CPLM-004507

Genbank Nucleotide ID

Protein Synonyms/Alias

Leukemia-associated phosphoprotein p18; Metablastin; Oncoprotein 18; Op18; Phosphoprotein p19; pp19; Prosolin; Protein Pr22; pp17

C1orf215; LAP18; OP18

Homo sapiens (Human)

Position	Peptide	Type	References
9	ASSDIQVKELEKRAS	acetylation	[1]
9	ASSDIQVKELEKRAS	ubiquitination	[2, 3]
29	LILSPRSKESVPEFP	acetylation	[4]
29	LILSPRSKESVPEFP	ubiquitination	[5]
52	LSLEEIQKKLEAAEE	ubiquitination	[3, 5, 6]
70	SHEAEVLKQLAEKRE	ubiquitination	[2, 3]
80	AEKREHEKEVLQKAI	acetylation	[1]
80	AEKREHEKEVLQKAI	ubiquitination	[2, 3]
85	HEKEVLQKAIEENNN	ubiquitination	[5, 7, 8]
95	EENNNFSKMAEEKLT	acetylation	[1]
95	EENNNFSKMAEEKLT	ubiquitination	[3, 5, 6, 7]
100	FSKMAEEKLTHKMEA	acetylation	[1, 9, 10]
100	FSKMAEEKLTHKMEA	ubiquitination	[8, 10]
119	REAQMAAKLERLREK	acetylation	[1, 9, 10, 11]
119	REAQMAAKLERLREK	ubiquitination	[5, 7, 8, 10, 12]
128	ERLREKDKHIEEVRK	acetylation	[1, 9, 10]
137	IEEVRKNKESKDPAD	acetylation	[10]
137	IEEVRKNKESKDPAD	ubiquitination	[10]
140	VRKNKESKDPADETE	acetylation	[10]
140	VRKNKESKDPADETE	ubiquitination	[5, 10]

[1] 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]
[2] 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]
[3] 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]
[4] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[5] 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]
[6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[7] 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]
[8] 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]
[9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[10] 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]
[11] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[12] 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]

Functional Description

Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser- 16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity).

DOMAIN 4 145 SLD.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 9 9 N6-acetyllysine.
MOD_RES 16 16 Phosphoserine.
MOD_RES 25 25 Phosphoserine; by CDK1, MAPK1 and MAPK3.
MOD_RES 31 31 Phosphoserine.
MOD_RES 38 38 Phosphoserine; by CDK1, MAPK1 and MAPK3.
MOD_RES 46 46 Phosphoserine (By similarity).
MOD_RES 63 63 Phosphoserine; by PKA.
MOD_RES 95 95 N6-acetyllysine.
MOD_RES 100 100 N6-acetyllysine.
MOD_RES 119 119 N6-acetyllysine.

Acetylation; Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Direct protein sequencing; Microtubule; Neurogenesis; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IEA:Compara.
GO:0005622; C:intracellular; IDA:LIFEdb.
GO:0016020; C:membrane; IEA:Compara.
GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO:0015631; F:tubulin binding; IDA:MGI.
GO:0007409; P:axonogenesis; IEA:Compara.
GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO:0007019; P:microtubule depolymerization; IDA:MGI.
GO:0007052; P:mitotic spindle organization; IDA:MGI.
GO:0031115; P:negative regulation of microtubule polymerization; IEA:Compara.
GO:0051272; P:positive regulation of cellular component movement; IEA:Compara.
GO:0009615; P:response to virus; IEP:UniProtKB.

IPR000956; Stathmin_fam.

PS00563; STATHMIN_1
PS01041; STATHMIN_2
PS51663; STATHMIN_3