Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q14683

- SMC1A_HUMAN

UniProt

Q14683 - SMC1A_HUMAN

(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)

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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 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
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_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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11111. SMC1A.

Subcellular locationi

Nucleus 1 Publication. Chromosome 1 Publication. Chromosome › centromere › kinetochore 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
Complete GO annotation...

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. 2 Publications
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

BgeeiQ14683.
CleanExiHS_SMC1A.
ExpressionAtlasiQ14683. baseline and differential.
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. 89 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.
GeneTreeiENSGT00580000081569.
HOGENOMiHOG000195481.
HOVERGENiHBG039593.
InParanoidiQ14683.
KOiK06636.
OMAiFNFKSYK.
PhylomeDBiQ14683.
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.

Q14683-1 [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 DSVSGSQRIS 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):143,233
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. 2 Publications
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 89 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 GC0XM053401.
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.
GeneTreei ENSGT00580000081569.
HOGENOMi HOG000195481.
HOVERGENi HBG039593.
InParanoidi Q14683.
KOi K06636.
OMAi FNFKSYK.
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

Bgeei Q14683.
CleanExi HS_SMC1A.
ExpressionAtlasi Q14683. baseline and differential.
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.
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. "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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 157 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

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 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.
© 2002– 2015 UniProt Consortium | License & Disclaimer