CPLM-012552

Genbank Nucleotide ID

Splicing factor 3B subunit 3

Protein Synonyms/Alias

Pre-mRNA-splicing factor SF3b 130 kDa subunit; SF3b130; STAF130; Spliceosome-associated protein 130; SAP 130

Homo sapiens (Human)

Position	Peptide	Type	References
75	FRLTGGTKDYIVVGS	ubiquitination	[1]
96	ILEYQPSKNMFEKIH	ubiquitination	[1, 2, 3, 4]
109	IHQETFGKSGCRRIV	acetylation	[5]
109	IHQETFGKSGCRRIV	ubiquitination	[3]
126	QFLAVDPKGRAVMIS	acetylation	[5]
126	QFLAVDPKGRAVMIS	ubiquitination	[3, 6]
137	VMISAIEKQKLVYIL	acetylation	[7]
137	VMISAIEKQKLVYIL	ubiquitination	[3, 6]
139	ISAIEKQKLVYILNR	ubiquitination	[2, 3, 4, 6, 8]
296	CSATHKTKSMFFFLA	ubiquitination	[1]
328	MVTEIRLKYFDTVPV	ubiquitination	[3, 9]
546	PGKKTIVKCAVNQRQ	ubiquitination	[3, 6, 9]
700	YLGSRPVKLFRVRMQ	ubiquitination	[2, 3, 4]
787	PLQYTPRKFVIHPES	ubiquitination	[3]
812	NAYTEATKAQRKQQM	ubiquitination	[1, 3, 9]
816	EATKAQRKQQMAEEM	ubiquitination	[3]
936	KLVNNGEKLEFLHKT	acetylation	[5]
936	KLVNNGEKLEFLHKT	ubiquitination	[1, 2, 3, 4]
942	EKLEFLHKTPVEEVP	ubiquitination	[1, 3, 6, 9, 10]
965	RVLIGVGKLLRVYDL	ubiquitination	[1, 2, 3, 4, 6, 8, 9, 10]
975	RVYDLGKKKLLRKCE	ubiquitination	[3]
980	GKKKLLRKCENKHIA	ubiquitination	[3]
984	LLRKCENKHIANYIS	ubiquitination	[3]
1049	DTVAGADKFGNICVV	ubiquitination	[3, 9, 11]
1074	DEDPTGNKALWDRGL	ubiquitination	[1, 2, 3, 4, 6, 9, 10, 12]
1088	LLNGASQKAEVIMNY	ubiquitination	[3, 9]
1171	RSYYFPVKNVIDGDL	ubiquitination	[3, 6, 9]
1189	FNSMEPNKQKNVSEE	ubiquitination	[3, 9]
1191	SMEPNKQKNVSEELD	ubiquitination	[1, 3]
1206	RTPPEVSKKLEDIRT	ubiquitination	[1, 3, 10]
1207	TPPEVSKKLEDIRTR	ubiquitination	[3]

[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] 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] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[9] 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]
[10] 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]
[11] 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]
[12] A data set of human endogenous protein ubiquitination sites.
Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]

Functional Description

Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron.

Alternative splicing; Complete proteome; mRNA processing; mRNA splicing; Nucleus; Polymorphism; Reference proteome; Spliceosome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc.
GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
GO:0006461; P:protein complex assembly; TAS:ProtInc.

IPR004871; Cleavage/polyA-sp_fac_asu_C.