Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002220
UniProt IDP53350
Primary gene name(s)PLK1
Synonym gene name(s)PLK
Protein nameSerine/threonine-protein kinase PLK1
Protein functionSerine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome, APC/C inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1 and WEE1. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex, gTuRC to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1, CCNB1 on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint, SAC regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning, PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069. Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage, By similarity. Phosphorylates CEP68 and is required for its degradation, PubMed:25503564. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope, PubMed:20679239. {ECO:0000250|UniProtKB:Q5F2C3, ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:12524548, ECO:0000269|PubMed:12738781, ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14734534, ECO:0000269|PubMed:15070733, ECO:0000269|PubMed:15148369, ECO:0000269|PubMed:15469984, ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16247472, ECO:0000269|PubMed:16980960, ECO:0000269|PubMed:17081991, ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17376779, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:18174154, ECO:0000269|PubMed:18331714, ECO:0000269|PubMed:18418051, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18521620, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19509060, ECO:0000269|PubMed:19597481, ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:8991084}.
Subcellular locationNucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24018379}. Cytoplasm, cytoskeleton, spindle. Midbody. Note=localization at the centrosome starts at the G1/S transition, PubMed:24018379. During early stages of mitosis, the phosphorylated form is detected on centrosomes and kinetochores. Localizes to the outer kinetochore. Presence of SGO1 and interaction with the phosphorylated form of BUB1 is required for the kinetochore localization. Localizes onto the central spindle by phosphorylating and docking at midzone proteins KIF20A/MKLP2 and PRC1. Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle. Localization to the centrosome is required for S phase progression, PubMed:24018379. {ECO:0000269|PubMed:24018379}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P53350
Gene Ontology
(Biological Process)
Complete annatation
anaphase-promoting complex-dependent catabolic process [GO:0031145];
cell proliferation [GO:0008283];
centrosome organization [GO:0051297];
cytokinesis [GO:0000910];
establishment of protein localization [GO:0045184];
female meiosis chromosome segregation [GO:0016321];
G2/M transition of mitotic cell cycle [GO:0000086];
G2 DNA damage checkpoint [GO:0031572];
homologous chromosome segregation [GO:0045143];
microtubule bundle formation [GO:0001578];
mitotic cytokinesis [GO:0000281];
mitotic nuclear division [GO:0007067];
mitotic nuclear envelope disassembly [GO:0007077];
mitotic sister chromatid segregation [GO:0000070];
mitotic spindle assembly checkpoint [GO:0007094];
negative regulation of apoptotic process [GO:0043066];
negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736];
negative regulation of transcription from RNA polymerase II promoter [GO:0000122];
nuclear envelope disassembly [GO:0051081];
peptidyl-serine phosphorylation [GO:0018105];
positive regulation of peptidyl-threonine phosphorylation [GO:0010800];
positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436];
positive regulation of protein localization to nucleus [GO:1900182];
positive regulation of proteolysis [GO:0045862];
positive regulation of ubiquitin protein ligase activity [GO:1904668];
positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition [GO:0051437];
positive regulation of ubiquitin-protein transferase activity [GO:0051443];
protein destabilization [GO:0031648];
protein localization to chromatin [GO:0071168];
protein localization to nuclear envelope [GO:0090435];
protein phosphorylation [GO:0006468];
protein ubiquitination [GO:0016567];
protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787];
regulation of cell cycle [GO:0051726];
regulation of cell cycle G2/M phase transition [GO:1902749];
regulation of mitotic cell cycle [GO:0007346];
regulation of mitotic metaphase/anaphase transition [GO:0030071];
regulation of mitotic spindle assembly [GO:1901673];
regulation of protein binding [GO:0043393];
regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle [GO:0051439];
sister chromatid cohesion [GO:0007062];
synaptonemal complex disassembly [GO:0070194]
Gene Ontology
(Molecular Function)
Complete annatation
anaphase-promoting complex binding [GO:0010997];
ATP binding [GO:0005524];
kinase activity [GO:0016301];
microtubule binding [GO:0008017];
protein kinase activity [GO:0004672];
protein kinase binding [GO:0019901];
protein serine/threonine kinase activity [GO:0004674]
Gene Ontology
(Cellular Component)
Complete annatation
centrosome [GO:0005813];
chromatin [GO:0000785];
condensed nuclear chromosome outer kinetochore [GO:0000942];
cytoplasm [GO:0005737];
cytosol [GO:0005829];
kinetochore [GO:0000776];
microtubule cytoskeleton [GO:0015630];
midbody [GO:0030496];
nucleolus [GO:0005730];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
spindle [GO:0005819];
spindle midzone [GO:0051233];
spindle pole [GO:0000922];
synaptonemal complex [GO:0000795]
Protein-protein interaction111362
Phylogenetic treeP53350
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
Brass et al., Science, 2008
Smith et al., J. Immunol, 2010
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. CD3-1.530151642428340.009068030885264090.0240199229354482
AZA vs. DISU-0.4196987096659210.4758649864673550.92964241515886
AZA vs. IL7-0.1970067913477720.7508301603353590.999311006273513
AZA vs. SAHA-0.7791924171358850.1923556680200880.55911479748068
DISU vs. CD31.10042246752670.02760030364220230.0668993370481682
DISU vs. IL70.2123945148763820.698169196642840.922508601927497
DISU vs. SAHA-0.3602824080705050.4851426511482780.815247437396848
DMSO vs. AZA-0.04433699181312230.9470011571423541
DMSO vs. CD31.467237870400080.01329821132079660.0317542484621652
DMSO vs. DISU0.370789713744180.5353667280541340.920620730880165
DMSO vs. IL7-0.1442152405544040.8192063569664230.962956477091318
DMSO vs. SAHA-0.7410948753707030.2224447827331520.567829491966688
HIV vs. Mock in Activation0.02692783891834690.9741619529543910.999983755607037
HIV vs. Mock in Latency0.06839311193329110.8753479406243570.999834320637052
IL7 vs. CD31.341088171956410.01499903964300360.0415971526290697
SAHA vs. CD30.7233093574387050.151410291175380.242765516332905
SAHA vs. IL7-0.5863464220050570.2921342763622730.539793096578194
(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 -0.594972 0.000305467
(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
1.192 1.796 2.804 2.971 1.21
(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

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB06897 3-[3-chloro-5-(5-{[(1S)-1-phenylethyl]amino}isoxazolo[5,4-c]pyridin-3-yl)phenyl]propan-1-ol experimental unknown unknown
DB06963 3-[3-(3-methyl-6-{[(1S)-1-phenylethyl]amino}-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide experimental unknown unknown
DB07186 4-(4-METHYLPIPERAZIN-1-YL)-N-[5-(2-THIENYLACETYL)-1,5-DIHYDROPYRROLO[3,4-C]PYRAZOL-3-YL]BENZAMIDE experimental unknown unknown
DB07789 1-[5-methyl-2-(trifluoromethyl)furan-3-yl]-3-[(2Z)-5-(2-{[6-(1H-1,2,4-triazol-3-ylamino)pyrimidin-4-yl]amino}ethyl)-1,3-thiazol-2(3H)-ylidene]urea experimental unknown unknown
DB08059 (1S,6BR,9AS,11R,11BR)-9A,11B-DIMETHYL-1-[(METHYLOXY)METHYL]-3,6,9-TRIOXO-1,6,6B,7,8,9,9A,10,11,11B-DECAHYDRO-3H-FURO[4,3,2-DE]INDENO[4,5-H][2]BENZOPYRAN-11-YL ACETATE experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1Q4K X-ray 2.3Å A/B/C=345-603.
1Q4O X-ray 2.2Å A/B=367-603.
1UMW X-ray 1.9Å A/B=367-603.
2OGQ X-ray 1.9Å A=365-603.
2OJX X-ray 2.8Å A=365-603.
2OU7 X-ray 2.4Å A=13-345.
2OWB X-ray 2.1Å A=13-345.
2RKU X-ray 1.9Å A=37-330.
2V5Q X-ray 2.3Å A/B=33-345.
2YAC X-ray 2.2Å A=36-345.
3BZI X-ray 2.1Å A=365-603.
3C5L X-ray 2.3Å A=373-593.
3FC2 X-ray 2.4Å A=13-345.
3FVH X-ray 1.5Å A=371-603.
3HIH X-ray 1.7Å A/B=371-593.
3HIK X-ray 1.7Å A=367-603.
3KB7 X-ray 2.5Å A=36-345.
3P2W X-ray 1.6Å A=371-594.
3P2Z X-ray 1.7Å A=371-594.
3P34 X-ray 1.4Å A=371-594.
3P35 X-ray 2.0Å A/B/C=371-594.
3P36 X-ray 1.5Å A=371-594.
3P37 X-ray 2.3Å A/B/C=371-594.
3Q1I X-ray 1.4Å A=371-594.
3RQ7 X-ray 1.5Å A=371-603.
3THB X-ray 2.5Å A=13-345.
4A4L X-ray 2.3Å A=36-345.
4A4O X-ray 2.7Å A=36-345.
4DFW X-ray 1.5Å A=367-603.
4E67 X-ray 2.1Å A=371-594.
4E9C X-ray 1.7Å A=371-594.
4E9D X-ray 2.7Å A=371-594.
4H5X X-ray 1.9Å A/B=367-603.
4H71 X-ray 1.9Å A/B=367-603.
4HAB X-ray 2.6Å A/B/C=371-593.
4HCO X-ray 2.7Å A/B=367-603.
4HY2 X-ray 2.0Å A=371-595.
4J52 X-ray 2.3Å A=38-330.
4J53 X-ray 2.5Å A=38-330.
4LKL X-ray 1.5Å A=372-593.
4LKM X-ray 2.0Å A/C=371-601.
4O56 X-ray 1.8Å A=367-603.
4O6W X-ray 1.4Å A=371-603.
4O9W X-ray 1.6Å A=373-594.
4RCP X-ray 1.6Å A=372-599.
4WHH X-ray 1.9Å A=371-603.
4WHK X-ray 1.8Å A=371-603.
4WHL X-ray 2.7Å A=371-603.
4X9R X-ray 1.4Å A=371-603.
4X9V X-ray 1.4Å A=371-603.
4X9W X-ray 1.8Å A=371-603.
5J19 X-ray 2.0Å A/B=367-594.

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

HIV Partner Interaction Type PubMed
Vpr interacts with 18445273
Vpu binds 23047923
Tat complexes with 22391203
Vpr affects 26401039
HIV-1 virus replication enhanced by expression of human gene 18854154
Pr55(Gag) interacts with 24447338
Tat interacts with 22391203

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04068 FoxO signaling pathway - Homo sapiens (human)
hsa04110 Cell cycle - Homo sapiens (human)
hsa04114 Oocyte meiosis - Homo sapiens (human)
hsa04914 Progesterone-mediated oocyte maturation - Homo sapiens (human)