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Q8CG48

- SMC2_MOUSE

UniProt

Q8CG48 - SMC2_MOUSE

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
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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
    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

    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-SubCell
    4. nuclear chromosome Source: Ensembl

    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

    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.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.
    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.
    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.

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 101 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