UniProt Accession

 SMC2_HUMAN; O95347; Q6IEE0; Q9P1P2 

Genbank Protein ID

 AF092563; AL833191; AL161791; AL354938; AL354938; AL161791; CH471105; BC130385; AF113673; BN000163 

Genbank Nucleotide ID

 AAC72360.1; CAI46187.1; CAI16866.1; CAI16866.1; CAI16923.1; CAI16923.1; EAW58973.1; AAI30386.1; AAF29579.1; CAD89875.1 

Protein Name

 Structural maintenance of chromosomes protein 2 

Protein Synonyms/Alias

 SMC protein 2; SMC-2; Chromosome-associated protein E; hCAP-E; XCAP-E homolog 

Gene Name

 SMC2 

Gene Synonyms/Alias

 CAPE; SMC2L1; PRO0324 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
4	****MHIKSIILEGF	ubiquitination	[1]
12	SIILEGFKSYAQRTE	ubiquitination	[1, 2, 3, 4]
68	NLQDLVYKNGQAGIT	ubiquitination	[1, 2, 3, 4, 5]
114	VVIGGRNKYLINGVN	acetylation	[6, 7]
114	VVIGGRNKYLINGVN	ubiquitination	[4, 5]
152	IMQGRITKVLNMKPP	ubiquitination	[1, 4]
157	ITKVLNMKPPEILSM	ubiquitination	[1]
177	GTRMYEYKKIAAQKT	ubiquitination	[1]
178	TRMYEYKKIAAQKTI	ubiquitination	[1]
183	YKKIAAQKTIEKKEA	ubiquitination	[1]
211	TPTIQKLKEERSSYL	ubiquitination	[1]
222	SSYLEYQKVMREIEH	acetylation	[6]
222	SSYLEYQKVMREIEH	ubiquitination	[1, 4]
272	EELSENDKKIKALNH	ubiquitination	[1]
275	SENDKKIKALNHEIE	ubiquitination	[1]
290	ELEKRKDKETGGILR	ubiquitination	[1, 4]
312	EAQRVNTKSQSAFDL	ubiquitination	[1]
320	SQSAFDLKKKNLACE	acetylation	[4, 6, 8]
321	QSAFDLKKKNLACEE	ubiquitination	[1]
330	NLACEESKRKELEKN	acetylation	[4]
336	SKRKELEKNMVEDSK	acetylation	[9]
343	KNMVEDSKTLAAKEK	acetylation	[7]
348	DSKTLAAKEKEVKKI	acetylation	[9]
353	AAKEKEVKKITDGLH	acetylation	[9]
493	SRDIGRLKETYEALL	ubiquitination	[1]
511	PNLRFAYKDPEKNWN	ubiquitination	[1, 4]
515	FAYKDPEKNWNRNCV	ubiquitination	[1, 5]
523	NWNRNCVKGLVASLI	ubiquitination	[1, 4]
533	VASLISVKDTSATTA	ubiquitination	[1]
562	DTEVTGKKLLERGEL	ubiquitination	[1]
580	YTIIPLNKISARCIA	ubiquitination	[5]
677	QAASILTKFQELKDV	acetylation	[6]
677	QAASILTKFQELKDV	ubiquitination	[1, 2, 3]
682	LTKFQELKDVQDELR	ubiquitination	[1, 4]
691	VQDELRIKENELRAL	ubiquitination	[1]
706	EEELAGLKNTAEKYR	ubiquitination	[1]
711	GLKNTAEKYRQLKQQ	ubiquitination	[1]
760	EESEETLKNTKEIQR	acetylation	[7]
837	KREHTSYKQQLEAVN	acetylation	[4]
911	NDSQLKIKELDHNIS	ubiquitination	[4]
936	AKVSKMLKDYDWINA	ubiquitination	[1]
958	PNSAYDFKTNNPKEA	ubiquitination	[1, 4]
963	DFKTNNPKEAGQRLQ	acetylation	[4]
971	EAGQRLQKLQEMKEK	acetylation	[4]
971	EAGQRLQKLQEMKEK	ubiquitination	[1]
1003	ERYNDLMKKKRIVEN	ubiquitination	[1]
1004	RYNDLMKKKRIVEND	ubiquitination	[1]
1014	IVENDKSKILTTIED	ubiquitination	[1]
1025	TIEDLDQKKNQALNI	ubiquitination	[1, 10]
1026	IEDLDQKKNQALNIA	ubiquitination	[1, 4]
1036	ALNIAWQKVNKDFGS	ubiquitination	[1, 4]
1079	VALGNTWKENLTELS	ubiquitination	[1, 4, 10]
1158	NNANVLFKTKFVDGV	acetylation	[6, 7]
1158	NNANVLFKTKFVDGV	ubiquitination	[1]
1160	ANVLFKTKFVDGVST	acetylation	[4, 6, 7, 8]
1160	ANVLFKTKFVDGVST	ubiquitination	[1, 2, 3, 4]
1178	FTQCQNGKISKEAKS	ubiquitination	[1, 4, 5]
1188	KEAKSKAKPPKGAHV	ubiquitination	[1]
1191	KSKAKPPKGAHVEV*	ubiquitination	[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] 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] 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] 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] 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]
 [6] 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]
 [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] 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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [10] 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] 

Functional Description

 Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. 

Sequence Annotation

 NP_BIND 32 39 ATP (Potential).
 REGION 508 671 Flexible hinge.
 MOD_RES 114 114 N6-acetyllysine.
 MOD_RES 222 222 N6-acetyllysine.
 MOD_RES 677 677 N6-acetyllysine.
 MOD_RES 1158 1158 N6-acetyllysine.
 MOD_RES 1160 1160 N6-acetyllysine.  

Keyword

 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil; Complete proteome; Cytoplasm; DNA condensation; Mitosis; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1197 AA 

Protein Sequence

Gene Ontology

 GO:0000796; C:condensin complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:InterPro.
 GO:0051383; P:kinetochore organization; IEA:Compara.
 GO:0010032; P:meiotic chromosome condensation; IEA:Compara.
 GO:0045132; P:meiotic chromosome segregation; IEA:Compara.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
 GO:0007062; P:sister chromatid cohesion; IEA:InterPro. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR003395; RecF/RecN/SMC.
 IPR024704; SMC.
 IPR027120; Smc2.
 IPR010935; SMC_hinge. 

Pfam

 PF06470; SMC_hinge
 PF02463; SMC_N 

SMART

 SM00968; SMC_hinge 

PROSITE

  

PRINTS