CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001218
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Splicing factor 3B subunit 1 
Protein Synonyms/Alias
 Pre-mRNA-splicing factor SF3b 155 kDa subunit; SF3b155; Spliceosome-associated protein 155; SAP 155 
Gene Name
 SF3B1 
Gene Synonyms/Alias
 SAP155 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MAKIAKTHEDIEAubiquitination[1]
81TSLLGQKKPGYHAPVubiquitination[2]
141DPFADGGKTPDPKMNacetylation[3, 4]
182KAKAGELKVVNGAAAubiquitination[5]
195AASQPPSKRKRRWDQubiquitination[1, 6]
214TPGATPKKLSSWDQAubiquitination[1]
290GATSSARKNRWDETPmethylation[7]
333TPTPGASKRKSRWDEubiquitination[1, 8]
413AMFPEGYKVLPPPAGsumoylation[9]
454QTEDRTMKSVNDQPSubiquitination[8]
468SGNLPFLKPDDIQYFubiquitination[6, 8]
493TLSPEEQKERKIMKLubiquitination[8]
499QKERKIMKLLLKIKNubiquitination[10, 11]
554QERHLLVKVIDRILYacetylation[3]
554QERHLLVKVIDRILYubiquitination[1, 2, 8, 12]
562VIDRILYKLDDLVRPacetylation[3]
700GLVDEQQKVRTISALubiquitination[4, 8]
785QSPDEEMKKIVLKVVubiquitination[8]
790EMKKIVLKVVKQCCGubiquitination[1, 4, 8]
793KIVLKVVKQCCGTDGubiquitination[1, 2, 4, 8, 12, 13, 14]
816EILPPFFKHFWQHRMubiquitination[1, 10, 11]
926NALGKRVKPYLPQICubiquitination[1]
963SRTAVVMKTCQEEKLubiquitination[1, 4]
1008VNVIGMHKMTPPIKDubiquitination[8]
1014HKMTPPIKDLLPRLTubiquitination[1, 8, 10, 11]
1025PRLTPILKNRHEKVQubiquitination[1, 8]
1030ILKNRHEKVQENCIDubiquitination[1]
1067FELLELLKAHKKAIRacetylation[3]
1102ATLLNNLKVQERQNRubiquitination[1, 6, 8, 10, 11]
1292PRIYNDDKNTYIRYEubiquitination[1, 4, 6, 8, 14]
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] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [8] 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]
 [9] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [14] 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] 
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
 REPEAT 529 568 HEAT 1.
 REPEAT 569 603 HEAT 2.
 REPEAT 604 641 HEAT 3.
 REPEAT 643 677 HEAT 4.
 REPEAT 680 718 HEAT 5.
 REPEAT 763 801 HEAT 6.
 REPEAT 843 881 HEAT 7.
 REPEAT 1010 1048 HEAT 8.
 REPEAT 1052 1090 HEAT 9.
 REPEAT 1122 1160 HEAT 10.
 REPEAT 1163 1201 HEAT 11.
 REGION 223 491 Interaction with PPP1R8.
 REGION 529 568 Interaction with SF3B14.
 MOD_RES 129 129 Phosphoserine.
 MOD_RES 141 141 N6-acetyllysine.
 MOD_RES 142 142 Phosphothreonine.
 MOD_RES 194 194 Phosphoserine.
 MOD_RES 203 203 Phosphothreonine.
 MOD_RES 207 207 Phosphothreonine.
 MOD_RES 211 211 Phosphothreonine.
 MOD_RES 223 223 Phosphothreonine.
 MOD_RES 227 227 Phosphothreonine.
 MOD_RES 244 244 Phosphothreonine.
 MOD_RES 248 248 Phosphothreonine (Probable).
 MOD_RES 267 267 Phosphothreonine.
 MOD_RES 278 278 Phosphothreonine (By similarity).
 MOD_RES 296 296 Phosphothreonine.
 MOD_RES 299 299 Phosphothreonine.
 MOD_RES 313 313 Phosphothreonine (Probable).
 MOD_RES 326 326 Phosphothreonine.
 MOD_RES 328 328 Phosphothreonine.
 MOD_RES 332 332 Phosphoserine.
 MOD_RES 341 341 Phosphothreonine.
 MOD_RES 344 344 Phosphoserine.
 MOD_RES 349 349 Phosphoserine.
 MOD_RES 350 350 Phosphothreonine.
 MOD_RES 354 354 Phosphothreonine.
 MOD_RES 400 400 Phosphoserine.
 MOD_RES 434 434 Phosphothreonine.
 MOD_RES 436 436 Phosphothreonine.
 MOD_RES 488 488 Phosphoserine.
 MOD_RES 554 554 N6-acetyllysine.
 MOD_RES 562 562 N6-acetyllysine.
 MOD_RES 1067 1067 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1304 AA 
Protein Sequence
MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR FAGYVTSIAA 60
TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ YDPFAEHRPP KIADREDEYK 120
KHRRTMIISP ERLDPFADGG KTPDPKMNAR TYMDVMREQH LTKEEREIRQ QLAEKAKAGE 180
LKVVNGAAAS QPPSKRKRRW DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK 240
GSETPGATPG SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE 300
RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST PVLTPGKTPI 360
GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS DEELDAMFPE GYKVLPPPAG 420
YVPIRTPARK LTATPTPLGG MTGFHMQTED RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV 480
DVDESTLSPE EQKERKIMKL LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM 540
SPTLEDQERH LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL 600
AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA VCKSKKSWQA 660
RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK VRTISALAIA ALAEAATPYG 720
IESFDSVLKP LWKGIRQHRG KGLAAFLKAI GYLIPLMDAE YANYYTREVM LILIREFQSP 780
DEEMKKIVLK VVKQCCGTDG VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL 840
ANKVGAAEII SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF 900
QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ AADLISRTAV 960
VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI VNVIGMHKMT PPIKDLLPRL 1020
TPILKNRHEK VQENCIDLVG RIADRGAEYV SAREWMRICF ELLELLKAHK KAIRRATVNT 1080
FGYIAKAIGP HDVLATLLNN LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE 1140
LNVQNGVLKS LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY 1200
GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC LQGLFHPARK 1260
VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYEL DYIL 1304 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0009952; P:anterior/posterior pattern specification; IEA:Compara.
 GO:0000398; P:mRNA splicing, via spliceosome; NAS:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR015016; SF3b_su1. 
Pfam
 PF08920; SF3b1 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS