P53350

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession PLK1_HUMAN; P53350;
Entrez ID 5347
GenBank Protein ID
GenBank Nucleotide ID
Protein Name Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1) (Serine/threonine-protein kinase 13) (STPK13)
Gene Name PLK1; PLK
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionSerine/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(view all)
Sequence
(Fasta)
MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR RRYVRGRFLG 60
KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM EISIHRSLAH QHVVGFHGFF 120
EDNDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN RVIHRDLKLG 180
NLFLNEDLEV KIGDFGLATK VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI 240
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL 300
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP LPERPREKEE 360
PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK 420
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLK 480
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK 540
LILCPLMAAV TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL 600
KAS 604

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Threonine PhosphorylationPediatric acute lymphoblastic leukemiaUT21023753023
[Reference]: Polo-like kinase 1 protein and Thr210 phosphorylation levels were higher in pediatric acute lymphoblastic leukemia (n=172) than in normal bone marrow mononuclear cells (n=10) (P<0.0001).
2Tyrosine PhosphorylationCervical cancer/carcinomaUY42527899378
[Reference]: Cervical Cancer Growth Is Regulated by a c-ABL-PLK1 Signaling Axis.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 2)
MESH:D005910 ; Glioma
MESH:D007938 ; Leukemia
GWASdb
(count: 1)
rs35635; Multiple complex diseases; Null

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 33)
(view all)
103       EKMSMEISIHRSLAH     dbPAF
137       LELCRRRSLLELHKR     dbPAF
2         ******MSAAVTAGK     dbPAF
210       YDGERKKTLCGTPNY     dbPAF
214       RKKTLCGTPNYIAPE     dbPAF
217       TLCGTPNYIAPEVLS     dbPAF
Acetylation
(count: 6)
19        RAPADPGKAGVPGVA     PLMD
474       SHPNSLMKKITLLKY     PLMD
589       YARTMVDKLLSSRSA     PLMD
61        VRGRFLGKGGFAKCF     PLMD
9         SAAVTAGKLARAPAD     PLMD
97        LKPHQREKMSMEISI     PLMD
Ubiquitination
(count: 25)
(view all)
143       RSLLELHKRRKALTE     PLMD
146       LELHKRRKALTEPEA     PLMD
178       RVIHRDLKLGNLFLN     PLMD
19        RAPADPGKAGVPGVA     PLMD
200       GDFGLATKVEYDGER     PLMD
209       EYDGERKKTLCGTPN     PLMD
Sumoylation
(count: 1)
200       GDFGLATKVEYDGER     PLMD
Glycation
(count: 2)
475       HPNSLMKKITLLKYF     PLMD
492       YMSEHLLKAGANITP     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource
A4QPB2P53350MINT
A5PL33P53350IntAct
E9PB60P53350MINT
E9PMS4P53350BioGRID
F5H0P3P53350MINT
G3V1P6P53350HPRD; DIP; MINT
H0YBT0P53350IntAct
H0YG33P53350IntAct
H9KV59P53350DIP
O00562P53350HPRD
O14788P53350MINT
O14818P53350HPRD
O15084P53350IntAct
O43663P53350HPRD; DIP
O43683P53350HPRD
O60271P53350IntAct
O60447P53350IntAct
O75170P53350IntAct
O75665P53350IntAct
O75914P53350MINT
O94762P53350HPRD; IntAct; MINT
O94805P53350MINT
O95251P53350DIP
O96017P53350DIP; IntAct;HPRD
P04637P53350HPRD; MINT
P05413P53350IntAct
P06748P53350HPRD
P06858P53350IntAct
P12272P53350IntAct
P13693P53350HPRD
P14635P53350HPRD
P16278P53350MINT
P19793P53350MINT
P20618P53350HPRD
P23258P53350HPRD
P23588P53350IntAct
P25205P53350HPRD; IntAct
P25786P53350HPRD
P25788P53350HPRD
P25789P53350HPRD
P28066P53350HPRD
P28070P53350HPRD
P28072P53350HPRD
P28074P53350HPRD
P30291P53350HPRD; IntAct
P30622P53350MINT
P33993P53350HPRD; IntAct
P35222P53350HPRD
P49720P53350HPRD
P49721P53350HPRD
P49736P53350HPRD; IntAct
P50748P53350BioGRID
P51587P53350HPRD
P53350P53350MINT
P53350P54727BioGRID; IntAct
P53350P56537MINT
P53350P60900HPRD
P53350P61968MINT
P53350P68366HPRD
P53350P78539IntAct
P53350P82094IntAct
P53350Q00987MINT
P53350Q01538HPRD
P53350Q02241HPRD
P53350Q08752MINT
P53350Q09472IntAct
P53350Q12888DIP
P53350Q13153MINT
P53350Q13158IntAct
P53350Q13188IntAct
P53350Q13410IntAct
P53350Q13472IntAct
P53350Q13526HPRD
P53350Q13625MINT
P53350Q13885HPRD
P53350Q13972MINT
P53350Q14168MINT
P53350Q155Q3MINT
P53350Q15811MINT
P53350Q16659MINT
P53350Q2NKX8IntAct
P53350Q53EZ4HPRD
P53350Q5SQH8MINT
P53350Q5T280MINT
P53350Q5TA45MINT
P53350Q5VYV7IntAct
P53350Q6PGQ7IntAct
P53350Q6UXH1MINT
P53350Q71F23DIP
P53350Q7L5D6HPRD; IntAct; MINT
P53350Q7Z3J3IntAct
P53350Q8IV63MINT
P53350Q8IW35IntAct
P53350Q8IXK0IntAct
P53350Q8IY92IntAct
P53350Q8IYT8IntAct
P53350Q8IZT6HPRD
P53350Q8N8A2IntAct
P53350Q8NB46IntAct
P53350Q8NDZ2MINT
P53350Q8TD16IntAct
P53350Q8TD19MINT
P53350Q8TDY2IntAct
P53350Q92574HPRD
P53350Q92844IntAct
P53350Q92889IntAct
P53350Q96G01IntAct
P53350Q96NT0MINT
P53350Q96RK0MINT
P53350Q99436HPRD
P53350Q99640HPRD
P53350Q9BQ83IntAct
P53350Q9BQQ3HPRD
P53350Q9BV68MINT
P53350Q9BZF3IntAct
P53350Q9H0H5DIP
P53350Q9H6R7IntAct
P53350Q9H773IntAct
P53350Q9H8V3HPRD
P53350Q9NQZ8MINT
P53350Q9NR09HPRD; IntAct
P53350Q9NWV8IntAct
P53350Q9NYY3DIP
P53350Q9NYZ3MINT
P53350Q9UBS3HPRD; IntAct; MINT
P53350Q9UI14IntAct
P53350Q9UKA1MINT
P53350Q9UKT4IntAct
P53350Q9Y266HPRD
P53350Q9Y2I6HPRD
P53350Q9Y2K6IntAct
P53350Q9Y5Q9IntAct
P53350Q9Y5V3IntAct; MINT;HPRD