SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8CG48

- SMC2_MOUSE

UniProt

Q8CG48 - SMC2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Structural maintenance of chromosomes protein 2

Gene
Smc2, Cape, Fin16, Smc2l1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: IntAct

GO - Biological processi

  1. kinetochore organization Source: MGI
  2. meiotic chromosome condensation Source: MGI
  3. meiotic chromosome segregation Source: MGI
  4. mitotic chromosome condensation Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA condensation, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196580. Condensation of Prophase Chromosomes.
REACT_196632. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:106067. Smc2.

Subcellular locationi

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.

GO - Cellular componenti

  1. condensed chromosome Source: MGI
  2. condensin complex Source: InterPro
  3. cytoplasm Source: UniProtKB-SubCell
  4. nuclear chromosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11911191Structural maintenance of chromosomes protein 2PRO_0000118996Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N6-acetyllysine By similarity
Modified residuei222 – 2221N6-acetyllysine By similarity
Modified residuei677 – 6771N6-acetyllysine By similarity
Modified residuei1158 – 11581N6-acetyllysine By similarity
Modified residuei1160 – 11601N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8CG48.
PaxDbiQ8CG48.
PRIDEiQ8CG48.

PTM databases

PhosphoSiteiQ8CG48.

Expressioni

Gene expression databases

ArrayExpressiQ8CG48.
BgeeiQ8CG48.
CleanExiMM_SMC2.
GenevestigatoriQ8CG48.

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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199677. 3 interactions.
IntActiQ8CG48. 1 interaction.
MINTiMINT-1748639.

Structurei

Secondary structure

1
1191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi519 – 5213
Beta strandi522 – 5254
Helixi526 – 5283
Beta strandi531 – 5333
Helixi535 – 5373
Helixi538 – 5458
Helixi546 – 5505
Beta strandi552 – 5554
Helixi557 – 56610
Beta strandi573 – 5775
Turni578 – 5803
Helixi588 – 59811
Beta strandi602 – 6054
Helixi606 – 6094
Helixi614 – 6163
Helixi617 – 6248
Beta strandi628 – 6325
Helixi633 – 6419
Turni643 – 6453
Beta strandi649 – 6513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L51X-ray1.51A506-666[»]
ProteinModelPortaliQ8CG48.
SMRiQ8CG48. Positions 2-195, 462-688, 945-1176.

Miscellaneous databases

EvolutionaryTraceiQ8CG48.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni508 – 671164Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili173 – 507335 Reviewed predictionAdd
BLAST
Coiled coili672 – 936265 Reviewed predictionAdd
BLAST
Coiled coili963 – 103169 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1085 – 112036Ala/Asp-rich (DA-box)Add
BLAST

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.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00550000074857.
HOVERGENiHBG106605.
InParanoidiQ52KE9.
KOiK06674.
OMAiCQNGKIP.
OrthoDBiEOG7SR4KV.
TreeFamiTF101157.

Family and domain databases

Gene3Di3.40.50.300. 4 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. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8CG48-1 [UniParc]FASTAAdd to Basket

« Hide

MYVKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG     50
ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEAHDE 100
ITVTRQVVIG GRNKYLINGV NANNTRVQDL FCSVGLNVNN PHFLIMQGRI 150
TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA AQKTIEKKEA KLKEIKTILE 200
EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL RAEDTKERSA 250
GELKEMQDKI VNLQEVLSEN EKKIKALNCE IEELERRKDK ETGGKLKSLE 300
DACAEAQRVN TKSQSAFDLK KKNLASEETK RKELQNSMAE DSKALAAKEK 350
EVKKITDGLH GLQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG 400
QMIACKNDIS KAQTEAKQAQ MKLKHAQQEL KSKQAEVKKM DSGYKKDQDA 450
FEAVKKAKEK LETEMKKLNY EENKEEKLLE KHRQLSRDIN NLKGKHEALL 500
AKFPNLQFAY KDPEKNWNRN SVKGLVASLI NVKDNSTATA LEVVAGERLY 550
NVVVDTEVTA KKLLEKGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP 600
DNVHVALSLV DYKPELQKGM EFVFGTTFVC NNMDNAKKVA FDKRIMTRTV 650
TLGGDVFDPH GTLSGGARSQ AASILTKFQE VKDVQDELRT KENELRALEE 700
ELAGLKNVAE KYRQLKQQWE MKTEEGDLLQ TKLQQSSYHK QQEELDALKK 750
TIEESEETLK STKEIQKKAE EKYEALENKM KNAEAEREKE LKDAQKKLDC 800
AKTKADASSK KMKEKQQEVE AITLELEELK REHASNEQQL DAVNEAIKAY 850
EGQIEKMAAE VAKNKESVNK AQDELMKQKQ IITAQDNIIK DKCAEVAKHN 900
LQNNESQLKI KELDHSISKH KREADDAAAK VSKMLSDYDW INAEKHLFGQ 950
PNSAYDFKTN NPKEAGQRLQ KLQEVKEKLG RNVNLRAMNV LTEAEERYND 1000
LMKKKRIVEN DKSKILATIE DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP 1050
GANAMLAPPE GQTVLDGLEF KVALGNTWKE NLTELSGGQR SLVALSLILS 1100
MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF IVVSLKEGMF 1150
NNANVLFKTK FVDGVSTVAR FTQSQAGKIP KEAKSRGKEP N 1191
Length:1,191
Mass (Da):134,239
Last modified:July 27, 2011 - v2
Checksum:i56CC351A7855D0BB
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621L → F in CAD59182. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_032043.3. NM_008017.3.
XP_006537673.1. XM_006537610.1.
UniGeneiMm.2999.

Genome annotation databases

EnsembliENSMUST00000102915; ENSMUSP00000099979; ENSMUSG00000028312.
ENSMUST00000117280; ENSMUSP00000113940; ENSMUSG00000028312.
GeneIDi14211.
KEGGimmu:14211.
UCSCiuc008swk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS18180.1.
RefSeqi NP_032043.3. NM_008017.3.
XP_006537673.1. XM_006537610.1.
UniGenei Mm.2999.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L51 X-ray 1.51 A 506-666 [» ]
ProteinModelPortali Q8CG48.
SMRi Q8CG48. Positions 2-195, 462-688, 945-1176.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199677. 3 interactions.
IntActi Q8CG48. 1 interaction.
MINTi MINT-1748639.

PTM databases

PhosphoSitei Q8CG48.

Proteomic databases

MaxQBi Q8CG48.
PaxDbi Q8CG48.
PRIDEi Q8CG48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102915 ; ENSMUSP00000099979 ; ENSMUSG00000028312 .
ENSMUST00000117280 ; ENSMUSP00000113940 ; ENSMUSG00000028312 .
GeneIDi 14211.
KEGGi mmu:14211.
UCSCi uc008swk.1. mouse.

Organism-specific databases

CTDi 10592.
MGIi MGI:106067. Smc2.

Phylogenomic databases

eggNOGi COG1196.
GeneTreei ENSGT00550000074857.
HOVERGENi HBG106605.
InParanoidi Q52KE9.
KOi K06674.
OMAi CQNGKIP.
OrthoDBi EOG7SR4KV.
TreeFami TF101157.

Enzyme and pathway databases

Reactomei REACT_196580. Condensation of Prophase Chromosomes.
REACT_196632. Condensation of Prometaphase Chromosomes.

Miscellaneous databases

EvolutionaryTracei Q8CG48.
NextBioi 285461.
PROi Q8CG48.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CG48.
Bgeei Q8CG48.
CleanExi MM_SMC2.
Genevestigatori Q8CG48.

Family and domain databases

Gene3Di 3.40.50.300. 4 hits.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR027120. Smc2.
IPR010935. SMC_hinge.
[Graphical view ]
PANTHERi PTHR18937:SF9. PTHR18937:SF9. 1 hit.
Pfami PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF005719. SMC. 1 hit.
SMARTi SM00968. SMC_hinge. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSMC2_MOUSE
AccessioniPrimary (citable) accession number: Q8CG48
Secondary accession number(s): Q52KE9
, Q61076, Q9CS17, Q9CSD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 100 of the entry and version 2 of the sequence. [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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi