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Reviewed, UniProtKB/Swiss-Prot Q8CG48 (SMC2_MOUSE)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Structural maintenance of chromosomes protein 2
Alternative name(s):
    Chromosome-associated protein E
    XCAP-E homolog
    FGF-inducible protein 16
Gene names
Name: Smc2
Synonyms: Cape, Fin16, Smc2l1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 an 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. 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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA condensation
Mitosis
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic chromosome condensation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchromosome

Inferred from electronic annotation. Source: InterPro

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Wasf2Q8BH432EBI-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)

Experimental info

Sequence conflict621F → L in BAB28654. Ref.2
Sequence conflict621F → L in BAB31946. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CG48-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 582C937D019FD893

FASTA1,191134,273
        10         20         30         40         50         60 
MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG ISNLSQVRAS 

        70         80         90        100        110        120 
NFQDLVYKNG 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: 14660695] [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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-284.
Strain: C57BL/6J.
Tissue: Embryo.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 562-570, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"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: 8649829] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 801-1191.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ534939 mRNA. Translation: CAD59182.1.
AK013109 mRNA. Translation: BAB28654.1.
AK019977 mRNA. Translation: BAB31946.1.
U42385 mRNA. Translation: AAB08867.1. Different initiation.
IPIIPI00889938.
UniGeneMm.2999

3D structure databases

HSSPHSSP built from PDB template 1IC2 based on UniProtKB P04268.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8CG48. 1 interaction.

PTM databases

PhosphoSiteQ8CG48.

Genome annotation databases

EnsemblENSMUSG00000028312. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:106067. Smc2.

Phylogenomic databases

HOVERGENQ8CG48.

Gene expression databases

ArrayExpressQ8CG48.
BgeeQ8CG48.
CleanExMM_SMC2.
GermOnlineENSMUSG00000028312. Mus musculus.

Family and domain databases

InterProIPR003395. RecF/RecN/SMC_N.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameSMC2_MOUSE
AccessionPrimary (citable) accession number: Q8CG48
Secondary accession number(s): Q61076, Q9CS17, Q9CSD8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents