Q9UQE7 (SMC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SMC3
Synonyms:	BAM, BMH, CSPG6, SMC3L1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1217 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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.
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 process	Cell cycle Cell division DNA damage DNA repair Meiosis Mitosis
Cellular component	Centromere Chromosome Nucleus
Disease	Disease mutation Mental retardation
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW meiotic nuclear division Inferred from direct assay PubMed 12498344. Source: UniProtKB mitosis Traceable author statement Ref.1. Source: ProtInc mitotic cell cycle Traceable author statement. Source: Reactome 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_component	basement 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_function	ATP 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 heterodimerization activity Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MCMBP	Q9BTE3	6	EBI-80718,EBI-749378
PDS5A	Q29RF7	4	EBI-80718,EBI-1175454
PDS5B	Q9NTI5	7	EBI-80718,EBI-1175604
RAD21	O60216	10	EBI-80718,EBI-80739
SMC1	P32908	4	EBI-80718,EBI-17402	From a different organism.
STAG1	Q8WVM7	10	EBI-80718,EBI-1175097
STAG2	Q8N3U4	9	EBI-80718,EBI-1057252

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1217	1217	Structural maintenance of chromosomes protein 3		PRO_0000119001
Regions
	Nucleotide binding	32 – 39	8	ATP Potential
	Region	505 – 667	163	Flexible hinge
	Coiled coil	179 – 350	172	Potential
	Coiled coil	393 – 503	111	Potential
	Coiled coil	669 – 916	248	Potential
	Coiled coil	958 – 989	32	Potential
	Compositional bias	1115 – 1150	36	Ala/Asp-rich (DA-box)
Amino acid modifications
	Modified residue	105	1	N6-acetyllysine Ref.13 Ref.16 Ref.18
	Modified residue	106	1	N6-acetyllysine Ref.13 Ref.16 Ref.18
	Modified residue	140	1	N6-acetyllysine Ref.18
	Modified residue	783	1	Phosphothreonine Ref.19
	Modified residue	787	1	Phosphoserine Ref.11 Ref.19
	Modified residue	1013	1	Phosphoserine By similarity
	Modified residue	1065	1	Phosphoserine Ref.11 Ref.15
	Modified residue	1067	1	Phosphoserine Ref.11 Ref.15 Ref.19 Ref.21
	Modified residue	1083	1	Phosphoserine Ref.19 Ref.21
	Modified residue	1190	1	N6-acetyllysine Ref.18
Natural variations
	Natural variant	491	1	Missing 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
	Mutagenesis	105	1	K → A: 20% loss of sister chromatid cohesion; when associated with A-106. Ref.13 Ref.16
	Mutagenesis	105	1	K → R: Stabilizes interaction with PDS5A and WAPAL; when associated with R-106. Ref.13 Ref.16
	Mutagenesis	106	1	K → A: 20% loss of sister chromatid cohesion; when associated with A-105. Ref.13 Ref.16
	Mutagenesis	106	1	K → R: Stabilizes interaction with PDS5A and WAPAL; when associated with R-105. Ref.13 Ref.16
	Sequence conflict	462	1	K → T in AAD32447. Ref.5
	Sequence conflict	509	1	I → V in AAD32447. Ref.5
	Sequence conflict	526	1	Q → P in AAD32447. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9UQE7 [UniParc]. Last modified March 25, 2003. Version 2. Checksum: 21EF9A08A5D8096A	FASTA	1,217	141,542
	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

References

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[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]	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. , 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. , 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. , 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.
RefSeq	NP_005436.1. NM_005445.3.
UniGene	Hs.24485.
3D structure databases
ProteinModelPortal	Q9UQE7.
SMR	Q9UQE7. Positions 1-239, 493-686, 987-1209.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	114574. 79 interactions.
DIP	DIP-29200N.
IntAct	Q9UQE7. 44 interactions.
MINT	MINT-3083875.
STRING	9606.ENSP00000354720.
PTM databases
PhosphoSite	Q9UQE7.
Polymorphism databases
DMDM	29337005.
Proteomic databases
PaxDb	Q9UQE7.
PRIDE	Q9UQE7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361804; ENSP00000354720; ENSG00000108055.
GeneID	9126.
KEGG	hsa:9126.
UCSC	uc001kze.3. human.
Organism-specific databases
CTD	9126.
GeneCards	GC10P112318.
HGNC	HGNC:2468. SMC3.
HPA	HPA037411. HPA043206.
MIM	606062. gene. 610759. phenotype.
neXtProt	NX_Q9UQE7.
Orphanet	199. Cornelia de Lange syndrome.
PharmGKB	PA26966.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1196.
HOGENOM	HOG000166512.
HOVERGEN	HBG039849.
InParanoid	Q9UQE7.
KO	K06669.
OMA	NKVLEHF.
OrthoDB	EOG73803T.
PhylomeDB	Q9UQE7.
TreeFam	TF105602.
Enzyme and pathway databases
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
Bgee	Q9UQE7.
CleanEx	HS_SMC3.
Genevestigator	Q9UQE7.
Family and domain databases
Gene3D	3.40.50.300. 3 hits.
InterPro	IPR027417. P-loop_NTPase. IPR003395. RecF/RecN/SMC_N. IPR010935. SMC_hinge. [Graphical view]
Pfam	PF06470. SMC_hinge. 1 hit. PF02463. SMC_N. 1 hit. [Graphical view]
SMART	SM00968. SMC_hinge. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 2 hits. SSF75553. SSF75553. 2 hits.
ProtoNet	Search...
Other
ChiTaRS	SMC3. human.
GeneWiki	SMC3.
GenomeRNAi	9126.
NextBio	34209.
PRO	Q9UQE7.
SOURCE	Search...

Entry information

Entry name

SMC3_HUMAN

Accession

Primary (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:	April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.