dbPTM

STIM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STIM1_MOUSE
UniProt AC	P70302
Protein Name	Stromal interaction molecule 1
Gene Name	Stim1
Organism	Mus musculus (Mouse).
Sequence Length	685
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Endoplasmic reticulum membrane Single-pass type I membrane protein . Sarcoplasmic reticulum . Cytoplasm, cytoskeleton . Translocates from the endoplasmic reticulum to the cell membrane in respon
Protein Description	Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit ORAI1. Involved in enamel formation. Activated following interaction with STIMATE, leading to promote STIM1 conformational switch..
Protein Sequence	MDVCARLALWLLWGLLLHQGQSLSHSHSEKNTGASSGATSEESTEAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVIQWLITYVELPQYEETFRKLQLTGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAERQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQLGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMGRAADEALNAMPSNGSHRLIEGVHPGSLVEKLPDSPALAKKTFMALNHGLDKAHSLMELNPSVPPGGSPLLDSSHSLSPSSPDPDTPSPVGDNRALQGSRNTRIPHLAGKKAMAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	HSHSEKNTGASSGAT CCCCCCCCCCCCCCC	45.23	30635358
35	Phosphorylation	SEKNTGASSGATSEE CCCCCCCCCCCCCCC	30.56	23684622
36	Phosphorylation	EKNTGASSGATSEES CCCCCCCCCCCCCCC	31.73	23984901
39	Phosphorylation	TGASSGATSEESTEA CCCCCCCCCCCCCHH	39.95	21743459
40	Phosphorylation	GASSGATSEESTEAE CCCCCCCCCCCCHHH	38.54	25521595
43	Phosphorylation	SGATSEESTEAEFCR CCCCCCCCCHHHEEC	27.74	23984901
44	Phosphorylation	GATSEESTEAEFCRI CCCCCCCCHHHEECC	42.36	23984901
131	N-linked_Glycosylation	WKSSEVYNWTVDEVI HHCCCCCCCCHHHHH	32.87	-
170	O-linked_Glycosylation	AMPRLAVTNTTMTGT CCCEEEEECCCCCEE	22.65	30059200
171	N-linked_Glycosylation	MPRLAVTNTTMTGTV CCEEEEECCCCCEEE	27.27	-
172	O-linked_Glycosylation	PRLAVTNTTMTGTVL CEEEEECCCCCEEEE	14.47	30059200
175	Phosphorylation	AVTNTTMTGTVLKMT EEECCCCCEEEEECC	27.84	-
257	Phosphorylation	GLHRAEQSLHDLQER HHHHHHHHHHHHHHH	21.12	25521595
312	Phosphorylation	EGTENERSRQKYAEE HCCCCHHHHHHHHHH	32.65	29899451
333	Ubiquitination	EALRKAEKELESHSS HHHHHHHHHHHHCCC	72.89	22790023
340	Phosphorylation	KELESHSSWYAPEAL HHHHHCCCCCCHHHH	20.77	25338131
361	Phosphorylation	THEVEVQYYNIKKQN HHHEEEEEEECCCCH	12.03	-
401	Phosphorylation	FHVAHSSSLDDVDHK EEECCCCCCHHCCHH	38.54	28542873
413	Ubiquitination	DHKILTAKQALSEVT CHHHHHHHHHHHHHH	30.76	22790023
413	Acetylation	DHKILTAKQALSEVT CHHHHHHHHHHHHHH	30.76	8275687
504	Phosphorylation	SSVRQRLTEPQLGLG HHHHHHHCCCCCCCC	48.05	22942356
512	Phosphorylation	EPQLGLGSQRDLTHS CCCCCCCCCCCCCCC	27.38	25521595
514	Methylation	QLGLGSQRDLTHSDS CCCCCCCCCCCCCCC	42.47	58859731
517	Phosphorylation	LGSQRDLTHSDSESS CCCCCCCCCCCCCCC	24.51	27742792
519	Phosphorylation	SQRDLTHSDSESSLH CCCCCCCCCCCCCCC	37.28	27087446
521	Phosphorylation	RDLTHSDSESSLHMS CCCCCCCCCCCCCCC	42.25	26824392
523	Phosphorylation	LTHSDSESSLHMSDR CCCCCCCCCCCCCCC	42.00	27742792
524	Phosphorylation	THSDSESSLHMSDRQ CCCCCCCCCCCCCCC	20.45	27742792
528	Phosphorylation	SESSLHMSDRQRVAP CCCCCCCCCCCCCCC	20.92	27742792
567	Phosphorylation	IEGVHPGSLVEKLPD EECCCCCCHHHHCCC	33.42	28542873
575	Phosphorylation	LVEKLPDSPALAKKT HHHHCCCCHHHHHHH	15.33	27087446
595	Phosphorylation	HGLDKAHSLMELNPS CCHHHHHHHHHHCCC	33.98	22817900
602	Phosphorylation	SLMELNPSVPPGGSP HHHHHCCCCCCCCCC	46.30	23984901
608	Phosphorylation	PSVPPGGSPLLDSSH CCCCCCCCCCCCCCC	20.49	23984901
613	Phosphorylation	GGSPLLDSSHSLSPS CCCCCCCCCCCCCCC	29.89	25293948
614	Phosphorylation	GSPLLDSSHSLSPSS CCCCCCCCCCCCCCC	19.43	25293948
616	Phosphorylation	PLLDSSHSLSPSSPD CCCCCCCCCCCCCCC	32.27	25293948
618	Phosphorylation	LDSSHSLSPSSPDPD CCCCCCCCCCCCCCC	26.25	25293948
620	Phosphorylation	SSHSLSPSSPDPDTP CCCCCCCCCCCCCCC	51.64	25293948
621	O-linked_Glycosylation	SHSLSPSSPDPDTPS CCCCCCCCCCCCCCC	36.38	30059200
621	Phosphorylation	SHSLSPSSPDPDTPS CCCCCCCCCCCCCCC	36.38	25293948
626	O-linked_Glycosylation	PSSPDPDTPSPVGDN CCCCCCCCCCCCCCC	30.93	30059200
628	Phosphorylation	SPDPDTPSPVGDNRA CCCCCCCCCCCCCCC	34.02	-
639	Phosphorylation	DNRALQGSRNTRIPH CCCCCCCCCCCCCCC	14.92	30635358
642	Phosphorylation	ALQGSRNTRIPHLAG CCCCCCCCCCCCHHC	28.94	30635358
660	Phosphorylation	MAEEDNGSIGEETDS HCCCCCCCCCCCCCC	33.40	25521595
665	Phosphorylation	NGSIGEETDSSPGRK CCCCCCCCCCCCCCC	36.56	27087446
667	Phosphorylation	SIGEETDSSPGRKKF CCCCCCCCCCCCCCC	45.94	25521595
668	Phosphorylation	IGEETDSSPGRKKFP CCCCCCCCCCCCCCC	33.90	25521595

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
257	S	Phosphorylation	Kinase	AMPKB1	Q9R078	PSP
521	S	Phosphorylation	Kinase	AMPKB1	Q9R078	PSP
575	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
575	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
608	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
608	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
621	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
621	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STIM1_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 STIM1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of STIM1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of STIM1_MOUSE

Related Literatures of Post-Translational Modification

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-257 AND SER-519, ANDMASS 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-519 AND SER-524, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASSSPECTROMETRY.	17208939 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-665 AND SER-668, ANDMASS SPECTROMETRY.	17203969 [Abstract]