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Q14683

- SMC1A_HUMAN

UniProt

Q14683 - SMC1A_HUMAN

Protein

Structural maintenance of chromosomes protein 1A

Gene

SMC1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Involved in chromosome cohesion during cell cycle and in DNA repair. 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.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: UniProtKB
    3. microtubule motor activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein heterodimerization activity Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: UniProtKB
    2. gene expression Source: Reactome
    3. meiotic nuclear division Source: UniProtKB
    4. mitotic cell cycle Source: Reactome
    5. mitotic cell cycle checkpoint Source: UniProtKB
    6. mitotic sister chromatid cohesion Source: UniProtKB
    7. mitotic sister chromatid segregation Source: UniProtKB
    8. mitotic spindle organization Source: UniProtKB
    9. mRNA splicing, via spliceosome Source: Reactome
    10. negative regulation of DNA endoreduplication Source: BHF-UCL
    11. response to radiation Source: UniProtKB
    12. RNA splicing Source: Reactome
    13. signal transduction in response to DNA damage Source: UniProtKB
    14. sister chromatid cohesion Source: BHF-UCL
    15. stem cell maintenance Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_75792. Meiotic synapsis.
    SignaLinkiQ14683.

    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):
    Sb1.8
    Gene namesi
    Name:SMC1A
    Synonyms:DXS423E, KIAA0178, SB1.8, SMC1, SMC1L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11111. SMC1A.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication. Chromosomecentromerekinetochore 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. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex. 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. Integral component of the functional centromere-kinetochore complex at the kinetochore region during mitosis.

    GO - Cellular componenti

    1. chromosome Source: Reactome
    2. chromosome, centromeric region Source: Reactome
    3. cohesin core heterodimer Source: UniProtKB
    4. condensed chromosome kinetochore Source: UniProtKB-SubCell
    5. condensed nuclear chromosome Source: ProtInc
    6. cytoplasm Source: HPA
    7. cytosol Source: Reactome
    8. kinetochore Source: UniProtKB
    9. meiotic cohesin complex Source: UniProtKB
    10. nucleoplasm Source: Reactome
    11. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Cornelia de Lange syndrome 2 (CDLS2) [MIM:300590]: A form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems. Characterized by facial dysmorphisms, abnormal hands and feet, growth delay, cognitive retardation, hirsutism, gastroesophageal dysfunction and cardiac, ophthalmologic and genitourinary anomalies.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 625Missing in CDLS2.
    VAR_062785
    Natural varianti133 – 1331F → V in CDLS2. 2 Publications
    VAR_062786
    Natural varianti141 – 1411E → K in CDLS2. 1 Publication
    VAR_062787
    Natural varianti196 – 1961R → H in CDLS2. 4 Publications
    VAR_062788
    Natural varianti268 – 2681Missing in CDLS2. 2 Publications
    VAR_062789
    Natural varianti306 – 3061Missing in CDLS2. 1 Publication
    VAR_062790
    Natural varianti398 – 3981R → Q in CDLS2. 1 Publication
    VAR_062791
    Natural varianti493 – 4931E → A in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 1 Publication
    VAR_026529
    Natural varianti496 – 4961R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 Publications
    VAR_062792
    Natural varianti496 – 4961R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 Publications
    VAR_062793
    Natural varianti683 – 6831Missing in CDLS2. 1 Publication
    VAR_062794
    Natural varianti693 – 6931R → G in CDLS2. 1 Publication
    VAR_062795
    Natural varianti711 – 7111R → Q in CDLS2. 1 Publication
    VAR_064542
    Natural varianti711 – 7111R → W in CDLS2. 2 Publications
    VAR_062796
    Natural varianti781 – 7811C → F in CDLS2. 1 Publication
    VAR_062797
    Natural varianti784 – 7841I → T in CDLS2. 1 Publication
    VAR_064543
    Natural varianti790 – 7901R → Q in CDLS2. 2 Publications
    VAR_062798
    Natural varianti816 – 8161R → G in CDLS2. 1 Publication
    VAR_062799
    Natural varianti832 – 8321Missing in CDLS2. 1 Publication
    VAR_026530
    Natural varianti1049 – 10491R → Q in CDLS2. 1 Publication
    VAR_062800
    Natural varianti1085 – 10851Y → C in CDLS2. 1 Publication
    VAR_062801
    Natural varianti1122 – 11221F → L in CDLS2. 2 Publications
    VAR_062802
    Natural varianti1123 – 11231R → W in CDLS2. 1 Publication
    VAR_062803

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi957 – 9571S → A: Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966. 1 Publication
    Mutagenesisi966 – 9661S → A: Reduces phosphorylation and the S-phase checkpoint activation. Increases sensitivity to DNA methylation. Abolishes S-phase activation; when associated with A-957. 2 Publications

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300590. phenotype.
    Orphaneti199. Cornelia de Lange syndrome.
    PharmGKBiPA35961.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12331233Structural maintenance of chromosomes protein 1APRO_0000118989Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei358 – 3581Phosphoserine1 Publication
    Modified residuei360 – 3601Phosphoserine3 Publications
    Modified residuei648 – 6481N6-acetyllysine1 Publication
    Modified residuei713 – 7131N6-acetyllysine1 Publication
    Modified residuei957 – 9571Phosphoserine; by ATM4 Publications
    Modified residuei966 – 9661Phosphoserine; by ATM and ATR4 Publications
    Modified residuei970 – 9701Phosphoserine1 Publication
    Modified residuei1037 – 10371N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated by ATM upon ionizing radiation in a NBS1-dependent manner. Phosphorylated by ATR upon DNA methylation in a MSH2/MSH6-dependent manner. Phosphorylation of Ser-957 and Ser-966 activates it and is required for S-phase checkpoint activation.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14683.
    PaxDbiQ14683.
    PeptideAtlasiQ14683.
    PRIDEiQ14683.

    PTM databases

    PhosphoSiteiQ14683.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14683.
    BgeeiQ14683.
    CleanExiHS_SMC1A.
    GenevestigatoriQ14683.

    Organism-specific databases

    HPAiCAB025404.
    HPA005499.

    Interactioni

    Subunit structurei

    Interacts with POLE. Interacts with SYCP2. Interacts with BRCA1. Found in a complex with CDCA5, SMC3 and RAD21, PDS5A/APRIN and PDS5B/SCC-112 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 BRCA1. Interacts with NDC80. Interacts with RPGR By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB83EBI-80690,EBI-6927928From a different organism.
    MCM7P339938EBI-80690,EBI-355924

    Protein-protein interaction databases

    BioGridi113871. 84 interactions.
    DIPiDIP-30911N.
    IntActiQ14683. 46 interactions.
    MINTiMINT-233274.
    STRINGi9606.ENSP00000323421.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14683.
    SMRiQ14683. Positions 2-223, 499-675, 990-1223.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni504 – 659156Flexible hingeAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili104 – 12421Sequence AnalysisAdd
    BLAST
    Coiled coili163 – 503341Sequence AnalysisAdd
    BLAST
    Coiled coili660 – 935276Sequence AnalysisAdd
    BLAST
    Coiled coili991 – 106878Sequence 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.
    HOGENOMiHOG000195481.
    HOVERGENiHBG039593.
    InParanoidiQ14683.
    KOiK06636.
    OMAiFKSYRGH.
    PhylomeDBiQ14683.
    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.

    Q14683-1 [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 DSVSGSQRIS 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):143,233
    Last modified:October 1, 2002 - v2
    Checksum:iE0A44CA7476C88A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti163 – 1642EL → DV in AAB34405. (PubMed:7757074)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281T → P.
    Corresponds to variant rs34530151 [ dbSNP | Ensembl ].
    VAR_052438
    Natural varianti58 – 625Missing in CDLS2.
    VAR_062785
    Natural varianti133 – 1331F → V in CDLS2. 2 Publications
    VAR_062786
    Natural varianti141 – 1411E → K in CDLS2. 1 Publication
    VAR_062787
    Natural varianti196 – 1961R → H in CDLS2. 4 Publications
    VAR_062788
    Natural varianti268 – 2681Missing in CDLS2. 2 Publications
    VAR_062789
    Natural varianti306 – 3061Missing in CDLS2. 1 Publication
    VAR_062790
    Natural varianti398 – 3981R → Q in CDLS2. 1 Publication
    VAR_062791
    Natural varianti493 – 4931E → A in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 1 Publication
    VAR_026529
    Natural varianti496 – 4961R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 Publications
    VAR_062792
    Natural varianti496 – 4961R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 2 Publications
    VAR_062793
    Natural varianti683 – 6831Missing in CDLS2. 1 Publication
    VAR_062794
    Natural varianti693 – 6931R → G in CDLS2. 1 Publication
    VAR_062795
    Natural varianti711 – 7111R → Q in CDLS2. 1 Publication
    VAR_064542
    Natural varianti711 – 7111R → W in CDLS2. 2 Publications
    VAR_062796
    Natural varianti781 – 7811C → F in CDLS2. 1 Publication
    VAR_062797
    Natural varianti784 – 7841I → T in CDLS2. 1 Publication
    VAR_064543
    Natural varianti790 – 7901R → Q in CDLS2. 2 Publications
    VAR_062798
    Natural varianti816 – 8161R → G in CDLS2. 1 Publication
    VAR_062799
    Natural varianti832 – 8321Missing in CDLS2. 1 Publication
    VAR_026530
    Natural varianti1049 – 10491R → Q in CDLS2. 1 Publication
    VAR_062800
    Natural varianti1085 – 10851Y → C in CDLS2. 1 Publication
    VAR_062801
    Natural varianti1122 – 11221F → L in CDLS2. 2 Publications
    VAR_062802
    Natural varianti1123 – 11231R → W in CDLS2. 1 Publication
    VAR_062803

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78271 mRNA. Translation: AAB34405.1.
    D80000 mRNA. Translation: BAA11495.2.
    AL161779, Z97054 Genomic DNA. Translation: CAI42089.1.
    Z97054, AL161779 Genomic DNA. Translation: CAI42646.1.
    BC112127 mRNA. Translation: AAI12128.1.
    CCDSiCCDS14352.1.
    PIRiI54383.
    RefSeqiNP_006297.2. NM_006306.3.
    UniGeneiHs.211602.

    Genome annotation databases

    EnsembliENST00000322213; ENSP00000323421; ENSG00000072501.
    GeneIDi8243.
    KEGGihsa:8243.
    UCSCiuc004dsg.3. human.

    Polymorphism databases

    DMDMi29336622.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78271 mRNA. Translation: AAB34405.1 .
    D80000 mRNA. Translation: BAA11495.2 .
    AL161779 , Z97054 Genomic DNA. Translation: CAI42089.1 .
    Z97054 , AL161779 Genomic DNA. Translation: CAI42646.1 .
    BC112127 mRNA. Translation: AAI12128.1 .
    CCDSi CCDS14352.1.
    PIRi I54383.
    RefSeqi NP_006297.2. NM_006306.3.
    UniGenei Hs.211602.

    3D structure databases

    ProteinModelPortali Q14683.
    SMRi Q14683. Positions 2-223, 499-675, 990-1223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113871. 84 interactions.
    DIPi DIP-30911N.
    IntActi Q14683. 46 interactions.
    MINTi MINT-233274.
    STRINGi 9606.ENSP00000323421.

    PTM databases

    PhosphoSitei Q14683.

    Polymorphism databases

    DMDMi 29336622.

    Proteomic databases

    MaxQBi Q14683.
    PaxDbi Q14683.
    PeptideAtlasi Q14683.
    PRIDEi Q14683.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322213 ; ENSP00000323421 ; ENSG00000072501 .
    GeneIDi 8243.
    KEGGi hsa:8243.
    UCSCi uc004dsg.3. human.

    Organism-specific databases

    CTDi 8243.
    GeneCardsi GC0XM053417.
    GeneReviewsi SMC1A.
    HGNCi HGNC:11111. SMC1A.
    HPAi CAB025404.
    HPA005499.
    MIMi 300040. gene.
    300590. phenotype.
    neXtProti NX_Q14683.
    Orphaneti 199. Cornelia de Lange syndrome.
    PharmGKBi PA35961.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1196.
    HOGENOMi HOG000195481.
    HOVERGENi HBG039593.
    InParanoidi Q14683.
    KOi K06636.
    OMAi FKSYRGH.
    PhylomeDBi Q14683.
    TreeFami TF101156.

    Enzyme and pathway databases

    Reactomei REACT_150266. Establishment of Sister Chromatid Cohesion.
    REACT_150421. Cohesin Loading onto Chromatin.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_75792. Meiotic synapsis.
    SignaLinki Q14683.

    Miscellaneous databases

    ChiTaRSi SMC1A. human.
    GeneWikii SMC1A.
    GenomeRNAii 8243.
    NextBioi 31006.
    PROi Q14683.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14683.
    Bgeei Q14683.
    CleanExi HS_SMC1A.
    Genevestigatori Q14683.

    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. "The human SB1.8 gene (DXS423E) encodes a putative chromosome segregation protein conserved in lower eukaryotes and prokaryotes."
      Rocques P.J., Clark J., Ball S., Crew J., Gill S., Christodoulou Z., Borts R.H., Louis E.J., Davies K.E., Cooper C.S.
      Hum. Mol. Genet. 4:243-249(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    2. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Brain.
    6. "SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint."
      Yazdi P.T., Wang Y., Zhao S., Patel N., Lee E.Y.-H.P., Qin J.
      Genes Dev. 16:571-582(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 945-984, FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT SER-957 AND SER-966, MUTAGENESIS OF SER-957 AND SER-966.
    7. "HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins."
      Chen Y., Sharp Z.D., Lee W.-H.
      J. Biol. Chem. 272:24081-24087(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDC80.
    8. "Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins."
      Zheng L., Chen Y., Lee W.-H.
      Mol. Cell. Biol. 19:5417-5428(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDC80.
    9. "Characterization of vertebrate cohesin complexes and their regulation in prophase."
      Sumara I., Vorlaufer E., Gieffers C., Peters B.H., Peters J.-M.
      J. Cell Biol. 151:749-762(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; STAG1 OR STAG2.
    10. Cited for: SUBCELLULAR LOCATION DURING CELL CYCLE.
    11. "MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation."
      Wang Y., Qin J.
      Proc. Natl. Acad. Sci. U.S.A. 100:15387-15392(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-966, MUTAGENESIS OF SER-966.
    12. "Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates."
      Rankin S., Ayad N.G., Kirschner M.W.
      Mol. Cell 18:185-200(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CDCA5; SMC3; RAD21; PDS5A AND PDS5B.
    13. Erratum
      Rankin S., Ayad N.G., Kirschner M.W.
      Mol. Cell 18:609-609(2005)
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-360 AND SER-966, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-957 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-648 AND LYS-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-957 AND SER-966, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: VARIANTS CDLS2 ALA-493 AND GLN-832 DEL.
    22. "Mutations in cohesin complex members SMC3 and SMC1A cause a mild variant of Cornelia de Lange syndrome with predominant mental retardation."
      Deardorff M.A., Kaur M., Yaeger D., Rampuria A., Korolev S., Pie J., Gil-Rodriguez C., Arnedo M., Loeys B., Kline A.D., Wilson M., Lillquist K., Siu V., Ramos F.J., Musio A., Jackson L.S., Dorsett D., Krantz I.D.
      Am. J. Hum. Genet. 80:485-494(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDLS2 58-VAL--ARG-62 DEL; VAL-133; HIS-196; CYS-496; HIS-496; TRP-711; GLN-790 AND LEU-1122.
    23. "Incidence and clinical features of X-linked Cornelia de Lange syndrome due to SMC1L1 mutations."
      Borck G., Zarhrate M., Bonnefont J.-P., Munnich A., Cormier-Daire V., Colleaux L.
      Hum. Mutat. 28:205-206(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDLS2 HIS-196 AND CYS-1085.
    24. Cited for: CHARACTERIZATION OF VARIANTS CDLS2 ALA-493; CYS-496 AND HIS-496, GENOMIC INSTABILITY OF CDLS CELL LINES TO IONIZING RADIATION.
    25. "SMC1A expression and mechanism of pathogenicity in probands with X-Linked Cornelia de Lange syndrome."
      Liu J., Feldman R., Zhang Z., Deardorff M.A., Haverfield E.V., Kaur M., Li J.R., Clark D., Kline A.D., Waggoner D.J., Das S., Jackson L.G., Krantz I.D.
      Hum. Mutat. 30:1535-1542(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDLS2 58-VAL--ARG-62 DEL; VAL-133; LYS-141; HIS-196; LYS-268 DEL; SER-306 DEL; GLN-398; CYS-496; HIS-496; GLU-683 DEL; GLY-693; TRP-711; PHE-781; GLN-790; GLY-816; GLN-1049; LEU-1122 AND TRP-1123.
    26. "Mutations and variants in the cohesion factor genes NIPBL, SMC1A, and SMC3 in a cohort of 30 unrelated patients with Cornelia de Lange syndrome."
      Pie J., Gil-Rodriguez M.C., Ciero M., Lopez-Vinas E., Ribate M.P., Arnedo M., Deardorff M.A., Puisac B., Legarreta J., de Karam J.C., Rubio E., Bueno I., Baldellou A., Calvo M.T., Casals N., Olivares J.L., Losada A., Hegardt F.G.
      , Krantz I.D., Gomez-Puertas P., Ramos F.J.
      Am. J. Med. Genet. A 152:924-929(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDLS2 HIS-196; LYS-268 DEL AND GLN-711.
    27. Cited for: VARIANT CDLS2 THR-784.

    Entry informationi

    Entry nameiSMC1A_HUMAN
    AccessioniPrimary (citable) accession number: Q14683
    Secondary accession number(s): O14995, Q16351, Q2M228
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Mutated Cornelia de Lange cell lines display genomic instability and sensitivity to ionizing radiation and interstrand cross-linking agents.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3