Q14683 - SMC1A_HUMAN
UniProt
Q14683 - SMC1A_HUMAN
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Protein
Structural maintenance of chromosomes protein 1A
Gene
SMC1A
Organism
Homo sapiens (Human)
Status
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Nucleotide bindingi | 32 – 39 | 8 | ATPSequence Analysis |   |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- chromatin binding Source: UniProtKB
- microtubule motor activity Source: UniProtKB
- poly(A) RNA binding Source: UniProtKB
- protein heterodimerization activity Source: UniProtKB
GO - Biological processi
- cell division Source: UniProtKB-KW
- DNA repair Source: UniProtKB
- gene expression Source: Reactome
- meiotic nuclear division Source: UniProtKB
- mitotic cell cycle Source: Reactome
- mitotic cell cycle checkpoint Source: UniProtKB
- mitotic sister chromatid cohesion Source: UniProtKB
- mitotic sister chromatid segregation Source: UniProtKB
- mitotic spindle organization Source: UniProtKB
- mRNA splicing, via spliceosome Source: Reactome
- negative regulation of DNA endoreduplication Source: BHF-UCL
- response to radiation Source: UniProtKB
- RNA splicing Source: Reactome
- signal transduction in response to DNA damage Source: UniProtKB
- sister chromatid cohesion Source: BHF-UCL
- stem cell maintenance Source: Ensembl
Keywords - Biological processi
Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, MitosisKeywords - Ligandi
ATP-binding, Nucleotide-bindingEnzyme 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. |
Names & Taxonomyi
| Protein namesi | Recommended name: Structural maintenance of chromosomes protein 1AShort 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 |
| Organismi | Homo sapiens (Human) |
| Taxonomic identifieri | 9606 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
| Proteomesi | UP000005640: Chromosome X |
Organism-specific databases
| HGNCi | HGNC: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.
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
- chromosome Source: Reactome
- chromosome, centromeric region Source: Reactome
- cohesin core heterodimer Source: UniProtKB
- condensed chromosome kinetochore Source: UniProtKB-SubCell
- condensed nuclear chromosome Source: ProtInc
- cytoplasm Source: HPA
- cytosol Source: Reactome
- kinetochore Source: UniProtKB
- meiotic cohesin complex Source: UniProtKB
- nucleolus Source: HPA
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
Keywords - Cellular componenti
Centromere, Chromosome, Kinetochore, NucleusPathology & Biotechi
Involvement in diseasei
Cornelia de Lange syndrome 26 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300590| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Natural varianti | 58 – 62 | 5 | Missing in CDLS2. 2 Publications | | VAR_062785 | |
| Natural varianti | 133 – 133 | 1 | F → V in CDLS2. 2 Publications | | VAR_062786 | |
| Natural varianti | 141 – 141 | 1 | E → K in CDLS2. 1 Publication | | VAR_062787 | |
| Natural varianti | 196 – 196 | 1 | R → H in CDLS2. 4 Publications | | VAR_062788 | |
| Natural varianti | 268 – 268 | 1 | Missing in CDLS2. 2 Publications | | VAR_062789 | |
| Natural varianti | 306 – 306 | 1 | Missing in CDLS2. 1 Publication | | VAR_062790 | |
| Natural varianti | 398 – 398 | 1 | R → Q in CDLS2. 1 Publication | | VAR_062791 | |
| Natural varianti | 493 – 493 | 1 | E → A 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_026529 | |
| Natural varianti | 496 – 496 | 1 | R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 Publications | | VAR_062792 | |
| Natural varianti | 496 – 496 | 1 | R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 Publications | | VAR_062793 | |
| Natural varianti | 683 – 683 | 1 | Missing in CDLS2. 1 Publication | | VAR_062794 | |
| Natural varianti | 693 – 693 | 1 | R → G in CDLS2. 1 Publication | | VAR_062795 | |
| Natural varianti | 711 – 711 | 1 | R → Q in CDLS2. 1 Publication | | VAR_064542 | |
| Natural varianti | 711 – 711 | 1 | R → W in CDLS2. 2 Publications | | VAR_062796 | |
| Natural varianti | 781 – 781 | 1 | C → F in CDLS2. 1 Publication | | VAR_062797 | |
| Natural varianti | 784 – 784 | 1 | I → T in CDLS2. 1 Publication | | VAR_064543 | |
| Natural varianti | 790 – 790 | 1 | R → Q in CDLS2. 2 Publications | | VAR_062798 | |
| Natural varianti | 816 – 816 | 1 | R → G in CDLS2. 1 Publication | | VAR_062799 | |
| Natural varianti | 832 – 832 | 1 | Missing in CDLS2. 1 Publication | | VAR_026530 | |
| Natural varianti | 1049 – 1049 | 1 | R → Q in CDLS2. 1 Publication | | VAR_062800 | |
| Natural varianti | 1085 – 1085 | 1 | Y → C in CDLS2. 1 Publication | | VAR_062801 | |
| Natural varianti | 1122 – 1122 | 1 | F → L in CDLS2. 2 Publications | | VAR_062802 | |
| Natural varianti | 1123 – 1123 | 1 | R → W in CDLS2. 1 Publication | | VAR_062803 |
Mutagenesis
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Mutagenesisi | 957 – 957 | 1 | S → A: Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966. 1 Publication | | ||
| Mutagenesisi | 966 – 966 | 1 | S → 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 retardationOrganism-specific databases
| MIMi | 300590. phenotype. |
| Orphaneti | 199. Cornelia de Lange syndrome. |
| PharmGKBi | PA35961. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Chaini | 1 – 1233 | 1233 | Structural maintenance of chromosomes protein 1A | | PRO_0000118989 | Add BLAST |
Amino acid modifications
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Modified residuei | 358 – 358 | 1 | Phosphoserine1 Publication | | ||
| Modified residuei | 360 – 360 | 1 | Phosphoserine3 Publications | | ||
| Modified residuei | 648 – 648 | 1 | N6-acetyllysine1 Publication | | ||
| Modified residuei | 713 – 713 | 1 | N6-acetyllysine1 Publication | | ||
| Modified residuei | 957 – 957 | 1 | Phosphoserine; by ATM4 Publications | | ||
| Modified residuei | 966 – 966 | 1 | Phosphoserine; by ATM and ATR4 Publications | | ||
| Modified residuei | 970 – 970 | 1 | Phosphoserine1 Publication | | ||
| Modified residuei | 1037 – 1037 | 1 | N6-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, PhosphoproteinProteomic databases
| MaxQBi | Q14683. |
| PaxDbi | Q14683. |
| PeptideAtlasi | Q14683. |
| PRIDEi | Q14683. |
PTM databases
| PhosphoSitei | Q14683. |
Expressioni
Gene expression databases
| Bgeei | Q14683. |
| CleanExi | HS_SMC1A. |
| ExpressionAtlasi | Q14683. baseline and differential. |
| Genevestigatori | Q14683. |
Organism-specific databases
| HPAi | CAB025404. 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
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Q99IB8 | 3 | EBI-80690,EBI-6927928 | From a different organism. | |
| MCM7 | P33993 | 8 | EBI-80690,EBI-355924 |
Protein-protein interaction databases
| BioGridi | 113871. 89 interactions. |
| DIPi | DIP-30911N. |
| IntActi | Q14683. 46 interactions. |
| MINTi | MINT-233274. |
| STRINGi | 9606.ENSP00000323421. |
Structurei
3D structure databases
| ProteinModelPortali | Q14683. |
| SMRi | Q14683. Positions 2-223, 499-675, 990-1223. |
| ModBasei | Search... |
| MobiDBi | Search... |
Family & Domainsi
Region
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Regioni | 504 – 659 | 156 | Flexible hinge | | Add BLAST |
Coiled coil
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Coiled coili | 104 – 124 | 21 | Sequence Analysis | | Add BLAST | |
| Coiled coili | 163 – 503 | 341 | Sequence Analysis | | Add BLAST | |
| Coiled coili | 660 – 935 | 276 | Sequence Analysis | | Add BLAST | |
| Coiled coili | 991 – 1068 | 78 | Sequence Analysis | | Add BLAST |
Compositional bias
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Compositional biasi | 1128 – 1163 | 36 | Ala/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
Keywords - Domaini
Coiled coilPhylogenomic databases
| eggNOGi | COG1196. |
| GeneTreei | ENSGT00580000081569. |
| HOGENOMi | HOG000195481. |
| HOVERGENi | HBG039593. |
| InParanoidi | Q14683. |
| KOi | K06636. |
| OMAi | FNFKSYK. |
| PhylomeDBi | Q14683. |
| TreeFami | TF101156. |
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. |
Sequencei
Sequence statusi: Complete.
Q14683-1 [UniParc]FASTAAdd to Basket
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
Experimental Info
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Sequence conflicti | 163 – 164 | 2 | EL → DV in AAB34405. (PubMed:7757074)Curated | |
Natural variant
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
|---|---|---|---|---|---|---|
| Natural varianti | 28 – 28 | 1 | T → P. Corresponds to variant rs34530151 [ dbSNP | Ensembl ]. | | VAR_052438 | |
| Natural varianti | 58 – 62 | 5 | Missing in CDLS2. 2 Publications | | VAR_062785 | |
| Natural varianti | 133 – 133 | 1 | F → V in CDLS2. 2 Publications | | VAR_062786 | |
| Natural varianti | 141 – 141 | 1 | E → K in CDLS2. 1 Publication | | VAR_062787 | |
| Natural varianti | 196 – 196 | 1 | R → H in CDLS2. 4 Publications | | VAR_062788 | |
| Natural varianti | 268 – 268 | 1 | Missing in CDLS2. 2 Publications | | VAR_062789 | |
| Natural varianti | 306 – 306 | 1 | Missing in CDLS2. 1 Publication | | VAR_062790 | |
| Natural varianti | 398 – 398 | 1 | R → Q in CDLS2. 1 Publication | | VAR_062791 | |
| Natural varianti | 493 – 493 | 1 | E → A 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_026529 | |
| Natural varianti | 496 – 496 | 1 | R → C in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 Publications | | VAR_062792 | |
| Natural varianti | 496 – 496 | 1 | R → H in CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins. 3 Publications | | VAR_062793 | |
| Natural varianti | 683 – 683 | 1 | Missing in CDLS2. 1 Publication | | VAR_062794 | |
| Natural varianti | 693 – 693 | 1 | R → G in CDLS2. 1 Publication | | VAR_062795 | |
| Natural varianti | 711 – 711 | 1 | R → Q in CDLS2. 1 Publication | | VAR_064542 | |
| Natural varianti | 711 – 711 | 1 | R → W in CDLS2. 2 Publications | | VAR_062796 | |
| Natural varianti | 781 – 781 | 1 | C → F in CDLS2. 1 Publication | | VAR_062797 | |
| Natural varianti | 784 – 784 | 1 | I → T in CDLS2. 1 Publication | | VAR_064543 | |
| Natural varianti | 790 – 790 | 1 | R → Q in CDLS2. 2 Publications | | VAR_062798 | |
| Natural varianti | 816 – 816 | 1 | R → G in CDLS2. 1 Publication | | VAR_062799 | |
| Natural varianti | 832 – 832 | 1 | Missing in CDLS2. 1 Publication | | VAR_026530 | |
| Natural varianti | 1049 – 1049 | 1 | R → Q in CDLS2. 1 Publication | | VAR_062800 | |
| Natural varianti | 1085 – 1085 | 1 | Y → C in CDLS2. 1 Publication | | VAR_062801 | |
| Natural varianti | 1122 – 1122 | 1 | F → L in CDLS2. 2 Publications | | VAR_062802 | |
| Natural varianti | 1123 – 1123 | 1 | R → 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. |
| CCDSi | CCDS14352.1. |
| PIRi | I54383. |
| RefSeqi | NP_006297.2. NM_006306.3. |
| UniGenei | Hs.211602. |
Genome annotation databases
| Ensembli | ENST00000322213; ENSP00000323421; ENSG00000072501. |
| GeneIDi | 8243. |
| KEGGi | hsa:8243. |
| UCSCi | uc004dsg.3. human. |
Polymorphism databases
| DMDMi | 29336622. |
Keywords - Coding sequence diversityi
PolymorphismCross-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
- "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. - "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. - "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. - "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. Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. - "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. - "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. - "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. - "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. - "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. - "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. - "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. - "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. - "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. - "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. - "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. - "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]. - "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. - "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]. - "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]. - "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. - "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. - "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. - "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. - "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. - "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. 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. - "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.
Entry informationi
| Entry namei | SMC1A_HUMAN | ||||||||
| Accessioni | Q14683Primary (citable) accession number: Q14683 Secondary accession number(s): O14995, Q16351, Q2M228 | ||||||||
| Entry historyi |
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| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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 proteomeDocuments
- Human chromosome XHuman chromosome X: entries, gene names and cross-references to MIM
- Human entries with polymorphisms or disease mutationsList of human entries with polymorphisms or disease mutations
- Human polymorphisms and disease mutationsIndex of human polymorphisms and disease mutations
- MIM cross-referencesOnline Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
- SIMILARITY commentsIndex of protein domains and families
External Data
Dasty 3Similar 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. |