CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012098
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Splicing factor 3B subunit 2 
Protein Synonyms/Alias
 Pre-mRNA-splicing factor SF3b 145 kDa subunit; SF3b145; SF3b150; Spliceosome-associated protein 145; SAP 145 
Gene Name
 SF3B2 
Gene Synonyms/Alias
 SAP145 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
198ERQQEIAKMGTPVPRubiquitination[1]
275KIPQALEKILQLKESacetylation[2]
275KIPQALEKILQLKESubiquitination[1, 3, 4, 5]
280LEKILQLKESRQEEMubiquitination[1, 3, 4, 5, 6, 7, 8]
352ESSGDREKDSTRSRGubiquitination[6]
387EPNFIFFKRIFEAFKubiquitination[8]
394KRIFEAFKLTDDVKKubiquitination[1, 4, 6]
400FKLTDDVKKEKEKEPubiquitination[6]
412KEPEKLDKLENSAAPubiquitination[4]
466RFTVAELKQLVARPDubiquitination[1, 3, 5, 6, 8]
486DVTAQDPKLLVHLKAubiquitination[1, 3, 5]
492PKLLVHLKATRNSVPubiquitination[1, 3, 4, 5, 8]
519QGKRGIEKPPFELPDubiquitination[1, 6, 8]
529FELPDFIKRTGIQEMubiquitination[1, 3, 4, 5, 6, 7, 8]
543MREALQEKEEQKTMKubiquitination[1, 6, 8]
563KVRPKMGKIDIDYQKubiquitination[1, 6, 8]
570KIDIDYQKLHDAFFKubiquitination[1, 3, 4, 5, 6]
577KLHDAFFKWQTKPKLubiquitination[3, 4, 5, 8]
605ETRLKEKKPGDLSDEubiquitination[1]
627PVGPNAHKVPPPWLIubiquitination[1, 4]
790LFTVLPEKRTATVGGubiquitination[6]
815MSTVMSRKGPAPELQubiquitination[6]
Reference
 [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] 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]
 [3] 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]
 [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] 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]
 [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] 
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. 
Sequence Annotation
 DOMAIN 24 58 SAP.
 MOD_RES 275 275 N6-acetyllysine.
 MOD_RES 289 289 Phosphoserine.
 MOD_RES 307 307 Phosphoserine.
 MOD_RES 309 309 Phosphoserine.
 MOD_RES 311 311 Phosphothreonine.
 MOD_RES 360 360 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.
 MOD_RES 431 431 Phosphoserine.
 MOD_RES 435 435 Phosphoserine.
 MOD_RES 436 436 Phosphoserine.
 MOD_RES 780 780 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Coiled coil; Complete proteome; Direct protein sequencing; Host-virus interaction; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 895 AA 
Protein Sequence
MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL VERLQSYTRQ 60
TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP PLQPPPPPPP PPPGLGLGFP 120
MAHPPNLGPP PPLRVGEPVA LSEEERLKLA QQQAALLMQQ EERAKQQGDH SLKEHELLEQ 180
QKRAAVLLEQ ERQQEIAKMG TPVPRPPQDM GQIGVRTPLG PRVAAPVGPV GPTPTVLPMG 240
APVPRPRGPP PPPGDENREM DDPSVGPKIP QALEKILQLK ESRQEEMNSQ QEEEEMETDA 300
RSSLGQSASE TEEDTVSVSK KEKNRKRRNR KKKKKPQRVR GVSSESSGDR EKDSTRSRGS 360
DSPAADVEIE YVTEEPEIYE PNFIFFKRIF EAFKLTDDVK KEKEKEPEKL DKLENSAAPK 420
KKGFEEEHKD SDDDSSDDEQ EKKPEAPKLS KKKLRRMNRF TVAELKQLVA RPDVVEMHDV 480
TAQDPKLLVH LKATRNSVPV PRHWCFKRKY LQGKRGIEKP PFELPDFIKR TGIQEMREAL 540
QEKEEQKTMK SKMREKVRPK MGKIDIDYQK LHDAFFKWQT KPKLTIHGDL YYEGKEFETR 600
LKEKKPGDLS DELRISLGMP VGPNAHKVPP PWLIAMQRYG PPPSYPNLKI PGLNSPIPES 660
CSFGYHAGGW GKPPVDETGK PLYGDVFGTN AAEFQTKTEE EEIDRTPWGE LEPSDEESSE 720
EEEEEESDED KPDETGFITP ADSGLITPGG FSSVPAGMET PELIELRKKK IEEAMDGSET 780
PQLFTVLPEK RTATVGGAMM GSTHIYDMST VMSRKGPAPE LQGVEVALAP EELELDPMAM 840
TQKYEEHVRE QQAQVEKEDF SDMVAEHAAK QKQKKRKAQP QDSRGGSKKY KEFKF 895 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 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:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR007180; DUF382.
 IPR006568; PSP.
 IPR003034; SAP_dom. 
Pfam
 PF04037; DUF382
 PF04046; PSP
 PF02037; SAP 
SMART
 SM00581; PSP
 SM00513; SAP 
PROSITE
 PS50800; SAP 
PRINTS