CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031959
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Scaffold attachment factor B1 
Protein Synonyms/Alias
 cDNA FLJ54744, highly similar to Scaffold attachment factor B 
Gene Name
 SAFB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
69DILGETCKSEPVKEEmethylation[1]
74TCKSEPVKEESSELEubiquitination[2]
128TAHAQSSKADSLLAVubiquitination[3]
137DSLLAVVKREPAEQPacetylation[4, 5, 6]
137DSLLAVVKREPAEQPubiquitination[7]
266TTRATDLKNLFSKYGacetylation[6]
266TTRATDLKNLFSKYGubiquitination[6, 7, 8]
271DLKNLFSKYGKVVGAacetylation[4]
271DLKNLFSKYGKVVGAubiquitination[7, 8]
279YGKVVGAKVVTNARSacetylation[6]
279YGKVVGAKVVTNARSubiquitination[6, 8]
318HKTELHGKMISVEKAacetylation[6]
411ERTVVMDKSKGVPVIacetylation[6]
Reference
 [1] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077]
 [2] 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]
 [3] 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]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [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] 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] 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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 759 AA 
Protein Sequence
MKVVILTKLK LPPRETRKHQ RGLAKIEDKE TINNLDTSSS DFTILQEIEE PSLEPENEKI 60
LDILGETCKS EPVKEESSEL EQPFAQDTSS VGPDRKLAEE EDLFDSAHPE EGDLDLASES 120
TAHAQSSKAD SLLAVVKREP AEQPGDGERT DCEPVGLEPA VEQSSAASEL AEASSEELAE 180
APTEAPSPEA RDSKEDGRKF DFDACNEVPP APKESSTSEG ADQKMSSPED DSDTKRLSKE 240
EKGRSSCGRN FWVSGLSSTT RATDLKNLFS KYGKVVGAKV VTNARSPGAR CYGFVTMSTA 300
EEATKCINHL HKTELHGKMI SVEKAKNEPV GKKTSDKRDS DGKKEKSSNS DRSTNLKRDD 360
KCDRKDDAKK GDDGSGEKSK DQDDQKPGPS ERSRATKSGS RGTERTVVMD KSKGVPVISV 420
KTSGSKERAS KSQDRKSASR EKRSVVSFDK VKEPRKSRDS ESHRVRERSE REQRMQAQWE 480
REERERLEIA RERLAFQRQR LERERMERER LERERMHVEH ERRREQERIH REREELRRQQ 540
ELRYEQERRP AVRRPYDLDR RDDAYWPEAK RAALDERYHS DFNRQDRFHD FDHRDRGRYP 600
DHSVDRREGS RSMMGEREGQ HYPERHGGPE RHGRDSRDGW GGYGSDKRMS EGRGLPPPPR 660
GRRDWGDHGR REDDRSWQGT ADGGMMDRDH KRWQGGERSM SGHSGPGHMM NRGGMSGRGS 720
FAPGGASRGH PIPHGGMQGG FGGQSRGSRP SDARFTRRY 759 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:InterPro. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
  
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS