CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017079
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Structural maintenance of chromosomes protein 5 
Protein Synonyms/Alias
 SMC protein 5; SMC-5; hSMC5 
Gene Name
 SMC5 
Gene Synonyms/Alias
 KIAA0594; SMC5L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31PSSEVPSKRKNSAPQubiquitination[1]
100ICLGLAGKPAFMGRAubiquitination[1]
109AFMGRADKVGFFVKRubiquitination[1]
115DKVGFFVKRGCSRGMubiquitination[1]
159NKKSTTQKIVEEKVAubiquitination[1]
189DKVGEFAKLSKIELLubiquitination[1, 2, 3]
192GEFAKLSKIELLEATubiquitination[1, 4, 5]
232LETSCKEKTEYLQKMubiquitination[1]
238EKTEYLQKMVQRNERubiquitination[1, 4, 5]
269LIEMLEAKRPWVEYEubiquitination[1]
286RQEYEEVKLVRDRVKubiquitination[1]
436ETLEKEKKSVDDHIVubiquitination[1]
452FDNLMNQKEDKLRQRubiquitination[1, 2, 6]
455LMNQKEDKLRQRFRDubiquitination[1]
492IMLTINMKDNKNAKYubiquitination[1]
495TINMKDNKNAKYIENubiquitination[1]
498MKDNKNAKYIENHIPubiquitination[1, 6, 7]
542VNAVIAPKSSYADKAubiquitination[1, 6]
548PKSSYADKAPSRSLNacetylation[8]
548PKSSYADKAPSRSLNubiquitination[1]
558SRSLNELKQYGFFSYubiquitination[1, 3, 4, 5, 7, 9]
595EVPVGTEKTRERIERubiquitination[1]
665QLKEIHRKLQAVDSGubiquitination[1]
714LEQKISSKLGSLKLMubiquitination[1]
719SSKLGSLKLMEQDTCubiquitination[1]
740RKASTKIKEINVQKAubiquitination[1]
746IKEINVQKAKLVTELubiquitination[1]
748EINVQKAKLVTELTNubiquitination[1]
895TIVQEYTKREEEIEQubiquitination[1, 6]
908EQLTEELKGKKVELDubiquitination[1, 6]
911TEELKGKKVELDQYRubiquitination[1]
925RENISQVKERWLNPLubiquitination[1, 6]
933ERWLNPLKELVEKINubiquitination[1]
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] 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]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [9] 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 repair of 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. Required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6. 
Sequence Annotation
 NP_BIND 80 87 ATP (Potential).
 REGION 446 646 Flexible hinge.
 MOD_RES 35 35 Phosphoserine.  
Keyword
 ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil; Complete proteome; DNA damage; DNA recombination; DNA repair; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Telomere; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1101 AA 
Protein Sequence
MATPSKKTST PSPQPSKRAL PRDPSSEVPS KRKNSAPQLP LLQSSGPFVE GSIVRISMEN 60
FLTYDICEVS PGPHLNMIVG ANGTGKSSIV CAICLGLAGK PAFMGRADKV GFFVKRGCSR 120
GMVEIELFRA SGNLVITREI DVAKNQSFWF INKKSTTQKI VEEKVAALNI QVGNLCQFLP 180
QDKVGEFAKL SKIELLEATE KSIGPPEMHK YHCELKNLRE KEKQLETSCK EKTEYLQKMV 240
QRNERYKQDV ERFYERKRHL DLIEMLEAKR PWVEYENVRQ EYEEVKLVRD RVKEEVRKLK 300
EGQIPVTCRI EEMENERHNL EARIKEKATD IKEASQKCKQ KQDVIERKDK HIEELQQALI 360
VKQNEELDRQ RRIGNTRKMI EDLQNELKTT ENCENLQPQI DAITNDLRRI QDEKALCEGE 420
IIDKRRERET LEKEKKSVDD HIVRFDNLMN QKEDKLRQRF RDTYDAVLWL RNNRDKFKQR 480
VCEPIMLTIN MKDNKNAKYI ENHIPSNDLR AFVFESQEDM EVFLKEVRDN KKLRVNAVIA 540
PKSSYADKAP SRSLNELKQY GFFSYLRELF DAPDPVMSYL CCQYHIHEVP VGTEKTRERI 600
ERVIQETRLK QIYTAEEKYV VKTSFYSNKV ISSNTSLKVA QFLTVTVDLE QRRHLEEQLK 660
EIHRKLQAVD SGLIALRETS KHLEHKDNEL RQKKKELLER KTKKRQLEQK ISSKLGSLKL 720
MEQDTCNLEE EERKASTKIK EINVQKAKLV TELTNLIKIC TSLHIQKVDL ILQNTTVISE 780
KNKLESDYMA ASSQLRLTEQ HFIELDENRQ RLLQKCKELM KRARQVCNLG AEQTLPQEYQ 840
TQVPTIPNGH NSSLPMVFQD LPNTLDEIDA LLTEERSRAS CFTGLNPTIV QEYTKREEEI 900
EQLTEELKGK KVELDQYREN ISQVKERWLN PLKELVEKIN EKFSNFFSSM QCAGEVDLHT 960
ENEEDYDKYG IRIRVKFRSS TQLHELTPHH QSGGERSVST MLYLMALQEL NRCPFRVVDE 1020
INQGMDPINE RRVFEMVVNT ACKENTSQYF FITPKLLQNL PYSEKMTVLF VYNGPHMLEP 1080
NTWNLKAFQR RRRRITFTQP S 1101 
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:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0090398; P:cellular senescence; IMP:UniProtKB.
 GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
 GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
 GO:0000722; P:telomere maintenance via recombination; IMP:UniProtKB. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR027131; SMC5. 
Pfam
 PF02463; SMC_N 
SMART
  
PROSITE
  
PRINTS