UniProt Accession

 SMC1A_HUMAN; Q14683; O14995; Q16351; Q2M228 

Genbank Protein ID

 S78271; D80000; AL161779; Z97054; Z97054; AL161779; BC112127 

Genbank Nucleotide ID

 AAB34405.1; BAA11495.2; CAI42089.1; CAI42089.1; CAI42646.1; CAI42646.1; AAI12128.1 

Protein Name

 Structural maintenance of chromosomes protein 1A 

Protein Synonyms/Alias

 SMC protein 1A; SMC-1-alpha; SMC-1A; Sb1.8 

Gene Name

 SMC1A 

Gene Synonyms/Alias

 DXS423E; KIAA0178; SB1.8; SMC1; SMC1L1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MGFLKLIEIENF	ubiquitination	[1, 2, 3]
13	LIEIENFKSYKGRQI	ubiquitination	[1, 2, 3, 4]
52	ISFVLGEKTSNLRVK	ubiquitination	[1, 2, 3]
72	IHGAPVGKPAANRAF	ubiquitination	[2]
106	VGGSSEYKINNKVVQ	ubiquitination	[1, 2, 3, 4, 5]
110	SEYKINNKVVQLHEY	ubiquitination	[1, 2, 3]
129	EKLGILIKARNFLVF	ubiquitination	[6]
149	SIAMKNPKERTALFE	ubiquitination	[2]
170	ELAQEYDKRKKEMVK	ubiquitination	[2, 6]
177	KRKKEMVKAEEDTQF	ubiquitination	[1, 2, 3, 6]
213	ADRYQRLKDEVVRAQ	ubiquitination	[2]
240	VEIEKLNKELASKNK	ubiquitination	[2]
282	REQQQIEKEIKEKDS	acetylation	[7, 8, 9]
437	ENQKRIEKLEEYITT	acetylation	[7]
437	ENQKRIEKLEEYITT	ubiquitination	[2]
467	TEEVEMAKRRIDEIN	ubiquitination	[2, 6]
500	ESSRQQRKAEIMESI	ubiquitination	[2]
508	AEIMESIKRLYPGSV	ubiquitination	[1, 3, 5]
528	DLCQPTQKKYQIAVT	ubiquitination	[2, 4]
529	LCQPTQKKYQIAVTK	ubiquitination	[2]
536	KYQIAVTKVLGKNMD	acetylation	[7]
536	KYQIAVTKVLGKNMD	ubiquitination	[1, 2, 3, 5]
540	AVTKVLGKNMDAIIV	ubiquitination	[1, 2, 3]
561	RDCIQYIKEQRGEPE	ubiquitination	[2, 4, 5]
579	PLDYLEVKPTDEKLR	ubiquitination	[2, 6]
584	EVKPTDEKLRELKGA	ubiquitination	[2]
606	RYEPPHIKKALQYAC	ubiquitination	[1, 3]
607	YEPPHIKKALQYACG	ubiquitination	[2]
637	FGGHQRHKTVALDGT	ubiquitination	[1, 2, 3]
648	LDGTLFQKSGVISGG	acetylation	[7]
648	LDGTLFQKSGVISGG	ubiquitination	[1, 3, 6, 10]
660	SGGASDLKAKARRWD	ubiquitination	[1, 2, 3, 4]
692	LKEQMKAKRKEAELR	ubiquitination	[2]
713	HGLQMRLKYSQSDLE	acetylation	[7]
713	HGLQMRLKYSQSDLE	ubiquitination	[2]
723	QSDLEQTKTRHLALN	ubiquitination	[2]
736	LNLQEKSKLESELAN	ubiquitination	[1, 2, 3, 9]
881	KNQHLAKKSEVNDKN	ubiquitination	[2]
897	EMEEIRKKLGGANKE	acetylation	[11]
910	KEMTHLQKEVTAIET	acetylation	[9]
918	EVTAIETKLEQKRSD	ubiquitination	[2]
944	DIKLPLSKGTMDDIS	ubiquitination	[2, 6, 10, 12]
1026	RIAAPNMKAMEKLES	ubiquitination	[2]
1030	PNMKAMEKLESVRDK	ubiquitination	[2, 6]
1037	KLESVRDKFQETSDE	ubiquitination	[1, 2, 3, 5, 6, 9, 10]
1056	RKRAKKAKQAFEQIK	ubiquitination	[2]
1063	KQAFEQIKKERFDRF	ubiquitination	[2, 9]
1120	YNCVAPGKRFRPMDN	ubiquitination	[2, 4, 12]
1196	LKEEFYTKAESLIGV	ubiquitination	[10, 12, 13]
1222	VLTFDLTKYPDANPN	ubiquitination	[1, 2, 3, 5, 6, 10]

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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [12] 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]
 [13] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 

Functional Description

 Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint. 

Sequence Annotation

 NP_BIND 32 39 ATP (Potential).
 REGION 504 659 Flexible hinge.
 MOD_RES 358 358 Phosphoserine.
 MOD_RES 360 360 Phosphoserine.
 MOD_RES 648 648 N6-acetyllysine.
 MOD_RES 713 713 N6-acetyllysine.
 MOD_RES 957 957 Phosphoserine; by ATM.
 MOD_RES 966 966 Phosphoserine; by ATM and ATR.
 MOD_RES 970 970 Phosphoserine.  

Keyword

 Acetylation; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; Kinetochore; Meiosis; Mental retardation; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1233 AA 

Protein Sequence

Gene Ontology

 GO:0008280; C:cohesin core heterodimer; TAS:UniProtKB.
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0000794; C:condensed nuclear chromosome; TAS:ProtInc.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000776; C:kinetochore; IDA:UniProtKB.
 GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0003777; F:microtubule motor activity; NAS:UniProtKB.
 GO:0000075; P:cell cycle checkpoint; IDA:UniProtKB.
 GO:0030261; P:chromosome condensation; IEA:InterPro.
 GO:0000910; P:cytokinesis; TAS:Reactome.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; TAS:UniProtKB.
 GO:0007126; P:meiosis; ISS:UniProtKB.
 GO:0007064; P:mitotic sister chromatid cohesion; TAS:UniProtKB.
 GO:0007052; P:mitotic spindle organization; TAS:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0032876; P:negative regulation of DNA endoreduplication; IMP:BHF-UCL.
 GO:0009314; P:response to radiation; IEP:UniProtKB.
 GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB.
 GO:0019827; P:stem cell maintenance; IEA:Compara. 

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