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Q9UQE7

- SMC3_HUMAN

UniProt

Q9UQE7 - SMC3_HUMAN

Protein

Structural maintenance of chromosomes protein 3

Gene

SMC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (25 Mar 2003)
      Previous versions | rss
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    Functioni

    Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement.2 Publications

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: Ensembl
    3. dynein binding Source: UniProtKB
    4. microtubule motor activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. meiotic nuclear division Source: UniProtKB
    3. mitotic cell cycle Source: Reactome
    4. mitotic nuclear division Source: ProtInc
    5. mitotic spindle organization Source: UniProtKB
    6. negative regulation of DNA endoreduplication Source: BHF-UCL
    7. regulation of DNA replication Source: UniProtKB
    8. signal transduction Source: UniProtKB
    9. sister chromatid cohesion Source: UniProtKB
    10. stem cell maintenance Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_75792. Meiotic synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Structural maintenance of chromosomes protein 3
    Short name:
    SMC protein 3
    Short name:
    SMC-3
    Alternative name(s):
    Basement membrane-associated chondroitin proteoglycan
    Short name:
    Bamacan
    Chondroitin sulfate proteoglycan 6
    Chromosome-associated polypeptide
    Short name:
    hCAP
    Gene namesi
    Name:SMC3
    Synonyms:BAM, BMH, CSPG6, SMC3L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2468. SMC3.

    Subcellular locationi

    Nucleus. Chromosome. Chromosomecentromere
    Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. The phosphorylated form at Ser-1083 is preferentially associated with unsynapsed chromosomal regions By similarity.By similarity

    GO - Cellular componenti

    1. basement membrane Source: ProtInc
    2. chromatin Source: UniProtKB
    3. chromosome Source: Reactome
    4. chromosome, centromeric region Source: Reactome
    5. cohesin complex Source: UniProtKB
    6. cytoplasm Source: UniProtKB
    7. cytosol Source: Reactome
    8. lateral element Source: Ensembl
    9. meiotic cohesin complex Source: UniProtKB
    10. nuclear matrix Source: UniProtKB
    11. nuclear meiotic cohesin complex Source: Ensembl
    12. nucleoplasm Source: Reactome
    13. nucleus Source: HPA
    14. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Cornelia de Lange syndrome 3 (CDLS3) [MIM:610759]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies. Cornelia de Lange syndrome type 3 is a mild form with absence of major structural anomalies. The phenotype in some instances approaches that of apparently non-syndromic mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti491 – 4911Missing in CDLS3; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 1 Publication
    VAR_032845

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi105 – 1051K → A: 20% loss of sister chromatid cohesion; when associated with A-106. 2 Publications
    Mutagenesisi105 – 1051K → R: Stabilizes interaction with PDS5A and WAPAL; when associated with R-106. 2 Publications
    Mutagenesisi106 – 1061K → A: 20% loss of sister chromatid cohesion; when associated with A-105. 2 Publications
    Mutagenesisi106 – 1061K → R: Stabilizes interaction with PDS5A and WAPAL; when associated with R-105. 2 Publications

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi610759. phenotype.
    Orphaneti199. Cornelia de Lange syndrome.
    PharmGKBiPA26966.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12171217Structural maintenance of chromosomes protein 3PRO_0000119001Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051N6-acetyllysine4 Publications
    Modified residuei106 – 1061N6-acetyllysine4 Publications
    Modified residuei140 – 1401N6-acetyllysine2 Publications
    Modified residuei783 – 7831Phosphothreonine1 Publication
    Modified residuei787 – 7871Phosphoserine2 Publications
    Modified residuei1013 – 10131PhosphoserineBy similarity
    Modified residuei1065 – 10651Phosphoserine2 Publications
    Modified residuei1067 – 10671Phosphoserine4 Publications
    Modified residuei1083 – 10831Phosphoserine2 Publications
    Modified residuei1190 – 11901N6-acetyllysine2 Publications

    Post-translational modificationi

    Phosphorylated at Ser-1083 in a SPO11-dependent manner.By similarity
    Acetylation at Lys-105 and Lys-106 by ESCO1 is important for genome stability and S phase sister chromatid cohesion. Regulated by DSCC1, it is required for processive DNA synthesis, coupling sister chromatid cohesion establishment during S phase to DNA replication. Deacetylation by HDAC8, regulates release of the cohesin complex from chromatin.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UQE7.
    PaxDbiQ9UQE7.
    PRIDEiQ9UQE7.

    PTM databases

    PhosphoSiteiQ9UQE7.

    Expressioni

    Gene expression databases

    BgeeiQ9UQE7.
    CleanExiHS_SMC3.
    GenevestigatoriQ9UQE7.

    Organism-specific databases

    HPAiHPA037411.
    HPA043206.

    Interactioni

    Subunit structurei

    Interacts with MXI1, MXD3 and MXD4. Interacts with SYCP2. Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/APRIN and PDS5B/SCC-112 By similarity. Forms a heterodimer with SMC1A or SMC1B in cohesin complexes. Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer attached via their hinge domain, RAD21 which link them, and one STAG protein (STAG1, STAG2 or STAG3), which interacts with RAD21. Also found in meiosis-specific cohesin complexes. Interacts with NUMA1, and forms a ternary complex with KIF3B and KIFAP3, suggesting a function in tethering the chromosomes to the spindle pole and in chromosome movement. Interacts with PDS5A and WAPAL; regulated by SMC3 acetylation. Interacts with RPGR By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MCMBPQ9BTE36EBI-80718,EBI-749378
    PDS5AQ29RF74EBI-80718,EBI-1175454
    PDS5BQ9NTI57EBI-80718,EBI-1175604
    RAD21O6021610EBI-80718,EBI-80739
    SMC1P329084EBI-80718,EBI-17402From a different organism.
    STAG1Q8WVM710EBI-80718,EBI-1175097
    STAG2Q8N3U49EBI-80718,EBI-1057252

    Protein-protein interaction databases

    BioGridi114574. 84 interactions.
    DIPiDIP-29200N.
    IntActiQ9UQE7. 46 interactions.
    MINTiMINT-3083875.
    STRINGi9606.ENSP00000354720.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UQE7.
    SMRiQ9UQE7. Positions 1-239, 493-686, 987-1206.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni505 – 667163Flexible hingeAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili179 – 350172Sequence AnalysisAdd
    BLAST
    Coiled coili393 – 503111Sequence AnalysisAdd
    BLAST
    Coiled coili669 – 916248Sequence AnalysisAdd
    BLAST
    Coiled coili958 – 98932Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1115 – 115036Ala/Asp-rich (DA-box)Add
    BLAST

    Domaini

    The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC1A or SMC1B, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 protein, forming a ring structure By similarity.By similarity

    Sequence similaritiesi

    Belongs to the SMC family. SMC3 subfamily.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1196.
    HOGENOMiHOG000166512.
    HOVERGENiHBG039849.
    InParanoidiQ9UQE7.
    KOiK06669.
    OMAiASINSIV.
    OrthoDBiEOG73803T.
    PhylomeDBiQ9UQE7.
    TreeFamiTF105602.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR010935. SMC_hinge.
    [Graphical view]
    PfamiPF06470. SMC_hinge. 1 hit.
    PF02463. SMC_N. 1 hit.
    [Graphical view]
    SMARTiSM00968. SMC_hinge. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF75553. SSF75553. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9UQE7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS     50
    DEFSHLRPEQ RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR 100
    VIGAKKDQYF LDKKMVTKND VMNLLESAGF SRSNPYYIVK QGKINQMATA 150
    PDSQRLKLLR EVAGTRVYDE RKEESISLMK ETEGKREKIN ELLKYIEERL 200
    HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD ELSAKRETSG 250
    EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK 300
    QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK 350
    FNSVKEKEER GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK 400
    SLDQAINDKK RQIAAIHKDL EDTEANKEKN LEQYNKLDQD LNEVKARVEE 450
    LDRKYYEVKN KKDELQSERN YLWREENAEQ QALAAKREDL EKKQQLLRAA 500
    TGKAILNGID SINKVLDHFR RKGINQHVQN GYHGIVMNNF ECEPAFYTCV 550
    EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY 600
    PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC 650
    ITLEGDQVSH RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL 700
    RRNIERINNE IDQLMNQMQQ IETQQRKFKA SRDSILSEMK MLKEKRQQSE 750
    KTFMPKQRSL QSLEASLHAM ESTRESLKAE LGTDLLSQLS LEDQKRVDAL 800
    NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL DQVEQELNEL 850
    RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS 900
    MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP 950
    QEAFEKYQTL SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL 1000
    IKRQEELDRG YKSIMELMNV LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG 1050
    GKATLVMKKG DVEGSQSQDE GEGSGESERG SGSQSSVPSV DQFTGVGIRV 1100
    SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY LFDEIDQALD 1150
    AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV 1200
    ITAEMAKDFV EDDTTHG 1217
    Length:1,217
    Mass (Da):141,542
    Last modified:March 25, 2003 - v2
    Checksum:i21EF9A08A5D8096A
    GO

    Sequence cautioni

    The sequence AAD32447.1 differs from that shown. Reason: Frameshift at positions 457, 488 and 523.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti462 – 4621K → T in AAD32447. (PubMed:11042152)Curated
    Sequence conflicti509 – 5091I → V in AAD32447. (PubMed:11042152)Curated
    Sequence conflicti526 – 5261Q → P in AAD32447. (PubMed:11042152)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti491 – 4911Missing in CDLS3; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 1 Publication
    VAR_032845

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020043 mRNA. Translation: AAC14893.1.
    AK289771 mRNA. Translation: BAF82460.1.
    AL359260 Genomic DNA. Translation: CAI16576.1.
    CH471066 Genomic DNA. Translation: EAW49557.1.
    AF067163 mRNA. Translation: AAD32447.1. Frameshift.
    AJ005015 mRNA. Translation: CAA06289.1.
    CCDSiCCDS31285.1.
    RefSeqiNP_005436.1. NM_005445.3.
    UniGeneiHs.24485.

    Genome annotation databases

    EnsembliENST00000361804; ENSP00000354720; ENSG00000108055.
    GeneIDi9126.
    KEGGihsa:9126.
    UCSCiuc001kze.3. human.

    Polymorphism databases

    DMDMi29337005.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF020043 mRNA. Translation: AAC14893.1 .
    AK289771 mRNA. Translation: BAF82460.1 .
    AL359260 Genomic DNA. Translation: CAI16576.1 .
    CH471066 Genomic DNA. Translation: EAW49557.1 .
    AF067163 mRNA. Translation: AAD32447.1 . Frameshift.
    AJ005015 mRNA. Translation: CAA06289.1 .
    CCDSi CCDS31285.1.
    RefSeqi NP_005436.1. NM_005445.3.
    UniGenei Hs.24485.

    3D structure databases

    ProteinModelPortali Q9UQE7.
    SMRi Q9UQE7. Positions 1-239, 493-686, 987-1206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114574. 84 interactions.
    DIPi DIP-29200N.
    IntActi Q9UQE7. 46 interactions.
    MINTi MINT-3083875.
    STRINGi 9606.ENSP00000354720.

    PTM databases

    PhosphoSitei Q9UQE7.

    Polymorphism databases

    DMDMi 29337005.

    Proteomic databases

    MaxQBi Q9UQE7.
    PaxDbi Q9UQE7.
    PRIDEi Q9UQE7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361804 ; ENSP00000354720 ; ENSG00000108055 .
    GeneIDi 9126.
    KEGGi hsa:9126.
    UCSCi uc001kze.3. human.

    Organism-specific databases

    CTDi 9126.
    GeneCardsi GC10P112318.
    GeneReviewsi SMC3.
    HGNCi HGNC:2468. SMC3.
    HPAi HPA037411.
    HPA043206.
    MIMi 606062. gene.
    610759. phenotype.
    neXtProti NX_Q9UQE7.
    Orphaneti 199. Cornelia de Lange syndrome.
    PharmGKBi PA26966.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1196.
    HOGENOMi HOG000166512.
    HOVERGENi HBG039849.
    InParanoidi Q9UQE7.
    KOi K06669.
    OMAi ASINSIV.
    OrthoDBi EOG73803T.
    PhylomeDBi Q9UQE7.
    TreeFami TF105602.

    Enzyme and pathway databases

    Reactomei REACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_75792. Meiotic synapsis.

    Miscellaneous databases

    ChiTaRSi SMC3. human.
    GeneWikii SMC3.
    GenomeRNAii 9126.
    NextBioi 34209.
    PROi Q9UQE7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UQE7.
    CleanExi HS_SMC3.
    Genevestigatori Q9UQE7.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR010935. SMC_hinge.
    [Graphical view ]
    Pfami PF06470. SMC_hinge. 1 hit.
    PF02463. SMC_N. 1 hit.
    [Graphical view ]
    SMARTi SM00968. SMC_hinge. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    SSF75553. SSF75553. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide."
      Shimizu K., Shirataki H., Honda T., Minami S., Takai Y.
      J. Biol. Chem. 273:6591-6594(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH KIFAP3, IDENTIFICATION IN A COMPLEX WITH KIFAP3 AND KIF3B.
      Tissue: B-cell.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1217.
      Tissue: Umbilical cord blood.
    6. Stanchi F., Bertocco E., Simionati B., Zimbello R., Lanfranchi G., Valle G.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 827-1217.
      Tissue: Neuron.
    7. "Characterization of vertebrate cohesin complexes and their regulation in prophase."
      Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.
      J. Cell Biol. 151:749-762(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, FUNCTION, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A; STAG1 OR STAG2.
    8. "A potential role for human cohesin in mitotic spindle aster assembly."
      Gregson H.C., Schmiesing J.A., Kim J.-S., Kobayashi T., Zhou S., Yokomori K.
      J. Biol. Chem. 276:47575-47582(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUMA1.
    9. "Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates."
      Rankin S., Ayad N.G., Kirschner M.W.
      Mol. Cell 18:185-200(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CDCA5; SMC1A; RAD21; PDS5A AND PDS5B.
    10. Erratum
      Rankin S., Ayad N.G., Kirschner M.W.
      Mol. Cell 18:609-609(2005)
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787; SER-1065 AND SER-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    13. "Acetylation of Smc3 by Eco1 is required for S phase sister chromatid cohesion in both human and yeast."
      Zhang J., Shi X., Li Y., Kim B.J., Jia J., Huang Z., Yang T., Fu X., Jung S.Y., Wang Y., Zhang P., Kim S.T., Pan X., Qin J.
      Mol. Cell 31:143-151(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-105 AND LYS-106, MUTAGENESIS OF LYS-105 AND LYS-106.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1065 AND SER-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Cohesin acetylation speeds the replication fork."
      Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.
      Nature 462:231-234(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-105 AND LYS-106, INTERACTION WITH PDS5A AND WAPAL, MUTAGENESIS OF LYS-105 AND LYS-106.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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-105; LYS-106; LYS-140 AND LYS-1190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-783; SER-787; SER-1067 AND SER-1083, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067 AND SER-1083, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION, DEACETYLATION BY HDAC8.
    23. "Mutations in cohesin complex members SMC3 and SMC1A cause a mild variant of Cornelia de Lange syndrome with predominant mental retardation."
      Deardorff M.A., Kaur M., Yaeger D., Rampuria A., Korolev S., Pie J., Gil-Rodriguez C., Arnedo M., Loeys B., Kline A.D., Wilson M., Lillquist K., Siu V., Ramos F.J., Musio A., Jackson L.S., Dorsett D., Krantz I.D.
      Am. J. Hum. Genet. 80:485-494(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CDLS3 GLU-491 DEL.
    24. Cited for: CHARACTERIZATION OF VARIANT CDLS3 GLU-491 DEL, GENOMIC INSTABILITY OF CDLS CELL LINES TO IONIZING RADIATION.

    Entry informationi

    Entry nameiSMC3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQE7
    Secondary accession number(s): A8K156, O60464, Q5T482
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 143 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

    Miscellaneous

    Mutated Cornelia de Lange cell lines display genomic instability and sensitivity to ionizing radiation and interstrand cross-linking agents.

    Caution

    Was originally isolated as a proteoglycan protein (explaining its name). Although not excluded, such secreted function is not clear.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3