dbPTM

P73_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P73_HUMAN
UniProt AC	O15350
Protein Name	Tumor protein p73
Gene Name	TP73
Organism	Homo sapiens (Human).
Sequence Length	636
Subcellular Localization	Nucleus . Cytoplasm. Accumulates in the nucleus in response to DNA damage.
Protein Description	Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein..
Protein Sequence	MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAQSTATSPDG ----CCCCCCCCCCC	15.52	28348404
5	Phosphorylation	---MAQSTATSPDGG ---CCCCCCCCCCCC	23.13	28348404
7	Phosphorylation	-MAQSTATSPDGGTT -CCCCCCCCCCCCCC	40.66	28348404
8	Phosphorylation	MAQSTATSPDGGTTF CCCCCCCCCCCCCCH	20.66	28348404
13 (in isoform 10)	Phosphorylation	-	33.56	-
13 (in isoform 12)	Phosphorylation	-	33.56	-
13 (in isoform 9)	Phosphorylation	-	33.56	-
13 (in isoform 8)	Phosphorylation	-	33.56	-
27	Phosphorylation	SSLEPDSTYFDLPQS HHCCCCCCEECCCCC	35.27	18418051
28	Phosphorylation	SLEPDSTYFDLPQSS HCCCCCCEECCCCCC	10.07	22817900
47	Phosphorylation	EVVGGTDSSMDVFHL CCCCCCCCCCEEEEC	27.66	14585975
48	Phosphorylation	VVGGTDSSMDVFHLE CCCCCCCCCEEEECC	23.08	-
86	Phosphorylation	AASASPYTPEHAASV HHHCCCCCHHHHCCC	26.11	12676926
99	Phosphorylation	SVPTHSPYAQPSSTF CCCCCCCCCCCCCCC	22.38	10381648
145	Phosphorylation	KSATWTYSPLLKKLY CCCCEECHHHHHHHH	11.16	24719451
152	Phosphorylation	SPLLKKLYCQIAKTC HHHHHHHHHHHHCCC	7.38	29496907
166	Phosphorylation	CPIQIKVSTPPPPGT CCEEEEECCCCCCCC	30.14	27080861
167	Phosphorylation	PIQIKVSTPPPPGTA CEEEEECCCCCCCCE	42.68	27067055
173	Phosphorylation	STPPPPGTAIRAMPV CCCCCCCCEEEEEEC	25.37	-
181	Phosphorylation	AIRAMPVYKKAEHVT EEEEEECCCCCHHHH	10.82	20873877
223	Phosphorylation	RVEGNNLSQYVDDPV EEECCCHHHHCCCCC	22.91	28787133
225	Phosphorylation	EGNNLSQYVDDPVTG ECCCHHHHCCCCCCC	11.50	28787133
235	Phosphorylation	DPVTGRQSVVVPYEP CCCCCCEEEEECCCC	18.60	22340593
289	Phosphorylation	GQVLGRRSFEGRICA CEEECCCCCCCCEEC	26.70	-
296 (in isoform 9)	Ubiquitination	-	10.52	21906983
296 (in isoform 8)	Ubiquitination	-	10.52	21906983
296 (in isoform 10)	Ubiquitination	-	10.52	21906983
321	Acetylation	ALNESSAKNGAASKR HHHHHHHHHCHHHHH	58.84	20167786
321	Neddylation	ALNESSAKNGAASKR HHHHHHHHHCHHHHH	58.84	-
326	Phosphorylation	SAKNGAASKRAFKQS HHHHCHHHHHHHHHC	23.34	24260401
327	Neddylation	AKNGAASKRAFKQSP HHHCHHHHHHHHHCC	42.91	-
327	Acetylation	AKNGAASKRAFKQSP HHHCHHHHHHHHHCC	42.91	20167786
331	Neddylation	AASKRAFKQSPPAVP HHHHHHHHHCCCCHH	49.21	-
331	Acetylation	AASKRAFKQSPPAVP HHHHHHHHHCCCCHH	49.21	11804596
333	Phosphorylation	SKRAFKQSPPAVPAL HHHHHHHCCCCHHCC	33.18	25056879
345	Ubiquitination	PALGAGVKKRRHGDE HCCCCCCCCCCCCCC	39.38	-
345	Ubiquitination	PALGAGVKKRRHGDE HCCCCCCCCCCCCCC	39.38	2190698
345 (in isoform 1)	Ubiquitination	-	39.38	21906983
345 (in isoform 2)	Ubiquitination	-	39.38	21906983
345 (in isoform 3)	Ubiquitination	-	39.38	21906983
345 (in isoform 4)	Ubiquitination	-	39.38	21906983
345 (in isoform 5)	Ubiquitination	-	39.38	21906983
345 (in isoform 6)	Ubiquitination	-	39.38	21906983
388	Phosphorylation	VPQPLVDSYRQQQQL CCHHHHHHHHHHHHH	18.09	22817900
412	Phosphorylation	PSYGPVLSPMNKVHG CCCCCCCCCCCHHCC	23.49	29978859
426	Phosphorylation	GGMNKLPSVNQLVGQ CCCCCCCCHHHHCCC	44.10	-
471	Phosphorylation	GEMSSSHSAQSMVSG CCCCCCCCCCHHHCC	29.92	21482671
568	Phosphorylation	LRSSNAATISIGGSG HHCCCCCEEEECCCH	16.91	-
627	Sumoylation	KARKQPIKEEFTEAE HHCCCCCHHHHHHCC	58.85	15572666
627	Sumoylation	KARKQPIKEEFTEAE HHCCCCCHHHHHHCC	58.85	-

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
27	T	Phosphorylation	Kinase	CK2A2	P19784	PSP
27	T	Phosphorylation	Kinase	PLK1	P53350	Uniprot
28	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
28	Y	Phosphorylation	Kinase	HCK	P08631	Uniprot
47	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
48	S	Phosphorylation	Kinase	PLK2	Q9NYY3	PSP
86	T	Phosphorylation	Kinase	CDK1	P06493	PSP
86	T	Phosphorylation	Kinase	CDK2	P24941	PSP
99	Y	Phosphorylation	Kinase	ABL	P00519	PSP
99	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
235	S	Phosphorylation	Kinase	AURKA	O14965	GPS
289	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
289	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
388	S	Phosphorylation	Kinase	PRKCB	P05771-2	GPS
388	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
426	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
471	S	Phosphorylation	Kinase	IKKB	O14920	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RCHY1	Q96PM5	PMID:21994467
-	K	Ubiquitination	E3 ubiquitin ligase	DDB1	Q16531	PMID:23085759
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:26025930
-	K	Ubiquitination	E3 ubiquitin ligase	MUL1	Q969V5	PMID:26435500
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO45	P0C2W1	PMID:19581926
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:15678106
-	K	Ubiquitination	E3 ubiquitin ligase	HECW2	Q9P2P5	PMID:12890487
-	K	Ubiquitination	E3 ubiquitin ligase	WWP2	O00308	PMID:25071155
-	K	Ubiquitination	E3 ubiquitin ligase	WWP1#WWP2	Q9H0M0#O00308	PMID:25071155

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
627	K	Sumoylation		10961991
Isoform alpha (but not isoform beta) is sumoylated on Lys-627, which potentiates proteasomal degradation but does not affect transcriptional activity.

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 P73_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RACK1_HUMAN	GNB2L1	physical	12761493
RB_HUMAN	RB1	physical	12761493
P73_HUMAN	TP73	physical	10961991
YAP1_HUMAN	YAP1	physical	11278685
MDM2_HUMAN	MDM2	physical	10207051
HIPK2_HUMAN	HIPK2	physical	11925430
MYC_HUMAN	MYC	physical	12080043
IKKA_HUMAN	CHUK	physical	17452332
ITCH_HUMAN	ITCH	physical	17110958
YAP1_HUMAN	YAP1	physical	17110958
ADHX_HUMAN	ADH5	physical	20308539
CBPC2_HUMAN	AGBL2	physical	20308539
SAHH_HUMAN	AHCY	physical	20308539
AKAP1_HUMAN	AKAP1	physical	20308539
ASF1A_HUMAN	ASF1A	physical	20308539
ASPM_HUMAN	ASPM	physical	20308539
BRD8_HUMAN	BRD8	physical	20308539
NPRL3_HUMAN	NPRL3	physical	20308539
RTCB_HUMAN	RTCB	physical	20308539
TPC11_HUMAN	TRAPPC11	physical	20308539
CF206_HUMAN	C6orf165	physical	20308539
CDT1_HUMAN	CDT1	physical	20308539
DAB2P_HUMAN	DAB2IP	physical	20308539
DDX23_HUMAN	DDX23	physical	20308539
DNJB6_HUMAN	DNAJB6	physical	20308539
DPH1_HUMAN	DPH1	physical	20308539
AGO1_HUMAN	AGO1	physical	20308539
AGO2_HUMAN	AGO2	physical	20308539
GAS8_HUMAN	GAS8	physical	20308539
IF2B1_HUMAN	IGF2BP1	physical	20308539
JPH1_HUMAN	JPH1	physical	20308539
LPPRC_HUMAN	LRPPRC	physical	20308539
MTHSD_HUMAN	MTHFSD	physical	20308539
MYL9_HUMAN	MYL9	physical	20308539
N4BP2_HUMAN	N4BP2	physical	20308539
PAX6_HUMAN	PAX6	physical	20308539
PIWL1_HUMAN	PIWIL1	physical	20308539
RNF38_HUMAN	RNF38	physical	20308539
SAS6_HUMAN	SASS6	physical	20308539
SMRD2_HUMAN	SMARCD2	physical	20308539
SPSB1_HUMAN	SPSB1	physical	20308539
STAG1_HUMAN	STAG1	physical	20308539
TPM3_HUMAN	TPM3	physical	20308539
TRM11_HUMAN	TRMT11	physical	20308539
TTLL5_HUMAN	TTLL5	physical	20308539
UBE4B_HUMAN	UBE4B	physical	16170377
ITCH_HUMAN	ITCH	physical	15678106
NEDD4_HUMAN	NEDD4	physical	15678106
RANB9_HUMAN	RANBP9	physical	15558019
KDM1A_HUMAN	KDM1A	physical	18573881
EP300_HUMAN	EP300	physical	15893728
HECW2_HUMAN	HECW2	physical	12890487
EP300_HUMAN	EP300	physical	15454570
HDAC1_HUMAN	HDAC1	physical	15454570
HDAC1_HUMAN	HDAC1	physical	17353261
HDAC2_HUMAN	HDAC2	physical	17353261
MDM2_HUMAN	MDM2	physical	20588255
CUL1_HUMAN	CUL1	physical	19581926
FBSP1_HUMAN	FBXO45	physical	19581926
EP300_HUMAN	EP300	physical	10648616
AMPH_HUMAN	AMPH	physical	11709703
YAP1_HUMAN	YAP1	physical	19111660
MDM2_HUMAN	MDM2	physical	10435614
IKKA_HUMAN	CHUK	physical	21482671
IKKB_HUMAN	IKBKB	physical	21482671
DAXX_HUMAN	DAXX	physical	12954772
ACK1_HUMAN	TNK2	physical	15175157
EP300_HUMAN	EP300	physical	15175157
MDM2_HUMAN	MDM2	physical	10469568
DAXX_HUMAN	DAXX	physical	15339933
KAT2B_HUMAN	KAT2B	physical	14614455
EP300_HUMAN	EP300	physical	19218448
ZN363_HUMAN	RCHY1	physical	21994467
DDB1_HUMAN	DDB1	physical	23085759
GRP75_HUMAN	HSPA9	physical	22340593
KAPCA_HUMAN	PRKACA	physical	22340593
MD2L1_HUMAN	MAD2L1	physical	22340593
CDC20_HUMAN	CDC20	physical	22340593
AURKA_HUMAN	AURKA	physical	22340593
PFD5_HUMAN	PFDN5	physical	11844794
MYC_HUMAN	MYC	physical	11844794
CCNA2_HUMAN	CCNA2	physical	12676926
TRI32_HUMAN	TRIM32	physical	23828567
YAP1_HUMAN	YAP1	physical	18280240
PLAL1_HUMAN	PLAGL1	physical	18663001
KAT2B_HUMAN	KAT2B	physical	18663001
EP300_HUMAN	EP300	physical	18663001
TAT_HV1H2	tat	physical	16135803
CCNT1_HUMAN	CCNT1	physical	16135803
ABL1_HUMAN	ABL1	physical	19442657
OAZ1_HUMAN	OAZ1	physical	20185758
SIR1_HUMAN	SIRT1	physical	16998810
EP300_HUMAN	EP300	physical	25675294
RL11_HUMAN	RPL11	physical	25301064
RL5_HUMAN	RPL5	physical	25301064
MDM2_HUMAN	MDM2	physical	25301064
MUL1_HUMAN	MUL1	physical	26435500
WWP2_HUMAN	WWP2	physical	25071155
P53_HUMAN	TP53	physical	21508668
CSK21_HUMAN	CSNK2A1	physical	25379016
P53_HUMAN	TP53	physical	9802988
P73_HUMAN	TP73	physical	9802988
TIF1B_HUMAN	TRIM28	physical	25893286
ABL1_HUMAN	ABL1	physical	25893286
MED15_HUMAN	MED15	physical	25893286
KPCD_HUMAN	PRKCD	physical	12097319

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 P73_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Inhibitory role of Plk1 in the regulation of p73-dependent apoptosisthrough physical interaction and phosphorylation."; Koida N., Ozaki T., Yamamoto H., Ono S., Koda T., Ando K., Okoshi R.,Kamijo T., Omura K., Nakagawara A.; J. Biol. Chem. 283:8555-8563(2008). Cited for: FUNCTION, PHOSPHORYLATION AT THR-27, AND MUTAGENESIS OF THR-27.	18174154 [Abstract]
"p73-mediated transcriptional activity is negatively regulated bypolo-like kinase 1."; Soond S.M., Barry S.P., Melino G., Knight R.A., Latchman D.S.,Stephanou A.; Cell Cycle 7:1214-1223(2008). Cited for: PHOSPHORYLATION AT THR-27.	18418051 [Abstract]
"Regulation of p73 by Hck through kinase-dependent and independentmechanisms."; Paliwal P., Radha V., Swarup G.; BMC Mol. Biol. 8:45-45(2007). Cited for: PHOSPHORYLATION AT TYR-28, SUBCELLULAR LOCATION, AND INTERACTION WITHHCK.	17535448 [Abstract]
"p73 is regulated by tyrosine kinase c-Abl in the apoptotic responseto DNA damage."; Yuan Z.-M., Shioya H., Ishiko T., Sun X., Gu J., Huang Y., Lu H.,Kharbanda S., Weichselbaum R., Kufe D.; Nature 399:814-817(1999). Cited for: INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-99 BY ABL1, ANDMUTAGENESIS OF TYR-99.	10391251 [Abstract]
Sumoylation
Reference	PubMed
"Covalent modification of p73alpha by SUMO-1. Two-hybrid screeningwith p73 identifies novel SUMO-1-interacting proteins and a SUMO-1interaction motif."; Minty A., Dumont X., Kaghad M., Caput D.; J. Biol. Chem. 275:36316-36323(2000). Cited for: SUMOYLATION AT LYS-627, AND MUTAGENESIS OF LYS-627.	10961991 [Abstract]

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