CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040692
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 SWI/SNF complex subunit SMARCC2 
Protein Synonyms/Alias
  
Gene Name
 SMARCC2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
157PKLLGKLKDIIKRHQubiquitination[1]
161GKLKDIIKRHQGTVTubiquitination[1]
275RRKKISAKTLTDEVNacetylation[2]
275RRKKISAKTLTDEVNubiquitination[3]
359VEEVTLPKTVNTKKDacetylation[2]
455EFFNGKNKSKTPEIYubiquitination[1]
457FNGKNKSKTPEIYLAubiquitination[1]
599FPDKGKEKPTDMQNFubiquitination[3]
725RVASAAAKSALEEFSubiquitination[1, 3, 4, 5]
733SALEEFSKMKEEVPTubiquitination[3]
735LEEFSKMKEEVPTALubiquitination[1, 5]
800EGQATDEKKEPKEPRacetylation[5]
903ALAAAAVKAKHLAAVubiquitination[3, 6, 7]
905AAAAVKAKHLAAVEEubiquitination[1, 3, 5, 6, 7, 8]
916AVEERKIKSLVALLVubiquitination[3]
928LLVETQMKKLEIKLRubiquitination[6, 7]
929LVETQMKKLEIKLRHubiquitination[1, 3, 5]
933QMKKLEIKLRHFEELubiquitination[1, 3]
971AFHMEQLKYAEMRARubiquitination[3, 4]
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] 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]
 [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] 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]
 [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] 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]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1245 AA 
Protein Sequence
MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ 60
EEVFGKHVSN APLTKLPIKC FLDFKAGGSL CHILAAAYKF KSDQGWRRYD FQNPSRMDRN 120
VEMFMTIEKS LVQNNCLSRP NIFLCPEIEP KLLGKLKDII KRHQGTVTED KNNASHVVYP 180
VPGNLEEEEW VRPVMKRDKQ VLLHWGYYPD SYDTWIPASE IEASVEDAPT PEKPRKVHAK 240
WILDTDTFNE WMNEEDYEVN DDKNPVSRRK KISAKTLTDE VNSPDSDRRD KKGGNYKKRK 300
RSPSPSPTPE AKKKNAKKGP STPYTKSKRG HREEEQEDLT KDMDEPSPVP NVEEVTLPKT 360
VNTKKDSESA PVKGGTMTDL DEQEDESMET TGKDEDENST GNKGEQTKNP DLHEDNVTEQ 420
THHIIIPSYA AWFDYNSVHA IERRALPEFF NGKNKSKTPE IYLAYRNFMI DTYRLNPQEY 480
LTSTACRRNL AGDVCAIMRV HAFLEQWGLI NYQVDAESRP TPMGPPPTSH FHVLADTPSG 540
LVPLQPKTPQ GRQVDADTKA GRKGKELDDL VPETAKGKPE LQTSASQQML NFPDKGKEKP 600
TDMQNFGLRT DMYTKKNVPS KSKAAASATR EWTEQETLLL LEALEMYKDD WNKVSEHVGS 660
RTQDECILHF LRLPIEDPYL EDSEASLGPL AYQPIPFSQS GNPVMSTVAF LASVVDPRVA 720
SAAAKSALEE FSKMKEEVPT ALVEAHVRKV EEAAKVTGKA DPAFGLESSG IAGTTSDEPE 780
RIEESGNDEA RVEGQATDEK KEPKEPREGG GAIEEEAKEK TSEAPKKDEE KGKEGDSEKE 840
SEKSDGDPIV DPEKEKEPKE GQEEVLKEVV ESEGERKTKV ERDIGEGNLS TAAAAALAAA 900
AVKAKHLAAV EERKIKSLVA LLVETQMKKL EIKLRHFEEL ETIMDREREA LEYQRQQLLA 960
DRQAFHMEQL KYAEMRARQQ HFQQMHQQQQ QPPPALPPGS QPIPPTGAAG PPAVHGLAVA 1020
PASVVPAPAG SGAPPGSLGP SEQIGQAGST AGPQQQQPAG APQPGAVPPG VPPPGPHGPS 1080
PFPNQQTPPS MMPGAVPGSG HPGVAGNAPL GLPFGMPPPP PPPAPSIIPF GSLADSISIN 1140
LPAPPNLHGH HHHLPFAPGT LPPPNLPVSM ANPLHPNLPA TTTMPSSLPL GPGLGSAAAQ 1200
SPAIVAAVQG NLLPSASPLP DPGTPLPPDP TAPSPGTVTP VPPPQ 1245 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro. 
Interpro
 IPR001357; BRCT_dom.
 IPR000953; Chromo_domain/shadow.
 IPR009057; Homeodomain-like.
 IPR001005; SANT/Myb.
 IPR017884; SANT_dom.
 IPR007526; SWIRM.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00249; Myb_DNA-binding
 PF04433; SWIRM 
SMART
 SM00298; CHROMO
 SM00717; SANT 
PROSITE
 PS51293; SANT
 PS50934; SWIRM 
PRINTS