dbPTM

PPP5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PPP5_HUMAN
UniProt AC	P53041
Protein Name	Serine/threonine-protein phosphatase 5
Gene Name	PPP5C
Organism	Homo sapiens (Human).
Sequence Length	499
Subcellular Localization	Nucleus . Cytoplasm . Cell membrane . Predominantly nuclear (PubMed:15383005). But also present in the cytoplasm (PubMed:15383005). Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner (PubMed:19948726).
Protein Description	Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2..
Protein Sequence	MAMAEGERTECAEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAMAEGERT ------CCCCCCCCC	13.09	19413330
26	Ubiquitination	PPADGALKRAEELKT CCCCCHHHHHHHHHH	49.37	-
26	Acetylation	PPADGALKRAEELKT CCCCCHHHHHHHHHH	49.37	26051181
32	Acetylation	LKRAEELKTQANDYF HHHHHHHHHHHHHHH	41.70	23236377
32	Ubiquitination	LKRAEELKTQANDYF HHHHHHHHHHHHHHH	41.70	21906983
40	Acetylation	TQANDYFKAKDYENA HHHHHHHHHCCHHHH	48.58	25953088
40	Ubiquitination	TQANDYFKAKDYENA HHHHHHHHHCCHHHH	48.58	21906983
42	Ubiquitination	ANDYFKAKDYENAIK HHHHHHHCCHHHHHH	62.53	-
42	Malonylation	ANDYFKAKDYENAIK HHHHHHHCCHHHHHH	62.53	26320211
44	Phosphorylation	DYFKAKDYENAIKFY HHHHHCCHHHHHHHH	15.46	28796482
49	Ubiquitination	KDYENAIKFYSQAIE CCHHHHHHHHHHCHH	35.52	21906983
74	Methylation	NRSLAYLRTECYGYA CCCHHHHHHHCCCHH	18.79	115488625
77	Glutathionylation	LAYLRTECYGYALGD HHHHHHHCCCHHCCC	2.93	22555962
77	S-nitrosylation	LAYLRTECYGYALGD HHHHHHHCCCHHCCC	2.93	2212679
78	Phosphorylation	AYLRTECYGYALGDA HHHHHHCCCHHCCCH	13.62	28152594
80	Phosphorylation	LRTECYGYALGDATR HHHHCCCHHCCCHHH	3.38	28152594
86	Phosphorylation	GYALGDATRAIELDK CHHCCCHHHHHHHCH	25.93	28152594
93	2-Hydroxyisobutyrylation	TRAIELDKKYIKGYY HHHHHHCHHHHHHHH	61.16	-
93	Acetylation	TRAIELDKKYIKGYY HHHHHHCHHHHHHHH	61.16	23749302
94	Ubiquitination	RAIELDKKYIKGYYR HHHHHCHHHHHHHHH	52.45	-
97	Ubiquitination	ELDKKYIKGYYRRAA HHCHHHHHHHHHHHH	37.46	-
97	Malonylation	ELDKKYIKGYYRRAA HHCHHHHHHHHHHHH	37.46	26320211
105	Phosphorylation	GYYRRAASNMALGKF HHHHHHHHHHHHHHH	26.59	22817900
107	Sulfoxidation	YRRAASNMALGKFRA HHHHHHHHHHHHHHH	2.78	30846556
111	2-Hydroxyisobutyrylation	ASNMALGKFRAALRD HHHHHHHHHHHHHCC	32.31	-
111	Acetylation	ASNMALGKFRAALRD HHHHHHHHHHHHHCC	32.31	25953088
111	Ubiquitination	ASNMALGKFRAALRD HHHHHHHHHHHHHCC	32.31	-
119	Phosphorylation	FRAALRDYETVVKVK HHHHHCCCEEEEECC	13.68	28796482
121	Phosphorylation	AALRDYETVVKVKPH HHHCCCEEEEECCCC	25.11	-
124	Ubiquitination	RDYETVVKVKPHDKD CCCEEEEECCCCCHH	39.96	-
135	Acetylation	HDKDAKMKYQECNKI CCHHHHHHHHHHHHH	42.97	25953088
141	Acetylation	MKYQECNKIVKQKAF HHHHHHHHHHHHHHH	61.61	25953088
141	Ubiquitination	MKYQECNKIVKQKAF HHHHHHHHHHHHHHH	61.61	-
158	2-Hydroxyisobutyrylation	AIAGDEHKRSVVDSL HHCCCHHHHCHHHCC	44.30	-
158	Ubiquitination	AIAGDEHKRSVVDSL HHCCCHHHHCHHHCC	44.30	-
176	Phosphorylation	SMTIEDEYSGPKLED ECEEEEECCCCCCCC	31.11	-
185	Ubiquitination	GPKLEDGKVTISFMK CCCCCCCCEEHHHHH	48.83	21906983
198	Phosphorylation	MKELMQWYKDQKKLH HHHHHHHHHHHHHHH	6.44	25332170
199	Ubiquitination	KELMQWYKDQKKLHR HHHHHHHHHHHHHHH	51.20	-
210	Phosphorylation	KLHRKCAYQILVQVK HHHHHHHHHHHHHHH	12.93	20049867
221	Phosphorylation	VQVKEVLSKLSTLVE HHHHHHHHHHHHHHH	36.40	20049867
229	Phosphorylation	KLSTLVETTLKETEK HHHHHHHHHCCCCCE	29.92	20049867
232	Ubiquitination	TLVETTLKETEKITV HHHHHHCCCCCEEEE	61.57	-
277	Phosphorylation	GDFVDRGSFSVEVIL CCCCCCCCCCHHHHH	18.42	-
279	Phosphorylation	FVDRGSFSVEVILTL CCCCCCCCHHHHHHH	21.04	-
285	Phosphorylation	FSVEVILTLFGFKLL CCHHHHHHHHCHHHH	14.66	-
309	Sulfoxidation	GNHETDNMNQIYGFE CCCCCCCCCHHCCCC	4.31	30846556
313	Phosphorylation	TDNMNQIYGFEGEVK CCCCCHHCCCCCCHH	13.14	25147952
320	Ubiquitination	YGFEGEVKAKYTAQM CCCCCCHHHEEHHHH	34.55	21906983
362	Phosphorylation	LFSEDGVTLDDIRKI EECCCCCCHHHHHHH	29.96	-
378	Phosphorylation	RNRQPPDSGPMCDLL HCCCCCCCCCCCHHC	51.04	22210691
387	Phosphorylation	PMCDLLWSDPQPQNG CCCHHCCCCCCCCCC	39.11	22210691
403	Phosphorylation	SISKRGVSCQFGPDV CCHHCCCCCCCCCCH	12.67	26552605
404	S-nitrosocysteine	ISKRGVSCQFGPDVT CHHCCCCCCCCCCHH	3.45	-
404	S-nitrosylation	ISKRGVSCQFGPDVT CHHCCCCCCCCCCHH	3.45	19483679
411	Phosphorylation	CQFGPDVTKAFLEEN CCCCCCHHHHHHHHC	24.84	26552605
412	Ubiquitination	QFGPDVTKAFLEENN CCCCCHHHHHHHHCC	36.67	-
422	Phosphorylation	LEENNLDYIIRSHEV HHHCCCCEEEECCEE	11.04	-
430	Ubiquitination	IIRSHEVKAEGYEVA EEECCEEEECCEEEE	37.42	-
434	Nitration	HEVKAEGYEVAHGGR CEEEECCEEEEECCE	9.95	-
434	Phosphorylation	HEVKAEGYEVAHGGR CEEEECCEEEEECCE	9.95	28796482
451	Phosphorylation	TVFSAPNYCDQMGNK EEEECCCCHHHCCCC	9.06	25147952

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
362	T	Phosphorylation	Kinase	CSNK1D	P48730	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PPP5_HUMAN !!

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 PPP5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XPO2_HUMAN	CSE1L	physical	16169070
GNA12_HUMAN	GNA12	physical	12176367
GNA13_HUMAN	GNA13	physical	12176367
M3K5_HUMAN	MAP3K5	physical	11689443
CRY2_HUMAN	CRY2	physical	9383998
HSP74_HUMAN	HSPA4	physical	15383005
HS90A_HUMAN	HSP90AA1	physical	15383005
ORF73_HHV8P	HHV8GK18_gp81	physical	22379092
A4_HUMAN	APP	physical	21832049
RRP44_HUMAN	DIS3	physical	22939629
ROA1_HUMAN	HNRNPA1	physical	22939629
TAU_HUMAN	MAPT	physical	12435421
ESR2_HUMAN	ESR2	physical	14764652
ESR1_HUMAN	ESR1	physical	14764652
HS90A_HUMAN	HSP90AA1	physical	16531226
STIP1_HUMAN	STIP1	physical	21360678
HSP7C_HUMAN	HSPA8	physical	21360678
HS90B_HUMAN	HSP90AB1	physical	21360678
HS90A_HUMAN	HSP90AA1	physical	21360678
TCPD_HUMAN	CCT4	physical	21360678
CDC37_HUMAN	CDC37	physical	21360678
CHRD1_MOUSE	Chordc1	physical	23184943
HS90A_HUMAN	HSP90AA1	physical	21235734
ABHEA_HUMAN	ABHD14A	physical	22863883
BZW2_HUMAN	BZW2	physical	22863883
IF6_HUMAN	EIF6	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
GSHB_HUMAN	GSS	physical	22863883
PNCB_HUMAN	NAPRT	physical	22863883
PA1B2_HUMAN	PAFAH1B2	physical	22863883
PAPS1_HUMAN	PAPSS1	physical	22863883
PLD3_HUMAN	PLD3	physical	22863883
GDS1_HUMAN	RAP1GDS1	physical	22863883
XPO1_HUMAN	XPO1	physical	22863883
HS90A_HUMAN	HSP90AA1	physical	25036637
TEBP_HUMAN	PTGES3	physical	25036637
CHRD1_HUMAN	CHORDC1	physical	25036637
HS90B_HUMAN	HSP90AB1	physical	25036637
CDC37_HUMAN	CDC37	physical	25036637
AHSA1_HUMAN	AHSA1	physical	25036637
DUT_HUMAN	DUT	physical	26344197
MINP1_HUMAN	MINPP1	physical	26344197
TATD1_HUMAN	TATDN1	physical	26344197
HS90A_HUMAN	HSP90AA1	physical	26496610
HS90B_HUMAN	HSP90AB1	physical	26496610
PSN2_HUMAN	PSEN2	physical	26496610
RBBP6_HUMAN	RBBP6	physical	26496610
KS6B1_HUMAN	RPS6KB1	physical	26496610
ABCF2_HUMAN	ABCF2	physical	26496610
UBP45_HUMAN	USP45	physical	26496610
HS90A_HUMAN	HSP90AA1	physical	19740745
HS90A_HUMAN	HSP90AA1	physical	27880917
HS90B_HUMAN	HSP90AB1	physical	27880917
HSP76_HUMAN	HSPA6	physical	27880917

Drug and Disease Associations

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

Regulatory Network of PPP5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]