CPLM-004921

Genbank Nucleotide ID

Cyclin-dependent kinase 11B

Protein Synonyms/Alias

Cell division cycle 2-like protein kinase 1; CLK-1; Cell division protein kinase 11B; Galactosyltransferase-associated protein kinase p58/GTA; PITSLRE serine/threonine-protein kinase CDC2L1; p58 CLK-1

CDC2L1; CDK11; PITSLREA; PK58

Homo sapiens (Human)

Position	Peptide	Type	References
20	LDEILQEKKRRKEQE	ubiquitination	[1, 2]
21	DEILQEKKRRKEQEE	ubiquitination	[2]
225	MREDYSDKVKASHWS	acetylation	[3]
459	VYRAKDKKTDEIVAL	ubiquitination	[2]
467	TDEIVALKRLKMEKE	ubiquitination	[1, 2, 4, 5]
475	RLKMEKEKEGFPITS	ubiquitination	[2]
491	REINTILKAQHPNIV	ubiquitination	[2]
564	WILHRDLKTSNLLLS	ubiquitination	[1, 2]
577	LSHAGILKVGDFGLA	ubiquitination	[2]
649	SEIDQINKVFKDLGT	ubiquitination	[2]
652	DQINKVFKDLGTPSE	ubiquitination	[2]
660	DLGTPSEKIWPGYSE	ubiquitination	[1, 2, 6, 7]
672	YSELPAVKKMTFSEH	ubiquitination	[1]
673	SELPAVKKMTFSEHP	ubiquitination	[2]
719	ISAEDGLKHEYFRET	ubiquitination	[1, 2, 4]
741	MFPTWPAKSEQQRVK	ubiquitination	[1, 2, 4]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression.

DOMAIN 438 723 Protein kinase.
NP_BIND 444 452 ATP (By similarity).
ACT_SITE 562 562 Proton acceptor (By similarity).
BINDING 467 467 ATP (By similarity).
MOD_RES 47 47 Phosphoserine (By similarity).
MOD_RES 115 115 Phosphoserine.
MOD_RES 277 277 Phosphoserine (By similarity).
MOD_RES 283 283 Phosphoserine (By similarity).
MOD_RES 482 482 Phosphoserine; by CDK7.
MOD_RES 488 488 Phosphothreonine; by CDK7.
MOD_RES 589 589 Phosphoserine.
MOD_RES 594 594 Phosphotyrosine.
MOD_RES 595 595 Phosphothreonine.
MOD_RES 751 751 Phosphothreonine (By similarity).
MOD_RES 752 752 Phosphoserine (By similarity).

Alternative initiation; Alternative splicing; Apoptosis; ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0005524; F:ATP binding; IDA:UniProtKB.
GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:EC.
GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO:0008283; P:cell proliferation; TAS:ProtInc.
GO:0007067; P:mitosis; NAS:UniProtKB.
GO:0001558; P:regulation of cell growth; IEP:UniProtKB.
GO:0050684; P:regulation of mRNA processing; IDA:UniProtKB.
GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB.

IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.

PS00107; PROTEIN_KINASE_ATP
PS50011; PROTEIN_KINASE_DOM
PS00108; PROTEIN_KINASE_ST