CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012259
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Scaffold attachment factor B2 
Protein Synonyms/Alias
 SAF-B2 
Gene Name
 SAFB2 
Gene Synonyms/Alias
 KIAA0138 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
225DILGETCKSEPVKEEsumoylation[1]
230TCKSEPVKEESSELEsumoylation[1]
230TCKSEPVKEESSELEubiquitination[2]
293DSLLAVVKREPAEQPacetylation[3]
293DSLLAVVKREPAEQPsumoylation[1, 4]
293DSLLAVVKREPAEQPubiquitination[5]
355DSKEDGRKFDFDACNubiquitination[6]
391FKEEKDIKPIIKDEKsumoylation[1]
424TTRATDLKNLFSKYGacetylation[3]
424TTRATDLKNLFSKYGubiquitination[5, 6]
429DLKNLFSKYGKVVGAacetylation[3]
429DLKNLFSKYGKVVGAubiquitination[5]
437YGKVVGAKVVTNARSubiquitination[6]
517RHHSVEIKIEKTVIKsumoylation[1, 4]
524KIEKTVIKKEEKIEKsumoylation[4, 7]
586GEPVISVKTTSRSKEubiquitination[8]
616RDILSFDKIKEQRERacetylation[3, 9, 10]
616RDILSFDKIKEQRERubiquitination[5, 11]
Reference
 [1] 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]
 [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] 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] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [5] 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]
 [6] 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]
 [7] A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells.
 Galisson F, Mahrouche L, Courcelles M, Bonneil E, Meloche S, Chelbi-Alix MK, Thibault P.
 Mol Cell Proteomics. 2011 Feb;10(2):M110.004796. [PMID: 21098080]
 [8] 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]
 [9] 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]
 [10] 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]
 [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
Functional Description
 Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation. 
Sequence Annotation
 DOMAIN 30 64 SAP.
 DOMAIN 407 485 RRM.
 REGION 600 953 Interacts with SAFB1.
 MOTIF 713 730 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 109 109 Phosphoserine.
 MOD_RES 201 201 Phosphothreonine.
 MOD_RES 207 207 Phosphoserine.
 MOD_RES 234 234 Phosphoserine (By similarity).
 MOD_RES 331 331 Phosphoserine (By similarity).
 MOD_RES 343 343 Phosphoserine (By similarity).
 MOD_RES 513 513 Phosphoserine.
 MOD_RES 616 616 N6-acetyllysine.
 CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor; RNA-binding; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 953 AA 
Protein Sequence
MAETLPGSGD SGPGTASLGP GVAETGTRRL SELRVIDLRA ELKKRNLDTG GNKSVLMERL 60
KKAVKEEGQD PDEIGIELEA TSKKSAKRCV KGLKMEEEGT EDNGLEDDSR DGQEDMEASL 120
ENLQNMGMMD MSVLDETEVA NSSAPDFGED GTDGLLDSFC DSKEYVAAQL RQLPAQPPEH 180
AVDGEGFKNT LETSSLNFKV TPDIEESLLE PENEKILDIL GETCKSEPVK EESSELEQPF 240
AQDTSSVGPD RKLAEEEDLF DSAHPEEGDL DLASESTAHA QSSKADSLLA VVKREPAEQP 300
GDGERTDCEP VGLEPAVEQS SAASELAEAS SEELAEAPTE APSPEARDSK EDGRKFDFDA 360
CNEVPPAPKE SSTSEGADQK MSSFKEEKDI KPIIKDEKGR VGSGSGRNLW VSGLSSTTRA 420
TDLKNLFSKY GKVVGAKVVT NARSPGARCY GFVTMSTSDE ATKCISHLHR TELHGRMISV 480
EKAKNEPAGK KLSDRKECEV KKEKLSSVDR HHSVEIKIEK TVIKKEEKIE KKEEKKPEDI 540
KKEEKDQDEL KPGPTNRSRV TKSGSRGMER TVVMDKSKGE PVISVKTTSR SKERSSKSQD 600
RKSESKEKRD ILSFDKIKEQ RERERQRQRE REIRETERRR EREQREREQR LEAFHERKEK 660
ARLQRERLQL ECQRQRLERE RMERERLERE RMRVERERRK EQERIHRERE ELRRQQEQLR 720
YEQERRPGRR PYDLDRRDDA YWPEGKRVAM EDRYRADFPR PDHRFHDFDH RDRGQYQDHA 780
IDRREGSRPM MGDHRDGQHY GDDRHGHGGP PERHGRDSRD GWGGYGSDKR LSEGRGLPPP 840
PRGGRDWGEH NQRLEEHQAR AWQGAMDAGA ASREHARWQG GERGLSGPSG PGHMASRGGV 900
AGRGGFAQGG HSQGHVVPGG GLEGGGVASQ DRGSRVPHPH PHPPPYPHFT RRY 953 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR003034; SAP_dom. 
Pfam
 PF00076; RRM_1
 PF02037; SAP 
SMART
 SM00360; RRM
 SM00513; SAP 
PROSITE
 PS50102; RRM
 PS50800; SAP 
PRINTS