PDCD5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDCD5_HUMAN
• UniProt AC: O14737
• Protein Name: Programmed cell death protein 5
• Gene Name: PDCD5
• Organism: Homo sapiens (Human).
• Sequence Length: 125
• Protein Description: May function in the process of apoptosis..
• Protein Sequence: MADEELEALRRQRLAELQAKHGDPGDAAQQEAKHREAEMRNSILAQVLDQSARARLSNLALVKPEKTKAVENYLIQMARYGQLSEKVSEQGLIEILKKVSQQTEKTTTVKFNRRKVMDSDEDDDY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADEELEAL ------CCHHHHHHH	32.68	22223895
10	Methylation	DEELEALRRQRLAEL HHHHHHHHHHHHHHH	39.47	115486729
20	Ubiquitination	RLAELQAKHGDPGDA HHHHHHHHHCCCCHH	34.85	21963094
20	Ubiquitination	RLAELQAKHGDPGDA HHHHHHHHHCCCCHH	34.85	21890473
20	2-Hydroxyisobutyrylation	RLAELQAKHGDPGDA HHHHHHHHHCCCCHH	34.85	-
20	Acetylation	RLAELQAKHGDPGDA HHHHHHHHHCCCCHH	34.85	25953088
33	Ubiquitination	DAAQQEAKHREAEMR HHHHHHHHHHHHHHH	42.30	21906983
33	Acetylation	DAAQQEAKHREAEMR HHHHHHHHHHHHHHH	42.30	-
33	Ubiquitination	DAAQQEAKHREAEMR HHHHHHHHHHHHHHH	42.30	21890473
33	Acetylation	DAAQQEAKHREAEMR HHHHHHHHHHHHHHH	42.30	21466224
42	Phosphorylation	REAEMRNSILAQVLD HHHHHHHHHHHHHHC	14.49	25850435
51	Phosphorylation	LAQVLDQSARARLSN HHHHHCHHHHHHHHC	21.27	23663014
57	Phosphorylation	QSARARLSNLALVKP HHHHHHHHCCCCCCH	25.01	28450419
63	Ubiquitination	LSNLALVKPEKTKAV HHCCCCCCHHHCHHH	48.59	23000965
63	Acetylation	LSNLALVKPEKTKAV HHCCCCCCHHHCHHH	48.59	19608861
63	Ubiquitination	LSNLALVKPEKTKAV HHCCCCCCHHHCHHH	48.59	21890473
63	Acetylation	LSNLALVKPEKTKAV HHCCCCCCHHHCHHH	48.59	-
66	Acetylation	LALVKPEKTKAVENY CCCCCHHHCHHHHHH	64.95	25953088
66	2-Hydroxyisobutyrylation	LALVKPEKTKAVENY CCCCCHHHCHHHHHH	64.95	-
66	Ubiquitination	LALVKPEKTKAVENY CCCCCHHHCHHHHHH	64.95	23000965
68	Ubiquitination	LVKPEKTKAVENYLI CCCHHHCHHHHHHHH	62.60	21890473
68	Ubiquitination	LVKPEKTKAVENYLI CCCHHHCHHHHHHHH	62.60	23000965
73	Phosphorylation	KTKAVENYLIQMARY HCHHHHHHHHHHHHH	7.53	22817900
73	Nitration	KTKAVENYLIQMARY HCHHHHHHHHHHHHH	7.53	-
77	Sulfoxidation	VENYLIQMARYGQLS HHHHHHHHHHHCHHC	1.49	30846556
79	Methylation	NYLIQMARYGQLSEK HHHHHHHHHCHHCHH	30.67	115486737
80	Phosphorylation	YLIQMARYGQLSEKV HHHHHHHHCHHCHHH	10.33	28152594
84	Phosphorylation	MARYGQLSEKVSEQG HHHHCHHCHHHHHHH	27.73	23403867
86	Ubiquitination	RYGQLSEKVSEQGLI HHCHHCHHHHHHHHH	47.92	33845483
88	Phosphorylation	GQLSEKVSEQGLIEI CHHCHHHHHHHHHHH	34.96	21712546
97	Acetylation	QGLIEILKKVSQQTE HHHHHHHHHHHCCCC	57.71	23236377
97	Neddylation	QGLIEILKKVSQQTE HHHHHHHHHHHCCCC	57.71	32015554
97	2-Hydroxyisobutyrylation	QGLIEILKKVSQQTE HHHHHHHHHHHCCCC	57.71	-
97	Ubiquitination	QGLIEILKKVSQQTE HHHHHHHHHHHCCCC	57.71	21906983
98	Ubiquitination	GLIEILKKVSQQTEK HHHHHHHHHHCCCCC	43.61	22817900
100	Phosphorylation	IEILKKVSQQTEKTT HHHHHHHHCCCCCCE	26.00	25072903
103	Phosphorylation	LKKVSQQTEKTTTVK HHHHHCCCCCCEEEE	31.63	20068231
105	2-Hydroxyisobutyrylation	KVSQQTEKTTTVKFN HHHCCCCCCEEEEEC	55.34	-
105	Ubiquitination	KVSQQTEKTTTVKFN HHHCCCCCCEEEEEC	55.34	22817900
105	Acetylation	KVSQQTEKTTTVKFN HHHCCCCCCEEEEEC	55.34	25953088
106	Phosphorylation	VSQQTEKTTTVKFNR HHCCCCCCEEEEECH	22.82	26074081
107	Phosphorylation	SQQTEKTTTVKFNRR HCCCCCCEEEEECHH	40.43	26074081
108	Phosphorylation	QQTEKTTTVKFNRRK CCCCCCEEEEECHHH	27.25	26074081
110	Acetylation	TEKTTTVKFNRRKVM CCCCEEEEECHHHCC	34.53	25953088
110	Ubiquitination	TEKTTTVKFNRRKVM CCCCEEEEECHHHCC	34.53	21906983
115	Ubiquitination	TVKFNRRKVMDSDED EEEECHHHCCCCCCC	38.38	22817900
119	Phosphorylation	NRRKVMDSDEDDDY- CHHHCCCCCCCCCC-	25.46	19616514
125	Phosphorylation	DSDEDDDY------- CCCCCCCC-------	27.70	23927012

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
119	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDCD5_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PDCD5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPA5_HUMAN	ACP5	physical	16169070
KAT5_HUMAN	KAT5	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
UT14A_HUMAN	UTP14A	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
KAT5_HUMAN	KAT5	physical	19308289
P53_HUMAN	TP53	physical	22914926
MDM2_HUMAN	MDM2	physical	22914926
KDM1A_HUMAN	KDM1A	physical	23455924
OTUD5_HUMAN	OTUD5	physical	25499082
P53_HUMAN	TP53	physical	25499082
STMN1_HUMAN	STMN1	physical	26344197
YAF2_HUMAN	YAF2	physical	25603536
ARRD5_HUMAN	ARRDC5	physical	25603536
AT1B1_HUMAN	ATP1B1	physical	25603536

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.

Related Literatures of Post-Translational Modification

Acetylation

"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-119, AND MASS SPECTROMETRY.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
PubMed: 19690332

"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-119, AND MASS SPECTROMETRY.
PubMed: 19413330

"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
PubMed: 18318008

"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 SER-119, AND MASSSPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
PubMed: 17081983

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASSSPECTROMETRY.
PubMed: 15302935