CPLM-016235

Genbank Nucleotide ID

Serine/threonine-protein kinase pim-3

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
5	***MLLSKFGSLAHL	ubiquitination	[1, 2]
24	GVDHLPVKILQPAKA	ubiquitination	[1, 2]
30	VKILQPAKADKESFE	ubiquitination	[1, 3]
38	ADKESFEKAYQVGAV	ubiquitination	[1, 2, 3, 4]
69	DGLPVAVKHVVKERV	ubiquitination	[1, 3]
73	VAVKHVVKERVTEWG	ubiquitination	[1, 3]
96	LEVVLLRKVGAAGGA	ubiquitination	[5]
172	GVVHRDIKDENLLVD	ubiquitination	[1, 2, 3, 4, 6]
186	DLRSGELKLIDFGSG	ubiquitination	[3, 4, 6]
197	FGSGALLKDTVYTDF	ubiquitination	[3, 4, 6]

[1] 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]
[2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[3] 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]
[4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[6] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]

Functional Description

Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth.

DOMAIN 40 293 Protein kinase.
NP_BIND 46 54 ATP (By similarity).
ACT_SITE 170 170 Proton acceptor (By similarity).
BINDING 69 69 ATP (By similarity).

Apoptosis; ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Proto-oncogene; Reference proteome; Serine/threonine-protein kinase; Transferase; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO:0016572; P:histone phosphorylation; IEA:Compara.
GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
GO:0046777; P:protein autophosphorylation; IEA:Compara.
GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.

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.

PS00107; PROTEIN_KINASE_ATP
PS50011; PROTEIN_KINASE_DOM
PS00108; PROTEIN_KINASE_ST