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Q14683 (SMC1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SMC1A
Synonyms:DXS423E, KIAA0178, SB1.8, SMC1, SMC1L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1233 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12

Subcellular location

Nucleus. Chromosome. Chromosomecentromerekinetochore. 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. Ref.10

Domain

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.

Post-translational modification

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. Ref.6 Ref.11

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Miscellaneous

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

Sequence similarities

Belongs to the SMC family. SMC1 subfamily.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Meiosis
Mitosis
   Cellular componentCentromere
Chromosome
Kinetochore
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Mental retardation
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: InterPro

DNA repair

Traceable author statement Ref.6. Source: UniProtKB

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

meiotic nuclear division

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle checkpoint

Inferred from direct assay Ref.6. Source: UniProtKB

mitotic sister chromatid cohesion

Traceable author statement Ref.10. Source: UniProtKB

mitotic sister chromatid segregation

Traceable author statement Ref.1. Source: UniProtKB

mitotic spindle organization

Traceable author statement Ref.10. Source: UniProtKB

negative regulation of DNA endoreduplication

Inferred from mutant phenotype PubMed 15917200. Source: BHF-UCL

response to radiation

Inferred from expression pattern Ref.6. Source: UniProtKB

signal transduction in response to DNA damage

Inferred from direct assay Ref.6. Source: UniProtKB

sister chromatid cohesion

Inferred from mutant phenotype PubMed 15917200. Source: BHF-UCL

stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromosome

Traceable author statement. Source: Reactome

chromosome, centromeric region

Traceable author statement. Source: Reactome

cohesin core heterodimer

Traceable author statement Ref.9. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed nuclear chromosome

Traceable author statement Ref.1. Source: ProtInc

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.10. Source: UniProtKB

meiotic cohesin complex

Inferred from direct assay PubMed 21242291. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from direct assay Ref.9. Source: UniProtKB

microtubule motor activity

Non-traceable author statement Ref.10. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6Ref.12PubMed 16438930. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.9PubMed 11590136. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB83EBI-80690,EBI-6927928From a different organism.
MCM7P339938EBI-80690,EBI-355924

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12331233Structural maintenance of chromosomes protein 1A
PRO_0000118989

Regions

Nucleotide binding32 – 398ATP Potential
Region504 – 659156Flexible hinge
Coiled coil104 – 12421 Potential
Coiled coil163 – 503341 Potential
Coiled coil660 – 935276 Potential
Coiled coil991 – 106878 Potential
Compositional bias1128 – 116336Ala/Asp-rich (DA-box)

Amino acid modifications

Modified residue3581Phosphoserine Ref.14
Modified residue3601Phosphoserine Ref.14 Ref.15 Ref.18
Modified residue6481N6-acetyllysine Ref.17
Modified residue7131N6-acetyllysine Ref.17
Modified residue9571Phosphoserine; by ATM Ref.6 Ref.15 Ref.16 Ref.18
Modified residue9661Phosphoserine; by ATM and ATR Ref.6 Ref.11 Ref.14 Ref.18
Modified residue9701Phosphoserine Ref.15
Modified residue10371N6-acetyllysine By similarity

Natural variations

Natural variant281T → P.
Corresponds to variant rs34530151 [ dbSNP | Ensembl ].
VAR_052438
Natural variant58 – 625Missing in CDLS2.
VAR_062785
Natural variant1331F → V in CDLS2. Ref.22 Ref.25
VAR_062786
Natural variant1411E → K in CDLS2. Ref.25
VAR_062787
Natural variant1961R → H in CDLS2. Ref.22 Ref.23 Ref.25 Ref.26
VAR_062788
Natural variant2681Missing in CDLS2. Ref.25 Ref.26
VAR_062789
Natural variant3061Missing in CDLS2. Ref.25
VAR_062790
Natural variant3981R → Q in CDLS2. Ref.25
VAR_062791
Natural variant4931E → A in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. Ref.21 Ref.24
VAR_026529
Natural variant4961R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. Ref.22 Ref.24 Ref.25
VAR_062792
Natural variant4961R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. Ref.22 Ref.24 Ref.25
VAR_062793
Natural variant6831Missing in CDLS2. Ref.25
VAR_062794
Natural variant6931R → G in CDLS2. Ref.25
VAR_062795
Natural variant7111R → Q in CDLS2. Ref.26
VAR_064542
Natural variant7111R → W in CDLS2. Ref.22 Ref.25
VAR_062796
Natural variant7811C → F in CDLS2. Ref.25
VAR_062797
Natural variant7841I → T in CDLS2. Ref.27
VAR_064543
Natural variant7901R → Q in CDLS2. Ref.22 Ref.25
VAR_062798
Natural variant8161R → G in CDLS2. Ref.25
VAR_062799
Natural variant8321Missing in CDLS2. Ref.21
VAR_026530
Natural variant10491R → Q in CDLS2. Ref.25
VAR_062800
Natural variant10851Y → C in CDLS2. Ref.23
VAR_062801
Natural variant11221F → L in CDLS2. Ref.22 Ref.25
VAR_062802
Natural variant11231R → W in CDLS2. Ref.25
VAR_062803

Experimental info

Mutagenesis9571S → A: Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966. Ref.6
Mutagenesis9661S → A: Reduces phosphorylation and the S-phase checkpoint activation. Increases sensitivity to DNA methylation. Abolishes S-phase activation; when associated with A-957. Ref.6 Ref.11
Sequence conflict163 – 1642EL → DV in AAB34405. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q14683 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: E0A44CA7476C88A6

FASTA1,233143,233
        10         20         30         40         50         60 
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT 

        70         80         90        100        110        120 
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE 

       130        140        150        160        170        180 
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE 

       190        200        210        220        230        240 
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK 

       250        260        270        280        290        300 
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK 

       310        320        330        340        350        360 
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS 

       370        380        390        400        410        420 
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK 

       430        440        450        460        470        480 
IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV 

       490        500        510        520        530        540 
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK 

       550        560        570        580        590        600 
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY 

       610        620        630        640        650        660 
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK 

       670        680        690        700        710        720 
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE 

       730        740        750        760        770        780 
QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF 

       790        800        810        820        830        840 
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ 

       850        860        870        880        890        900 
TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG 

       910        920        930        940        950        960 
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGSSQGE 

       970        980        990       1000       1010       1020 
DSVSGSQRIS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI 

      1030       1040       1050       1060       1070       1080 
AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN 

      1090       1100       1110       1120       1130       1140 
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL 

      1150       1160       1170       1180       1190       1200 
LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL 

      1210       1220       1230 
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Localization of human SMC1 protein at kinetochores."
Gregson H.C., Van Hooser A.A., Ball A.R. Jr., Brinkley B.R., Yokomori K.
Chromosome Res. 10:267-277(2002) [PubMed] [Europe PMC] [Abstract]
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"X-linked Cornelia de Lange syndrome owing to SMC1L1 mutations."
Musio A., Selicorni A., Focarelli M.L., Gervasini C., Milani D., Russo S., Vezzoni P., Larizza L.
Nat. Genet. 38:528-530(2006) [PubMed] [Europe PMC] [Abstract]
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]"Cornelia de Lange syndrome mutations in SMC1A or SMC3 affect binding to DNA."
Revenkova E., Focarelli M.L., Susani L., Paulis M., Bassi M.T., Mannini L., Frattini A., Delia D., Krantz I., Vezzoni P., Jessberger R., Musio A.
Hum. Mol. Genet. 18:418-427(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Hypertrophic cardiomyopathy in a girl with Cornelia de Lange syndrome due to mutation in SMC1A."
Limongelli G., Russo S., Digilio M.C., Masciadri M., Pacileo G., Fratta F., Martone F., Maddaloni V., D'Alessandro R., Calabro P., Russo M.G., Calabro R., Larizza L.
Am. J. Med. Genet. A 152:2127-2129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CDLS2 THR-784.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14352.1.
PIRI54383.
RefSeqNP_006297.2. NM_006306.3.
UniGeneHs.211602.

3D structure databases

ProteinModelPortalQ14683.
SMRQ14683. Positions 2-223, 499-675, 990-1223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113871. 85 interactions.
DIPDIP-30911N.
IntActQ14683. 45 interactions.
MINTMINT-233274.
STRING9606.ENSP00000323421.

PTM databases

PhosphoSiteQ14683.

Polymorphism databases

DMDM29336622.

Proteomic databases

MaxQBQ14683.
PaxDbQ14683.
PeptideAtlasQ14683.
PRIDEQ14683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322213; ENSP00000323421; ENSG00000072501.
ENST00000594240; ENSP00000471583; ENSG00000269384.
GeneID8243.
KEGGhsa:8243.
UCSCuc004dsg.3. human.

Organism-specific databases

CTD8243.
GeneCardsGC0XM053417.
GeneReviewsSMC1A.
HGNCHGNC:11111. SMC1A.
HPACAB025404.
HPA005499.
MIM300040. gene.
300590. phenotype.
neXtProtNX_Q14683.
Orphanet199. Cornelia de Lange syndrome.
PharmGKBPA35961.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1196.
HOGENOMHOG000195481.
HOVERGENHBG039593.
InParanoidQ14683.
KOK06636.
OMAFKSYRGH.
PhylomeDBQ14683.
TreeFamTF101156.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_71. Gene Expression.
SignaLinkQ14683.

Gene expression databases

ArrayExpressQ14683.
BgeeQ14683.
CleanExHS_SMC1A.
GenevestigatorQ14683.

Family and domain databases

Gene3D3.40.50.300. 4 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR010935. SMC_hinge.
[Graphical view]
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSMC1A. human.
GeneWikiSMC1A.
GenomeRNAi8243.
NextBio31006.
PROQ14683.
SOURCESearch...

Entry information

Entry nameSMC1A_HUMAN
AccessionPrimary (citable) accession number: Q14683
Secondary accession number(s): O14995, Q16351, Q2M228
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM