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Protein

Structural maintenance of chromosomes protein 2

Gene

Smc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • kinetochore organization Source: MGI
  • meiotic chromosome condensation Source: MGI
  • meiotic chromosome segregation Source: MGI
  • mitotic chromosome condensation Source: MGI

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-2299718 Condensation of Prophase Chromosomes
R-MMU-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
FGF-inducible protein 16
XCAP-E homolog
Gene namesi
Name:Smc2
Synonyms:Cape, Fin16, Smc2l1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:106067 Smc2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001189961 – 1191Structural maintenance of chromosomes protein 2Add BLAST1191

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei114N6-acetyllysineBy similarity1
Modified residuei222N6-acetyllysineBy similarity1
Modified residuei677N6-acetyllysineBy similarity1
Modified residuei1158N6-acetyllysineBy similarity1
Modified residuei1160N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8CG48
MaxQBiQ8CG48
PaxDbiQ8CG48
PeptideAtlasiQ8CG48
PRIDEiQ8CG48

PTM databases

iPTMnetiQ8CG48
PhosphoSitePlusiQ8CG48
SwissPalmiQ8CG48

Expressioni

Gene expression databases

BgeeiENSMUSG00000028312
CleanExiMM_SMC2
ExpressionAtlasiQ8CG48 baseline and differential
GenevisibleiQ8CG48 MM

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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Wasf2Q8BH434EBI-643436,EBI-643162

GO - Molecular functioni

Protein-protein interaction databases

BioGridi1996775 interactors.
CORUMiQ8CG48
IntActiQ8CG48 3 interactors.
STRINGi10090.ENSMUSP00000099979

Structurei

Secondary structure

11191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi519 – 521Combined sources3
Beta strandi522 – 525Combined sources4
Helixi526 – 528Combined sources3
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 – 641Combined sources9
Turni643 – 645Combined sources3
Beta strandi649 – 651Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51A506-666[»]
ProteinModelPortaliQ8CG48
SMRiQ8CG48
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CG48

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 – 936Sequence analysisAdd BLAST265
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
HOVERGENiHBG106605
InParanoidiQ8CG48
KOiK06674
OMAiHNKIAME
OrthoDBiEOG091G03K8
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
IPR036277 SMC_hinge_sf
PfamiView protein in Pfam
PF06470 SMC_hinge, 1 hit
PF02463 SMC_N, 1 hit
PIRSFiPIRSF005719 SMC, 1 hit
SMARTiView protein in SMART
SM00968 SMC_hinge, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF75553 SSF75553, 1 hit

Sequencei

Sequence statusi: Complete.

Q8CG48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG
60 70 80 90 100
ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEAHDE
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 RAEDTKERSA
260 270 280 290 300
GELKEMQDKI VNLQEVLSEN EKKIKALNCE IEELERRKDK ETGGKLKSLE
310 320 330 340 350
DACAEAQRVN TKSQSAFDLK KKNLASEETK RKELQNSMAE DSKALAAKEK
360 370 380 390 400
EVKKITDGLH GLQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG
410 420 430 440 450
QMIACKNDIS KAQTEAKQAQ MKLKHAQQEL KSKQAEVKKM DSGYKKDQDA
460 470 480 490 500
FEAVKKAKEK LETEMKKLNY EENKEEKLLE KHRQLSRDIN NLKGKHEALL
510 520 530 540 550
AKFPNLQFAY KDPEKNWNRN SVKGLVASLI NVKDNSTATA LEVVAGERLY
560 570 580 590 600
NVVVDTEVTA KKLLEKGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP
610 620 630 640 650
DNVHVALSLV DYKPELQKGM EFVFGTTFVC NNMDNAKKVA FDKRIMTRTV
660 670 680 690 700
TLGGDVFDPH GTLSGGARSQ AASILTKFQE VKDVQDELRT KENELRALEE
710 720 730 740 750
ELAGLKNVAE KYRQLKQQWE MKTEEGDLLQ TKLQQSSYHK QQEELDALKK
760 770 780 790 800
TIEESEETLK STKEIQKKAE EKYEALENKM KNAEAEREKE LKDAQKKLDC
810 820 830 840 850
AKTKADASSK KMKEKQQEVE AITLELEELK REHASNEQQL DAVNEAIKAY
860 870 880 890 900
EGQIEKMAAE VAKNKESVNK AQDELMKQKQ IITAQDNIIK DKCAEVAKHN
910 920 930 940 950
LQNNESQLKI KELDHSISKH KREADDAAAK VSKMLSDYDW INAEKHLFGQ
960 970 980 990 1000
PNSAYDFKTN NPKEAGQRLQ KLQEVKEKLG RNVNLRAMNV LTEAEERYND
1010 1020 1030 1040 1050
LMKKKRIVEN DKSKILATIE 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 FTQSQAGKIP KEAKSRGKEP N
Length:1,191
Mass (Da):134,239
Last modified:July 27, 2011 - v2
Checksum:i56CC351A7855D0BB
GO

Sequence cautioni

The sequence AAB08867 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti62L → F in CAD59182 (PubMed:14660695).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ534939 mRNA Translation: CAD59182.1
AK013109 mRNA Translation: BAB28654.1
AK019977 mRNA Translation: BAB31946.1
AL732619 Genomic DNA Translation: CAM14006.1
CH466565 Genomic DNA Translation: EDL02299.1
BC094380 mRNA Translation: AAH94380.1
U42385 mRNA Translation: AAB08867.1 Different initiation.
CCDSiCCDS18180.1
RefSeqiNP_001288341.1, NM_001301412.1
NP_032043.3, NM_008017.4
UniGeneiMm.2999

Genome annotation databases

EnsembliENSMUST00000102915; ENSMUSP00000099979; ENSMUSG00000028312
ENSMUST00000117280; ENSMUSP00000113940; ENSMUSG00000028312
GeneIDi14211
KEGGimmu:14211
UCSCiuc008swk.2 mouse

Similar proteinsi

Entry informationi

Entry nameiSMC2_MOUSE
AccessioniPrimary (citable) accession number: Q8CG48
Secondary accession number(s): Q52KE9
, Q61076, Q9CS17, Q9CSD8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: July 27, 2011
Last modified: March 28, 2018
This is version 132 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome