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Q9CW03

- SMC3_MOUSE

UniProt

Q9CW03 - SMC3_MOUSE

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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

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

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. meiotic nuclear division Source: UniProtKB
  3. mitotic sister chromatid cohesion Source: InterPro
  4. mitotic spindle organization Source: UniProtKB
  5. negative regulation of DNA endoreduplication Source: Ensembl
  6. regulation of DNA replication Source: UniProtKB
  7. signal transduction Source: UniProtKB
  8. stem cell maintenance Source: MGI
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_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-KW
  3. cohesin core heterodimer Source: InterPro
  4. cytoplasm Source: UniProtKB
  5. lateral element Source: MGI
  6. meiotic cohesin complex Source: UniProtKB
  7. nuclear matrix Source: UniProtKB
  8. nuclear meiotic cohesin complex Source: MGI
  9. nucleoplasm Source: Reactome
  10. nucleus Source: MGI
  11. spindle pole Source: UniProtKB
Complete GO annotation...

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

BgeeiQ9CW03.
CleanExiMM_SMC3.
ExpressionAtlasiQ9CW03. baseline and differential.
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. 17 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.
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.

Q9CW03-1 [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 SINKVLEHFR 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):141,556
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. 17 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

Bgeei Q9CW03.
CleanExi MM_SMC3.
ExpressionAtlasi Q9CW03. baseline and differential.
Genevestigatori Q9CW03.

Family and domain databases

Gene3Di 3.40.50.300. 3 hits.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR029685. SMC3.
IPR010935. SMC_hinge.
[Graphical view ]
PANTHERi PTHR18937:SF164. PTHR18937:SF164. 1 hit.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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