O95347 (SMC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Structural maintenance of chromosomes protein 2
Short name=SMC protein 2
Short name=SMC-2

Alternative name(s):
Chromosome-associated protein E
Short name=hCAP-E
XCAP-E homolog

Gene names

Name:	SMC2
Synonyms:	CAPE, SMC2L1
ORF Names:	PRO0324

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1197 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9
Subunit structure	Forms a heterodimer with SMC4. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRRN1/CAPH, CNAP1/CAPD2 and CAPG. Interacts with BRD4 (isoform B) leading to insulate chromatin from DNA damage response pathway. Ref.1 Ref.8 Ref.9 Ref.12
Subcellular location	Nucleus. Cytoplasm. Chromosome. Note: In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. Ref.8
Domain	The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer By similarity.
Sequence similarities	Belongs to the SMC family. SMC2 subfamily.
Sequence caution	The sequence AAC72360.1 differs from that shown. Reason: Frameshift at positions 890 and 908. The sequence AAF29579.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA condensation Mitosis
Cellular component	Chromosome Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Inferred from electronic annotation. Source: InterPro kinetochore organization Inferred from electronic annotation. Source: Ensembl meiotic chromosome condensation Inferred from electronic annotation. Source: Ensembl meiotic chromosome segregation Inferred from electronic annotation. Source: Ensembl mitotic cell cycle Traceable author statement. Source: Reactome mitotic chromosome condensation Inferred from direct assay Ref.9. Source: UniProtKB
Cellular_component	condensed chromosome Inferred from direct assay PubMed 12589063. Source: UniProtKB condensin complex Inferred from direct assay Ref.8Ref.9. Source: UniProtKB cytoplasm Inferred from direct assay Ref.8PubMed 12589063. Source: UniProtKB cytosol Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 19056867. Source: UniProt nuclear chromosome Inferred from direct assay Ref.8. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 12589063. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction PubMed 12589063Ref.12. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCAPH	Q15003	2	EBI-355822,EBI-1046410
NCAPH2	Q6IBW4	2	EBI-355822,EBI-2548296
SMC4	Q9NTJ3	3	EBI-355822,EBI-356173

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95347-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O95347-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1091-1099: SLVALSLIL → QKQQNHTTG
     1100-1197: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1197	1197	Structural maintenance of chromosomes protein 2		PRO_0000118995
Regions
	Nucleotide binding	32 – 39	8	ATP Potential
	Region	508 – 671	164	Flexible hinge
	Coiled coil	173 – 507	335	Potential
	Coiled coil	672 – 926	255	Potential
	Coiled coil	963 – 1031	69	Potential
	Compositional bias	1085 – 1120	36	Ala/Asp-rich (DA-box)
Amino acid modifications
	Modified residue	114	1	N6-acetyllysine Ref.10
	Modified residue	222	1	N6-acetyllysine Ref.10
	Modified residue	677	1	N6-acetyllysine Ref.10
	Modified residue	1158	1	N6-acetyllysine Ref.10
	Modified residue	1160	1	N6-acetyllysine Ref.10
Natural variations
	Alternative sequence	1091 – 1099	9	SLVALSLIL → QKQQNHTTG in isoform 2.		VSP_007243
	Alternative sequence	1100 – 1197	98	Missing in isoform 2.		VSP_007244
	Natural variant	1009	1	E → K. Corresponds to variant rs4562395 [ dbSNP | Ensembl ].		VAR_047489
Experimental info
	Sequence conflict	294	1	G → V in AAC72360. Ref.1
	Sequence conflict	916	1	N → H in AAC72360. Ref.1
	Sequence conflict	998	1	Y → C in AAC72360. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 15EBB56B31FC1364	FASTA	1,197	135,656
	10 20 30 40 50 60 MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS 70 80 90 100 110 120 NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE ITVTRQVVIG GRNKYLINGV 130 140 150 160 170 180 NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA 190 200 210 220 230 240 AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL 250 260 270 280 290 300 LAEDTKVRSA EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE 310 320 330 340 350 360 DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK EVKKITDGLH 370 380 390 400 410 420 ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMMACKNDIS KAQTEAKQAQ 430 440 450 460 470 480 MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA LEAVKRLKEK LEAEMKKLNY EENKEESLLE 490 500 510 520 530 540 KRRQLSRDIG RLKETYEALL ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA 550 560 570 580 590 600 LELVAGERLY NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP 610 620 630 640 650 660 DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV TLGGDVFDPH 670 680 690 700 710 720 GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE ELAGLKNTAE KYRQLKQQWE 730 740 750 760 770 780 MKTEEADLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK NTKEIQRKAE EKYEVLENKM 790 800 810 820 830 840 KNAEAERERE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL 850 860 870 880 890 900 EAVNEAIKSY ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK 910 920 930 940 950 960 EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ PNSAYDFKTN 970 980 990 1000 1010 1020 NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND LMKKKRIVEN DKSKILTTIE 1030 1040 1050 1060 1070 1080 DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE 1090 1100 1110 1120 1130 1140 NLTELSGGQR SLVALSLILS MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF 1150 1160 1170 1180 1190 IVVSLKEGMF NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV
	Isoform 2 [UniParc]. Checksum: 68BB895EA6EBA265	FASTA	1,099	124,926
	10 20 30 40 50 60 MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS 70 80 90 100 110 120 NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE ITVTRQVVIG GRNKYLINGV 130 140 150 160 170 180 NANNTRVQDL FCSVGLNVNN PHFLIMQGRI TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA 190 200 210 220 230 240 AQKTIEKKEA KLKEIKTILE EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL 250 260 270 280 290 300 LAEDTKVRSA EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE 310 320 330 340 350 360 DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK EVKKITDGLH 370 380 390 400 410 420 ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMMACKNDIS KAQTEAKQAQ 430 440 450 460 470 480 MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA LEAVKRLKEK LEAEMKKLNY EENKEESLLE 490 500 510 520 530 540 KRRQLSRDIG RLKETYEALL ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA 550 560 570 580 590 600 LELVAGERLY NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP 610 620 630 640 650 660 DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV TLGGDVFDPH 670 680 690 700 710 720 GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE ELAGLKNTAE KYRQLKQQWE 730 740 750 760 770 780 MKTEEADLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK NTKEIQRKAE EKYEVLENKM 790 800 810 820 830 840 KNAEAERERE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL 850 860 870 880 890 900 EAVNEAIKSY ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK 910 920 930 940 950 960 EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ PNSAYDFKTN 970 980 990 1000 1010 1020 NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND LMKKKRIVEN DKSKILTTIE 1030 1040 1050 1060 1070 1080 DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP GANAMLAPPE GQTVLDGLEF KVALGNTWKE 1090 NLTELSGGQR QKQQNHTTG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics." Schmiesing J.A., Ball A.R. Jr., Gregson H.C., Alderton J.M., Zhou S., Yokomori K. Proc. Natl. Acad. Sci. U.S.A. 95:12906-12911(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SMC4. Tissue: Teratocarcinoma.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph node.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[6]	"Functional prediction of the coding sequences of 32 new genes deduced by analysis of cDNA clones from human fetal liver." Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W., Bi J., Zhang Y., Liu M., He F. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1197 (ISOFORM 2). Tissue: Fetal liver.
[7]	"The evolution of SMC proteins: phylogenetic analysis and structural implications." Cobbe N., Heck M.M.S. Mol. Biol. Evol. 21:332-347(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
[8]	"A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the early stage of mitotic chromosome condensation." Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K. Mol. Cell. Biol. 20:6996-7006(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4 AND CNAP1, SUBCELLULAR LOCATION.
[9]	"Chromosome condensation by a human condensin complex in Xenopus egg extracts." Kimura K., Cuvier O., Hirano T. J. Biol. Chem. 276:5417-5420(2001) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; BRRN1; CNAP1 AND CAPG, FUNCTION OF THE COMPLEX.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-222; LYS-677; LYS-1158 AND LYS-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"The bromodomain protein Brd4 insulates chromatin from DNA damage signalling." Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C., Cannell I.G., Bryson B.D., Rameseder J., Lee M.J., Blake E.J., Fydrych A., Ho R., Greenberger B.A., Chen G.C., Maffa A., Del Rosario A.M., Root D.E., Carpenter A.E. , Hahn W.C., Sabatini D.M., Chen C.C., White F.M., Bradner J.E., Yaffe M.B. Nature 498:246-250(2013) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BRD4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF092563 mRNA. Translation: AAC72360.1. Frameshift. AL833191 mRNA. Translation: CAI46187.1. AL161791, AL354938 Genomic DNA. Translation: CAI16866.1. AL354938, AL161791 Genomic DNA. Translation: CAI16923.1. CH471105 Genomic DNA. Translation: EAW58973.1. BC130385 mRNA. Translation: AAI30386.1. AF113673 mRNA. Translation: AAF29579.1. Different initiation. BN000163 mRNA. Translation: CAD89875.1.
CCDS	CCDS35086.1. [O95347-1]
RefSeq	NP_001036015.1. NM_001042550.1. [O95347-1] NP_001036016.1. NM_001042551.1. [O95347-1] NP_001252531.1. NM_001265602.1. [O95347-1] NP_006435.2. NM_006444.2. [O95347-1] XP_006716996.1. XM_006716933.1. [O95347-1]
UniGene	Hs.119023.
3D structure databases
ProteinModelPortal	O95347.
SMR	O95347. Positions 1-273, 462-688, 945-1172.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	115841. 38 interactions.
DIP	DIP-35422N.
IntAct	O95347. 15 interactions.
MINT	MINT-1161754.
STRING	9606.ENSP00000286398.
PTM databases
PhosphoSite	O95347.
Proteomic databases
MaxQB	O95347.
PaxDb	O95347.
PRIDE	O95347.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000286398; ENSP00000286398; ENSG00000136824. [O95347-1] ENST00000303219; ENSP00000306152; ENSG00000136824. [O95347-2] ENST00000374787; ENSP00000363919; ENSG00000136824. [O95347-1] ENST00000374793; ENSP00000363925; ENSG00000136824. [O95347-1] ENST00000493955; ENSP00000431534; ENSG00000136824.
GeneID	10592.
KEGG	hsa:10592.
UCSC	uc004bbv.3. human. [O95347-1]
Organism-specific databases
CTD	10592.
GeneCards	GC09P106856.
H-InvDB	HIX0008250.
HGNC	HGNC:14011. SMC2.
MIM	605576. gene.
neXtProt	NX_O95347.
PharmGKB	PA37833.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1196.
HOGENOM	HOG000228249.
HOVERGEN	HBG106605.
InParanoid	O95347.
KO	K06674.
OMA	CQNGKIP.
OrthoDB	EOG7SR4KV.
PhylomeDB	O95347.
TreeFam	TF101157.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
ArrayExpress	O95347.
Bgee	O95347.
CleanEx	HS_SMC2.
Genevestigator	O95347.
Family and domain databases
Gene3D	3.40.50.300. 3 hits.
InterPro	IPR027417. P-loop_NTPase. IPR003395. RecF/RecN/SMC_N. IPR024704. SMC. IPR027120. Smc2. IPR010935. SMC_hinge. [Graphical view]
PANTHER	PTHR18937:SF9. PTHR18937:SF9. 1 hit.
Pfam	PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 2 hits. [Graphical view]
PIRSF	PIRSF005719. SMC. 1 hit.
SMART	SM00968. SMC_hinge. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 2 hits. SSF75553. SSF75553. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SMC2. human.
GeneWiki	SMC2.
GenomeRNAi	10592.
NextBio	40225.
PRO	O95347.
SOURCE	Search...

Entry information

Entry name

SMC2_HUMAN

Accession

Primary (citable) accession number: O95347
Secondary accession number(s): Q6IEE0, Q9P1P2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	November 25, 2008
Last modified:	July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.