERACTION:
CC Q00536; Q92624: APPBP2; NbExp=3; IntAct=EBI-726261, EBI-743771;
CC Q00536; Q8ND76-1: CCNY; NbExp=7; IntAct=EBI-726261, EBI-11615526;
CC Q00536; Q8N7R7: CCNYL1; NbExp=4; IntAct=EBI-726261, EBI-10103094;
CC Q00536; Q15436: SEC23A; NbExp=3; IntAct=EBI-726261, EBI-81088;
CC Q00536; O43829: ZBTB14; NbExp=3; IntAct=EBI-726261, EBI-10176632;
CC Q00536-3; P30281: CCND3; NbExp=3; IntAct=EBI-12401765, EBI-375013;
CC Q00536-3; O43829: ZBTB14; NbExp=3; IntAct=EBI-12401765, EBI-10176632;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory
CC vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
CC Synapse, synaptosome {ECO:0000250}. Note=Colocalizes with insulin in
CC pancreas islets. Recruited to the cell membrane by CCNY.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q00536-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00536-2; Sequence=VSP_046134;
CC Name=3;
CC IsoId=Q00536-3; Sequence=VSP_046342;
CC -!- TISSUE SPECIFICITY: Detected in pancreas islets (at protein level).
CC Detected in brain and pancreas. {ECO:0000269|PubMed:22798068}.
CC -!- PTM: Phosphorylation at Ser-153 inhibits kinase activity.
CC {ECO:0000269|PubMed:22798068}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH15607.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X66363; CAA47006.1; -; mRNA.
DR EMBL; BT006827; AAP35473.1; -; mRNA.
DR EMBL; AK290145; BAF82834.1; -; mRNA.
DR EMBL; AK301832; BAH13564.1; -; mRNA.
DR EMBL; AL096791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471164; EAW59295.1; -; Genomic_DNA.
DR EMBL; CH471164; EAW59297.1; -; Genomic_DNA.
DR EMBL; BC001048; AAH01048.1; ALT_INIT; mRNA.
DR EMBL; BC015607; AAH15607.1; ALT_INIT; mRNA.
DR CCDS; CCDS14276.1; -. [Q00536-1]
DR CCDS; CCDS48101.1; -. [Q00536-3]
DR CCDS; CCDS55408.1; -. [Q00536-2]
DR PIR; S23385; S23385.
DR RefSeq; NP_001163931.1; NM_001170460.1. [Q00536-2]
DR RefSeq; NP_006192.1; NM_006201.4. [Q00536-1]
DR RefSeq; NP_148978.2; NM_033018.3. [Q00536-3]
DR RefSeq; XP_016885059.1; XM_017029570.1. [Q00536-1]
DR RefSeq; XP_016885060.1; XM_017029571.1. [Q00536-1]
DR RefSeq; XP_016885061.1; XM_017029572.1. [Q00536-1]
DR RefSeq; XP_016885062.1; XM_017029573.1. [Q00536-1]
DR PDB; 3MTL; X-ray; 2.40 A; A=163-478.
DR PDB; 5G6V; X-ray; 2.20 A; A/B=163-478.
DR PDBsum; 3MTL; -.
DR PDBsum; 5G6V; -.
DR AlphaFoldDB; Q00536; -.
DR SMR; Q00536; -.
DR BioGRID; 111154; 122.
DR ComplexPortal; CPX-379; Cyclin Y-CDK16 complex.
DR IntAct; Q00536; 47.
DR MINT; Q00536; -.
DR STRING; 9606.ENSP00000276052; -.
DR BindingDB; Q00536; -.
DR ChEMBL; CHEMBL4597; -.
DR DrugBank; DB07766; (2Z,3E)-2,3'-biindole-2',3(1H,1'H)-dione 3-{O-[(3R)-3,4-dihydroxybutyl]oxime}.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q00536; -.
DR GlyGen; Q00536; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q00536; -.
DR PhosphoSitePlus; Q00536; -.
DR BioMuta; CDK16; -.
DR DMDM; 266425; -.
DR EPD; Q00536; -.
DR jPOST; Q00536; -.
DR MassIVE; Q00536; -.
DR MaxQB; Q00536; -.
DR PaxDb; Q00536; -.
DR PeptideAtlas; Q00536; -.
DR PRIDE; Q00536; -.
DR ProteomicsDB; 57854; -. [Q00536-1]
DR Antibodypedia; 374; 235 antibodies from 31 providers.
DR DNASU; 5127; -.
DR Ensembl; ENST00000276052.10; ENSP00000276052.6; ENSG00000102225.17. [Q00536-2]
DR Ensembl; ENST00000357227.9; ENSP00000349762.4; ENSG00000102225.17. [Q00536-1]
DR Ensembl; ENST00000457458.6; ENSP00000405798.2; ENSG00000102225.17. [Q00536-3]
DR Ensembl; ENST00000518022.5; ENSP00000429751.1; ENSG00000102225.17. [Q00536-1]
DR GeneID; 5127; -.
DR KEGG; hsa:5127; -.
DR MANE-Select; ENST00000357227.9; ENSP00000349762.4; NM_006201.5; NP_006192.1.
DR UCSC; uc004dho.4; human. [Q00536-1]
DR CTD; 5127; -.
DR DisGeNET; 5127; -.
DR GeneCards; CDK16; -.
DR HGNC; HGNC:8749; CDK16.
DR HPA; ENSG00000102225; Tissue enhanced (skeletal).
DR MIM; 311550; gene.
DR neXtProt; NX_Q00536; -.
DR OpenTargets; ENSG00000102225; -.
DR PharmGKB; PA33095; -.
DR VEuPathDB; HostDB:ENSG00000102225; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000156963; -.
DR InParanoid; Q00536; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q00536; -.
DR TreeFam; TF106508; -.
DR BRENDA; 2.7.11.22; 2681.
DR PathwayCommons; Q00536; -.
DR SignaLink; Q00536; -.
DR SIGNOR; Q00536; -.
DR BioGRID-ORCS; 5127; 12 hits in 742 CRISPR screens.
DR ChiTaRS; CDK16; human.
DR GeneWiki; PCTK1; -.
DR GenomeRNAi; 5127; -.
DR Pharos; Q00536; Tchem.
DR PRO; PR:Q00536; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q00536; protein.
DR Bgee; ENSG00000102225; Expressed in right hemisphere of cerebellum and 193 other tissues.
DR ExpressionAtlas; Q00536; baseline and differential.
DR Genevisible; Q00536; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0030252; P:growth hormone secretion; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Differentiation; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Spermatogenesis; Synapse; Synaptosome; Transferase.
FT CHAIN 1..496
FT /note="Cyclin-dependent kinase 16"
FT /id="PRO_0000086484"
FT DOMAIN 165..446
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 171..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 12
FT /note="Phosphoserine; by BRSK2"
FT /evidence="ECO:0000269|PubMed:22798068,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 95
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63686"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MPLYGRARDHVTHPSILGTRPGRPMAGPITAAVPEKICNGAFCSCSG
FT AFPLDPNNPSLGPLPSISHLNLRTQIAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046134"
FT VAR_SEQ 1
FT /note="M -> MQSEIAM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046342"
FT MUTAGEN 12
FT /note="S->A: Abolishes phosphorylation by BRSK2. Abolishes
FT effect on insulin secretion."
FT /evidence="ECO:0000269|PubMed:22798068"
FT MUTAGEN 119
FT /note="S->A: Strongly reduces interaction with CCNY."
FT /evidence="ECO:0000269|PubMed:22184064"
FT MUTAGEN 153
FT /note="S->A: Constitutively activated, due to loss of an
FT inhibitory phosphorylation site. Increases interaction with
FT CCNY."
FT /evidence="ECO:0000269|PubMed:22184064,
FT ECO:0000269|PubMed:22798068"
FT MUTAGEN 153
FT /note="S->D: Abolishes interaction with CCNY."
FT /evidence="ECO:0000269|PubMed:22184064,
FT ECO:0000269|PubMed:22798068"
FT MUTAGEN 194
FT /note="K->A: Loss of kinase activity. Abolishes effect on
FT insulin secretion."
FT /evidence="ECO:0000269|PubMed:22184064,
FT ECO:0000269|PubMed:22798068"
FT MUTAGEN 194
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:22184064,
FT ECO:0000269|PubMed:22798068"
FT CONFLICT 25
FT /note="N -> D (in Ref. 3; BAH13564)"
FT /evidence="ECO:0000305"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:5G6V"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:5G6V"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 260..279
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3MTL"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5G6V"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:3MTL"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:5G6V"
FT TURN 330..335
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 342..357
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:5G6V"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 417..426
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 444..449
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:5G6V"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:5G6V"
SQ SEQUENCE 496 AA; 55716 MW; 9A5DDD34A5E5CBBB CRC64;
MDRMKKIKRQ LSMTLRGGRG IDKTNGAPEQ IGLDESGGGG GSDPGEAPTR AAPGELRSAR
GPLSSAPEIV HEDLKMGSDG ESDQASATSS DEVQSPVRVR MRNHPPRKIS TEDINKRLSL
PADIRLPEGY LEKLTLNSPI FDKPLSRRLR RVSLSEIGFG KLETYIKLDK LGEGTYATVY
KGKSKLTDNL VALKEIRLEH EEGAPCTAIR EVSLLKDLKH ANIVTLHDII HTEKSLTLVF
EYLDKDLKQY LDDCGNIINM HNVKLFLFQL LRGLAYCHRQ KVLHRDLKPQ NLLINERGEL
KLADFGLARA KSIPTKTYSN EVVTLWYRPP DILLGSTDYS TQIDMWGVGC IFYEMATGRP
LFPGSTVEEQ LHFIFRILGT PTEETWPGIL SNEEFKTYNY PKYRAEALLS HAPRLDSDGA
DLLTKLLQFE GRNRISAEDA MKHPFFLSLG ERIHKLPDTT SIFALKEIQL QKEASLRSSS
MPDSGRPAFR VVDTEF
