dbPTM

PDC10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDC10_HUMAN
UniProt AC	Q9BUL8
Protein Name	Programmed cell death protein 10
Gene Name	PDCD10
Organism	Homo sapiens (Human).
Sequence Length	212
Subcellular Localization	Cytoplasm. Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side. Cell membrane Peripheral membrane protein Cytoplasmic side. Partially co-localizes with endogenous PXN at the leading edges of migrating cells.
Protein Description	Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. [PubMed: 27807006 Important for cell migration, and for normal structure and assembly of the Golgi complex]
Protein Sequence	MRMTMEEMKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGLTQDIIMKILEKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIPDEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDGKAINVFVSANRLIHQTNLILQTFKTVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MRMTMEEMKNE ----CCCCHHHHHHH	15.86	23401153
27	Phosphorylation	MPLYAVMYPVFNELE HHHHHHHHHHHHHHH	6.94	22210691
39	Phosphorylation	ELERVNLSAAQTLRA HHHHCCCCHHHHHHH	19.16	22210691
43	Phosphorylation	VNLSAAQTLRAAFIK CCCCHHHHHHHHHHH	17.31	19370760
50	Ubiquitination	TLRAAFIKAEKENPG HHHHHHHHHHHHCCC	44.00	-
53	2-Hydroxyisobutyrylation	AAFIKAEKENPGLTQ HHHHHHHHHCCCCCH	68.59	-
53	Ubiquitination	AAFIKAEKENPGLTQ HHHHHHHHHCCCCCH	68.59	-
64	Sulfoxidation	GLTQDIIMKILEKKS CCCHHHHHHHHHHCC	1.95	21406390
65	Ubiquitination	LTQDIIMKILEKKSV CCHHHHHHHHHHCCC	33.46	-
70	Ubiquitination	IMKILEKKSVEVNFT HHHHHHHCCCCCCCC	50.81	21890473
106	Ubiquitination	EFQDLNEKARALKQI HHHHHHHHHHHHHHH	41.94	-
106	2-Hydroxyisobutyrylation	EFQDLNEKARALKQI HHHHHHHHHHHHHHH	41.94	-
111	2-Hydroxyisobutyrylation	NEKARALKQILSKIP HHHHHHHHHHHHCCC	34.02	-
111	Acetylation	NEKARALKQILSKIP HHHHHHHHHHHHCCC	34.02	27452117
115	Phosphorylation	RALKQILSKIPDEIN HHHHHHHHCCCHHHH	30.12	24719451
116	Ubiquitination	ALKQILSKIPDEIND HHHHHHHCCCHHHHH	55.61	-
124	Methylation	IPDEINDRVRFLQTI CCHHHHHHHHHHHHH	19.61	115486707
132	Ubiquitination	VRFLQTIKDIASAIK HHHHHHHHHHHHHHH	46.61	21890473
150	Ubiquitination	DTVNNVFKKYQYQNR HHHHHHHHHHHHHHH	46.41	21890473
150	Succinylation	DTVNNVFKKYQYQNR HHHHHHHHHHHHHHH	46.41	23954790
172	Malonylation	KEFVKYSKSFSDTLK HHHHHHCCCHHHHHH	53.05	26320211
172	Ubiquitination	KEFVKYSKSFSDTLK HHHHHHCCCHHHHHH	53.05	-
177	Phosphorylation	YSKSFSDTLKTYFKD HCCCHHHHHHHHCCC	29.02	26503892
179	Ubiquitination	KSFSDTLKTYFKDGK CCHHHHHHHHCCCCC	43.18	19608861
179	Acetylation	KSFSDTLKTYFKDGK CCHHHHHHHHCCCCC	43.18	19608861
180	Phosphorylation	SFSDTLKTYFKDGKA CHHHHHHHHCCCCCE	36.98	26503892
181	Phosphorylation	FSDTLKTYFKDGKAI HHHHHHHHCCCCCEE	13.67	26503892
183	Ubiquitination	DTLKTYFKDGKAINV HHHHHHCCCCCEEEE	55.98	-
186	Sumoylation	KTYFKDGKAINVFVS HHHCCCCCEEEEEEE	57.11	28112733
201	Phosphorylation	ANRLIHQTNLILQTF HHHHHHHHHHHHHHH	20.17	-

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
39	S	Phosphorylation	Kinase	STK25	O00506	GPS
39	S	Phosphorylation	Kinase	MST4	Q9P289	PSP
43	T	Phosphorylation	Kinase	STK25	O00506	GPS
43	T	Phosphorylation	Kinase	MST4	Q9P289	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PDC10_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 PDC10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
2AAA_HUMAN	PPP2R1A	physical	18782753
PP2AA_HUMAN	PPP2CA	physical	18782753
STRN_HUMAN	STRN	physical	18782753
STRP1_HUMAN	STRIP1	physical	18782753
STRN3_HUMAN	STRN3	physical	18782753
STK26_HUMAN	STK26	physical	18782753
2AAB_HUMAN	PPP2R1B	physical	18782753
STRN4_HUMAN	STRN4	physical	18782753
STK25_HUMAN	STK25	physical	18782753
STK24_HUMAN	STK24	physical	18782753
PHOCN_HUMAN	MOB4	physical	18782753
CT2NL_HUMAN	CTTNBP2NL	physical	18782753
SIKE1_HUMAN	SIKE1	physical	18782753
SLMAP_HUMAN	SLMAP	physical	18782753
FGOP2_HUMAN	FGFR1OP2	physical	18782753
ICLN_HUMAN	CLNS1A	physical	22863883
CNN2_HUMAN	CNN2	physical	22863883
EHD1_HUMAN	EHD1	physical	22863883
EZRI_HUMAN	EZR	physical	22863883
HXK1_HUMAN	HK1	physical	22863883
NOL3_HUMAN	NOL3	physical	22863883
PCNA_HUMAN	PCNA	physical	22863883
STK26_HUMAN	STK26	physical	25416956
CD019_HUMAN	C4orf19	physical	25416956
PYRG1_HUMAN	CTPS1	physical	26344197
HNRPF_HUMAN	HNRNPF	physical	26344197
PPME1_HUMAN	PPME1	physical	26344197
STK24_HUMAN	STK24	physical	26344197
STK25_HUMAN	STK25	physical	26344197
STK26_HUMAN	STK26	physical	26344197
STK24_HUMAN	STK24	physical	21516116
STK25_HUMAN	STK25	physical	28514442
STK24_HUMAN	STK24	physical	28514442
STK26_HUMAN	STK26	physical	28514442
SLMAP_HUMAN	SLMAP	physical	28514442
STRN3_HUMAN	STRN3	physical	28514442
STRN_HUMAN	STRN	physical	28514442
FGOP2_HUMAN	FGFR1OP2	physical	28514442
CT2NL_HUMAN	CTTNBP2NL	physical	28514442
STRP1_HUMAN	STRIP1	physical	28514442
SIKE1_HUMAN	SIKE1	physical	28514442
STRN4_HUMAN	STRN4	physical	28514442

Drug and Disease Associations

Kegg Disease
H00534	Cerebral cavernous malformation
OMIM Disease
603285	Cerebral cavernous malformations 3 (CCM3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PDC10_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-179, AND MASS SPECTROMETRY.	19608861 [Abstract]