CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-042038
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Structural maintenance of chromosomes protein 1A 
Protein Synonyms/Alias
  
Gene Name
 SMC1A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MGFLKLIEIENFubiquitination[1, 2]
13LIEIENFKSYKGRQIubiquitination[1, 2, 3, 4]
52ISFVLGEKTSNLRVKubiquitination[1, 2]
72IHGAPVGKPAANRAFubiquitination[2, 5]
106VGGSSEYKINNKVVQubiquitination[1, 2, 4, 5]
110SEYKINNKVVQLHEYubiquitination[1, 2]
203ENQKRIEKLEEYITTacetylation[5]
203ENQKRIEKLEEYITTubiquitination[2]
233TEEVEMAKRRIDEINubiquitination[2, 3]
266ESSRQQRKAEIMESIubiquitination[2, 5]
274AEIMESIKRLYPGSVubiquitination[1]
294DLCQPTQKKYQIAVTubiquitination[2, 4]
295LCQPTQKKYQIAVTKubiquitination[2]
302KYQIAVTKVLGKNMDubiquitination[1, 2, 5]
306AVTKVLGKNMDAIIVacetylation[5]
306AVTKVLGKNMDAIIVubiquitination[1, 2]
327RDCIQYIKEQRGEPEubiquitination[2, 4, 5]
345PLDYLEVKPTDEKLRacetylation[6]
345PLDYLEVKPTDEKLRubiquitination[2, 7]
350EVKPTDEKLRELKGAubiquitination[2, 5]
372RYEPPHIKKALQYACubiquitination[1]
373YEPPHIKKALQYACGubiquitination[2, 5]
403FGGHQRHKTVALDGTubiquitination[1, 2, 5]
414LDGTLFQKSGVISGGubiquitination[1, 5, 7, 8]
426SGGASDLKAKARRWDubiquitination[1, 2, 4, 5]
458LKEQMKAKRKEAELRubiquitination[2]
479HGLQMRLKYSQSDLEacetylation[5, 9]
479HGLQMRLKYSQSDLEubiquitination[2, 5]
489QSDLEQTKTRHLALNubiquitination[2, 5]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 516 AA 
Protein Sequence
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT 60
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE 120
LEKLGILIKA RNFLVFQVKK YHRLKEEASK RAATLAQELE KFNRDQKADQ DRLDLEERKK 180
VETEAKIKQK LREIEENQKR IEKLEEYITT SKQSLEEQKK LEGELTEEVE MAKRRIDEIN 240
KELNQVMEQL GDARIDRQES SRQQRKAEIM ESIKRLYPGS VYGRLIDLCQ PTQKKYQIAV 300
TKVLGKNMDA IIVDSEKTGR DCIQYIKEQR GEPETFLPLD YLEVKPTDEK LRELKGAKLV 360
IDVIRYEPPH IKKALQYACG NALVCDNVED ARRIAFGGHQ RHKTVALDGT LFQKSGVISG 420
GASDLKAKAR RWDEKAVDKL KEKKERLTEE LKEQMKAKRK EAELRQVQSQ AHGLQMRLKY 480
SQSDLEQTKT RHLALNLQVG PGLQPCSPKA IHTFLA 516 
Gene Ontology
 GO:0005694; C:chromosome; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0051276; P:chromosome organization; IEA:InterPro. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR010935; SMC_hinge. 
Pfam
 PF06470; SMC_hinge
 PF02463; SMC_N 
SMART
 SM00968; SMC_hinge 
PROSITE
  
PRINTS