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Q9CU62 (SMC1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 1A

Short name=SMC protein 1A
Short name=SMC-1-alpha
Short name=SMC-1A
Alternative name(s):
Chromosome segregation protein SmcB
Sb1.8
Gene names
Name:Smc1a
Synonyms:Sb1.8, Smc1, Smc1l1, Smcb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1233 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in chromosome cohesion during cell cycle and in DNA repair. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, and works as a downstream effector in the ATM/NBS1 branch of S-phase checkpoint By similarity. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms 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. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.

Subunit structure

Interacts with POLE and BRCA1. Interacts with SYCP2. Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/APRIN and PDS5B/SCC-112. Interacts with NDC80 By similarity. Forms a heterodimer with SMC3 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. In germ cell cohesin complexes, SMC1A is mutually exclusive with SMC1B. Interacts with RPGR By similarity. Ref.1 Ref.5

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. Note: Associates with chromatin. The phosphorylated form on Ser-957 and Ser-966 associates with chromatin during G1/S/G2 phases but not during M phase, suggesting that phosphorylation does not regulate cohesin function By similarity. 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. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex.

Tissue specificity

Ubiquitous.

Domain

The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, 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 upon ionizing radiation or DNA methylation. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation By similarity.

Sequence similarities

Belongs to the SMC family. SMC1 subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Meiosis
Mitosis
   Cellular componentCentromere
Chromosome
Nucleus
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: InterPro

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

meiotic nuclear division

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA endoreduplication

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction in response to DNA damage

Inferred from sequence or structural similarity. Source: UniProtKB

sister chromatid cohesion

Inferred from electronic annotation. Source: Ensembl

stem cell maintenance

Inferred from mutant phenotype PubMed 20720539. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

meiotic cohesin complex

Inferred from direct assay PubMed 21527826. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

mediator complex binding

Inferred from direct assay PubMed 20720539. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12331233Structural maintenance of chromosomes protein 1A
PRO_0000118990

Regions

Nucleotide binding32 – 398ATP Potential
Region504 – 666163Flexible hinge
Coiled coil104 – 12421 Potential
Coiled coil163 – 503341 Potential
Coiled coil667 – 935269 Potential
Coiled coil988 – 106881 Potential
Compositional bias1128 – 116336Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue3581Phosphoserine By similarity
Modified residue3601Phosphoserine By similarity
Modified residue6481N6-acetyllysine By similarity
Modified residue7131N6-acetyllysine By similarity
Modified residue9571Phosphoserine By similarity
Modified residue9661Phosphoserine By similarity
Modified residue9701Phosphoserine By similarity
Modified residue10371N6-acetyllysine Ref.6

Experimental info

Sequence conflict3211N → H in AAD27753. Ref.1
Sequence conflict6791E → G in AAD27753. Ref.1
Sequence conflict9221K → E in AAD27753. Ref.1
Sequence conflict9441K → E in AAD27753. Ref.1
Sequence conflict9771A → G in BAE43202. Ref.4
Sequence conflict10131Q → R in AAD27753. Ref.1

Secondary structure

........................................ 1233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CU62 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: E62CEB174854D9A6

FASTA1,233143,235
        10         20         30         40         50         60 
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT 

        70         80         90        100        110        120 
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE 

       130        140        150        160        170        180 
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE 

       190        200        210        220        230        240 
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK 

       250        260        270        280        290        300 
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK 

       310        320        330        340        350        360 
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS 

       370        380        390        400        410        420 
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK 

       430        440        450        460        470        480 
IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV 

       490        500        510        520        530        540 
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK 

       550        560        570        580        590        600 
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY 

       610        620        630        640        650        660 
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK 

       670        680        690        700        710        720 
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE 

       730        740        750        760        770        780 
QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF 

       790        800        810        820        830        840 
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ 

       850        860        870        880        890        900 
TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG 

       910        920        930        940        950        960 
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGSSQGE 

       970        980        990       1000       1010       1020 
ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI 

      1030       1040       1050       1060       1070       1080 
AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN 

      1090       1100       1110       1120       1130       1140 
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL 

      1150       1160       1170       1180       1190       1200 
LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL 

      1210       1220       1230 
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ 

« Hide

References

« Hide 'large scale' references
[1]"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], CHARACTERIZATION, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3 AND RAD21.
Tissue: Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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. expand/collapse author list , 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 1-301 AND 977-1233.
Strain: C57BL/6J and NOD.
Tissue: Hippocampus, Pancreas and Thymus.
[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]"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-1037, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF047600 mRNA. Translation: AAD27753.1.
AL672180 Genomic DNA. Translation: CAM23830.1.
BC131667 mRNA. Translation: AAI31668.1.
AK007334 mRNA. Translation: BAE43202.1.
AK013648 mRNA. Translation: BAB28937.1.
AK017948 mRNA. Translation: BAB31016.3.
AK088183 mRNA. Translation: BAC40193.1.
CCDSCCDS30473.1.
RefSeqNP_062684.2. NM_019710.2.
UniGeneMm.482095.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70A461-685[»]
ProteinModelPortalQ9CU62.
SMRQ9CU62. Positions 499-675.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204874. 14 interactions.
DIPDIP-57021N.
IntActQ9CU62. 5 interactions.
MINTMINT-4134829.
STRING10090.ENSMUSP00000044645.

PTM databases

PhosphoSiteQ9CU62.

Proteomic databases

MaxQBQ9CU62.
PaxDbQ9CU62.
PRIDEQ9CU62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133.
GeneID24061.
KEGGmmu:24061.
UCSCuc009upx.2. mouse.

Organism-specific databases

CTD8243.
MGIMGI:1344345. Smc1a.

Phylogenomic databases

eggNOGCOG1196.
GeneTreeENSGT00580000081569.
HOGENOMHOG000195481.
HOVERGENHBG039593.
InParanoidA2AFQ5.
KOK06636.
OMAFKSYRGH.
OrthoDBEOG7K3TK5.
TreeFamTF101156.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressQ9CU62.
BgeeQ9CU62.
CleanExMM_SMC1A.
GenevestigatorQ9CU62.

Family and domain databases

Gene3D3.40.50.300. 4 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9CU62.
NextBio304025.
PROQ9CU62.
SOURCESearch...

Entry information

Entry nameSMC1A_MOUSE
AccessionPrimary (citable) accession number: Q9CU62
Secondary accession number(s): A2AFQ5 expand/collapse secondary AC list , Q3V480, Q9CUX9, Q9D959, Q9WTU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 120 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot