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Q9CU62

- SMC1A_MOUSE

UniProt

Q9CU62 - SMC1A_MOUSE

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Protein

Structural maintenance of chromosomes protein 1A

Gene

Smc1a

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: UniProtKB
  3. mediator complex binding Source: MGI
  4. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. meiotic nuclear division Source: UniProtKB
  3. mitotic cell cycle checkpoint Source: UniProtKB
  4. mitotic sister chromatid cohesion Source: InterPro
  5. negative regulation of DNA endoreduplication Source: Ensembl
  6. response to radiation Source: UniProtKB
  7. signal transduction in response to DNA damage 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 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
ProteomesiUP000000589: 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

  1. cohesin core heterodimer Source: InterPro
  2. cytoplasm Source: Ensembl
  3. kinetochore Source: UniProtKB
  4. meiotic cohesin complex Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12331233Structural maintenance of chromosomes protein 1APRO_0000118990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei358 – 3581PhosphoserineBy similarity
Modified residuei360 – 3601PhosphoserineBy similarity
Modified residuei648 – 6481N6-acetyllysineBy similarity
Modified residuei713 – 7131N6-acetyllysineBy similarity
Modified residuei957 – 9571PhosphoserineBy similarity
Modified residuei966 – 9661PhosphoserineBy similarity
Modified residuei970 – 9701PhosphoserineBy similarity
Modified residuei1037 – 10371N6-acetyllysine1 Publication

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

MaxQBiQ9CU62.
PaxDbiQ9CU62.
PRIDEiQ9CU62.

PTM databases

PhosphoSiteiQ9CU62.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9CU62.
CleanExiMM_SMC1A.
ExpressionAtlasiQ9CU62. baseline and differential.
GenevestigatoriQ9CU62.

Interactioni

Subunit structurei

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.By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi204874. 14 interactions.
DIPiDIP-57021N.
IntActiQ9CU62. 9 interactions.
MINTiMINT-4134829.
STRINGi10090.ENSMUSP00000044645.

Structurei

Secondary structure

1
1233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi501 – 51010
Helixi512 – 5143
Beta strandi515 – 5184
Helixi519 – 5224
Beta strandi523 – 5275
Helixi528 – 5303
Helixi531 – 5388
Helixi539 – 5424
Beta strandi545 – 5484
Helixi550 – 56213
Beta strandi568 – 5725
Turni573 – 5753
Helixi583 – 5875
Beta strandi592 – 5943
Helixi595 – 5973
Beta strandi598 – 6025
Helixi603 – 6053
Helixi606 – 6127
Turni613 – 6153
Beta strandi617 – 6215
Helixi622 – 6309
Beta strandi631 – 6344
Beta strandi638 – 6403
Beta strandi652 – 6543
Helixi656 – 6627
Helixi665 – 6706
Turni671 – 6733

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WD5X-ray2.70A461-685[»]
ProteinModelPortaliQ9CU62.
SMRiQ9CU62. Positions 499-675.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CU62.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni504 – 666163Flexible hingeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili104 – 12421Sequence AnalysisAdd
BLAST
Coiled coili163 – 503341Sequence AnalysisAdd
BLAST
Coiled coili667 – 935269Sequence AnalysisAdd
BLAST
Coiled coili988 – 106881Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1128 – 116336Ala/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 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

eggNOGiCOG1196.
GeneTreeiENSGT00580000081569.
HOGENOMiHOG000195481.
HOVERGENiHBG039593.
InParanoidiQ9CU62.
KOiK06636.
OMAiFKSYRGH.
OrthoDBiEOG7K3TK5.
TreeFamiTF101156.

Family and domain databases

Gene3Di3.40.50.300. 4 hits.
InterProiIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029683. SMC1A.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERiPTHR18937:SF170. PTHR18937:SF170. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3211N → H in AAD27753. (PubMed:10375619)Curated
Sequence conflicti679 – 6791E → G in AAD27753. (PubMed:10375619)Curated
Sequence conflicti922 – 9221K → E in AAD27753. (PubMed:10375619)Curated
Sequence conflicti944 – 9441K → E in AAD27753. (PubMed:10375619)Curated
Sequence conflicti977 – 9771A → G in BAE43202. (PubMed:16141072)Curated
Sequence conflicti1013 – 10131Q → R in AAD27753. (PubMed:10375619)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS30473.1.
RefSeqi NP_062684.2. NM_019710.2.
UniGenei Mm.482095.

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 A 461-685 [» ]
ProteinModelPortali Q9CU62.
SMRi Q9CU62. Positions 499-675.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204874. 14 interactions.
DIPi DIP-57021N.
IntActi Q9CU62. 9 interactions.
MINTi MINT-4134829.
STRINGi 10090.ENSMUSP00000044645.

PTM databases

PhosphoSitei Q9CU62.

Proteomic databases

MaxQBi Q9CU62.
PaxDbi Q9CU62.
PRIDEi Q9CU62.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000045312 ; ENSMUSP00000044645 ; ENSMUSG00000041133 .
GeneIDi 24061.
KEGGi mmu:24061.
UCSCi uc009upx.2. mouse.

Organism-specific databases

CTDi 8243.
MGIi MGI:1344345. Smc1a.

Phylogenomic databases

eggNOGi COG1196.
GeneTreei ENSGT00580000081569.
HOGENOMi HOG000195481.
HOVERGENi HBG039593.
InParanoidi Q9CU62.
KOi K06636.
OMAi FKSYRGH.
OrthoDBi EOG7K3TK5.
TreeFami TF101156.

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

EvolutionaryTracei Q9CU62.
NextBioi 304025.
PROi Q9CU62.
SOURCEi Search...

Gene expression databases

Bgeei Q9CU62.
CleanExi MM_SMC1A.
ExpressionAtlasi Q9CU62. baseline and differential.
Genevestigatori Q9CU62.

Family and domain databases

Gene3Di 3.40.50.300. 4 hits.
InterProi IPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR029683. SMC1A.
IPR010935. SMC_hinge.
[Graphical view ]
PANTHERi PTHR18937:SF170. PTHR18937:SF170. 1 hit.
Pfami PF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF005719. SMC. 1 hit.
SMARTi SM00968. SMC_hinge. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.

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: October 29, 2014
This is version 123 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

External Data

Dasty 3