CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037343
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Structural maintenance of chromosomes protein 
Protein Synonyms/Alias
  
Gene Name
 SMC4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
409EFKSIPAKSNNIINEubiquitination[1]
539EKEKELQKLTQEETNacetylation[2]
548TQEETNFKSLVHDLFacetylation[2, 3]
548TQEETNFKSLVHDLFubiquitination[1]
562FQKVEEAKSSLAMNRubiquitination[1]
573AMNRSRGKVLDAIIQubiquitination[1]
582LDAIIQEKKSGRIPGacetylation[2, 3]
582LDAIIQEKKSGRIPGubiquitination[4, 5]
673PRLFDLVKVKDEKIRubiquitination[3]
735GGGSKVMKGRMGSSLubiquitination[1]
772AMQIQEQKVQLEERVubiquitination[1]
795EMRNTLEKFTASIQRubiquitination[1]
828VLATAPDKKKQKLLEubiquitination[1]
880KLKAQQDKLDKINKQubiquitination[1]
963ESLPEIQKEHRNLLQubiquitination[3]
973RNLLQELKVIQENEHubiquitination[1]
984ENEHALQKDALSIKLacetylation[2, 3]
984ENEHALQKDALSIKLubiquitination[1]
1008AEHNSKIKYWHKEISubiquitination[1]
1073GAIAEYKKKEELYLQubiquitination[1, 3, 6]
1074AIAEYKKKEELYLQRubiquitination[6]
1087QRVAELDKITYERDSubiquitination[1, 3, 7]
1162PPKKSWKKIFNLSGGubiquitination[1, 3, 4, 7]
1242DRLIGIYKTYNITKSubiquitination[1, 3, 5, 7]
1248YKTYNITKSVAVNPKubiquitination[1, 3, 4, 5, 6]
1255KSVAVNPKEIASKGLubiquitination[1, 3, 4]
1260NPKEIASKGLC****ubiquitination[1, 3, 4, 8]
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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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
 1263 AA 
Protein Sequence
MPRKGTQPST ARRREEGPPP PSPDGASSDA EPEPPSGRTE SPATAAAMTN EAGAPRLMIT 60
HIVNQNFKSY AGEKILGPFH KRFSCIIGPN GSGKSNVIDS MLFVFGYRAQ KIRSKKLSVL 120
IHNSDEHKDI QSCTVEVHFQ KIIDKEGDDY EVIPNSNFYV SRTACRDNTS VYHISGKKKT 180
FKDVGNLLRS HGIDLDHNRF LILQGEVEQI AMMKPKGQTE HDEGMLEYLE DIIGCGRLNE 240
PIKVLCRRVE ILNEHRGEKL NRVKMVEKEK DALEGEKNIA IEFLTLENEI FRKKNHVCQY 300
YIYELQKRIA EMETQKEKIH EDTKEINEKS NILSNEMKAK NKDVKDTEKK LNKITKFIEE 360
NKEKFTQLDL EDVQVREKLK HATSKAKKLE KQLQKDKEKV EEFKSIPAKS NNIINETTTR 420
NNALEKEKEK EEKKLKEVMD SLKQETQGLQ KEKESREKEL MGFSKSVNEA RSKMDVAQSE 480
LDIYLSRHNT AVSQLTKAKE ALIAASETLK ERKAAIRDIE GKLPQTEQEL KEKEKELQKL 540
TQEETNFKSL VHDLFQKVEE AKSSLAMNRS RGKVLDAIIQ EKKSGRIPGI YGRLGDLGAI 600
DEKYDVAISS CCHALDYIVV DSIDIAQECV NFLKRQNIGV ATFIGLDKMA VWAKKMTEIQ 660
TPENTPRLFD LVKVKDEKIR QAFYFALRDT LVADNLDQAT RVAYQKDRRW RVVTLQGQII 720
EQSGTMTGGG SKVMKGRMGS SLVIEISEEE VNKMESQLQN DSKKAMQIQE QKVQLEERVV 780
KLRHSEREMR NTLEKFTASI QRLIEQEEYL NVQVKELEAN VLATAPDKKK QKLLEENVSA 840
FKTEYDAVAE KAGKVEAEVK RLHNTIVEIN NHKLKAQQDK LDKINKQLDE CASAITKAQV 900
AIKTADRNLQ KAQDSVLRTE KEIKDTEKEV DDLTAELKSL EDKAAEVVKN TNAAEESLPE 960
IQKEHRNLLQ ELKVIQENEH ALQKDALSIK LKLEQIDGHI AEHNSKIKYW HKEISKISLH 1020
PIEDNPIEEI SVLSPEDLEA IKNPDSITNQ IALLEARCHE MKPNLGAIAE YKKKEELYLQ 1080
RVAELDKITY ERDSFRQAYE DLRKQRLNEF MAGFYIITNK LKENYQMLTL GGDAELELVD 1140
SLDPFSEGIM FSVRPPKKSW KKIFNLSGGE KTLSSLALVF ALHHYKPTPL YFMDEIDAAL 1200
DFKNVSIVAF YIYEQTKNAQ FIIISLRNNM FEISDRLIGI YKTYNITKSV AVNPKEIASK 1260
GLC 1263 
Gene Ontology
 GO:0005694; C:chromosome; IEA:InterPro.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0030261; P:chromosome condensation; IEA:InterPro.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:InterPro.
 GO:0007062; P:sister chromatid cohesion; IEA:InterPro. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR024704; SMC.
 IPR010935; SMC_hinge. 
Pfam
 PF06470; SMC_hinge
 PF02463; SMC_N 
SMART
 SM00968; SMC_hinge 
PROSITE
  
PRINTS