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UniProtKB - O95347 (SMC2_HUMAN)

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Protein

Structural maintenance of chromosomes protein 2

Gene

SMC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Biological processCell cycle, Cell division, DNA condensation, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SMC2
Synonyms:CAPE, SMC2L1
ORF Names:PRO0324
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:14011. SMC2.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Chromosome 1 Publication

    • 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.

GO - Cellular componenti

  • condensed chromosome Source: UniProtKB
  • condensin complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nuclear chromosome Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi10592.
MalaCardsiSMC2.
OpenTargetsiENSG00000136824.
PharmGKBiPA37833.

Polymorphism and mutation databases

BioMutaiSMC2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001189951 – 1197Structural maintenance of chromosomes protein 2Add BLAST1197

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei114N6-acetyllysineCombined sources1
Modified residuei222N6-acetyllysineCombined sources1
Modified residuei677N6-acetyllysineCombined sources1
Modified residuei1158N6-acetyllysineCombined sources1
Modified residuei1160N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO95347.
MaxQBiO95347.
PaxDbiO95347.
PeptideAtlasiO95347.
PRIDEiO95347.

PTM databases

iPTMnetiO95347.
PhosphoSitePlusiO95347.

Expressioni

Gene expression databases

BgeeiENSG00000136824.
CleanExiHS_SMC2.
ExpressionAtlasiO95347. baseline and differential.
GenevisibleiO95347. HS.

Organism-specific databases

HPAiHPA071309.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi115841. 79 interactors.
DIPiDIP-35422N.
IntActiO95347. 35 interactors.
MINTiMINT-1161754.
STRINGi9606.ENSP00000286398.

Structurei

Secondary structure

11197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi476 – 502Combined sources27
Helixi504 – 506Combined sources3
Helixi519 – 521Combined sources3
Beta strandi522 – 525Combined sources4
Helixi526 – 529Combined sources4
Beta strandi531 – 533Combined sources3
Helixi535 – 537Combined sources3
Helixi538 – 545Combined sources8
Helixi546 – 550Combined sources5
Beta strandi552 – 555Combined sources4
Helixi557 – 566Combined sources10
Beta strandi573 – 577Combined sources5
Turni578 – 580Combined sources3
Helixi588 – 598Combined sources11
Beta strandi602 – 605Combined sources4
Helixi606 – 609Combined sources4
Helixi614 – 616Combined sources3
Helixi617 – 624Combined sources8
Beta strandi628 – 632Combined sources5
Helixi633 – 640Combined sources8
Turni643 – 645Combined sources3
Beta strandi649 – 651Combined sources3
Beta strandi656 – 658Combined sources3
Turni659 – 661Combined sources3
Beta strandi662 – 666Combined sources5
Helixi674 – 704Combined sources31

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U4PX-ray1.89A476-707[»]
ProteinModelPortaliO95347.
SMRiO95347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni508 – 671Flexible hingeAdd BLAST164

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili173 – 507Sequence analysisAdd BLAST335
Coiled coili672 – 926Sequence analysisAdd BLAST255
Coiled coili963 – 1031Sequence analysisAdd BLAST69

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1085 – 1120Ala/Asp-rich (DA-box)Add BLAST36

Domaini

The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC4, forming a V-shaped heterodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC2 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0933. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00550000074857.
HOGENOMiHOG000228249.
HOVERGENiHBG106605.
InParanoidiO95347.
KOiK06674.
OMAiHNKIAME.
OrthoDBiEOG091G03K8.
PhylomeDBiO95347.
TreeFamiTF101157.

Family and domain databases

CDDicd03273. ABC_SMC2_euk. 1 hit.
InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2_ABC.
IPR010935. SMC_hinge.
PfamiView protein in Pfam
PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 2 hits.
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiView protein in SMART
SM00968. SMC_hinge. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95347-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG 
        60         70         80         90        100
ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE 
       110        120        130        140        150
ITVTRQVVIG GRNKYLINGV NANNTRVQDL FCSVGLNVNN PHFLIMQGRI 
       160        170        180        190        200
TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA AQKTIEKKEA KLKEIKTILE 
       210        220        230        240        250
EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL LAEDTKVRSA 
       260        270        280        290        300
EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE 
       310        320        330        340        350
DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK 
       360        370        380        390        400
EVKKITDGLH ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG 
       410        420        430        440        450
QMMACKNDIS KAQTEAKQAQ MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA 
       460        470        480        490        500
LEAVKRLKEK LEAEMKKLNY EENKEESLLE KRRQLSRDIG RLKETYEALL 
       510        520        530        540        550
ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA LELVAGERLY 
       560        570        580        590        600
NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP 
       610        620        630        640        650
DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV 
       660        670        680        690        700
TLGGDVFDPH GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE 
       710        720        730        740        750
ELAGLKNTAE KYRQLKQQWE MKTEEADLLQ TKLQQSSYHK QQEELDALKK 
       760        770        780        790        800
TIEESEETLK NTKEIQRKAE EKYEVLENKM KNAEAERERE LKDAQKKLDC 
       810        820        830        840        850
AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL EAVNEAIKSY 
       860        870        880        890        900
ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK 
       910        920        930        940        950
EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ 
       960        970        980        990       1000
PNSAYDFKTN NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND 
      1010       1020       1030       1040       1050
LMKKKRIVEN DKSKILTTIE DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP 
      1060       1070       1080       1090       1100
GANAMLAPPE GQTVLDGLEF KVALGNTWKE NLTELSGGQR SLVALSLILS 
      1110       1120       1130       1140       1150
MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF IVVSLKEGMF 
      1160       1170       1180       1190 
NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV
Length:1,197
Mass (Da):135,656
Last modified:November 25, 2008 - v2
Checksum:i15EBB56B31FC1364
GO
Isoform 2 (identifier: O95347-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:1,099
Mass (Da):124,926
Checksum:i68BB895EA6EBA265
GO

Sequence cautioni

The sequence AAC72360 differs from that shown. Reason: Frameshift at positions 890 and 908.Curated
The sequence AAF29579 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti294G → V in AAC72360 (PubMed:9789013).Curated1
Sequence conflicti916N → H in AAC72360 (PubMed:9789013).Curated1
Sequence conflicti998Y → C in AAC72360 (PubMed:9789013).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0474891009E → K. Corresponds to variant dbSNP:rs4562395Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0072431091 – 1099SLVALSLIL → QKQQNHTTG in isoform 2. 1 Publication9
Alternative sequenceiVSP_0072441100 – 1197Missing in isoform 2. 1 PublicationAdd BLAST98

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35086.1. [O95347-1]
RefSeqiNP_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_006716933.3. [O95347-1]
XP_011516450.1. XM_011518148.2. [O95347-1]
XP_011516451.1. XM_011518149.2. [O95347-1]
XP_011516455.1. XM_011518153.1. [O95347-2]
XP_016869695.1. XM_017014206.1. [O95347-1]
XP_016869696.1. XM_017014207.1. [O95347-1]
XP_016869697.1. XM_017014208.1. [O95347-1]
UniGeneiHs.119023.

Genome annotation databases

EnsembliENST00000286398; ENSP00000286398; ENSG00000136824. [O95347-1]
ENST00000374787; ENSP00000363919; ENSG00000136824. [O95347-1]
ENST00000374793; ENSP00000363925; ENSG00000136824. [O95347-1]
GeneIDi10592.
KEGGihsa:10592.
UCSCiuc004bbw.4. human. [O95347-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSMC2_HUMAN
AccessioniPrimary (citable) accession number: O95347
Secondary accession number(s): Q6IEE0, Q9P1P2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 25, 2008
Last modified: August 30, 2017
This is version 154 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families