dbPTM

FETUA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FETUA_MOUSE
UniProt AC	P29699
Protein Name	Alpha-2-HS-glycoprotein
Gene Name	Ahsg
Organism	Mus musculus (Mouse).
Sequence Length	345
Subcellular Localization	Secreted.
Protein Description	Probably involved in differentiation..
Protein Sequence	MKSLVLLLCFAQLWGCQSAPQGTGLGFRELACDDPEAEQVALLAVDYLNNHLLQGFKQVLNQIDKVKVWSRRPFGVVYEMEVDTLETTCHALDPTPLANCSVRQLTEHAVEGDCDFHILKQDGQFRVMHTQCHSTPDSAEDVRKLCPRCPLLTPFNDTNVVHTVNTALAAFNTQNNGTYFKLVEISRAQNVPLPVSTLVEFVIAATDCTAKEVTDPAKCNLLAEKQHGFCKANLMHNLGGEEVSVACKLFQTQPQPANANAVGPVPTANAALPADPPASVVVGPVVVPRGLSDHRTYHDLRHAFSPVASVESASGETLHSPKVGQPGAAGPVSPMCPGRIRHFKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
65	Ubiquitination	QVLNQIDKVKVWSRR HHHHHHCCCEEEECC	45.65	22790023
99	N-linked_Glycosylation	LDPTPLANCSVRQLT CCCCCCCCCCHHHHH	26.69	17330941
114	S-palmitoylation	EHAVEGDCDFHILKQ HHHHHCCCCEEEEEC	9.89	26165157
130	Phosphorylation	GQFRVMHTQCHSTPD CEEEEEEEECCCCCC	18.13	24925903
134	Phosphorylation	VMHTQCHSTPDSAED EEEEECCCCCCCHHH	49.62	24925903
135	Phosphorylation	MHTQCHSTPDSAEDV EEEECCCCCCCHHHH	13.88	24925903
138	Phosphorylation	QCHSTPDSAEDVRKL ECCCCCCCHHHHHHH	34.46	25521595
156	N-linked_Glycosylation	CPLLTPFNDTNVVHT CCCCCCCCCCCHHHC	57.30	17330941
176	N-linked_Glycosylation	AAFNTQNNGTYFKLV HHHCCCCCCCEEEEE	34.07	16944957
208	S-palmitoylation	FVIAATDCTAKEVTD HHHHHCCCCCCCCCC	3.28	28526873
219	Glutathionylation	EVTDPAKCNLLAEKQ CCCCHHHCCHHHHHH	4.75	24333276
225	Ubiquitination	KCNLLAEKQHGFCKA HCCHHHHHHCCCEEH	41.82	22790023
296	Phosphorylation	RGLSDHRTYHDLRHA CCCCCCCCHHHHHHH	23.07	24719451
305	Phosphorylation	HDLRHAFSPVASVES HHHHHHCCCCEEEEC	21.17	25521595
309	Phosphorylation	HAFSPVASVESASGE HHCCCCEEEECCCCC	27.01	25521595
312	Phosphorylation	SPVASVESASGETLH CCCEEEECCCCCCCC	26.11	25521595
314	Phosphorylation	VASVESASGETLHSP CEEEECCCCCCCCCC	46.57	25521595
317	Phosphorylation	VESASGETLHSPKVG EECCCCCCCCCCCCC	33.04	25521595
320	Phosphorylation	ASGETLHSPKVGQPG CCCCCCCCCCCCCCC	29.54	24925903
333	Phosphorylation	PGAAGPVSPMCPGRI CCCCCCCCCCCCCCE	15.28	-
336	S-palmitoylation	AGPVSPMCPGRIRHF CCCCCCCCCCCEEEE	3.52	28526873

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 FETUA_MOUSE !!

Functions of PTM Sites

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

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 FETUA_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of FETUA_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; Bernhard O.K., Kapp E.A., Simpson R.J.; J. Proteome Res. 6:987-995(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99; ASN-156 AND ASN-176,AND MASS SPECTROMETRY.	17330941 [Abstract]
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography."; Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.; J. Proteome Res. 5:2438-2447(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176, AND MASSSPECTROMETRY.	16944957 [Abstract]
Phosphorylation
Reference	PubMed
"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-138; SER-309 ANDSER-312, 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-138, AND MASSSPECTROMETRY.	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-305; SER-309; SER-312AND SER-314, AND MASS SPECTROMETRY.	17242355 [Abstract]