dbPTM

PP4C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PP4C_HUMAN
UniProt AC	P60510
Protein Name	Serine/threonine-protein phosphatase 4 catalytic subunit
Gene Name	PPP4C
Organism	Homo sapiens (Human).
Sequence Length	307
Subcellular Localization	Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Description	Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase (By similarity). In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin..
Protein Sequence	MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEISDLDR ------CCCHHHHHH	23.88	22223895
15	Methylation	DRQIEQLRRCELIKE HHHHHHHHHCHHHCH	40.68	115488613
21	Acetylation	LRRCELIKESEVKAL HHHCHHHCHHHHHHH	68.74	26051181
21	Ubiquitination	LRRCELIKESEVKAL HHHCHHHCHHHHHHH	68.74	-
26	Ubiquitination	LIKESEVKALCAKAR HHCHHHHHHHHHHHH	31.43	21906983
31	Ubiquitination	EVKALCAKAREILVE HHHHHHHHHHHHHHC	47.16	21906983
31	Acetylation	EVKALCAKAREILVE HHHHHHHHHHHHHHC	47.16	25953088
47	Phosphorylation	SNVQRVDSPVTVCGD CCCCCCCCCEEEECC	20.57	27732954
50	Phosphorylation	QRVDSPVTVCGDIHG CCCCCCEEEECCCCC	17.29	27251275
63	Ubiquitination	HGQFYDLKELFRVGG CCCEECHHHHHCCCC	49.85	21906983
77	Phosphorylation	GDVPETNYLFMGDFV CCCCCCCEEECCCCC	14.56	-
104	Phosphorylation	LLALKVRYPDRITLI HHHHHCCCCCCEEEE	16.69	28509920
107	Methylation	LKVRYPDRITLIRGN HHCCCCCCEEEEECC	21.20	115488619
109	Phosphorylation	VRYPDRITLIRGNHE CCCCCCEEEEECCCC	19.61	28509920
121	Phosphorylation	NHESRQITQVYGFYD CCCHHHHHEEEECHH	12.02	24043423
124	Phosphorylation	SRQITQVYGFYDECL HHHHHEEEECHHHHH	7.53	28152594
127	Phosphorylation	ITQVYGFYDECLRKY HHEEEECHHHHHHHH	13.38	28152594
133	Ubiquitination	FYDECLRKYGSVTVW CHHHHHHHHCCEEHH	40.80	-
168	Phosphorylation	FCVHGGLSPSIQTLD EEEECCCCCCHHCHH	21.63	25693802
170	Phosphorylation	VHGGLSPSIQTLDQI EECCCCCCHHCHHHH	24.77	25693802
173	Phosphorylation	GLSPSIQTLDQIRTI CCCCCHHCHHHHCCC	30.54	25693802
183	Ubiquitination	QIRTIDRKQEVPHDG HHCCCCCCCCCCCCC	47.24	-
193	Glutathionylation	VPHDGPMCDLLWSDP CCCCCCCCCEEECCC	3.62	22555962
242	Sulfoxidation	CRAHQLVMEGYKWHF HHHHHHHHCCCCEEE	4.49	30846556
298	Phosphorylation	QETRGIPSKKPVADY CCCCCCCCCCCCHHH	51.93	24719451
299	Ubiquitination	ETRGIPSKKPVADYF CCCCCCCCCCCHHHC	56.60	-
300	Acetylation	TRGIPSKKPVADYFL CCCCCCCCCCHHHCC	49.41	25953088
300	Ubiquitination	TRGIPSKKPVADYFL CCCCCCCCCCHHHCC	49.41	-
305	Phosphorylation	SKKPVADYFL----- CCCCCHHHCC-----	9.31	27642862
307	Methylation	KPVADYFL------- CCCHHHCC-------	5.81	25130464

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
Oops, there are no upstream regulatory protein records of PP4C_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
307	L	Methylation		25130464
Methylation at the C-terminal Leu-307 is critical for interactions with regulatory subunits and functions in DNA repair.

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 PP4C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P4R3A_HUMAN	SMEK1	physical	17353931
TIPRL_HUMAN	TIPRL	physical	17353931
P4R3B_HUMAN	SMEK2	physical	17353931
PP4R1_HUMAN	PPP4R1	physical	17353931
2AAA_HUMAN	PPP2R1A	physical	17353931
PP2AB_HUMAN	PPP2CB	physical	17353931
PP4R2_HUMAN	PPP4R2	physical	17353931
CCDC6_HUMAN	CCDC6	physical	17353931
BAG6_HUMAN	BAG6	physical	17353931
PRP16_HUMAN	DHX38	physical	18715871
P4R3A_HUMAN	SMEK1	physical	18715871
TCPB_HUMAN	CCT2	physical	18715871
PP4R2_HUMAN	PPP4R2	physical	18715871
TCPA_HUMAN	TCP1	physical	18715871
TCPE_HUMAN	CCT5	physical	18715871
TCPG_HUMAN	CCT3	physical	18715871
TCPZ_HUMAN	CCT6A	physical	18715871
P4R3B_HUMAN	SMEK2	physical	18715871
TCPD_HUMAN	CCT4	physical	18715871
IGBP1_HUMAN	IGBP1	physical	18715871
PP4R1_HUMAN	PPP4R1	physical	18715871
TCPH_HUMAN	CCT7	physical	18715871
CCDC6_HUMAN	CCDC6	physical	18715871
PP4R4_HUMAN	PPP4R4	physical	18715871
2AAA_HUMAN	PPP2R1A	physical	18715871
2A5D_HUMAN	PPP2R5D	physical	18715871
IGBP1_HUMAN	IGBP1	physical	16085932
PP4R1_HUMAN	PPP4R1	physical	16085932
PP4R2_HUMAN	PPP4R2	physical	16085932
TCPA_HUMAN	TCP1	physical	16085932
TCPB_HUMAN	CCT2	physical	16085932
TCPG_HUMAN	CCT3	physical	16085932
TCPD_HUMAN	CCT4	physical	16085932
TCPE_HUMAN	CCT5	physical	16085932
TCPZ_HUMAN	CCT6A	physical	16085932
TCPH_HUMAN	CCT7	physical	16085932
TCPQ_HUMAN	CCT8	physical	16085932
P4R3A_HUMAN	SMEK1	physical	16085932
P4R3B_HUMAN	SMEK2	physical	16085932
TRAF6_HUMAN	TRAF6	physical	18634786
M4K1_HUMAN	MAP4K1	physical	15364934
P4R3A_HUMAN	SMEK1	physical	20876121
P4R3B_HUMAN	SMEK2	physical	20876121
PP4R2_HUMAN	PPP4R2	physical	20876121
GLYL3_HUMAN	GLYATL3	physical	19156129
PLOD3_HUMAN	PLOD3	physical	19156129
PP4R2_HUMAN	PPP4R2	physical	19156129
WDR81_HUMAN	WDR81	physical	19156129
ADT4_HUMAN	SLC25A31	physical	19156129
TRM1L_HUMAN	TRMT1L	physical	19156129
PP4R4_HUMAN	PPP4R4	physical	19156129
P4R3B_HUMAN	SMEK2	physical	19156129
P4R3A_HUMAN	SMEK1	physical	19156129
ATD3A_HUMAN	ATAD3A	physical	19156129
TCPE_HUMAN	CCT5	physical	19156129
TCPQ_HUMAN	CCT8	physical	19156129
TCPB_HUMAN	CCT2	physical	19156129
TCPD_HUMAN	CCT4	physical	19156129
TCPH_HUMAN	CCT7	physical	19156129
PP4R1_HUMAN	PPP4R1	physical	19156129
CCDC6_HUMAN	CCDC6	physical	19156129
TCPG_HUMAN	CCT3	physical	19156129
TCPA_HUMAN	TCP1	physical	19156129
2A5D_HUMAN	PPP2R5D	physical	19156129
2AAA_HUMAN	PPP2R1A	physical	19156129
IGBP1_HUMAN	IGBP1	physical	19156129
EF1A1_HUMAN	EEF1A1	physical	19156129
TCPZ_HUMAN	CCT6A	physical	19156129
ATD3B_HUMAN	ATAD3B	physical	19156129
TBA3C_HUMAN	TUBA3C	physical	19156129
TIF1B_HUMAN	TRIM28	physical	22491012
NEMO_HUMAN	IKBKG	physical	24109239
SPF27_HUMAN	BCAS2	physical	27880917
CCDC6_HUMAN	CCDC6	physical	27880917
CDC5L_HUMAN	CDC5L	physical	27880917
CLAP2_HUMAN	CLASP2	physical	27880917
PRP16_HUMAN	DHX38	physical	27880917
IGBP1_HUMAN	IGBP1	physical	27880917
2AAA_HUMAN	PPP2R1A	physical	27880917
2ABA_HUMAN	PPP2R2A	physical	27880917
2A5D_HUMAN	PPP2R5D	physical	27880917
PP4R1_HUMAN	PPP4R1	physical	27880917
PP4R2_HUMAN	PPP4R2	physical	27880917
PP4R4_HUMAN	PPP4R4	physical	27880917
PRP19_HUMAN	PRPF19	physical	27880917
P4R3A_HUMAN	SMEK1	physical	27880917
P4R3B_HUMAN	SMEK2	physical	27880917
SPT5H_HUMAN	SUPT5H	physical	27880917
TIPRL_HUMAN	TIPRL	physical	27880917

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 PP4C_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]

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