CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019634
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Structural maintenance of chromosomes protein 6 
Protein Synonyms/Alias
 SMC protein 6; SMC-6; hSMC6 
Gene Name
 SMC6 
Gene Synonyms/Alias
 SMC6L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107TNRGSSLKGFVKDGQubiquitination[1]
111SSLKGFVKDGQNSADubiquitination[1, 2]
201SKQFLQSKNEGDKYKubiquitination[1]
220ATQLEQMKEDYSYIMubiquitination[2]
230YSYIMETKERTKEQIubiquitination[1, 2, 3]
268IAGLSTMKTNLESLKubiquitination[3]
275KTNLESLKHEMAWAVubiquitination[1]
658SSENTRPKFLSRDVDubiquitination[3]
784ENKYDAIKFKINQLSacetylation[4]
786KYDAIKFKINQLSELubiquitination[3]
812DSEVDNQKRGKRHYEubiquitination[3]
862PERIEVEKSASILDKubiquitination[1, 2, 3, 4]
908TYLDLDSKVRTLKKFubiquitination[1]
917RTLKKFIKLLGEIMEubiquitination[3]
928EIMEHRFKTYQQFRRubiquitination[1, 3]
978VQPGEGNKAAFNDMRubiquitination[2]
1060MSSLPSSKLIRILRMubiquitination[1, 2, 3, 5]
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] 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] 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] 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]
 [5] 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] 
Functional Description
 Core component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. 
Sequence Annotation
 NP_BIND 76 83 ATP (Potential).
 REGION 452 659 Flexible hinge.
 MOD_RES 669 669 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Chromosome; Coiled coil; Complete proteome; DNA damage; DNA recombination; DNA repair; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Telomere; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1091 AA 
Protein Sequence
MAKRKEENFS SPKNAKRPRQ EELEDFDKDG DEDECKGTTL TAAEVGIIES IHLKNFMCHS 60
MLGPFKFGSN VNFVVGNNGS GKSAVLTALI VGLGGRAVAT NRGSSLKGFV KDGQNSADIS 120
ITLRNRGDDA FKASVYGNSI LIQQHISIDG SRSYKLKSAT GSVVSTRKEE LIAILDHFNI 180
QVDNPVSVLT QEMSKQFLQS KNEGDKYKFF MKATQLEQMK EDYSYIMETK ERTKEQIHQG 240
EERLTELKRQ CVEKEERFQS IAGLSTMKTN LESLKHEMAW AVVNEIEKQL NAIRDNIKIG 300
EDRAARLDRK MEEQQVRLNE AEQKYKDIQD KLEKISEETN ARAPECMALK ADVVAKKRAY 360
NEAEVLYNRS LNEYKALKKD DEQLCKRIEE LKKSTDQSLE PERLERQKKI SWLKERVKAF 420
QNQENSVNQE IEQFQQAIEK DKEEHGKIKR EELDVKHALS YNQRQLKELK DSKTDRLKRF 480
GPNVPALLEA IDDAYRQGHF TYKPVGPLGA CIHLRDPELA LAIESCLKGL LQAYCCHNHA 540
DERVLQALMK RFYLPGTSRP PIIVSEFRNE IYDVRHRAAY HPDFPTVLTA LEIDNAVVAN 600
SLIDMRGIET VLLIKNNSVA RAVMQSQKPP KNCREAFTAD GDQVFAGRYY SSENTRPKFL 660
SRDVDSEISD LENEVENKTA QILNLQQHLS ALEKDIKHNE ELLKRCQLHY KELKMKIRKN 720
ISEIRELENI EEHQSVDIAT LEDEAQENKS KMKMVEEHME QQKENMEHLK SLKIEAENKY 780
DAIKFKINQL SELADPLKDE LNLADSEVDN QKRGKRHYEE KQKEHLDTLN KKKRELDMKE 840
KELEEKMSQA RQICPERIEV EKSASILDKE INRLRQKIQA EHASHGDREE IMRQYQEARE 900
TYLDLDSKVR TLKKFIKLLG EIMEHRFKTY QQFRRCLTLR CKLYFDNLLS QRAYCGKMNF 960
DHKNETLSIS VQPGEGNKAA FNDMRALSGG ERSFSTVCFI LSLWSIAESP FRCLDEFDVY 1020
MDMVNRRIAM DLILKMADSQ RFRQFILLTP QSMSSLPSSK LIRILRMSDP ERGQTTLPFR 1080
PVTQEEDDDQ R 1091 
Gene Ontology
 GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0090398; P:cellular senescence; IMP:UniProtKB.
 GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
 GO:0000722; P:telomere maintenance via recombination; IMP:UniProtKB. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR027132; SMC6. 
Pfam
 PF02463; SMC_N 
SMART
  
PROSITE
  
PRINTS