dbPTM

PLK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLK1_HUMAN
UniProt AC	P53350
Protein Name	Serine/threonine-protein kinase PLK1
Gene Name	PLK1
Organism	Homo sapiens (Human).
Sequence Length	603
Subcellular Localization	Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Midbody. localization at the centrosome starts at the G1/S transition (PubMed:24018379). During earl
Protein Description	Serine/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, WEE1 and HNRNPU. 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]
Protein Sequence	MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSAAVTAGK ------CCCCHHHHH	25.57	22814378
2	Phosphorylation	------MSAAVTAGK ------CCCCHHHHH	25.57	20068231
6	Phosphorylation	--MSAAVTAGKLARA --CCCCHHHHHHHCC	25.60	17192257
9	Acetylation	SAAVTAGKLARAPAD CCCHHHHHHHCCCCC	36.19	23954790
9	Ubiquitination	SAAVTAGKLARAPAD CCCHHHHHHHCCCCC	36.19	24816145
19	Acetylation	RAPADPGKAGVPGVA CCCCCCCCCCCCCCC	47.56	26051181
19	Ubiquitination	RAPADPGKAGVPGVA CCCCCCCCCCCCCCC	47.56	33845483
38	Ubiquitination	PAAAPPAKEIPEVLV CCCCCCHHHCCCEEC	63.05	21906983
49	Phosphorylation	EVLVDPRSRRRYVRG CEECCCCHHCHHCCC	35.21	22817900
61	Acetylation	VRGRFLGKGGFAKCF CCCCCCCCCCCCCEE	58.99	25953088
61	Ubiquitination	VRGRFLGKGGFAKCF CCCCCCCCCCCCCEE	58.99	27667366
66	Ubiquitination	LGKGGFAKCFEISDA CCCCCCCCEEEECCC	36.88	29967540
71	Phosphorylation	FAKCFEISDADTKEV CCCEEEECCCCCCHH	21.39	29396449
75	Phosphorylation	FEISDADTKEVFAGK EEECCCCCCHHHCCC	30.72	29396449
76	Ubiquitination	EISDADTKEVFAGKI EECCCCCCHHHCCCC	53.05	29967540
82	Ubiquitination	TKEVFAGKIVPKSLL CCHHHCCCCCCHHHH	36.78	33845483
86	Ubiquitination	FAGKIVPKSLLLKPH HCCCCCCHHHHCCHH	42.73	29967540
91	Ubiquitination	VPKSLLLKPHQREKM CCHHHHCCHHHHHCH	40.18	32015554
97	Acetylation	LKPHQREKMSMEISI CCHHHHHCHHEEEEH	38.16	25953088
99	Phosphorylation	PHQREKMSMEISIHR HHHHHCHHEEEEHHH	25.08	20860994
103	Phosphorylation	EKMSMEISIHRSLAH HCHHEEEEHHHHHHH	10.07	17192257
137	Phosphorylation	LELCRRRSLLELHKR HHHHHHHHHHHHHHH	35.18	19804365
143	Ubiquitination	RSLLELHKRRKALTE HHHHHHHHHHHHCCC	67.53	-
146	Ubiquitination	LELHKRRKALTEPEA HHHHHHHHHCCCHHH	52.35	-
178	Ubiquitination	RVIHRDLKLGNLFLN CEECCCCCCCCEECC	59.65	-
200	Ubiquitination	GDFGLATKVEYDGER CCCCEEEEEEECCCC	27.71	21906983
209	Ubiquitination	EYDGERKKTLCGTPN EECCCCCCEECCCCC	53.61	29967540
210	Phosphorylation	YDGERKKTLCGTPNY ECCCCCCEECCCCCC	30.25	23927012
214	Phosphorylation	RKKTLCGTPNYIAPE CCCEECCCCCCCCHH	13.83	23401153
217	Phosphorylation	TLCGTPNYIAPEVLS EECCCCCCCCHHHHH	10.32	21945579
224	Phosphorylation	YIAPEVLSKKGHSFE CCCHHHHHCCCCCCE	37.18	21945579
225	Ubiquitination	IAPEVLSKKGHSFEV CCHHHHHCCCCCCEE	59.62	29967540
226	Ubiquitination	APEVLSKKGHSFEVD CHHHHHCCCCCCEEE	59.48	-
265	Ubiquitination	ETYLRIKKNEYSIPK HHHHHHHCCCCCCCC	53.27	29967540
268	Phosphorylation	LRIKKNEYSIPKHIN HHHHCCCCCCCCCCC	22.69	20068231
269	Phosphorylation	RIKKNEYSIPKHINP HHHCCCCCCCCCCCH	26.66	29970186
272	Ubiquitination	KNEYSIPKHINPVAA CCCCCCCCCCCHHHH	56.28	23000965
309	Phosphorylation	DEFFTSGYIPARLPI CCCCCCCCCCCCCCE	11.96	27642862
326	Phosphorylation	LTIPPRFSIAPSSLD EECCCCCCCCCCCCC	21.08	25850435
330	Phosphorylation	PRFSIAPSSLDPSNR CCCCCCCCCCCCCCC	34.21	23663014
331	Phosphorylation	RFSIAPSSLDPSNRK CCCCCCCCCCCCCCC	35.41	25159151
335	Phosphorylation	APSSLDPSNRKPLTV CCCCCCCCCCCCCCH	49.27	29396449
338	Ubiquitination	SLDPSNRKPLTVLNK CCCCCCCCCCCHHCC	48.94	21963094
338	Sumoylation	SLDPSNRKPLTVLNK CCCCCCCCCCCHHCC	48.94	28112733
341	Phosphorylation	PSNRKPLTVLNKGLE CCCCCCCCHHCCCCC	31.32	27470641
345	Ubiquitination	KPLTVLNKGLENPLP CCCCHHCCCCCCCCC	61.79	29967540
358	Ubiquitination	LPERPREKEEPVVRE CCCCCCCCCCCCCCC	69.52	29901268
366	Phosphorylation	EEPVVRETGEVVDCH CCCCCCCCCCEEEEC	28.25	21712546
375	Phosphorylation	EVVDCHLSDMLQQLH CEEEECHHHHHHHHH	9.41	17192257
383	Phosphorylation	DMLQQLHSVNASKPS HHHHHHHHCCCCCHH	26.17	25159151
387	Phosphorylation	QLHSVNASKPSERGL HHHHCCCCCHHHCCC	39.64	18669648
388	Ubiquitination	LHSVNASKPSERGLV HHHCCCCCHHHCCCC	50.59	29967540
413	Ubiquitination	IPIFWVSKWVDYSDK EEEEEEECCCCCHHH	41.43	29967540
425	Phosphorylation	SDKYGLGYQLCDNSV HHHCCCCCCCCCCCE	11.89	-
445	Phosphorylation	DSTRLILYNDGDSLQ CCCEEEEECCCCCEE	12.29	-
450	Phosphorylation	ILYNDGDSLQYIERD EEECCCCCEEEEEEC	23.93	25159151
459	Phosphorylation	QYIERDGTESYLTVS EEEEECCCCEEEEEC	26.50	-
461	Phosphorylation	IERDGTESYLTVSSH EEECCCCEEEEECCC	25.86	17192257
462	Phosphorylation	ERDGTESYLTVSSHP EECCCCEEEEECCCC	10.52	-
464	Phosphorylation	DGTESYLTVSSHPNS CCCCEEEEECCCCCC	15.31	17192257
466	Phosphorylation	TESYLTVSSHPNSLM CCEEEEECCCCCCHH	20.07	30631047
467	Phosphorylation	ESYLTVSSHPNSLMK CEEEEECCCCCCHHH	38.33	28555341
474	Acetylation	SHPNSLMKKITLLKY CCCCCHHHHHHHHHH	46.44	23236377
474	Ubiquitination	SHPNSLMKKITLLKY CCCCCHHHHHHHHHH	46.44	23000965
475	Ubiquitination	HPNSLMKKITLLKYF CCCCHHHHHHHHHHH	27.27	23000965
480	Ubiquitination	MKKITLLKYFRNYMS HHHHHHHHHHHHHHH	45.51	23000965
492	Sumoylation	YMSEHLLKAGANITP HHHHHHHHCCCCCCC	51.65	-
492	Ubiquitination	YMSEHLLKAGANITP HHHHHHHHCCCCCCC	51.65	23000965
498	Phosphorylation	LKAGANITPREGDEL HHCCCCCCCCCCCHH	18.99	17307877
561	Phosphorylation	DEKRDFRTYRLSLLE CCCCCCHHHHHHHHH	17.00	22199227
562	Phosphorylation	EKRDFRTYRLSLLEE CCCCCHHHHHHHHHH	12.80	22199227
565	Phosphorylation	DFRTYRLSLLEEYGC CCHHHHHHHHHHHCH	23.16	21815630
574	Ubiquitination	LEEYGCCKELASRLR HHHHCHHHHHHHHHH	60.89	33845483
578	Phosphorylation	GCCKELASRLRYART CHHHHHHHHHHHHHH	44.46	-
582	Phosphorylation	ELASRLRYARTMVDK HHHHHHHHHHHHHHH	12.67	24719451
589	Ubiquitination	YARTMVDKLLSSRSA HHHHHHHHHHHCCCH	39.66	23000965
589	Acetylation	YARTMVDKLLSSRSA HHHHHHHHHHHCCCH	39.66	25953088
592	Phosphorylation	TMVDKLLSSRSASNR HHHHHHHHCCCHHHH	33.86	24719451
593	Phosphorylation	MVDKLLSSRSASNRL HHHHHHHCCCHHHHH	30.17	24719451
597	Phosphorylation	LLSSRSASNRLKAS- HHHCCCHHHHHCCC-	24.59	22202082

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
49	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
137	S	Phosphorylation	Kinase	MAP3K8	P41279	GPS
137	S	Phosphorylation	Kinase	PLK2	Q9NYY3	PSP
210	T	Phosphorylation	Kinase	AURA	O14965	PSP
210	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
210	T	Phosphorylation	Kinase	MAP3K8	P41279	GPS
210	T	Phosphorylation	Kinase	STK10	O94804	PhosphoELM
217	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
326	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
383	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
425	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
445	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:21700221
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL22	Q53GT1	PMID:23455478
-	K	Ubiquitination	E3 ubiquitin ligase	CHFR	Q96EP1	PMID:11807090

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
137	S	Phosphorylation	12207013
Autophosphorylation and phosphorylation of Ser-137 may not be significant for the activation of PLK1 during mitosis, but may enhance catalytic activity during recovery after DNA damage checkpoint.
210	T	Phosphorylation	12207013
Catalytic activity is enhanced by phosphorylation of Thr-210.
210	T	Phosphorylation	12207013
Dephosphorylation at Thr-210 at centrosomes is probably mediated by protein phosphatase 1C (PP1C), via interaction with PPP1R12A/MYPT1.
210	T	Phosphorylation	12207013
Phosphorylation at Thr-210 is first detected on centrosomes in the G2 phase of the cell cycle, peaks in prometaphase and gradually disappears from centrosomes during anaphase.
492	K	ubiquitylation	23455478
Monoubiquitination at Lys-492 by the BCR(KLHL22) ubiquitin ligase complex does not lead to degradation: it promotes PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PLK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRCA2_HUMAN	BRCA2	physical	14647413
BRCA2_HUMAN	BRCA2	physical	12815053
NUDC_HUMAN	NUDC	physical	12852857
DCTN1_HUMAN	DCTN1	physical	12852857
MPIP3_HUMAN	CDC25C	physical	11202906
PIN1_HUMAN	PIN1	physical	9499405
TSC1_HUMAN	TSC1	physical	16339216
TSC2_HUMAN	TSC2	physical	16339216
CHK2_HUMAN	CHEK2	physical	12493754
PSA7_HUMAN	PSMA7	physical	11205743
PSA5_HUMAN	PSMA5	physical	11205743
PSA2_HUMAN	PSMA2	physical	11205743
PSA6_HUMAN	PSMA6	physical	11205743
PSB1_HUMAN	PSMB1	physical	11205743
PSB3_HUMAN	PSMB3	physical	11205743
PSA1_HUMAN	PSMA1	physical	11205743
PSA3_HUMAN	PSMA3	physical	11205743
PSA4_HUMAN	PSMA4	physical	11205743
PSB5_HUMAN	PSMB5	physical	11205743
PSB6_HUMAN	PSMB6	physical	11205743
PSB7_HUMAN	PSMB7	physical	11205743
BORA_HUMAN	BORA	physical	18378770
CYLD_HUMAN	CYLD	physical	17495026
JIP4_HUMAN	SPAG9	physical	19596235
BICD2_HUMAN	BICD2	physical	19596235
ERC6L_HUMAN	ERCC6L	physical	19596235
BORA_HUMAN	BORA	physical	19596235
WDCP_HUMAN	C2orf44	physical	19596235
PP6R2_HUMAN	PPP6R2	physical	19596235
TMF1_HUMAN	TMF1	physical	19596235
BICD1_HUMAN	BICD1	physical	19596235
DCTP1_HUMAN	DCTPP1	physical	19596235
FABPH_HUMAN	FABP3	physical	19596235
ANR44_HUMAN	ANKRD44	physical	19596235
OSBL6_HUMAN	OSBPL6	physical	19596235
LIPL_HUMAN	LPL	physical	19596235
PTHR_HUMAN	PTHLH	physical	19596235
BT1A1_HUMAN	BTN1A1	physical	19596235
CEP97_HUMAN	CEP97	physical	19596235
SRPX_HUMAN	SRPX	physical	19596235
ANR28_HUMAN	ANKRD28	physical	19596235
ANR52_HUMAN	ANKRD52	physical	19596235
SLX4I_HUMAN	SLX4IP	physical	19596235
TF3C3_HUMAN	GTF3C3	physical	19596235
RGPD4_HUMAN	RGPD4	physical	19596235
SLX4_HUMAN	SLX4	physical	19596235
XPF_HUMAN	ERCC4	physical	19596235
CLSPN_HUMAN	CLSPN	physical	16885021
PIN1_HUMAN	PIN1	physical	16118204
FBX5_HUMAN	FBXO5	physical	15469984
TANK_HUMAN	TANK	physical	20484576
NEMO_HUMAN	IKBKG	physical	20484576
TOPRS_HUMAN	TOPORS	physical	19473992
CTNB1_HUMAN	CTNNB1	physical	21610149
TF65_HUMAN	RELA	physical	21610149
ACL6B_HUMAN	ACTL6B	physical	21900206
CIC_HUMAN	CIC	physical	21900206
RXRA_HUMAN	RXRA	physical	21900206
RN126_HUMAN	RNF126	physical	21900206
LRP5L_HUMAN	LRP5L	physical	21900206
CC115_HUMAN	CCDC115	physical	21900206
FBXL5_HUMAN	FBXL5	physical	21900206
VRK3_HUMAN	VRK3	physical	21900206
IF6_HUMAN	EIF6	physical	21900206
PPID_HUMAN	PPID	physical	21900206
LMO4_HUMAN	LMO4	physical	21900206
CI114_HUMAN	C9orf114	physical	21900206
MPP2_HUMAN	MPP2	physical	21900206
ZNF71_HUMAN	ZNF71	physical	21900206
BGAL_HUMAN	GLB1	physical	21900206
ASPP2_HUMAN	TP53BP2	physical	21900206
SIMC1_HUMAN	SIMC1	physical	21900206
BAG6_HUMAN	BAG6	physical	21900206
CF136_HUMAN	C6orf136	physical	21900206
INT11_HUMAN	CPSF3L	physical	21900206
ITSN1_HUMAN	ITSN1	physical	21900206
TBA1A_HUMAN	TUBA1A	physical	10191277
TBB3_HUMAN	TUBB3	physical	10191277
TBG1_HUMAN	TUBG1	physical	10191277
DNHD1_HUMAN	DNHD1	physical	21507953
CENPQ_HUMAN	CENPQ	physical	21454580
CASB_HUMAN	CSN2	physical	21454580
IKKB_HUMAN	IKBKB	physical	18957422
TARA_HUMAN	TRIOBP	physical	22820163
CALL5_HUMAN	CALML5	physical	16934469
HSF1_HUMAN	HSF1	physical	18794143
MPIP3_HUMAN	CDC25C	physical	19503101
BUB1B_HUMAN	BUB1B	physical	19503101
CASB_HUMAN	CSN2	physical	7790358
CASA1_HUMAN	CSN1S1	physical	7790358
TOPRS_HUMAN	TOPORS	physical	19821153
BUB1_HUMAN	BUB1	physical	16760428
BUB1B_HUMAN	BUB1B	physical	17376779
MDM2_HUMAN	MDM2	physical	19833129
P53_HUMAN	TP53	physical	19833129
MDM2_MOUSE	Mdm2	physical	19833129
NINL_HUMAN	NINL	physical	12852856
WEE1_HUMAN	WEE1	physical	15070733
STAG2_HUMAN	STAG2	physical	15737063
SYUA_HUMAN	SNCA	physical	19889641
SYUB_HUMAN	SNCB	physical	19889641
A4_HUMAN	APP	physical	21832049
AURKA_HUMAN	AURKA	physical	22939629
QORX_HUMAN	TP53I3	physical	22939629
HSP74_HUMAN	HSPA4	physical	21887822
KLH22_HUMAN	KLHL22	physical	23455478
KLH21_HUMAN	KLHL21	physical	23455478
KLHL9_HUMAN	KLHL9	physical	23455478
CUL2_HUMAN	CUL2	physical	23455478
BUB1B_HUMAN	BUB1B	physical	23455478
SGT1_HUMAN	SUGT1	physical	22869522
CENPU_HUMAN	CENPU	physical	19597481
MPIP3_HUMAN	CDC25C	physical	19597481
TP53B_HUMAN	TP53BP1	physical	20126263
CHK2_HUMAN	CHEK2	physical	20126263
CDC20_HUMAN	CDC20	physical	23643811
TANK_HUMAN	TANK	physical	21988832
PRAF1_HUMAN	RABAC1	physical	21988832
BUB1B_HUMAN	BUB1B	physical	24067371
KLH22_HUMAN	KLHL22	physical	24067371
FZR1_HUMAN	FZR1	physical	23972993
BRCA1_HUMAN	BRCA1	physical	24067368
BORA_HUMAN	BORA	physical	24067368
RPGP1_HUMAN	RAP1GAP	physical	25329897
CC14A_HUMAN	CDC14A	physical	19390576
SLX4_HUMAN	SLX4	physical	25852190
SGT1_MOUSE	Sugt1	physical	22869522
BICD2_HUMAN	BICD2	physical	26186194
BORA_HUMAN	BORA	physical	26186194
PP6R2_HUMAN	PPP6R2	physical	26186194
RAI14_HUMAN	RAI14	physical	26186194
TOPB1_HUMAN	TOPBP1	physical	26186194
KAT8_HUMAN	KAT8	physical	26186194
CLUS_HUMAN	CLU	physical	26186194
KIF2C_HUMAN	KIF2C	physical	24931513
REST_HUMAN	REST	physical	25453754
DDX17_HUMAN	DDX17	physical	26344197
RIR2_HUMAN	RRM2	physical	26344197
SMC3_HUMAN	SMC3	physical	26344197
ATP7A_HUMAN	ATP7A	physical	26496610
CIRBP_HUMAN	CIRBP	physical	26496610
DYN2_HUMAN	DNM2	physical	26496610
DSC1_HUMAN	DSC1	physical	26496610
DSG1_HUMAN	DSG1	physical	26496610
MECP2_HUMAN	MECP2	physical	26496610
RON_HUMAN	MST1R	physical	26496610
NDUAA_HUMAN	NDUFA10	physical	26496610
PIPNA_HUMAN	PITPNA	physical	26496610
CTIP_HUMAN	RBBP8	physical	26496610
EVI5_HUMAN	EVI5	physical	26496610
VAMP4_HUMAN	VAMP4	physical	26496610
EED_HUMAN	EED	physical	26496610
CHD1L_HUMAN	CHD1L	physical	26496610
ORC3_HUMAN	ORC3	physical	26496610
SACS_HUMAN	SACS	physical	26496610
DAAF5_HUMAN	DNAAF5	physical	26496610
HMCES_HUMAN	HMCES	physical	26496610
BIRC6_HUMAN	BIRC6	physical	26496610
EP15R_HUMAN	EPS15L1	physical	26496610
TUT7_HUMAN	ZCCHC6	physical	26496610
RM55_HUMAN	MRPL55	physical	26496610
RP25L_HUMAN	RPP25L	physical	26496610
FOXO3_HUMAN	FOXO3	physical	26280018
BRCA1_HUMAN	BRCA1	physical	25483079
TP53B_HUMAN	TP53BP1	physical	25607646
UBP16_HUMAN	USP16	physical	26323689
BUB1B_HUMAN	BUB1B	physical	26323689
PRKN_HUMAN	PARK2	physical	26387737
RICTR_HUMAN	RICTOR	physical	25714006
MAPK2_HUMAN	MAPKAPK2	physical	18695677
TOP2A_HUMAN	TOP2A	physical	18695677
MYC_HUMAN	MYC	physical	27773673
FBXW7_HUMAN	FBXW7	physical	27773673
PTEN_HUMAN	PTEN	physical	25047839
NEDD4_HUMAN	NEDD4	physical	25047839
RGCC_HUMAN	RGCC	physical	17146433
BICD2_HUMAN	BICD2	physical	28514442
PP6R2_HUMAN	PPP6R2	physical	28514442
TOPB1_HUMAN	TOPBP1	physical	28514442
TMF1_HUMAN	TMF1	physical	28514442
RAI14_HUMAN	RAI14	physical	28514442
CA226_HUMAN	C1orf226	physical	28514442
BORA_HUMAN	BORA	physical	28514442
MPRIP_HUMAN	MPRIP	physical	28514442
RHG05_HUMAN	ARHGAP5	physical	28514442
JIP4_HUMAN	SPAG9	physical	28514442
PRRC1_HUMAN	PRRC1	physical	28514442
MAVS_HUMAN	MAVS	physical	28514442
CAPON_HUMAN	NOS1AP	physical	28514442
STXB4_HUMAN	STXBP4	physical	28514442
TBK1_HUMAN	TBK1	physical	28514442
SATB2_HUMAN	SATB2	physical	28514442
XPF_HUMAN	ERCC4	physical	28514442
HDAC2_HUMAN	HDAC2	physical	27173435
SPAG5_HUMAN	SPAG5	physical	27173435
SMC1A_HUMAN	SMC1A	physical	27173435
HSF1_HUMAN	HSF1	physical	27173435
FOXJ1_HUMAN	FOXJ1	physical	27173435
IFT43_HUMAN	IFT43	physical	27173435
SRBP1_HUMAN	SREBF1	physical	27579997
B2CL1_HUMAN	BCL2L1	physical	22617334
CDC20_HUMAN	CDC20	physical	26912231
STK3_HUMAN	STK3	physical	27566175

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PLK1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-103; THR-210;THR-214; SER-375; SER-450; SER-461; THR-464 AND THR-498, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Identification of phosphorylation sites in the polo-like kinases Plx1and Plk1 by a novel strategy based on element and electrospray highresolution mass spectrometry."; Wind M., Kelm O., Nigg E.A., Lehmann W.D.; Proteomics 2:1516-1523(2002). Cited for: PHOSPHORYLATION AT SER-335.	12442251 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Polo-like kinase-1 is activated by aurora A to promote checkpointrecovery."; Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R.,Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.; Nature 455:119-123(2008). Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-210 BY AURKA,SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-82; SER-137; ASP-176 ANDTHR-210.	18615013 [Abstract]
"Myosin phosphatase-targeting subunit 1 regulates mitosis byantagonizing polo-like kinase 1."; Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M.,Hartshorne D.J., Matsumura F.; Dev. Cell 14:787-797(2008). Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A, PHOSPHORYLATION AT THR-210,DEPHOSPHORYLATION BY PPP1C, SUBCELLULAR LOCATION, AND MUTAGENESIS OFHIS-538 AND LYS-540.	18477460 [Abstract]
"Phosphorylation of threonine 210 and the role of serine 137 in theregulation of mammalian polo-like kinase."; Jang Y.-J., Ma S., Terada Y., Erikson R.L.; J. Biol. Chem. 277:44115-44120(2002). Cited for: FUNCTION, PHOSPHORYLATION AT SER-137 AND THR-210, AND MUTAGENESIS OFLYS-82; SER-137 AND THR-210.	12207013 [Abstract]

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