CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037880
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Splicing factor 3B subunit 2 
Protein Synonyms/Alias
  
Gene Name
 SF3B2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
335ESSGDREKDSTRSRGubiquitination[1]
370EPNFIFFKRIFEAFKubiquitination[2, 3]
377KRIFEAFKLTDDVKKubiquitination[1, 4]
383FKLTDDVKKEKEKEPubiquitination[1]
395KEPEKLDKLENSAAPacetylation[5]
449RFTVAELKQLVARPDubiquitination[1, 3, 4, 6]
469DVTAQDPKLLVHLKAubiquitination[4, 6]
475PKLLVHLKATRNSVPubiquitination[3, 4, 6]
490VPRHWCFKRKYLQGKmethylation[7]
502QGKRGIEKPPFELPDubiquitination[1, 3, 4]
512FELPDFIKRTGIQEMubiquitination[1, 3, 4, 6, 8, 9]
526MREALQEKEEQKTMKacetylation[9]
526MREALQEKEEQKTMKubiquitination[1, 3, 4, 9]
546KVRPKMGKIDIDYQKubiquitination[1, 3, 4, 9]
553KIDIDYQKLHDAFFKubiquitination[1, 4, 6, 9]
560KLHDAFFKWQTKPKLacetylation[5]
560KLHDAFFKWQTKPKLubiquitination[3, 6]
587FETRLKEKKPGDLSDubiquitination[9]
588ETRLKEKKPGDLSDEubiquitination[4, 9]
610PVGPNAHKVPPPWLIubiquitination[4]
773LFTVLPEKRTATVGGubiquitination[1]
Reference
 [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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] 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]
 [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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 878 AA 
Protein Sequence
MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL VERLQSYTRQ 60
TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP PLQPPPPPPP PPPGLGLGFP 120
MAHPPNLGPP PPLRVGEPVA LSEEERLKLA QQQAALLMQQ EERAKQAAVL LEQERQQEIA 180
KMGTPVPRPP QDMGQIGVRT PLGPRVAAPV GPVGPTPTVL PMGAPVPRPR GPPPPPGDEN 240
REMDDPSVGP KIPQALEKIL QLKESRQEEM NSQQEEEEME TDARSSLGQS ASETEEDTVS 300
VSKKEKNRKR RNRKKKKKPQ RVRGVSSESS GDREKDSTRS RGSDSPAADV EIEYVTEEPE 360
IYEPNFIFFK RIFEAFKLTD DVKKEKEKEP EKLDKLENSA APKKKGFEEE HKDSDDDSSD 420
DEQEKKPEAP KLSKKKLRRM NRFTVAELKQ LVARPDVVEM HDVTAQDPKL LVHLKATRNS 480
VPVPRHWCFK RKYLQGKRGI EKPPFELPDF IKRTGIQEMR EALQEKEEQK TMKSKMREKV 540
RPKMGKIDID YQKLHDAFFK WQTKPKLTIH GDLYYEGKEF ETRLKEKKPG DLSDELRISL 600
GMPVGPNAHK VPPPWLIAMQ RYGPPPSYPN LKIPGLNSPI PESCSFGYHA GGWGKPPVDE 660
TGKPLYGDVF GTNAAEFQTK TEEEEIDRTP WGELEPSDEE SSEEEEEEES DEDKPDETGF 720
ITPADSGLIT PGGFSSVPAG METPELIELR KKKIEEAMDG SETPQLFTVL PEKRTATVGG 780
AMMGSTHIYD MSTVMSRKGP APELQGVEVA LAPEELELDP MAMTQKYEEH VREQQAQVEK 840
EDFSDMVAEH AAKQKQKKRK AQPQDSRGGS KKYKEFKF 878 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003676; F:nucleic acid binding; IEA:InterPro. 
Interpro
 IPR007180; DUF382.
 IPR006568; PSP.
 IPR003034; SAP_dom. 
Pfam
 PF04037; DUF382
 PF04046; PSP
 PF02037; SAP 
SMART
 SM00581; PSP
 SM00513; SAP 
PROSITE
 PS50800; SAP 
PRINTS