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Q8CG47

- SMC4_MOUSE

UniProt

Q8CG47 - SMC4_MOUSE

Protein

Structural maintenance of chromosomes protein 4

Gene

Smc4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 bindingi111 – 1188ATPSequence Analysis

    GO - Molecular functioni

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

    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: UniProtKB

    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 4
    Short name:
    SMC protein 4
    Short name:
    SMC-4
    Alternative name(s):
    Chromosome-associated polypeptide C
    XCAP-C homolog
    Gene namesi
    Name:Smc4
    Synonyms:Capc, Smc4l1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1917349. Smc4.

    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. condensin complex Source: Ensembl
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12861286Structural maintenance of chromosomes protein 4PRO_0000119008Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211PhosphoserineBy similarity
    Modified residuei27 – 271PhosphoserineBy similarity
    Modified residuei40 – 401PhosphoserineBy similarity
    Modified residuei141 – 1411PhosphoserineBy similarity
    Modified residuei379 – 3791N6-acetyllysine1 Publication
    Modified residuei677 – 6771N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8CG47.
    PaxDbiQ8CG47.
    PRIDEiQ8CG47.

    PTM databases

    PhosphoSiteiQ8CG47.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8CG47.
    BgeeiQ8CG47.
    CleanExiMM_SMC4.
    GenevestigatoriQ8CG47.

    Interactioni

    Subunit structurei

    Forms a heterodimer with SMC2. 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
    Yy1Q008992EBI-6921575,EBI-6921536

    Protein-protein interaction databases

    BioGridi213863. 1 interaction.
    IntActiQ8CG47. 1 interaction.

    Structurei

    Secondary structure

    1
    1286
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi596 – 60712
    Beta strandi608 – 6103
    Beta strandi613 – 6164
    Helixi617 – 6193
    Helixi625 – 6273
    Helixi628 – 6347
    Helixi636 – 6394
    Beta strandi640 – 6445
    Helixi646 – 65813
    Beta strandi666 – 6683
    Helixi669 – 6713
    Helixi673 – 6753
    Helixi685 – 6873
    Helixi691 – 6944
    Helixi700 – 71011
    Beta strandi714 – 7185
    Helixi719 – 7268
    Beta strandi735 – 7373
    Beta strandi749 – 7513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L51X-ray1.51B595-752[»]
    ProteinModelPortaliQ8CG47.
    SMRiQ8CG47. Positions 595-752.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8CG47.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni590 – 767178Flexible hingeAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili270 – 589320Sequence AnalysisAdd
    BLAST
    Coiled coili768 – 1018251Sequence AnalysisAdd
    BLAST
    Coiled coili1068 – 113366Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi64 – 696Poly-Pro
    Compositional biasi1189 – 122436Ala/Asp-rich (DA-box)Add
    BLAST

    Domaini

    The hinge domain, which separates the large intramolecular coiled coil regions, allows the heterodimerization with SMC2, forming a V-shaped heterodimer.By similarity

    Sequence similaritiesi

    Belongs to the SMC family. SMC4 subfamily.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1196.
    GeneTreeiENSGT00580000081617.
    HOGENOMiHOG000184777.
    HOVERGENiHBG106696.
    InParanoidiQ8CG47.
    KOiK06675.
    OMAiPSEEIDN.
    OrthoDBiEOG7RJPQJ.
    PhylomeDBiQ8CG47.
    TreeFamiTF101158.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR024704. SMC.
    IPR010935. SMC_hinge.
    [Graphical view]
    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.

    Q8CG47-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRKGTKPST ACHQEEGPPP SQDGAHSDEE MEQPAGEAES AAPAKPPGEE     50
    LDNRSLEEIL NSIPPPPPPA MASEAGAPRL MITHIVNQNF KSYAGEKVLG 100
    PFHKRFSCII GPNGSGKSNV IDSMLFVFGY RAQKIRSKKL SVLIHNSDEH 150
    KDIQSCTVEV HFQKIIDKEG DDYEVLPNSN FYVSRTAYRD STSVYHISGK 200
    KKTFKDVGNL LRSHGIDLDH NRFLILQGEV EQIAMMKPKG QTEHDEGMLE 250
    YLEDIIGCGR LNEPIKVLCR RVEILNEHRG EKLNRVKMVE KEKDALEGEK 300
    NIAIEFLTLE NEMFKKKNHI CQYYIYDLQN RIAEITTQKE KIHEDTKEIT 350
    EKSNVLSNEM KAKNSAVKDV EKKLNKVTKF IEQNKEKFTQ LDLEDVQVRE 400
    KLKHATSKAK KLEKQLQKDK EKVEELKSVP AKSKTVINET TTRNNSLEKE 450
    REKEEKKLKE VMDSLKQETQ GLQKEKEIQE KELMGFNKSV NEARSKMEVA 500
    QSELDIYLSR HNTAVSQLSK AKEALITASE TLKERKAAIK DINTKLPQTQ 550
    QELKEKEKEL QKLTQEEINL KSLVHDLFQK VEEAKSSLAM NRSRGKVLDA 600
    IIQEKKSGRI PGIYGRLGDL GAIDEKYDIA ISSCCHALDY IVVDSIDTAQ 650
    ECVNFLKKHN IGIATFIGLD KMTVWAKKMS KIQTPENTPR LFDLVKVKNE 700
    EIRQAFYFAL RDTLVANNLD QATRVAYQRD RRWRVVTLQG QIIEQSGTMS 750
    GGGSKVMRGR MGSSVIDEIS VEEVNKMESQ LERHSKQAMQ IQEQKVQHEE 800
    AVVKLRHSER DMRNTLEKFA ASIQGLSEQE EYLCVQIKEL EANVLTTAPD 850
    RKQQKLLEEN VSVFKKEYDA VAEKAGKVEA EIKRLHNTII DINNRKLKAQ 900
    QNKLDTINKQ LDECASAITK AQVAIKTADR NLKKAQDSVC RTEKEIKDTE 950
    KEINDLKTEL KNIEDKAEEV INNTKTAETS LPEIQKEHRN LLQELKVIQE 1000
    NEHALQKDAL SIKLKLEQID GHISEHNSKI KYWQKEISKI KLHPVEDNPV 1050
    ETVAVLSQEE LEAIKNPESI TNEIALLEAQ CREMKPNLGA IAEYKKKEDL 1100
    YLQRVAELDK ITSERDNFRQ AYEDLRKQRL NEFMAGFYVI TNKLKENYQM 1150
    LTLGGDAELE LVDSLDPFSE GIMFSVRPPK KSWKKIFNLS GGEKTLSSLA 1200
    LVFALHHYKP TPLYFMDEID AALDFKNVSI VAFYIYEQTK NAQFIIISLR 1250
    NNMFEISDRL IGIYKTYNST KSVAVNPKQI ASKGLC 1286
    Length:1,286
    Mass (Da):146,895
    Last modified:March 1, 2003 - v1
    Checksum:iCFEAD84199C3CEB5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti454 – 4541E → V in BAC40608. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ534940 mRNA. Translation: CAD59183.1.
    BC005507 mRNA. Translation: AAH05507.1.
    BC062939 mRNA. Translation: AAH62939.1.
    AK088350 mRNA. Translation: BAC40297.1.
    AK088846 mRNA. Translation: BAC40608.2.
    CCDSiCCDS17401.1.
    RefSeqiNP_598547.1. NM_133786.3.
    XP_006502108.1. XM_006502045.1.
    XP_006502109.1. XM_006502046.1.
    UniGeneiMm.206841.

    Genome annotation databases

    EnsembliENSMUST00000042901; ENSMUSP00000047872; ENSMUSG00000034349.
    GeneIDi70099.
    KEGGimmu:70099.
    UCSCiuc008pma.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ534940 mRNA. Translation: CAD59183.1 .
    BC005507 mRNA. Translation: AAH05507.1 .
    BC062939 mRNA. Translation: AAH62939.1 .
    AK088350 mRNA. Translation: BAC40297.1 .
    AK088846 mRNA. Translation: BAC40608.2 .
    CCDSi CCDS17401.1.
    RefSeqi NP_598547.1. NM_133786.3.
    XP_006502108.1. XM_006502045.1.
    XP_006502109.1. XM_006502046.1.
    UniGenei Mm.206841.

    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 B 595-752 [» ]
    ProteinModelPortali Q8CG47.
    SMRi Q8CG47. Positions 595-752.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213863. 1 interaction.
    IntActi Q8CG47. 1 interaction.

    PTM databases

    PhosphoSitei Q8CG47.

    Proteomic databases

    MaxQBi Q8CG47.
    PaxDbi Q8CG47.
    PRIDEi Q8CG47.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000042901 ; ENSMUSP00000047872 ; ENSMUSG00000034349 .
    GeneIDi 70099.
    KEGGi mmu:70099.
    UCSCi uc008pma.1. mouse.

    Organism-specific databases

    CTDi 10051.
    MGIi MGI:1917349. Smc4.

    Phylogenomic databases

    eggNOGi COG1196.
    GeneTreei ENSGT00580000081617.
    HOGENOMi HOG000184777.
    HOVERGENi HBG106696.
    InParanoidi Q8CG47.
    KOi K06675.
    OMAi PSEEIDN.
    OrthoDBi EOG7RJPQJ.
    PhylomeDBi Q8CG47.
    TreeFami TF101158.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi SMC4. mouse.
    EvolutionaryTracei Q8CG47.
    NextBioi 330998.
    PROi Q8CG47.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CG47.
    Bgeei Q8CG47.
    CleanExi MM_SMC4.
    Genevestigatori Q8CG47.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR024704. SMC.
    IPR010935. SMC_hinge.
    [Graphical view ]
    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 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 and C57BL/6J.
      Tissue: Brain and Mammary tumor.
    3. "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 1-602.
      Strain: NOD.
      Tissue: Thymus.
    4. "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-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSMC4_MOUSE
    AccessioniPrimary (citable) accession number: Q8CG47
    Secondary accession number(s): Q8BTS7, Q8BTY9, Q99K21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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