dbPTM

OSTP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	OSTP_MOUSE
UniProt AC	P10923
Protein Name	Osteopontin
Gene Name	Spp1
Organism	Mus musculus (Mouse).
Sequence Length	294
Subcellular Localization	Secreted.
Protein Description	Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.; Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity..
Protein Sequence	MRLAVICFCLFGIASSLPVKVTDSGSSEEKLYSLHPDPIATWLVPDPSQKQNLLAPQNAVSSEEKDDFKQETLPSNSNESHDHMDDDDDDDDDDGDHAESEDSVDSDESDESHHSDESDETVTASTQADTFTPIVPTVDVPNGRGDSLAYGLRSKSRSFQVSDEQYPDATDEDLTSHMKSGESKESLDVIPVAQLLSMPSDQDNNGKGSHESSQLDEPSLETHRLEHSKESQESADQSDVIDSQASSKASLEHQSHKFHSHKDKLVLDPKSKEDDRYLKFRISHELESSSSEVN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	SSLPVKVTDSGSSEE HCCCEEECCCCCCCH	20.80	27087446
24	Phosphorylation	LPVKVTDSGSSEEKL CCEEECCCCCCCHHH	31.07	27087446
26	Phosphorylation	VKVTDSGSSEEKLYS EEECCCCCCCHHHHH	38.23	27087446
27	Phosphorylation	KVTDSGSSEEKLYSL EECCCCCCCHHHHHC	53.99	27087446
32	Phosphorylation	GSSEEKLYSLHPDPI CCCCHHHHHCCCCCC	21.91	22668510
33	Phosphorylation	SSEEKLYSLHPDPIA CCCHHHHHCCCCCCE	30.55	22668510
61	Phosphorylation	LAPQNAVSSEEKDDF CCCCCCCCHHHCCCC	29.62	25521595
62	Phosphorylation	APQNAVSSEEKDDFK CCCCCCCHHHCCCCH	43.08	25521595
75	Phosphorylation	FKQETLPSNSNESHD CHHCCCCCCCCCCCC	56.88	17500062
77	Phosphorylation	QETLPSNSNESHDHM HCCCCCCCCCCCCCC	46.44	17500062
80	Phosphorylation	LPSNSNESHDHMDDD CCCCCCCCCCCCCCC	38.17	17500062
100	Phosphorylation	DDGDHAESEDSVDSD CCCCCCCCCCCCCCC	47.70	17500062
103	Phosphorylation	DHAESEDSVDSDESD CCCCCCCCCCCCCCC	24.63	17500062
106	Phosphorylation	ESEDSVDSDESDESH CCCCCCCCCCCCCCC	40.91	17500062
109	Phosphorylation	DSVDSDESDESHHSD CCCCCCCCCCCCCCC	52.23	17500062
112	Phosphorylation	DSDESDESHHSDESD CCCCCCCCCCCCCCC	31.33	17500062
115	Phosphorylation	ESDESHHSDESDETV CCCCCCCCCCCCCCE	37.34	17500062
118	Phosphorylation	ESHHSDESDETVTAS CCCCCCCCCCCEEHH	45.82	17500062
123	O-linked_Glycosylation	DESDETVTASTQADT CCCCCCEEHHCCCCC	23.47	-
132	O-linked_Glycosylation	STQADTFTPIVPTVD HCCCCCCCCEECEEC	17.75	-
137	O-linked_Glycosylation	TFTPIVPTVDVPNGR CCCCEECEECCCCCC	20.60	-
147	Phosphorylation	VPNGRGDSLAYGLRS CCCCCCCCHHHHHHC	20.09	21183079
154	Phosphorylation	SLAYGLRSKSRSFQV CHHHHHHCCCCEEEC	39.77	24899341
156	Phosphorylation	AYGLRSKSRSFQVSD HHHHHCCCCEEECCC	34.11	30635358
158	Phosphorylation	GLRSKSRSFQVSDEQ HHHCCCCEEECCCCC	27.41	26160508
162	Phosphorylation	KSRSFQVSDEQYPDA CCCEEECCCCCCCCC	25.33	27180971
166	Phosphorylation	FQVSDEQYPDATDED EECCCCCCCCCCCHH	10.88	27180971
170	Phosphorylation	DEQYPDATDEDLTSH CCCCCCCCCHHHHHH	47.50	27087446
175	Phosphorylation	DATDEDLTSHMKSGE CCCCHHHHHHHHCCC	28.98	27087446
176	Phosphorylation	ATDEDLTSHMKSGES CCCHHHHHHHHCCCC	28.96	30635358
180	Phosphorylation	DLTSHMKSGESKESL HHHHHHHCCCCHHHC	39.97	27087446
183	Phosphorylation	SHMKSGESKESLDVI HHHHCCCCHHHCCCC	45.29	27087446
186	Phosphorylation	KSGESKESLDVIPVA HCCCCHHHCCCCCHH	33.34	17500062
200	Phosphorylation	AQLLSMPSDQDNNGK HHHHCCCCCCCCCCC	38.98	-
209	Phosphorylation	QDNNGKGSHESSQLD CCCCCCCCCCCCCCC	27.80	25195567
212	Phosphorylation	NGKGSHESSQLDEPS CCCCCCCCCCCCCCC	20.26	25195567
213	Phosphorylation	GKGSHESSQLDEPSL CCCCCCCCCCCCCCH	31.60	29550500
219	Phosphorylation	SSQLDEPSLETHRLE CCCCCCCCHHHHHHH	36.47	17500062
222	Phosphorylation	LDEPSLETHRLEHSK CCCCCHHHHHHHHCH	20.00	29550500
228	Phosphorylation	ETHRLEHSKESQESA HHHHHHHCHHHHHCC	28.83	27087446
231	Phosphorylation	RLEHSKESQESADQS HHHHCHHHHHCCCHH	42.88	27087446
234	Phosphorylation	HSKESQESADQSDVI HCHHHHHCCCHHHHH	29.52	27087446
238	Phosphorylation	SQESADQSDVIDSQA HHHCCCHHHHHCHHH	34.10	25159016
243	Phosphorylation	DQSDVIDSQASSKAS CHHHHHCHHHHHHHH	19.27	23429704
247	Phosphorylation	VIDSQASSKASLEHQ HHCHHHHHHHHHHHH	34.94	25195567
250	Phosphorylation	SQASSKASLEHQSHK HHHHHHHHHHHHHHC	37.72	27087446
255	Phosphorylation	KASLEHQSHKFHSHK HHHHHHHHHCCCCCC	30.47	-
260	Phosphorylation	HQSHKFHSHKDKLVL HHHHCCCCCCCCEEE	35.05	-
271	Phosphorylation	KLVLDPKSKEDDRYL CEEECCCCCCCCHHH	46.82	26824392
283	Phosphorylation	RYLKFRISHELESSS HHHHHHHHHHHHCCC	13.47	27087446
288	Phosphorylation	RISHELESSSSEVN- HHHHHHHCCCCCCC-	48.41	27087446
289	Phosphorylation	ISHELESSSSEVN-- HHHHHHCCCCCCC--	28.62	27087446
290	Phosphorylation	SHELESSSSEVN--- HHHHHCCCCCCC---	39.53	27087446
291	Phosphorylation	HELESSSSEVN---- HHHHCCCCCCC----	47.73	27087446

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 OSTP_MOUSE !!

Functions of PTM Sites

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

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of OSTP_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-231 AND SER-234, ANDMASS SPECTROMETRY.	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-26; SER-27; SER-61;SER-62 AND SER-283, AND MASS SPECTROMETRY.	19367708 [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-283; SER-288 ANDSER-290, AND MASS SPECTROMETRY.	17242355 [Abstract]