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Q9CW03

- SMC3_MOUSE

UniProt

Q9CW03 - SMC3_MOUSE

Protein

Structural maintenance of chromosomes protein 3

Gene

Smc3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (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.1 Publication

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: MGI
    3. dynein binding Source: UniProtKB
    4. mediator complex binding Source: MGI
    5. protein binding Source: IntAct

    GO - Biological processi

    1. chromosome organization Source: InterPro
    2. DNA repair Source: UniProtKB-KW
    3. meiotic nuclear division Source: UniProtKB
    4. mitotic nuclear division Source: UniProtKB-KW
    5. mitotic spindle organization Source: UniProtKB
    6. negative regulation of DNA endoreduplication Source: Ensembl
    7. regulation of DNA replication Source: UniProtKB
    8. signal transduction Source: UniProtKB
    9. stem cell maintenance Source: MGI

    Keywords - Biological processi

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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196614. Establishment of Sister Chromatid Cohesion.
    REACT_196634. Cohesin Loading onto Chromatin.
    REACT_198626. Meiotic synapsis.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_75800. 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 segregation protein SmcD
    Mad member-interacting protein 1
    Gene namesi
    Name:Smc3
    Synonyms:Bam, Bmh, Cspg6, Mmip1, Smc3l1, Smcd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1339795. Smc3.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication. Chromosomecentromere 1 Publication
    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.

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. chromosome, centromeric region Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. lateral element Source: MGI
    5. meiotic cohesin complex Source: UniProtKB
    6. nuclear matrix Source: UniProtKB
    7. nuclear meiotic cohesin complex Source: MGI
    8. nucleoplasm Source: Reactome
    9. nucleus Source: MGI
    10. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi807 – 8071L → P: Abolishes interaction with MXI1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12171217Structural maintenance of chromosomes protein 3PRO_0000119002Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Modified residuei106 – 1061N6-acetyllysine1 Publication
    Modified residuei140 – 1401N6-acetyllysineBy similarity
    Modified residuei783 – 7831PhosphothreonineBy similarity
    Modified residuei787 – 7871Phosphoserine1 Publication
    Modified residuei1013 – 10131Phosphoserine1 Publication
    Modified residuei1065 – 10651PhosphoserineBy similarity
    Modified residuei1067 – 10671PhosphoserineBy similarity
    Modified residuei1083 – 10831Phosphoserine1 Publication
    Modified residuei1190 – 11901N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated at Ser-1083 in a SPO11-dependent manner.3 Publications
    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 By similarity. Deacetylation by HDAC8, regulates release of the cohesin complex from chromatin By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CW03.
    PaxDbiQ9CW03.
    PRIDEiQ9CW03.

    PTM databases

    PhosphoSiteiQ9CW03.

    Expressioni

    Tissue specificityi

    Widely expressed, with higher expression in testis and brain.

    Gene expression databases

    ArrayExpressiQ9CW03.
    BgeeiQ9CW03.
    CleanExiMM_SMC3.
    GenevestigatoriQ9CW03.

    Interactioni

    Subunit structurei

    Interacts with NUMA1, and forms a ternary complex with KIF3B and KIFAP3, suggesting a function in tethering the chromosomes to the spindle pole and a function in chromosome movement. Interacts with SYCP2. Found in a complex with SMC1A, CDCA5 and RAD21, PDS5A/APRIN and PDS5B/SCC-112. Interacts with PDS5A and WAPAL; regulated by SMC3 acetylation 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 MXI1, MXD3 and MXD4. Interacts with RPGR By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Mecp2Q9Z2D63EBI-2550068,EBI-1188816

    Protein-protein interaction databases

    BioGridi198951. 12 interactions.
    DIPiDIP-57028N.
    IntActiQ9CW03. 15 interactions.
    MINTiMINT-4134864.

    Structurei

    Secondary structure

    1
    1217
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi495 – 4984
    Turni499 – 5013
    Helixi502 – 52221
    Helixi526 – 5294
    Beta strandi532 – 5354
    Helixi536 – 5383
    Beta strandi539 – 5413
    Helixi544 – 5463
    Helixi547 – 5548
    Helixi557 – 5593
    Beta strandi561 – 5644
    Helixi566 – 57813
    Beta strandi585 – 5895
    Turni590 – 5923
    Beta strandi604 – 6085
    Helixi609 – 6124
    Helixi617 – 6193
    Helixi620 – 6278
    Beta strandi630 – 6356
    Helixi636 – 64510
    Beta strandi649 – 6513
    Beta strandi664 – 6663
    Helixi676 – 68510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WD5X-ray2.70B484-696[»]
    ProteinModelPortaliQ9CW03.
    SMRiQ9CW03. Positions 1-239, 493-686, 987-1206.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CW03.

    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.
    GeneTreeiENSGT00580000081628.
    HOGENOMiHOG000166512.
    HOVERGENiHBG039849.
    InParanoidiQ9CW03.
    KOiK06669.
    OMAiASINSIV.
    OrthoDBiEOG73803T.
    PhylomeDBiQ9CW03.
    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.

    Q9CW03-1 [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 SINKVLEHFR 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):141,556
    Last modified:March 25, 2003 - v2
    Checksum:i11FF55165BE6A88E
    GO

    Sequence cautioni

    The sequence CAA75400.1 differs from that shown. Reason: Frameshift at positions 522, 1018 and 1144.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti999 – 9991K → R in CAA75400. (PubMed:9528857)Curated
    Sequence conflicti1175 – 11751F → L(PubMed:9528857)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF141294 mRNA. Translation: AAD42073.1.
    AF047601 mRNA. Translation: AAD27754.1.
    Y15128 mRNA. Translation: CAA75400.1. Frameshift.
    AK005647 mRNA. Translation: BAB24167.1.
    CCDSiCCDS38025.1.
    RefSeqiNP_031816.2. NM_007790.3.
    UniGeneiMm.14910.

    Genome annotation databases

    EnsembliENSMUST00000025930; ENSMUSP00000025930; ENSMUSG00000024974.
    GeneIDi13006.
    KEGGimmu:13006.
    UCSCiuc008hwy.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF141294 mRNA. Translation: AAD42073.1 .
    AF047601 mRNA. Translation: AAD27754.1 .
    Y15128 mRNA. Translation: CAA75400.1 . Frameshift.
    AK005647 mRNA. Translation: BAB24167.1 .
    CCDSi CCDS38025.1.
    RefSeqi NP_031816.2. NM_007790.3.
    UniGenei Mm.14910.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WD5 X-ray 2.70 B 484-696 [» ]
    ProteinModelPortali Q9CW03.
    SMRi Q9CW03. Positions 1-239, 493-686, 987-1206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198951. 12 interactions.
    DIPi DIP-57028N.
    IntActi Q9CW03. 15 interactions.
    MINTi MINT-4134864.

    PTM databases

    PhosphoSitei Q9CW03.

    Proteomic databases

    MaxQBi Q9CW03.
    PaxDbi Q9CW03.
    PRIDEi Q9CW03.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025930 ; ENSMUSP00000025930 ; ENSMUSG00000024974 .
    GeneIDi 13006.
    KEGGi mmu:13006.
    UCSCi uc008hwy.2. mouse.

    Organism-specific databases

    CTDi 9126.
    MGIi MGI:1339795. Smc3.

    Phylogenomic databases

    eggNOGi COG1196.
    GeneTreei ENSGT00580000081628.
    HOGENOMi HOG000166512.
    HOVERGENi HBG039849.
    InParanoidi Q9CW03.
    KOi K06669.
    OMAi ASINSIV.
    OrthoDBi EOG73803T.
    PhylomeDBi Q9CW03.
    TreeFami TF105602.

    Enzyme and pathway databases

    Reactomei REACT_196614. Establishment of Sister Chromatid Cohesion.
    REACT_196634. Cohesin Loading onto Chromatin.
    REACT_198626. Meiotic synapsis.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    ChiTaRSi SMC3. mouse.
    EvolutionaryTracei Q9CW03.
    NextBioi 282832.
    PROi Q9CW03.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CW03.
    Bgeei Q9CW03.
    CleanExi MM_SMC3.
    Genevestigatori Q9CW03.

    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. "Complete cDNA cloning, genomic organization, chromosomal assignment, functional characterization of the promoter, and expression of the murine Bamacan gene."
      Ghiselli G., Siracusa L.D., Iozzo R.V.
      J. Biol. Chem. 274:17384-17393(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of the components of the putative mammalian sister chromatid cohesion complex."
      Darwiche N., Freeman L.A., Strunnikov A.
      Gene 233:39-47(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1A AND RAD21.
    3. "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of mad family members on C-myc."
      Gupta K., Anand G., Yin X.Y., Prochownik E.V.
      Oncogene 16:1149-1159(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 478-1217, INTERACTION WITH MXI1; MXD3 AND MXD4, MUTAGENESIS OF LEU-807.
      Tissue: Embryo.
    4. "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 887-1217.
      Strain: C57BL/6J.
      Tissue: Testis.
    5. "Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis I."
      Prieto I., Suja J.A., Pezzi N., Kremer L., Martinez-A C., Rufas J.S., Barbero J.L.
      Nat. Cell Biol. 3:761-766(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAG3.
    6. Cited for: INTERACTION WITH SMC1B.
    7. "Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry."
      Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.
      Rapid Commun. Mass Spectrom. 18:2169-2176(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1013.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    9. "Phosphorylation of chromosome core components may serve as axis marks for the status of chromosomal events during mammalian meiosis."
      Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D., Hoeoeg C.
      PLoS Genet. 8:E1002485-E1002485(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1083.
    10. "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-105 AND LYS-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSMC3_MOUSE
    AccessioniPrimary (citable) accession number: Q9CW03
    Secondary accession number(s): O35667, Q9QUS3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 25, 2003
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

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

    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