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Q9UQE7 - SMC3_HUMAN

UniProt

Q9UQE7 - SMC3_HUMAN

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Protein

Structural maintenance of chromosomes protein 3

Gene

SMC3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 heterodimerization activity Source: UniProtKB

GO - Biological processi

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

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:2468. SMC3.

Subcellular locationi

Nucleus. Chromosome. Chromosome › centromere
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. cohesin core heterodimer Source: InterPro
  7. cytoplasm Source: UniProtKB
  8. cytosol Source: Reactome
  9. lateral element Source: Ensembl
  10. meiotic cohesin complex Source: UniProtKB
  11. nuclear matrix Source: UniProtKB
  12. nuclear meiotic cohesin complex Source: Ensembl
  13. nucleoplasm Source: HPA
  14. nucleus Source: ProtInc
  15. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cornelia de Lange syndrome 31 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:610759
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. 2 Publications
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-acetyllysine3 Publications
Modified residuei106 – 1061N6-acetyllysine3 Publications
Modified residuei140 – 1401N6-acetyllysine1 Publication
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-acetyllysine1 Publication

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. 86 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.
GeneTreeiENSGT00580000081628.
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.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF164. PTHR18937:SF164. 1 hit.
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

        10         20         30         40         50
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS 
        60         70         80         90        100
DEFSHLRPEQ RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR 
       110        120        130        140        150
VIGAKKDQYF LDKKMVTKND VMNLLESAGF SRSNPYYIVK QGKINQMATA 
       160        170        180        190        200
PDSQRLKLLR EVAGTRVYDE RKEESISLMK ETEGKREKIN ELLKYIEERL 
       210        220        230        240        250
HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD ELSAKRETSG 
       260        270        280        290        300
EKSRQLRDAQ QDARDKMEDI ERQVRELKTK ISAMKEEKEQ LSAERQEQIK 
       310        320        330        340        350
QRTKLELKAK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK 
       360        370        380        390        400
FNSVKEKEER GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK 
       410        420        430        440        450
SLDQAINDKK RQIAAIHKDL EDTEANKEKN LEQYNKLDQD LNEVKARVEE 
       460        470        480        490        500
LDRKYYEVKN KKDELQSERN YLWREENAEQ QALAAKREDL EKKQQLLRAA 
       510        520        530        540        550
TGKAILNGID SINKVLDHFR RKGINQHVQN GYHGIVMNNF ECEPAFYTCV 
       560        570        580        590        600
EVTAGNRLFY HIVDSDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY 
       610        620        630        640        650
PETNDAIPMI SKLRYNPRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC 
       660        670        680        690        700
ITLEGDQVSH RGALTGGYYD TRKSRLELQK DVRKAEEELG ELEAKLNENL 
       710        720        730        740        750
RRNIERINNE IDQLMNQMQQ IETQQRKFKA SRDSILSEMK MLKEKRQQSE 
       760        770        780        790        800
KTFMPKQRSL QSLEASLHAM ESTRESLKAE LGTDLLSQLS LEDQKRVDAL 
       810        820        830        840        850
NDEIRQLQQE NRQLLNERIK LEGIITRVET YLNENLRKRL DQVEQELNEL 
       860        870        880        890        900
RETEGGTVLT ATTSELEAIN KRVKDTMARS EDLDNSIDKT EAGIKELQKS 
       910        920        930        940        950
MERWKNMEKE HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP 
       960        970        980        990       1000
QEAFEKYQTL SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL 
      1010       1020       1030       1040       1050
IKRQEELDRG YKSIMELMNV LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG 
      1060       1070       1080       1090       1100
GKATLVMKKG DVEGSQSQDE GEGSGESERG SGSQSSVPSV DQFTGVGIRV 
      1110       1120       1130       1140       1150
SFTGKQGEMR EMQQLSGGQK SLVALALIFA IQKCDPAPFY LFDEIDQALD 
      1160       1170       1180       1190       1200
AQHRKAVSDM IMELAVHAQF ITTTFRPELL ESADKFYGVK FRNKVSHIDV 
      1210 
ITAEMAKDFV EDDTTHG
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. Curated

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. 2 Publications
VAR_032845

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi114574. 86 interactions.
DIPiDIP-29200N.
IntActiQ9UQE7. 46 interactions.
MINTiMINT-3083875.
STRINGi9606.ENSP00000354720.

PTM databases

PhosphoSiteiQ9UQE7.

Polymorphism databases

DMDMi29337005.

Proteomic databases

MaxQBiQ9UQE7.
PaxDbiQ9UQE7.
PRIDEiQ9UQE7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9126.
GeneCardsiGC10P112318.
GeneReviewsiSMC3.
HGNCiHGNC:2468. SMC3.
HPAiHPA037411.
HPA043206.
MIMi606062. gene.
610759. phenotype.
neXtProtiNX_Q9UQE7.
Orphaneti199. Cornelia de Lange syndrome.
PharmGKBiPA26966.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1196.
GeneTreeiENSGT00580000081628.
HOGENOMiHOG000166512.
HOVERGENiHBG039849.
InParanoidiQ9UQE7.
KOiK06669.
OMAiASINSIV.
OrthoDBiEOG73803T.
PhylomeDBiQ9UQE7.
TreeFamiTF105602.

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.

Miscellaneous databases

ChiTaRSiSMC3. human.
GeneWikiiSMC3.
GenomeRNAii9126.
NextBioi34209.
PROiQ9UQE7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UQE7.
CleanExiHS_SMC3.
GenevestigatoriQ9UQE7.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF164. PTHR18937:SF164. 1 hit.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.