dbPTM

HDGF_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HDGF_MOUSE
UniProt AC	P51859
Protein Name	Hepatoma-derived growth factor
Gene Name	Hdgf
Organism	Mus musculus (Mouse).
Sequence Length	237
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor (By similarity)..
Protein Sequence	MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCAAEPEVEPEAHEGDGDKKGSAEGSSDEEGKLVIDEPAKEKNEKGTLKRRAGDVLEDSPKRPKESGDHEEEDKEIAALEGERPLPVEVEKNSTPSEPDSGQGPPAEEEEGEEEAAKEEAEAQGVRDHESL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRSNRQKE ------CCCCHHCCC	44.40	21183079
11	Ubiquitination	SNRQKEYKCGDLVFA CHHCCCCCCCCEEHH	32.60	22790023
12	S-nitrosocysteine	NRQKEYKCGDLVFAK HHCCCCCCCCEEHHH	5.12	-
12	Glutathionylation	NRQKEYKCGDLVFAK HHCCCCCCCCEEHHH	5.12	24333276
12	S-nitrosylation	NRQKEYKCGDLVFAK HHCCCCCCCCEEHHH	5.12	22178444
38	Ubiquitination	DEMPEAAVKSTANKY HHCCHHHHHHHCCCE	6.93	27667366
39	Ubiquitination	EMPEAAVKSTANKYQ HCCHHHHHHHCCCEE	37.04	22790023
44	Acetylation	AVKSTANKYQVFFFG HHHHHCCCEEEEEEE	34.30	-
70	Ubiquitination	LFPYEESKEKFGKPN CCCHHHHHHHHCCCC	69.10	22790023
80	Ubiquitination	FGKPNKRKGFSEGLW HCCCCCCCCCCCCCE	66.95	22790023
83	Phosphorylation	PNKRKGFSEGLWEIE CCCCCCCCCCCEEEC	39.15	25338131
96	Ubiquitination	IENNPTVKASGYQSS ECCCCCCCCCCCCCC	39.03	22790023
98	Phosphorylation	NNPTVKASGYQSSQK CCCCCCCCCCCCCCC	32.11	28285833
102	Phosphorylation	VKASGYQSSQKKSCA CCCCCCCCCCCCCCC	26.67	-
103	Phosphorylation	KASGYQSSQKKSCAA CCCCCCCCCCCCCCC	30.41	27841257
105	Acetylation	SGYQSSQKKSCAAEP CCCCCCCCCCCCCCC	48.91	7618901
107	Phosphorylation	YQSSQKKSCAAEPEV CCCCCCCCCCCCCCC	18.94	25521595
114	Ubiquitination	SCAAEPEVEPEAHEG CCCCCCCCCCCCCCC	25.28	27667366
117	Ubiquitination	AEPEVEPEAHEGDGD CCCCCCCCCCCCCCC	49.50	27667366
125	Ubiquitination	AHEGDGDKKGSAEGS CCCCCCCCCCCCCCC	65.64	22790023
128	Phosphorylation	GDGDKKGSAEGSSDE CCCCCCCCCCCCCCC	31.84	24925903
132	Phosphorylation	KKGSAEGSSDEEGKL CCCCCCCCCCCCCCE	26.56	27087446
133	Phosphorylation	KGSAEGSSDEEGKLV CCCCCCCCCCCCCEE	60.95	27087446
146	Ubiquitination	LVIDEPAKEKNEKGT EEECCCCCHHCCCCC	78.80	22790023
165	Phosphorylation	AGDVLEDSPKRPKES HHHCCCCCCCCCCCC	23.97	24925903
172	Phosphorylation	SPKRPKESGDHEEED CCCCCCCCCCCHHHH	56.50	26239621
180	Acetylation	GDHEEEDKEIAALEG CCCHHHHHHHHHHCC	55.06	23806337
199	Phosphorylation	PVEVEKNSTPSEPDS CEEEECCCCCCCCCC	53.41	25521595
200	Phosphorylation	VEVEKNSTPSEPDSG EEEECCCCCCCCCCC	39.98	25521595
202	Phosphorylation	VEKNSTPSEPDSGQG EECCCCCCCCCCCCC	62.95	27087446
206	Phosphorylation	STPSEPDSGQGPPAE CCCCCCCCCCCCCHH	43.67	25521595
236	Phosphorylation	QGVRDHESL------ CCCCCCCCC------	35.64	22324799

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 HDGF_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
165	S	Phosphorylation		17242355
Phosphorylation at Ser-165 is likely to be required for secretion.

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 HDGF_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HDGF_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of HDGF_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133AND SER-165, AND MASS SPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133AND SER-202, AND MASS SPECTROMETRY.	17242355 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132 ANDSER-133, AND MASS SPECTROMETRY.	17622165 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-202 ANDSER-206, AND MASS SPECTROMETRY.	15345747 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.	14729942 [Abstract]

show