CPLM-022935

Genbank Nucleotide ID

Protein Synonyms/Alias

MLL septin-like fusion protein MSF-A; MLL septin-like fusion protein; Ovarian/Breast septin; Ov/Br septin; Septin D1

Homo sapiens (Human)

Position	Peptide	Type	References
62	TVASSTQKFQDLGVK	ubiquitination	[1]
186	PATDAAPKRVEIQMP	ubiquitination	[2]
262	TPRDAGLKQAPASRN	ubiquitination	[1]
271	APASRNEKAPVDFGY	ubiquitination	[1]
320	TLINTLFKSKISRKS	ubiquitination	[1]
322	INTLFKSKISRKSVQ	ubiquitination	[1]
326	FKSKISRKSVQPTSE	ubiquitination	[1]
338	TSEERIPKTIEIKSI	ubiquitination	[1]
343	IPKTIEIKSITHDIE	ubiquitination	[1]
352	ITHDIEEKGVRMKLT	acetylation	[3]
352	ITHDIEEKGVRMKLT	ubiquitination	[1]
357	EEKGVRMKLTVIDTP	ubiquitination	[1]
389	FINDQYEKYLQEEVN	ubiquitination	[1]
431	PLDIEFMKRLSKVVN	ubiquitination	[1]
435	EFMKRLSKVVNIVPV	ubiquitination	[1, 2, 4]
445	NIVPVIAKADTLTLE	ubiquitination	[1]
476	GIDVYPQKEFDEDSE	ubiquitination	[1, 2, 5, 6, 7, 8, 9]
490	EDRLVNEKFREMIPF	ubiquitination	[1, 2, 4, 5, 6, 8, 9, 10]
511	HEYQVNGKRILGRKT	ubiquitination	[1, 7, 9]
517	GKRILGRKTKWGTIE	ubiquitination	[1]
519	RILGRKTKWGTIEVE	ubiquitination	[1, 9]
549	RTHMQNIKDITSSIH	ubiquitination	[1, 9]

[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] 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]
[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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[5] 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]
[6] 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]
[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] 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]
[9] 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]
[10] 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

Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri.

NP_BIND 305 312 GTP (By similarity).
NP_BIND 445 453 GTP (By similarity).
BINDING 339 339 GTP (By similarity).
BINDING 365 365 GTP; via amide nitrogen (By similarity).
BINDING 501 501 GTP; via amide nitrogen and carbonyl
BINDING 516 516 GTP (By similarity).
MOD_RES 30 30 Phosphoserine.
MOD_RES 38 38 Phosphothreonine.
MOD_RES 42 42 Phosphothreonine.
MOD_RES 82 82 Phosphoserine.
MOD_RES 85 85 Phosphoserine.
MOD_RES 96 96 Phosphoserine.
MOD_RES 142 142 Phosphothreonine.
MOD_RES 160 160 Phosphoserine (By similarity).
MOD_RES 278 278 Phosphotyrosine.
MOD_RES 327 327 Phosphoserine.

Alternative splicing; Cell cycle; Cell division; Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; GTP-binding; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005874; C:microtubule; IDA:UniProtKB.
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO:0001725; C:stress fiber; IDA:UniProtKB.
GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO:0003924; F:GTPase activity; TAS:ProtInc.
GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.

IPR000038; Cell_div_GTP-bd.
IPR027417; P-loop_NTPase.