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Q8CG48 (SMC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
FGF-inducible protein 16
XCAP-E homolog
Gene names
Name:Smc2
Synonyms:Cape, Fin16, Smc2l1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1191 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 By similarity.

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 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Chromosome By similarity. 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 By similarity.

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 AAB08867.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Wasf2Q8BH434EBI-643436,EBI-643162

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11911191Structural maintenance of chromosomes protein 2
PRO_0000118996

Regions

Nucleotide binding32 – 398ATP Potential
Region508 – 671164Flexible hinge
Coiled coil173 – 507335 Potential
Coiled coil672 – 936265 Potential
Coiled coil963 – 103169 Potential
Compositional bias1085 – 112036Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue1141N6-acetyllysine By similarity
Modified residue2221N6-acetyllysine By similarity
Modified residue6771N6-acetyllysine By similarity
Modified residue11581N6-acetyllysine By similarity
Modified residue11601N6-acetyllysine Ref.8

Experimental info

Sequence conflict621L → F in CAD59182. Ref.1

Secondary structure

................................. 1191
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CG48 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 56CC351A7855D0BB

FASTA1,191134,239
        10         20         30         40         50         60 
MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS 

        70         80         90        100        110        120 
NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEAHDE 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 
RAEDTKERSA GELKEMQDKI VNLQEVLSEN EKKIKALNCE IEELERRKDK ETGGKLKSLE 

       310        320        330        340        350        360 
DACAEAQRVN TKSQSAFDLK KKNLASEETK RKELQNSMAE DSKALAAKEK EVKKITDGLH 

       370        380        390        400        410        420 
GLQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG QMIACKNDIS KAQTEAKQAQ 

       430        440        450        460        470        480 
MKLKHAQQEL KSKQAEVKKM DSGYKKDQDA FEAVKKAKEK LETEMKKLNY EENKEEKLLE 

       490        500        510        520        530        540 
KHRQLSRDIN NLKGKHEALL AKFPNLQFAY KDPEKNWNRN SVKGLVASLI NVKDNSTATA 

       550        560        570        580        590        600 
LEVVAGERLY NVVVDTEVTA KKLLEKGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP 

       610        620        630        640        650        660 
DNVHVALSLV DYKPELQKGM EFVFGTTFVC NNMDNAKKVA FDKRIMTRTV TLGGDVFDPH 

       670        680        690        700        710        720 
GTLSGGARSQ AASILTKFQE VKDVQDELRT KENELRALEE ELAGLKNVAE KYRQLKQQWE 

       730        740        750        760        770        780 
MKTEEGDLLQ TKLQQSSYHK QQEELDALKK TIEESEETLK STKEIQKKAE EKYEALENKM 

       790        800        810        820        830        840 
KNAEAEREKE LKDAQKKLDC AKTKADASSK KMKEKQQEVE AITLELEELK REHASNEQQL 

       850        860        870        880        890        900 
DAVNEAIKAY EGQIEKMAAE VAKNKESVNK AQDELMKQKQ IITAQDNIIK DKCAEVAKHN 

       910        920        930        940        950        960 
LQNNESQLKI KELDHSISKH KREADDAAAK VSKMLSDYDW INAEKHLFGQ PNSAYDFKTN 

       970        980        990       1000       1010       1020 
NPKEAGQRLQ KLQEVKEKLG RNVNLRAMNV LTEAEERYND LMKKKRIVEN DKSKILATIE 

      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 FTQSQAGKIP KEAKSRGKEP N 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-284.
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-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].
Strain: C57BL/6.
Tissue: Brain.
[6]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 562-570, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[7]"Induction of expression of growth-related genes by FGF-4 in mouse fibroblasts."
Guthridge M.A., Seldin M., Basilico C.
Oncogene 12:1267-1278(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 801-1191.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_032043.3. NM_008017.3.
XP_006537673.1. XM_006537610.1.
UniGeneMm.2999.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51A506-666[»]
ProteinModelPortalQ8CG48.
SMRQ8CG48. Positions 1-170, 462-688, 945-1169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199677. 2 interactions.
IntActQ8CG48. 1 interaction.
MINTMINT-1748639.

PTM databases

PhosphoSiteQ8CG48.

Proteomic databases

PaxDbQ8CG48.
PRIDEQ8CG48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102915; ENSMUSP00000099979; ENSMUSG00000028312.
ENSMUST00000117280; ENSMUSP00000113940; ENSMUSG00000028312.
GeneID14211.
KEGGmmu:14211.
UCSCuc008swk.1. mouse.

Organism-specific databases

CTD10592.
MGIMGI:106067. Smc2.

Phylogenomic databases

eggNOGCOG1196.
GeneTreeENSGT00550000074857.
HOVERGENHBG106605.
InParanoidQ52KE9.
KOK06674.
OMACQNGKIP.
OrthoDBEOG7SR4KV.
TreeFamTF101157.

Gene expression databases

ArrayExpressQ8CG48.
BgeeQ8CG48.
CleanExMM_SMC2.
GenevestigatorQ8CG48.

Family and domain databases

Gene3D3.40.50.300. 4 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. 1 hit.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8CG48.
NextBio285461.
PROQ8CG48.
SOURCESearch...

Entry information

Entry nameSMC2_MOUSE
AccessionPrimary (citable) accession number: Q8CG48
Secondary accession number(s): Q52KE9 expand/collapse secondary AC list , Q61076, Q9CS17, Q9CSD8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot