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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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
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

WithEntry#Exp.IntActNotes
NCAPHQ150033EBI-355822,EBI-1046410
NCAPH2Q6IBW42EBI-355822,EBI-2548296
SMC4Q9NTJ33EBI-355822,EBI-356173

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115841. 78 interactors.
DIPiDIP-35422N.
IntActiO95347. 37 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.
OMAiCQNGKIP.
OrthoDBiEOG091G03K8.
PhylomeDBiO95347.
TreeFamiTF101157.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 1 hit.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 2 hits.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
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 rs4562395dbSNPEnsembl.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

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi115841. 78 interactors.
DIPiDIP-35422N.
IntActiO95347. 37 interactors.
MINTiMINT-1161754.
STRINGi9606.ENSP00000286398.

PTM databases

iPTMnetiO95347.
PhosphoSitePlusiO95347.

Polymorphism and mutation databases

BioMutaiSMC2.

Proteomic databases

EPDiO95347.
MaxQBiO95347.
PaxDbiO95347.
PeptideAtlasiO95347.
PRIDEiO95347.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi10592.
DisGeNETi10592.
GeneCardsiSMC2.
H-InvDBHIX0008250.
HGNCiHGNC:14011. SMC2.
HPAiHPA071309.
MalaCardsiSMC2.
MIMi605576. gene.
neXtProtiNX_O95347.
OpenTargetsiENSG00000136824.
PharmGKBiPA37833.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSMC2. human.
GeneWikiiSMC2.
GenomeRNAii10592.
PROiO95347.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF9. PTHR18937:SF9. 1 hit.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 2 hits.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC2_HUMAN
AccessioniPrimary (citable) accession number: O95347
Secondary accession number(s): Q6IEE0, Q9P1P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 148 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.