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Q8CG48

- SMC2_MOUSE

UniProt

Q8CG48 - SMC2_MOUSE

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Protein

Structural maintenance of chromosomes protein 2

Gene

Smc2

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

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).By similarity

GO - Cellular componenti

  1. condensed chromosome Source: MGI
  2. condensin complex Source: InterPro
  3. cytoplasm Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: Ensembl
  5. 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-acetyllysineBy similarity
Modified residuei222 – 2221N6-acetyllysineBy similarity
Modified residuei677 – 6771N6-acetyllysineBy similarity
Modified residuei1158 – 11581N6-acetyllysineBy similarity
Modified residuei1160 – 11601N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8CG48.
PaxDbiQ8CG48.
PRIDEiQ8CG48.

PTM databases

PhosphoSiteiQ8CG48.

Expressioni

Gene expression databases

BgeeiQ8CG48.
CleanExiMM_SMC2.
ExpressionAtlasiQ8CG48. baseline and differential.
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).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 – 5213Combined sources
Beta strandi522 – 5254Combined sources
Helixi526 – 5283Combined sources
Beta strandi531 – 5333Combined sources
Helixi535 – 5373Combined sources
Helixi538 – 5458Combined sources
Helixi546 – 5505Combined sources
Beta strandi552 – 5554Combined sources
Helixi557 – 56610Combined sources
Beta strandi573 – 5775Combined sources
Turni578 – 5803Combined sources
Helixi588 – 59811Combined sources
Beta strandi602 – 6054Combined sources
Helixi606 – 6094Combined sources
Helixi614 – 6163Combined sources
Helixi617 – 6248Combined sources
Beta strandi628 – 6325Combined sources
Helixi633 – 6419Combined sources
Turni643 – 6453Combined sources
Beta strandi649 – 6513Combined sources

3D structure databases

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

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 – 507335Sequence AnalysisAdd
BLAST
Coiled coili672 – 936265Sequence AnalysisAdd
BLAST
Coiled coili963 – 103169Sequence AnalysisAdd
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.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00550000074857.
HOVERGENiHBG106605.
InParanoidiQ8CG48.
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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621L → F in CAD59182. (PubMed:14660695)Curated

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.1. mouse.

Cross-referencesi

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.
CCDSi CCDS18180.1.
RefSeqi NP_001288341.1. NM_001301412.1.
NP_032043.3. NM_008017.4.
UniGenei Mm.2999.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 Q8CG48.
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

Bgeei Q8CG48.
CleanExi MM_SMC2.
ExpressionAtlasi Q8CG48. baseline and differential.
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: November 26, 2014
This is version 103 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