CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024490
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Structural maintenance of chromosomes flexible hinge domain-containing protein 1 
Protein Synonyms/Alias
 SMC hinge domain-containing protein 1 
Gene Name
 SMCHD1 
Gene Synonyms/Alias
 KIAA0650 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36YLFDRREKESELGDRubiquitination[1]
177LFDETQGKPAVAVIDubiquitination[1]
192NGRGMTSKQLNNWAVubiquitination[1, 2, 3, 4]
291SGYIRNRKPSDSVHIubiquitination[1]
448DDPCFPSKLKDEDDEubiquitination[1]
450PCFPSKLKDEDDEDDubiquitination[1]
463DDCFILEKAARGKRPubiquitination[1]
496FDWCTPPKKRGLAPIubiquitination[1]
497DWCTPPKKRGLAPIEubiquitination[1]
580QIKFTLFKGVITRPDubiquitination[2, 4]
619GQLVKTIKTLPLFYGubiquitination[1, 2, 4]
668VRTVPIAKLDRTVAEacetylation[5]
668VRTVPIAKLDRTVAEubiquitination[1]
771HISQHGGKWPYWFKKacetylation[6, 7]
784KKMENIQKLGNYTLKubiquitination[2, 3, 4]
812AGRPLPSKAIKFSVKubiquitination[1, 2, 4, 8, 9, 10, 11]
815PLPSKAIKFSVKEGKubiquitination[1, 5]
822KFSVKEGKPEKFSFGubiquitination[1]
891VIRGVTAKGPVNSCQubiquitination[1]
912KVTLPGLKEDSQILKubiquitination[1]
1019RIEIPSCKDVAPVEKubiquitination[1]
1048IFSVEGQKAIQIKHQubiquitination[2, 3, 4]
1090ITSALAEKIKVNWTPubiquitination[11]
1256LISGPPAKLLLIDWPubiquitination[2, 4]
1266LIDWPELKESIPVINubiquitination[1, 11]
1304HVKISLTKASNLKLMubiquitination[1]
1349QVKAIYNKSIIEGPIacetylation[6, 12]
1349QVKAIYNKSIIEGPIubiquitination[5]
1374KPVRLNVKYDKDASFubiquitination[1, 2, 3, 4, 5]
1437TFSCNKIKDNDKEDGubiquitination[1, 5]
1557DTPLFIGKVRTLEFPubiquitination[1, 8, 11]
1618FMFYNDVKKQQQMAAubiquitination[11]
1619MFYNDVKKQQQMAALubiquitination[1]
1703LSEQEELKKKPRRSCacetylation[5, 6, 12]
1725GSGDVLGKIAHLAQIubiquitination[1]
1782PLDSIYKKTLPDWKRubiquitination[1]
1798LPHFRNGKLYFKPIGacetylation[6]
1802RNGKLYFKPIGDPVFubiquitination[1, 2, 4, 5]
1872DRIRSNGKFGGLQNKacetylation[5, 6]
1950QELDEHEKNLKLIEEubiquitination[2, 4]
1958NLKLIEEKLGMTPIRubiquitination[1, 2, 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] 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]
 [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] 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]
 [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 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]
 [7] 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]
 [8] 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]
 [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]
 [10] 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]
 [11] 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]
 [12] 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] 
Functional Description
 Required for maintenance of X inactivation in females and hypermethylation of CpG islands associated with inactive X. Involved in a pathway that mediates the methylation of a subset of CpG islands slowly and requires the de novo methyltransferase DNMT3B (By similarity). Required for DUX4 silencing in somatic cells. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 1349 1349 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Chromosome; Complete proteome; Direct protein sequencing; Disease mutation; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2005 AA 
Protein Sequence
MAAADGGGPG GASVGTEEDG GGVGHRTVYL FDRREKESEL GDRPLQVGER SDYAGFRACV 60
CQTLGISPEE KFVITTTSRK EITCDNFDET VKDGVTLYLL QSVNQLLLTA TKERIDFLPH 120
YDTLVKSGMY EYYASEGQNP LPFALAELID NSLSATSRNI GVRRIQIKLL FDETQGKPAV 180
AVIDNGRGMT SKQLNNWAVY RLSKFTRQGD FESDHSGYVR PVPVPRSLNS DISYFGVGGK 240
QAVFFVGQSA RMISKPADSQ DVHELVLSKE DFEKKEKNKE AIYSGYIRNR KPSDSVHITN 300
DDERFLHHLI IEEKEKDSFT AVVITGVQPE HIQYLKNYFH LWTRQLAHIY HYYIHGPKGN 360
EIRTSKEVEP FNNIDIEISM FEKGKVPKIV NLREIQDDMQ TLYVNTAADS FEFKAHVEGD 420
GVVEGIIRYH PFLYDRETYP DDPCFPSKLK DEDDEDDCFI LEKAARGKRP IFECFWNGRL 480
IPYTSVEDFD WCTPPKKRGL APIECYNRIS GALFTNDKFQ VSTNKLTFMD LELKLKDKNT 540
LFTRILNGQE QRMKIDREFA LWLKDCHEKY DKQIKFTLFK GVITRPDLPS KKQGPWATYA 600
AIEWDGKIYK AGQLVKTIKT LPLFYGSIVR FFLYGDHDGE VYATGGEVQI AMEPQALYDE 660
VRTVPIAKLD RTVAEKAVKK YVEDEMARLP DRLSVTWPEG DELLPNEVRP AGTPIGALRI 720
EILNKKGEAM QKLPGTSHGG SKKLLVELKV ILHSSSGNKE IISHISQHGG KWPYWFKKME 780
NIQKLGNYTL KLQVVLNESN ADTYAGRPLP SKAIKFSVKE GKPEKFSFGL LDLPFRVGVP 840
FNIPLEFQDE FGHTSQLVTD IQPVLEASGL SLHYEEITKG PNCVIRGVTA KGPVNSCQGK 900
NYNLKVTLPG LKEDSQILKI RLLPGHPRRL KVKPDSEILV IENGTAFPFQ VEVLDESDNI 960
TAQPKLIVHC KFSGAPNLPV YVVDCSSSGT SILTGSAIQV QNIKKDQTLK ARIEIPSCKD 1020
VAPVEKTIKL LPSSHVARLQ IFSVEGQKAI QIKHQDEVNW IAGDIMHNLI FQMYDEGERE 1080
INITSALAEK IKVNWTPEIN KEHLLQGLLP DVQVPTSVKD MRYCQVSFQD DHVSLESAFT 1140
VRPLPDEPKH LKCEMKGGKT VQMGQELQGE VVIIITDQYG NQIQAFSPSS LSSLSIAGVG 1200
LDSSNLKTTF QENTQSISVR GIKFIPGPPG NKDLCFTWRE FSDFIRVQLI SGPPAKLLLI 1260
DWPELKESIP VINGRDLQNP IIVQLCDQWD NPAPVQHVKI SLTKASNLKL MPSNQQHKTD 1320
EKGRANLGVF SVFAPRGEHT LQVKAIYNKS IIEGPIIKLM ILPDPEKPVR LNVKYDKDAS 1380
FLAGGLFTDF MISVISEDDS IIKNINPARI SMKMWKLSTS GNRPPANAET FSCNKIKDND 1440
KEDGCFYFRD KVIPNKVGTY CIQFGFMMDK TNILNSEQVI VEVLPNQPVK LVPKIKPPTP 1500
AVSNVRSVAS RTLVRDLHLS ITDDYDNHTG IDLVGTIIAT IKGSNEEDTD TPLFIGKVRT 1560
LEFPFVNGSA EIMSLVLAES SPGRDSTEYF IVFEPRLPLL SRTLEPYILP FMFYNDVKKQ 1620
QQMAALTKEK DQLSQSIVMY KSLFEASQQL LNEMKCQVEE ARLKEAQLRN ELKIHNIDIP 1680
TTQQVPHIEA LLKRKLSEQE ELKKKPRRSC TLPNYTKGSG DVLGKIAHLA QIEDDRAAMV 1740
ISWHLASDMD CVVTLTTDAA RRIYDETQGR QQVLPLDSIY KKTLPDWKRS LPHFRNGKLY 1800
FKPIGDPVFA RDLLTFPDNV EHCETVFGML LGDTIILDNL DAANHYRKEV VKITHCPTLL 1860
TRDGDRIRSN GKFGGLQNKA PPMDKLRGMV FGAPVPKQCL ILGEQIDLLQ QYRSAVCKLD 1920
SVNKDLNSQL EYLRTPDMRK KKQELDEHEK NLKLIEEKLG MTPIRKCNDS LRHSPKVETT 1980
DCPVPPKRMR REATRQNRII TKTDV 2005 
Gene Ontology
 GO:0001740; C:Barr body; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0051276; P:chromosome organization; IEA:InterPro.
 GO:0060821; P:inactivation of X chromosome by DNA methylation; IEA:Compara. 
Interpro
 IPR003594; HATPase_ATP-bd.
 IPR010935; SMC_hinge. 
Pfam
 PF06470; SMC_hinge 
SMART
 SM00968; SMC_hinge 
PROSITE
  
PRINTS