Database ID | HIV0001931 |
UniProt ID | P51955 |
Primary gene name(s) | NEK2 |
Synonym gene name(s) | NEK2A, NLK1 |
Protein name | Serine/threonine-protein kinase Nek2 |
Protein function | Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation, essential for the formation of bipolar spindles and high-fidelity chromosome separation by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly, PubMed:24554434. NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis, PubMed:25704143. Involved in the regulation of centrosome disjunction, PubMed:26220856. {ECO:0000269|PubMed:11742531, ECO:0000269|PubMed:12857871, ECO:0000269|PubMed:14978040, ECO:0000269|PubMed:15358203, ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:17283141, ECO:0000269|PubMed:17621308, ECO:0000269|PubMed:17626005, ECO:0000269|PubMed:18086858, ECO:0000269|PubMed:18297113, ECO:0000269|PubMed:20034488, ECO:0000269|PubMed:21076410, ECO:0000269|PubMed:24554434, ECO:0000269|PubMed:25704143, ECO:0000269|PubMed:26220856}.; FUNCTION: Isoform 1: Phosphorylates and activates NEK11 in G1/S-arrested cells. {ECO:0000269|PubMed:15161910}.; FUNCTION: Isoform 2: Not present in the nucleolus and, in contrast to isoform 1, does not phosphorylate and activate NEK11 in G1/S-arrested cells. {ECO:0000269|PubMed:15161910}. |
Subcellular location | Isoform 1: Nucleus. Nucleus, nucleolus {ECO:0000269|PubMed:15161910}. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26220856}. Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Chromosome, centromere {ECO:0000250}. Note=STK3/MST2 and SAV1 are required for its targeting to the centrosome. Colocalizes with SGO1 and MAD1L1 at the kinetochore. Not associated with kinetochore in the interphase but becomes associated with it upon the breakdown of the nuclear envelope. Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end.; SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Predominantly cytoplasmic.; SUBCELLULAR LOCATION: Isoform 4: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Predominantly nuclear. |
ECO code | Click here for more information. |
Amino acid sequence FASTA format: P51955 |
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Gene Ontology (Biological Process) Complete annatation | blastocyst development [GO:0001824]; cell division [GO:0051301]; centrosome separation [GO:0051299]; chromosome segregation [GO:0007059]; G2/M transition of mitotic cell cycle [GO:0000086]; meiotic cell cycle [GO:0051321]; mitotic nuclear division [GO:0007067]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly [GO:0090307]; negative regulation of centriole-centriole cohesion [GO:1903126]; negative regulation of DNA binding [GO:0043392]; positive regulation of telomerase activity [GO:0051973]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of attachment of spindle microtubules to kinetochore [GO:0051988]; regulation of mitotic centrosome separation [GO:0046602]; regulation of mitotic nuclear division [GO:0007088]; spindle assembly [GO:0051225] |
Gene Ontology (Molecular Function) Complete annatation | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein phosphatase binding [GO:0019903]; protein serine/threonine kinase activity [GO:0004674] |
Gene Ontology (Cellular Component) Complete annatation | centrosome [GO:0005813]; condensed chromosome kinetochore [GO:0000777]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinetochore [GO:0000776]; microtubule [GO:0005874]; midbody [GO:0030496]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein complex [GO:0043234]; spindle pole [GO:0000922] |
Protein-protein interaction | 110826 |
Phylogenetic tree | P51955 |
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) |
Up-regulated;
Down-regulated
For brief introduction to each study, please go to the help page.
(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 |
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Experimental Condition | Log2 Fold Change | P value | Adjusted P value |
AZA vs. CD3 | -0.534336222234717 | 0.699614071959931 | 0.785736459953806 |
AZA vs. DISU | -0.0200010358699199 | 0.973850689747274 | 0.997811953897277 |
AZA vs. IL7 | -0.0179956642574994 | 0.976742206972112 | 0.999311006273513 |
AZA vs. SAHA | -0.443033101272265 | 0.432625762529713 | 0.781755064058127 |
DISU vs. CD3 | 0.503782917471303 | 0.712230544063723 | 0.798168405413469 |
DISU vs. IL7 | -0.0076701501075511 | 0.989570114241844 | 0.999065831444279 |
DISU vs. SAHA | -0.423489038277031 | 0.425036995882693 | 0.776890584262731 |
DMSO vs. AZA | -0.0303054549484143 | 0.958645950444682 | 1 |
DMSO vs. CD3 | 0.484903048405091 | 0.727166670340856 | 0.801255550664497 |
DMSO vs. DISU | -0.0152538358129691 | 0.977799580900349 | 0.995772380333035 |
DMSO vs. IL7 | 0.0208110997753617 | 0.970243429674904 | 0.993912727803016 |
DMSO vs. SAHA | -0.418378098360063 | 0.394826252647238 | 0.739030076461782 |
HIV vs. Mock in Activation | -0.30788233346154 | 0.895566844560839 | 0.999983755607037 |
HIV vs. Mock in Latency | 0.360493994618932 | 0.536962235634309 | 0.999834320637052 |
IL7 vs. CD3 | 0.526771187992053 | 0.700152711884702 | 0.796904162669948 |
SAHA vs. CD3 | 0.0641269711297706 | 0.964187928082991 | 0.976031639691618 |
SAHA vs. IL7 | -0.428166323281722 | 0.426658423375322 | 0.669106229084436 |
(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 |
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Log2 Fold Change | P Value | ||
unknown | unknown |
(1). Imbeault et al., PloS Pathog., 2012 Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells |
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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) |
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Log2 Fold Change | unknown | ||||
(3). Li et al., J. Immunol., 2013 Lymphatic tissue |
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Acute Fold Change | Acute P Value | Asymt Fold Change | Asypt P Value | AIDS Fold Change | AIDS P Value |
3.1 | 0.000804265 | 1.8 | 0.038955253 | 2 | 0.11310395 |
(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 |
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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 |
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Test Status | Log2 Fold Change | P Value | |||
OK | 0.336271 | 0.015495 | |||
(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) |
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Log2 Fold Change | P Value | ||||
0.018 | 0.008 |
(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 |
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6 h | 24 h | 48 h | 72 h | RTi | ||
2.014 | 1.751 | 3.39 | 5.087 | 1.857 | ||
(2). Navare et al., Virology, 2012 SUP-T1 cell line |
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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 |
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Affymetrix Prob ID | Fold Change | In CD8? | Category | |||
204641_at | 4.76 | Yes | upregulated in CD4+ cells | |||
204641_at | 8.98 | Yes | upregulated in CD8+ cells |
Drugbank ID | Drug Name | Drug Status | Pharmacological Action | Drug Action |
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DB07180 | 5-[(Z)-(5-CHLORO-2-OXO-1,2-DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]-N-(DIETHYLAMINO)ETHYL]-2,4-DIMETHYL-1H-PYRROLE-3-CARBOXAMIDE | experimental | unknown | unknown |
PDB Accession | Method | Resolution | Chain | Structure Preview |
---|---|---|---|---|
2JAV | X-ray | 2.2Å | A=1-271. | ![]() |
2W5A | X-ray | 1.5Å | A=1-271. | ![]() |
2W5B | X-ray | 2.4Å | A=1-271. | ![]() |
2W5H | X-ray | 2.3Å | A=1-271. | ![]() |
2WQO | X-ray | 2.1Å | A=1-271. | ![]() |
2XK3 | X-ray | 2.2Å | A=1-271. | ![]() |
2XK4 | X-ray | 2.1Å | A=1-271. | ![]() |
2XK6 | X-ray | 2.2Å | A=1-271. | ![]() |
2XK7 | X-ray | 1.9Å | A=1-271. | ![]() |
2XK8 | X-ray | 2.0Å | A=1-271. | ![]() |
2XKC | X-ray | 2.5Å | A=1-271. | ![]() |
2XKD | X-ray | 1.9Å | A=1-271. | ![]() |
2XKE | X-ray | 2.2Å | A=1-271. | ![]() |
2XKF | X-ray | 2.3Å | A=1-271. | ![]() |
2XNM | X-ray | 1.8Å | A=1-271. | ![]() |
2XNN | X-ray | 2.5Å | A=1-271. | ![]() |
2XNO | X-ray | 1.9Å | A=1-271. | ![]() |
2XNP | X-ray | 1.9Å | A=1-271. | ![]() |
4A4X | X-ray | 2.4Å | A=1-271. | ![]() |
4AFE | X-ray | 2.6Å | A=1-271. | ![]() |
HIV Partner | Interaction Type | PubMed |
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Pr55(Gag) | interacts with |
24447338 |
Pathway Accession Number | Description | not found |
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