Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002772
UniProt IDQ14683
Primary gene name(s)SMC1A
Synonym gene name(s)DXS423E, KIAA0178, SB1.8, SMC1, SMC1L1
Protein nameStructural maintenance of chromosomes protein 1A
Protein functionInvolved 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. {ECO:0000269|PubMed:11877377}.
Subcellular locationNucleus {ECO:0000269|PubMed:12199140}. Chromosome {ECO:0000269|PubMed:12199140}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12199140}. 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.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: Q14683
Gene Ontology
(Biological Process)
Complete annatation
cell division [GO:0051301];
DNA repair [GO:0006281];
meiotic nuclear division [GO:0007126];
mitotic cell cycle checkpoint [GO:0007093];
mitotic sister chromatid cohesion [GO:0007064];
mitotic sister chromatid segregation [GO:0000070];
mitotic spindle organization [GO:0007052];
negative regulation of DNA endoreduplication [GO:0032876];
protein sumoylation [GO:0016925];
response to radiation [GO:0009314];
signal transduction in response to DNA damage [GO:0042770];
sister chromatid cohesion [GO:0007062];
stem cell population maintenance [GO:0019827]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
chromatin binding [GO:0003682];
poly(A RNA binding [GO:0044822];
protein heterodimerization activity [GO:0046982]
Gene Ontology
(Cellular Component)
Complete annatation
chromosome [GO:0005694];
chromosome, centromeric region [GO:0000775];
cohesin core heterodimer [GO:0008280];
condensed chromosome kinetochore [GO:0000777];
condensed nuclear chromosome [GO:0000794];
cytoplasm [GO:0005737];
cytosol [GO:0005829];
kinetochore [GO:0000776];
meiotic cohesin complex [GO:0030893];
nucleoplasm [GO:0005654];
nucleus [GO:0005634]
Protein-protein interaction113871
Phylogenetic treeQ14683
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
      unknown
Brass et al., Science, 2008
      unknown
Smith et al., J. Immunol, 2010
      unknown
Interferon-stimulated
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model


DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD30.6645727991636350.04641468870139050.0939009648466253
AZA vs. DISU-0.0008383144370186940.997353216531610.999297613676408
AZA vs. IL70.3465956363382850.07151912490665220.750701789497193
AZA vs. SAHA-0.8753214255724470.0004230180879264410.0114480694028782
DISU vs. CD3-0.677233435187240.06433189659691770.132153040242837
DISU vs. IL70.3380452380270010.1791866839452540.548029876338953
DISU vs. SAHA-0.8728770647759260.003039852506120270.0454951510623024
DMSO vs. AZA0.04297280681921230.7969802126520021
DMSO vs. CD3-0.6302363705761440.05237244822586820.100155348249184
DMSO vs. DISU0.042641849965320.861109042681270.984640346119887
DMSO vs. IL70.3105463220706660.0838889248075630.541827567041137
DMSO vs. SAHA-0.9253683236614590.0001124312089206820.00385102443100819
HIV vs. Mock in Activation0.3013445762890630.6295654598054910.999983755607037
HIV vs. Mock in Latency0.07135951045307210.6654114817143420.999834320637052
IL7 vs. CD3-0.3111372579998140.335502427427350.473912824087526
SAHA vs. CD3-1.563578033499741.48578075274131e-058.87815858200297e-05
SAHA vs. IL7-1.224669573152457.53137415099303e-073.5495278732519e-05
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) FALSE
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK 0.119623 0.443006
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
1.018 0.982 0.909 0.842 0.939
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
unknown unknown unknown unknown

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

not found

Protein Secondary Structure       (annotations from PDB)      top

not found

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Envelope surface glycoprotein gp120 complexes with 23125841
Gag-Pol complexes with 23125841
Vpr downregulates 21875947
Pr55(Gag) complexes with 23125841
Nef complexes with 23125841

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04110 Cell cycle - Homo sapiens (human)
hsa04114 Oocyte meiosis - Homo sapiens (human)
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