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Protein

Structural maintenance of chromosomes protein 1A

Gene

Smc1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 39ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2468052. Establishment of Sister Chromatid Cohesion.
R-MMU-2470946. Cohesin Loading onto Chromatin.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Smc1a
Synonyms:Sb1.8, Smc1, Smc1l1, Smcb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1344345. Smc1a.

Subcellular locationi

  • 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.By similarity

GO - Cellular componenti

  • cohesin core heterodimer Source: InterPro
  • cytoplasm Source: MGI
  • kinetochore Source: UniProtKB
  • meiotic cohesin complex Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001189901 – 1233Structural maintenance of chromosomes protein 1AAdd BLAST1233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei358PhosphoserineBy similarity1
Modified residuei360PhosphoserineBy similarity1
Modified residuei648N6-acetyllysineBy similarity1
Modified residuei713N6-acetyllysineBy similarity1
Modified residuei957PhosphoserineBy similarity1
Modified residuei962PhosphoserineBy similarity1
Modified residuei966PhosphoserineBy similarity1
Modified residuei970PhosphoserineBy similarity1
Modified residuei1037N6-acetyllysineCombined sources1

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CU62.
MaxQBiQ9CU62.
PaxDbiQ9CU62.
PeptideAtlasiQ9CU62.
PRIDEiQ9CU62.

PTM databases

iPTMnetiQ9CU62.
PhosphoSitePlusiQ9CU62.

Expressioni

Tissue specificityi

Ubiquitous (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000041133.
CleanExiMM_SMC1A.
ExpressionAtlasiQ9CU62. baseline and differential.
GenevisibleiQ9CU62. MM.

Interactioni

Subunit structurei

Interacts with POLE and BRCA1. Interacts with SYCP2. Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/SCC-112 and PDS5B/APRIN. 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). Interacts with BRAT1 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AtrxQ616874EBI-2550016,EBI-2657527
Cep290Q6A0782EBI-2550016,EBI-1811999
Mecp2Q9Z2D63EBI-2550016,EBI-1188816

GO - Molecular functioni

  • mediator complex binding Source: MGI
  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi204874. 40 interactors.
DIPiDIP-57021N.
IntActiQ9CU62. 37 interactors.
MINTiMINT-4134829.
STRINGi10090.ENSMUSP00000044645.

Structurei

Secondary structure

11233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi501 – 510Combined sources10
Helixi512 – 514Combined sources3
Beta strandi515 – 518Combined sources4
Helixi519 – 522Combined sources4
Beta strandi523 – 527Combined sources5
Helixi528 – 530Combined sources3
Helixi531 – 538Combined sources8
Helixi539 – 542Combined sources4
Beta strandi545 – 548Combined sources4
Helixi550 – 562Combined sources13
Beta strandi568 – 572Combined sources5
Turni573 – 575Combined sources3
Helixi583 – 587Combined sources5
Beta strandi592 – 594Combined sources3
Helixi595 – 597Combined sources3
Beta strandi598 – 602Combined sources5
Helixi603 – 605Combined sources3
Helixi606 – 612Combined sources7
Turni613 – 615Combined sources3
Beta strandi617 – 621Combined sources5
Helixi622 – 630Combined sources9
Beta strandi631 – 634Combined sources4
Beta strandi638 – 640Combined sources3
Beta strandi652 – 654Combined sources3
Helixi656 – 662Combined sources7
Helixi665 – 670Combined sources6
Turni671 – 673Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70A461-685[»]
ProteinModelPortaliQ9CU62.
SMRiQ9CU62.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CU62.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni504 – 666Flexible hingeAdd BLAST163

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili104 – 124Sequence analysisAdd BLAST21
Coiled coili163 – 503Sequence analysisAdd BLAST341
Coiled coili667 – 935Sequence analysisAdd BLAST269
Coiled coili988 – 1068Sequence analysisAdd BLAST81

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1128 – 1163Ala/Asp-rich (DA-box)Add BLAST36

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the SMC family. SMC1 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0018. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00580000081569.
HOGENOMiHOG000195481.
HOVERGENiHBG039593.
InParanoidiQ9CU62.
KOiK06636.
OMAiKHMDFQR.
OrthoDBiEOG091G00R5.
TreeFamiTF101156.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029683. SMC1A_metazoan.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF170. PTHR18937:SF170. 3 hits.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CU62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG
60 70 80 90 100
EKTSNLRVKT LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG
110 120 130 140 150
GSSEYKINNK VVQLHEYSEE LEKLGILIKA RNFLVFQGAV ESIAMKNPKE
160 170 180 190 200
RTALFEEISR SGELAQEYDK RKKEMVKAEE DTQFNYHRKK NIAAERKEAK
210 220 230 240 250
QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK ELASKNKEIE
260 270 280 290 300
KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
310 320 330 340 350
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF
360 370 380 390 400
EERMEEESQS QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ
410 420 430 440 450
KADQDRLDLE ERKKVETEAK IKQKLREIEE NQKRIEKLEE YITTSKQSLE
460 470 480 490 500
EQKKLEGELT EEVEMAKRRI DEINKELNQV MEQLGDARID RQESSRQQRK
510 520 530 540 550
AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK NMDAIIVDSE
560 570 580 590 600
KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY
610 620 630 640 650
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG
660 670 680 690 700
VISGGASDLK AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ
710 720 730 740 750
VQSQAHGLQM RLKYSQSDLE QTKTRHLALN LQEKSKLESE LANFGPRIND
760 770 780 790 800
IKRIIQSRER EMKDLKEKMN QVEDEVFEEF CREIGVRNIR EFEEEKVKRQ
810 820 830 840 850
NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ TVKKDENEIE
860 870 880 890 900
KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG
910 920 930 940 950
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI
960 970 980 990 1000
SQEEGSSQGE ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK
1010 1020 1030 1040 1050
QEMNTLQQKL NEQQSVLQRI AAPNMKAMEK LESVRDKFQE TSDEFEAARK
1060 1070 1080 1090 1100
RAKKAKQAFE QIKKERFDRF NACFESVATN IDEIYKALSR NSSAQAFLGP
1110 1120 1130 1140 1150
ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL LFAIHSYKPA
1160 1170 1180 1190 1200
PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL
1210 1220 1230
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ
Length:1,233
Mass (Da):143,235
Last modified:July 27, 2011 - v4
Checksum:iE62CEB174854D9A6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti321N → H in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti679E → G in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti922K → E in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti944K → E in AAD27753 (PubMed:10375619).Curated1
Sequence conflicti977A → G in BAE43202 (PubMed:16141072).Curated1
Sequence conflicti1013Q → R in AAD27753 (PubMed:10375619).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30473.1.
RefSeqiNP_062684.2. NM_019710.2.
UniGeneiMm.482095.

Genome annotation databases

EnsembliENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133.
GeneIDi24061.
KEGGimmu:24061.
UCSCiuc009upx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS30473.1.
RefSeqiNP_062684.2. NM_019710.2.
UniGeneiMm.482095.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70A461-685[»]
ProteinModelPortaliQ9CU62.
SMRiQ9CU62.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204874. 40 interactors.
DIPiDIP-57021N.
IntActiQ9CU62. 37 interactors.
MINTiMINT-4134829.
STRINGi10090.ENSMUSP00000044645.

PTM databases

iPTMnetiQ9CU62.
PhosphoSitePlusiQ9CU62.

Proteomic databases

EPDiQ9CU62.
MaxQBiQ9CU62.
PaxDbiQ9CU62.
PeptideAtlasiQ9CU62.
PRIDEiQ9CU62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133.
GeneIDi24061.
KEGGimmu:24061.
UCSCiuc009upx.2. mouse.

Organism-specific databases

CTDi8243.
MGIiMGI:1344345. Smc1a.

Phylogenomic databases

eggNOGiKOG0018. Eukaryota.
COG1196. LUCA.
GeneTreeiENSGT00580000081569.
HOGENOMiHOG000195481.
HOVERGENiHBG039593.
InParanoidiQ9CU62.
KOiK06636.
OMAiKHMDFQR.
OrthoDBiEOG091G00R5.
TreeFamiTF101156.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2468052. Establishment of Sister Chromatid Cohesion.
R-MMU-2470946. Cohesin Loading onto Chromatin.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

EvolutionaryTraceiQ9CU62.
PROiQ9CU62.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000041133.
CleanExiMM_SMC1A.
ExpressionAtlasiQ9CU62. baseline and differential.
GenevisibleiQ9CU62. MM.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029683. SMC1A_metazoan.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF170. PTHR18937:SF170. 3 hits.
PfamiPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFiPIRSF005719. SMC. 1 hit.
SMARTiSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSMC1A_MOUSE
AccessioniPrimary (citable) accession number: Q9CU62
Secondary accession number(s): A2AFQ5
, Q3V480, Q9CUX9, Q9D959, Q9WTU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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 one 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.