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O95347

- SMC2_HUMAN

UniProt

O95347 - SMC2_HUMAN

Protein

Structural maintenance of chromosomes protein 2

Gene

SMC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      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.1 Publication

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. kinetochore organization Source: Ensembl
    2. meiotic chromosome condensation Source: Ensembl
    3. meiotic chromosome segregation Source: Ensembl
    4. mitotic cell cycle Source: Reactome
    5. 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_150260. Condensation of Prometaphase Chromosomes.
    REACT_172744. Condensation of Prophase 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
    Short name:
    hCAP-E
    XCAP-E homolog
    Gene namesi
    Name:SMC2
    Synonyms:CAPE, SMC2L1
    ORF Names:PRO0324
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:14011. SMC2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Chromosome 1 Publication
    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.

    GO - Cellular componenti

    1. condensed chromosome Source: UniProtKB
    2. condensin complex Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. nuclear chromosome Source: UniProtKB
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37833.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11971197Structural maintenance of chromosomes protein 2PRO_0000118995Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO95347.
    PaxDbiO95347.
    PRIDEiO95347.

    PTM databases

    PhosphoSiteiO95347.

    Expressioni

    Gene expression databases

    ArrayExpressiO95347.
    BgeeiO95347.
    CleanExiHS_SMC2.
    GenevestigatoriO95347.

    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. Interacts with BRD4 (isoform B), leading to insulate chromatin from DNA damage response pathway.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NCAPHQ150032EBI-355822,EBI-1046410
    NCAPH2Q6IBW42EBI-355822,EBI-2548296
    SMC4Q9NTJ33EBI-355822,EBI-356173

    Protein-protein interaction databases

    BioGridi115841. 38 interactions.
    DIPiDIP-35422N.
    IntActiO95347. 15 interactions.
    MINTiMINT-1161754.
    STRINGi9606.ENSP00000286398.

    Structurei

    3D structure databases

    ProteinModelPortaliO95347.
    SMRiO95347. Positions 1-273, 462-688, 945-1172.
    ModBaseiSearch...
    MobiDBiSearch...

    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 – 926255Sequence 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.
    HOGENOMiHOG000228249.
    HOVERGENiHBG106605.
    InParanoidiO95347.
    KOiK06674.
    OMAiCQNGKIP.
    OrthoDBiEOG7SR4KV.
    PhylomeDBiO95347.
    TreeFamiTF101157.

    Family and domain databases

    Gene3Di3.40.50.300. 3 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. 2 hits.
    [Graphical view]
    PIRSFiPIRSF005719. SMC. 1 hit.
    SMARTiSM00968. SMC_hinge. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF75553. SSF75553. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95347-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MHIKSIILEG FKSYAQRTEV NGFDPLFNAI TGLNGSGKSN ILDSICFLLG     50
    ISNLSQVRAS NLQDLVYKNG QAGITKASVS ITFDNSDKKQ SPLGFEVHDE 100
    ITVTRQVVIG GRNKYLINGV NANNTRVQDL FCSVGLNVNN PHFLIMQGRI 150
    TKVLNMKPPE ILSMIEEAAG TRMYEYKKIA AQKTIEKKEA KLKEIKTILE 200
    EEITPTIQKL KEERSSYLEY QKVMREIEHL SRLYIAYQFL LAEDTKVRSA 250
    EELKEMQDKV IKLQEELSEN DKKIKALNHE IEELEKRKDK ETGGILRSLE 300
    DALAEAQRVN TKSQSAFDLK KKNLACEESK RKELEKNMVE DSKTLAAKEK 350
    EVKKITDGLH ALQEASNKDA EALAAAQQHF NAVSAGLSSN EDGAEATLAG 400
    QMMACKNDIS KAQTEAKQAQ MKLKHAQQEL KNKQAEVKKM DSGYRKDQEA 450
    LEAVKRLKEK LEAEMKKLNY EENKEESLLE KRRQLSRDIG RLKETYEALL 500
    ARFPNLRFAY KDPEKNWNRN CVKGLVASLI SVKDTSATTA LELVAGERLY 550
    NVVVDTEVTG KKLLERGELK RRYTIIPLNK ISARCIAPET LRVAQNLVGP 600
    DNVHVALSLV EYKPELQKAM EFVFGTTFVC DNMDNAKKVA FDKRIMTRTV 650
    TLGGDVFDPH GTLSGGARSQ AASILTKFQE LKDVQDELRI KENELRALEE 700
    ELAGLKNTAE KYRQLKQQWE MKTEEADLLQ TKLQQSSYHK QQEELDALKK 750
    TIEESEETLK NTKEIQRKAE EKYEVLENKM KNAEAERERE LKDAQKKLDC 800
    AKTKADASSK KMKEKQQEVE AITLELEELK REHTSYKQQL EAVNEAIKSY 850
    ESQIEVMAAE VAKNKESVNK AQEEVTKQKE VITAQDTVIK AKYAEVAKHK 900
    EQNNDSQLKI KELDHNISKH KREAEDGAAK VSKMLKDYDW INAERHLFGQ 950
    PNSAYDFKTN NPKEAGQRLQ KLQEMKEKLG RNVNMRAMNV LTEAEERYND 1000
    LMKKKRIVEN DKSKILTTIE DLDQKKNQAL NIAWQKVNKD FGSIFSTLLP 1050
    GANAMLAPPE GQTVLDGLEF KVALGNTWKE NLTELSGGQR SLVALSLILS 1100
    MLLFKPAPIY ILDEVDAALD LSHTQNIGQM LRTHFTHSQF IVVSLKEGMF 1150
    NNANVLFKTK FVDGVSTVAR FTQCQNGKIS KEAKSKAKPP KGAHVEV 1197
    Length:1,197
    Mass (Da):135,656
    Last modified:November 25, 2008 - v2
    Checksum:i15EBB56B31FC1364
    GO
    Isoform 2 (identifier: O95347-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1091-1099: SLVALSLIL → QKQQNHTTG
         1100-1197: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,099
    Mass (Da):124,926
    Checksum:i68BB895EA6EBA265
    GO

    Sequence cautioni

    The sequence AAC72360.1 differs from that shown. Reason: Frameshift at positions 890 and 908.
    The sequence AAF29579.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941G → V in AAC72360. (PubMed:9789013)Curated
    Sequence conflicti916 – 9161N → H in AAC72360. (PubMed:9789013)Curated
    Sequence conflicti998 – 9981Y → C in AAC72360. (PubMed:9789013)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1009 – 10091E → K.
    Corresponds to variant rs4562395 [ dbSNP | Ensembl ].
    VAR_047489

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1091 – 10999SLVALSLIL → QKQQNHTTG in isoform 2. 1 PublicationVSP_007243
    Alternative sequencei1100 – 119798Missing in isoform 2. 1 PublicationVSP_007244Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092563 mRNA. Translation: AAC72360.1. Frameshift.
    AL833191 mRNA. Translation: CAI46187.1.
    AL161791, AL354938 Genomic DNA. Translation: CAI16866.1.
    AL354938, AL161791 Genomic DNA. Translation: CAI16923.1.
    CH471105 Genomic DNA. Translation: EAW58973.1.
    BC130385 mRNA. Translation: AAI30386.1.
    AF113673 mRNA. Translation: AAF29579.1. Different initiation.
    BN000163 mRNA. Translation: CAD89875.1.
    CCDSiCCDS35086.1. [O95347-1]
    RefSeqiNP_001036015.1. NM_001042550.1. [O95347-1]
    NP_001036016.1. NM_001042551.1. [O95347-1]
    NP_001252531.1. NM_001265602.1. [O95347-1]
    NP_006435.2. NM_006444.2. [O95347-1]
    XP_006716996.1. XM_006716933.1. [O95347-1]
    UniGeneiHs.119023.

    Genome annotation databases

    EnsembliENST00000286398; ENSP00000286398; ENSG00000136824. [O95347-1]
    ENST00000374787; ENSP00000363919; ENSG00000136824. [O95347-1]
    ENST00000374793; ENSP00000363925; ENSG00000136824. [O95347-1]
    ENST00000493955; ENSP00000431534; ENSG00000136824.
    GeneIDi10592.
    KEGGihsa:10592.
    UCSCiuc004bbv.3. human. [O95347-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092563 mRNA. Translation: AAC72360.1 . Frameshift.
    AL833191 mRNA. Translation: CAI46187.1 .
    AL161791 , AL354938 Genomic DNA. Translation: CAI16866.1 .
    AL354938 , AL161791 Genomic DNA. Translation: CAI16923.1 .
    CH471105 Genomic DNA. Translation: EAW58973.1 .
    BC130385 mRNA. Translation: AAI30386.1 .
    AF113673 mRNA. Translation: AAF29579.1 . Different initiation.
    BN000163 mRNA. Translation: CAD89875.1 .
    CCDSi CCDS35086.1. [O95347-1 ]
    RefSeqi NP_001036015.1. NM_001042550.1. [O95347-1 ]
    NP_001036016.1. NM_001042551.1. [O95347-1 ]
    NP_001252531.1. NM_001265602.1. [O95347-1 ]
    NP_006435.2. NM_006444.2. [O95347-1 ]
    XP_006716996.1. XM_006716933.1. [O95347-1 ]
    UniGenei Hs.119023.

    3D structure databases

    ProteinModelPortali O95347.
    SMRi O95347. Positions 1-273, 462-688, 945-1172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115841. 38 interactions.
    DIPi DIP-35422N.
    IntActi O95347. 15 interactions.
    MINTi MINT-1161754.
    STRINGi 9606.ENSP00000286398.

    PTM databases

    PhosphoSitei O95347.

    Proteomic databases

    MaxQBi O95347.
    PaxDbi O95347.
    PRIDEi O95347.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286398 ; ENSP00000286398 ; ENSG00000136824 . [O95347-1 ]
    ENST00000374787 ; ENSP00000363919 ; ENSG00000136824 . [O95347-1 ]
    ENST00000374793 ; ENSP00000363925 ; ENSG00000136824 . [O95347-1 ]
    ENST00000493955 ; ENSP00000431534 ; ENSG00000136824 .
    GeneIDi 10592.
    KEGGi hsa:10592.
    UCSCi uc004bbv.3. human. [O95347-1 ]

    Organism-specific databases

    CTDi 10592.
    GeneCardsi GC09P106856.
    H-InvDB HIX0008250.
    HGNCi HGNC:14011. SMC2.
    MIMi 605576. gene.
    neXtProti NX_O95347.
    PharmGKBi PA37833.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1196.
    HOGENOMi HOG000228249.
    HOVERGENi HBG106605.
    InParanoidi O95347.
    KOi K06674.
    OMAi CQNGKIP.
    OrthoDBi EOG7SR4KV.
    PhylomeDBi O95347.
    TreeFami TF101157.

    Enzyme and pathway databases

    Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.
    REACT_172744. Condensation of Prophase Chromosomes.

    Miscellaneous databases

    ChiTaRSi SMC2. human.
    GeneWikii SMC2.
    GenomeRNAii 10592.
    NextBioi 40225.
    PROi O95347.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95347.
    Bgeei O95347.
    CleanExi HS_SMC2.
    Genevestigatori O95347.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 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. 2 hits.
    [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. "Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics."
      Schmiesing J.A., Ball A.R. Jr., Gregson H.C., Alderton J.M., Zhou S., Yokomori K.
      Proc. Natl. Acad. Sci. U.S.A. 95:12906-12911(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SMC4.
      Tissue: Teratocarcinoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lymph node.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 1).
      Tissue: Brain.
    6. "Functional prediction of the coding sequences of 32 new genes deduced by analysis of cDNA clones from human fetal liver."
      Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W., Bi J., Zhang Y., Liu M., He F.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1197 (ISOFORM 2).
      Tissue: Fetal liver.
    7. "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: IDENTIFICATION.
    8. "A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the early stage of mitotic chromosome condensation."
      Schmiesing J.A., Gregson H.C., Zhou S., Yokomori K.
      Mol. Cell. Biol. 20:6996-7006(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4 AND CNAP1, SUBCELLULAR LOCATION.
    9. "Chromosome condensation by a human condensin complex in Xenopus egg extracts."
      Kimura K., Cuvier O., Hirano T.
      J. Biol. Chem. 276:5417-5420(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; BRRN1; CNAP1 AND CAPG, FUNCTION OF THE COMPLEX.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-222; LYS-677; LYS-1158 AND LYS-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: INTERACTION WITH BRD4.

    Entry informationi

    Entry nameiSMC2_HUMAN
    AccessioniPrimary (citable) accession number: O95347
    Secondary accession number(s): Q6IEE0, Q9P1P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3