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Q9UQE7 (SMC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SMC3
Synonyms:BAM, BMH, CSPG6, SMC3L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.16

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.16

Subcellular location

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.

Domain

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.

Post-translational modification

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. Ref.13 Ref.16 Ref.22

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.24

Miscellaneous

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

Sequence similarities

Belongs to the SMC family. SMC3 subfamily.

Caution

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

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Meiosis
Mitosis
   Cellular componentCentromere
Chromosome
Nucleus
   DiseaseDisease mutation
Mental retardation
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

meiotic nuclear division

Inferred from direct assay PubMed 12498344. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Traceable author statement Ref.1. Source: ProtInc

mitotic spindle organization

Inferred from expression pattern Ref.8. Source: UniProtKB

negative regulation of DNA endoreduplication

Inferred from mutant phenotype PubMed 15917200. Source: BHF-UCL

regulation of DNA replication

Inferred from mutant phenotype Ref.16. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 12651860. Source: UniProtKB

sister chromatid cohesion

Non-traceable author statement Ref.8. Source: UniProtKB

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Traceable author statement PubMed 9015313. Source: ProtInc

chromatin

Inferred from direct assay PubMed 16682347Ref.16. Source: UniProtKB

chromosome

Traceable author statement. Source: Reactome

chromosome, centromeric region

Traceable author statement. Source: Reactome

cohesin complex

Non-traceable author statement Ref.1. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

lateral element

Inferred from electronic annotation. Source: Ensembl

meiotic cohesin complex

Inferred from direct assay PubMed 21242291. Source: UniProtKB

nuclear matrix

Inferred from direct assay Ref.8. Source: UniProtKB

nuclear meiotic cohesin complex

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

spindle pole

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: Ensembl

dynein binding

Inferred from direct assay Ref.8. Source: UniProtKB

microtubule motor activity

Non-traceable author statement Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.9PubMed 16682347Ref.16Ref.1. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12171217Structural maintenance of chromosomes protein 3
PRO_0000119001

Regions

Nucleotide binding32 – 398ATP Potential
Region505 – 667163Flexible hinge
Coiled coil179 – 350172 Potential
Coiled coil393 – 503111 Potential
Coiled coil669 – 916248 Potential
Coiled coil958 – 98932 Potential
Compositional bias1115 – 115036Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue1051N6-acetyllysine Ref.13 Ref.16 Ref.18
Modified residue1061N6-acetyllysine Ref.13 Ref.16 Ref.18
Modified residue1401N6-acetyllysine Ref.18
Modified residue7831Phosphothreonine Ref.19
Modified residue7871Phosphoserine Ref.11 Ref.19
Modified residue10131Phosphoserine By similarity
Modified residue10651Phosphoserine Ref.11 Ref.15
Modified residue10671Phosphoserine Ref.11 Ref.15 Ref.19 Ref.21
Modified residue10831Phosphoserine Ref.19 Ref.21
Modified residue11901N6-acetyllysine Ref.18

Natural variations

Natural variant4911Missing in CDLS3; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. Ref.23 Ref.24
VAR_032845

Experimental info

Mutagenesis1051K → A: 20% loss of sister chromatid cohesion; when associated with A-106. Ref.13 Ref.16
Mutagenesis1051K → R: Stabilizes interaction with PDS5A and WAPAL; when associated with R-106. Ref.13 Ref.16
Mutagenesis1061K → A: 20% loss of sister chromatid cohesion; when associated with A-105. Ref.13 Ref.16
Mutagenesis1061K → R: Stabilizes interaction with PDS5A and WAPAL; when associated with R-105. Ref.13 Ref.16
Sequence conflict4621K → T in AAD32447. Ref.5
Sequence conflict5091I → V in AAD32447. Ref.5
Sequence conflict5261Q → P in AAD32447. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9UQE7 [UniParc].

Last modified March 25, 2003. Version 2.
Checksum: 21EF9A08A5D8096A

FASTA1,217141,542
        10         20         30         40         50         60 
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ 

        70         80         90        100        110        120 
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND 

       130        140        150        160        170        180 
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK 

       190        200        210        220        230        240 
ETEGKREKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD 

       250        260        270        280        290        300 
ELSAKRETSG EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK 

       310        320        330        340        350        360 
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FNSVKEKEER 

       370        380        390        400        410        420 
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAIHKDL 

       430        440        450        460        470        480 
EDTEANKEKN LEQYNKLDQD LNEVKARVEE LDRKYYEVKN KKDELQSERN YLWREENAEQ 

       490        500        510        520        530        540 
QALAAKREDL EKKQQLLRAA TGKAILNGID SINKVLDHFR RKGINQHVQN GYHGIVMNNF 

       550        560        570        580        590        600 
ECEPAFYTCV EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY 

       610        620        630        640        650        660 
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH 

       670        680        690        700        710        720 
RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL RRNIERINNE IDQLMNQMQQ 

       730        740        750        760        770        780 
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE 

       790        800        810        820        830        840 
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL 

       850        860        870        880        890        900 
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS 

       910        920        930        940        950        960 
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL 

       970        980        990       1000       1010       1020 
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG YKSIMELMNV 

      1030       1040       1050       1060       1070       1080 
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSGESERG 

      1090       1100       1110       1120       1130       1140 
SGSQSSVPSV DQFTGVGIRV SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY 

      1150       1160       1170       1180       1190       1200 
LFDEIDQALD AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV 

      1210 
ITAEMAKDFV EDDTTHG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle."
Deardorff M.A., Bando M., Nakato R., Watrin E., Itoh T., Minamino M., Saitoh K., Komata M., Katou Y., Clark D., Cole K.E., De Baere E., Decroos C., Di Donato N., Ernst S., Francey L.J., Gyftodimou Y., Hirashima K. expand/collapse author list , Hullings M., Ishikawa Y., Jaulin C., Kaur M., Kiyono T., Lombardi P.M., Magnaghi-Jaulin L., Mortier G.R., Nozaki N., Petersen M.B., Seimiya H., Siu V.M., Suzuki Y., Takagaki K., Wilde J.J., Willems P.J., Prigent C., Gillessen-Kaesbach G., Christianson D.W., Kaiser F.J., Jackson L.G., Hirota T., Krantz I.D., Shirahige K.
Nature 489:313-317(2012) [PubMed] [Europe PMC] [Abstract]
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]"Cornelia de Lange syndrome mutations in SMC1A or SMC3 affect binding to DNA."
Revenkova E., Focarelli M.L., Susani L., Paulis M., Bassi M.T., Mannini L., Frattini A., Delia D., Krantz I., Vezzoni P., Jessberger R., Musio A.
Hum. Mol. Genet. 18:418-427(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CDLS3 GLU-491 DEL, GENOMIC INSTABILITY OF CDLS CELL LINES TO IONIZING RADIATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31285.1.
RefSeqNP_005436.1. NM_005445.3.
UniGeneHs.24485.

3D structure databases

ProteinModelPortalQ9UQE7.
SMRQ9UQE7. Positions 1-239, 493-686, 987-1206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114574. 85 interactions.
DIPDIP-29200N.
IntActQ9UQE7. 45 interactions.
MINTMINT-3083875.
STRING9606.ENSP00000354720.

PTM databases

PhosphoSiteQ9UQE7.

Polymorphism databases

DMDM29337005.

Proteomic databases

MaxQBQ9UQE7.
PaxDbQ9UQE7.
PRIDEQ9UQE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361804; ENSP00000354720; ENSG00000108055.
GeneID9126.
KEGGhsa:9126.
UCSCuc001kze.3. human.

Organism-specific databases

CTD9126.
GeneCardsGC10P112318.
GeneReviewsSMC3.
HGNCHGNC:2468. SMC3.
HPAHPA037411.
HPA043206.
MIM606062. gene.
610759. phenotype.
neXtProtNX_Q9UQE7.
Orphanet199. Cornelia de Lange syndrome.
PharmGKBPA26966.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1196.
HOGENOMHOG000166512.
HOVERGENHBG039849.
InParanoidQ9UQE7.
KOK06669.
OMAASINSIV.
OrthoDBEOG73803T.
PhylomeDBQ9UQE7.
TreeFamTF105602.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

BgeeQ9UQE7.
CleanExHS_SMC3.
GenevestigatorQ9UQE7.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 2 hits.
ProtoNetSearch...

Other

ChiTaRSSMC3. human.
GeneWikiSMC3.
GenomeRNAi9126.
NextBio34209.
PROQ9UQE7.
SOURCESearch...

Entry information

Entry nameSMC3_HUMAN
AccessionPrimary (citable) accession number: Q9UQE7
Secondary accession number(s): A8K156, O60464, Q5T482
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM