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O95347 (SMC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1197 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processCell cycle
Cell division
DNA condensation
Mitosis
   Cellular componentChromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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_componentcondensed 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_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterodimerization activity

Inferred from physical interaction Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11971197Structural maintenance of chromosomes protein 2
PRO_0000118995

Regions

Nucleotide binding32 – 398ATP Potential
Region508 – 671164Flexible hinge
Coiled coil173 – 507335 Potential
Coiled coil672 – 926255 Potential
Coiled coil963 – 103169 Potential
Compositional bias1085 – 112036Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue1141N6-acetyllysine Ref.10
Modified residue2221N6-acetyllysine Ref.10
Modified residue6771N6-acetyllysine Ref.10
Modified residue11581N6-acetyllysine Ref.10
Modified residue11601N6-acetyllysine Ref.10

Natural variations

Alternative sequence1091 – 10999SLVALSLIL → QKQQNHTTG in isoform 2.
VSP_007243
Alternative sequence1100 – 119798Missing in isoform 2.
VSP_007244
Natural variant10091E → K.
Corresponds to variant rs4562395 [ dbSNP | Ensembl ].
VAR_047489

Experimental info

Sequence conflict2941G → V in AAC72360. Ref.1
Sequence conflict9161N → H in AAC72360. Ref.1
Sequence conflict9981Y → C in AAC72360. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 15EBB56B31FC1364

FASTA1,197135,656
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 68BB895EA6EBA265
Show »

FASTA1,099124,926

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_001036015.1. NM_001042550.1.
NP_001036016.1. NM_001042551.1.
NP_001252531.1. NM_001265602.1.
NP_006435.2. NM_006444.2.
UniGeneHs.119023.

3D structure databases

ProteinModelPortalO95347.
SMRO95347. Positions 1-273, 462-688, 945-1172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115841. 36 interactions.
DIPDIP-35422N.
IntActO95347. 15 interactions.
MINTMINT-1161754.
STRING9606.ENSP00000286398.

PTM databases

PhosphoSiteO95347.

Proteomic databases

PaxDbO95347.
PRIDEO95347.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286398; ENSP00000286398; ENSG00000136824. [O95347-1]
ENST00000303219; ENSP00000306152; ENSG00000136824. [O95347-2]
ENST00000374787; ENSP00000363919; ENSG00000136824. [O95347-1]
ENST00000374793; ENSP00000363925; ENSG00000136824. [O95347-1]
ENST00000493955; ENSP00000431534; ENSG00000136824.
GeneID10592.
KEGGhsa:10592.
UCSCuc004bbv.3. human. [O95347-1]

Organism-specific databases

CTD10592.
GeneCardsGC09P106856.
H-InvDBHIX0008250.
HGNCHGNC:14011. SMC2.
MIM605576. gene.
neXtProtNX_O95347.
PharmGKBPA37833.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1196.
HOGENOMHOG000228249.
HOVERGENHBG106605.
InParanoidO95347.
KOK06674.
OMACQNGKIP.
OrthoDBEOG7SR4KV.
PhylomeDBO95347.
TreeFamTF101157.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressO95347.
BgeeO95347.
CleanExHS_SMC2.
GenevestigatorO95347.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERPTHR18937:SF9. PTHR18937:SF9. 1 hit.
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 2 hits.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSMC2. human.
GeneWikiSMC2.
GenomeRNAi10592.
NextBio40225.
PROO95347.
SOURCESearch...

Entry information

Entry nameSMC2_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM