Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9CU62

- SMC1A_MOUSE

UniProt

Q9CU62 - SMC1A_MOUSE

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. meiotic nuclear division Source: UniProtKB
    3. mitotic cell cycle checkpoint Source: UniProtKB
    4. mitotic nuclear division Source: UniProtKB-KW
    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. sister chromatid cohesion Source: Ensembl
    9. stem cell maintenance Source: MGI

    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. cytoplasm Source: Ensembl
    2. kinetochore Source: UniProtKB
    3. meiotic cohesin complex Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB

    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

    ArrayExpressiQ9CU62.
    BgeeiQ9CU62.
    CleanExiMM_SMC1A.
    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. 7 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.
    InParanoidiA2AFQ5.
    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.
    IPR010935. SMC_hinge.
    [Graphical view]
    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

    MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG     50
    EKTSNLRVKT LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG 100
    GSSEYKINNK VVQLHEYSEE LEKLGILIKA RNFLVFQGAV ESIAMKNPKE 150
    RTALFEEISR SGELAQEYDK RKKEMVKAEE DTQFNYHRKK NIAAERKEAK 200
    QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK ELASKNKEIE 250
    KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK 300
    AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF 350
    EERMEEESQS QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ 400
    KADQDRLDLE ERKKVETEAK IKQKLREIEE NQKRIEKLEE YITTSKQSLE 450
    EQKKLEGELT EEVEMAKRRI DEINKELNQV MEQLGDARID RQESSRQQRK 500
    AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK NMDAIIVDSE 550
    KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY 600
    EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG 650
    VISGGASDLK AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ 700
    VQSQAHGLQM RLKYSQSDLE QTKTRHLALN LQEKSKLESE LANFGPRIND 750
    IKRIIQSRER EMKDLKEKMN QVEDEVFEEF CREIGVRNIR EFEEEKVKRQ 800
    NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ TVKKDENEIE 850
    KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG 900
    ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI 950
    SQEEGSSQGE ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK 1000
    QEMNTLQQKL NEQQSVLQRI AAPNMKAMEK LESVRDKFQE TSDEFEAARK 1050
    RAKKAKQAFE QIKKERFDRF NACFESVATN IDEIYKALSR NSSAQAFLGP 1100
    ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL LFAIHSYKPA 1150
    PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL 1200
    IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ 1233
    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. 7 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 A2AFQ5.
    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

    ArrayExpressi Q9CU62.
    Bgeei Q9CU62.
    CleanExi MM_SMC1A.
    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.
    IPR010935. SMC_hinge.
    [Graphical view ]
    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

    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 1, 2014
    This is version 122 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