STIM1_HUMAN - dbPTM
STIM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STIM1_HUMAN
UniProt AC Q13586
Protein Name Stromal interaction molecule 1
Gene Name STIM1
Organism Homo sapiens (Human).
Sequence Length 685
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Endoplasmic reticulum membrane
Single-pass type I membrane protein . Cytoplasm, cytoskeleton . Sarcoplasmic reticulum . Translocates from the endoplasmic reticulum to the cell membrane in response
Protein Description Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. [PubMed: 15866891]
Protein Sequence MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMSRAADEALNAMTSNGSHRLIEGVHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSPSAPPGGSPHLDSSRSHSPSSPDPDTPSPVGDSRALQASRNTRIPHLAGKKAVAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
34O-linked_GlycosylationHSEKATGTSSGANSE
CCCCCCCCCCCCCCC		18.50OGP
35O-linked_GlycosylationSEKATGTSSGANSEE
CCCCCCCCCCCCCCC		28.28OGP
40PhosphorylationGTSSGANSEESTAAE
CCCCCCCCCCCHHHH		42.0528857561
44O-linked_GlycosylationGANSEESTAAEFCRI
CCCCCCCHHHHHHCC		32.92OGP
53AcetylationAEFCRIDKPLCHSED
HHHHCCCCCCCCCCC		37.2026822725
56GlutathionylationCRIDKPLCHSEDEKL
HCCCCCCCCCCCCCC		4.5022833525
126PhosphorylationDLWKAWKSSEVYNWT
HHHHHHHCCCCCCCC		22.4924043423
127PhosphorylationLWKAWKSSEVYNWTV
HHHHHHCCCCCCCCH		27.6224043423
130PhosphorylationAWKSSEVYNWTVDEV
HHHCCCCCCCCHHHH		10.8424043423
131N-linked_GlycosylationWKSSEVYNWTVDEVV
HHCCCCCCCCHHHHH		32.8711983428
131N-linked_GlycosylationWKSSEVYNWTVDEVV
HHCCCCCCCCHHHHH		32.8711983428
133PhosphorylationSSEVYNWTVDEVVQW
CCCCCCCCHHHHHHH		17.9124043423
143PhosphorylationEVVQWLITYVELPQY
HHHHHHHHHHCCHHH		21.2424043423
144PhosphorylationVVQWLITYVELPQYE
HHHHHHHHHCCHHHH		5.7324043423
150PhosphorylationTYVELPQYEETFRKL
HHHCCHHHHHHHHHH		17.5024043423
153PhosphorylationELPQYEETFRKLQLS
CCHHHHHHHHHHHHC		19.4624043423
156UbiquitinationQYEETFRKLQLSGHA
HHHHHHHHHHHCCCC		36.07-
170O-linked_GlycosylationAMPRLAVTNTTMTGT
CCCEEEEECCCCCEE		22.6530059200
171N-linked_GlycosylationMPRLAVTNTTMTGTV
CCEEEEECCCCCEEE		27.278707854
171N-linked_GlycosylationMPRLAVTNTTMTGTV
CCEEEEECCCCCEEE		27.278707854
175PhosphorylationAVTNTTMTGTVLKMT
EEECCCCCEEEEECC		27.8426552605
177PhosphorylationTNTTMTGTVLKMTDR
ECCCCCEEEEECCCC		17.3126552605
182PhosphorylationTGTVLKMTDRSHRQK
CEEEEECCCCHHHHH		27.0326552605
185PhosphorylationVLKMTDRSHRQKLQL
EEECCCCHHHHHHHH		26.3226552605
236PhosphorylationFAYIQNRYSKEHMKK
HHHHHHHCCHHHHHH		31.48-
246UbiquitinationEHMKKMMKDLEGLHR
HHHHHHHHHHHHHHH		56.51-
246MalonylationEHMKKMMKDLEGLHR
HHHHHHHHHHHHHHH		56.5126320211
257PhosphorylationGLHRAEQSLHDLQER
HHHHHHHHHHHHHHH		21.1229255136
267UbiquitinationDLQERLHKAQEEHRT
HHHHHHHHHHHHHCC		57.2521906983
2792-HydroxyisobutyrylationHRTVEVEKVHLEKKL
HCCEEEEHHHHHHHH		39.88-
279UbiquitinationHRTVEVEKVHLEKKL
HCCEEEEHHHHHHHH		39.88-
285UbiquitinationEKVHLEKKLRDEINL
EHHHHHHHHHHHHHH		39.10-
294UbiquitinationRDEINLAKQEAQRLK
HHHHHHHHHHHHHHH		52.41-
315UbiquitinationENERSRQKYAEEELE
CCHHHHHHHHHHHHH		45.37-
330UbiquitinationQVREALRKAEKELES
HHHHHHHHHHHHHHH		62.84-
333UbiquitinationEALRKAEKELESHSS
HHHHHHHHHHHHCCC		72.89-
337PhosphorylationKAEKELESHSSWYAP
HHHHHHHHCCCCCCH		41.0923403867
339PhosphorylationEKELESHSSWYAPEA
HHHHHHCCCCCCHHH		31.6723403867
340PhosphorylationKELESHSSWYAPEAL
HHHHHCCCCCCHHHH		20.7723403867
342PhosphorylationLESHSSWYAPEALQK
HHHCCCCCCHHHHHH		17.7723403867
361PhosphorylationTHEVEVQYYNIKKQN
HHHHEEEEEECCCCC		12.03-
371UbiquitinationIKKQNAEKQLLVAKE
CCCCCHHHEEEHHHH		43.78-
377UbiquitinationEKQLLVAKEGAEKIK
HHEEEHHHHHHHHHH		49.56-
377AcetylationEKQLLVAKEGAEKIK
HHEEEHHHHHHHHHH		49.5625953088
389PhosphorylationKIKKKRNTLFGTFHV
HHHHHHCCCEEEEEE		27.7427251275
393PhosphorylationKRNTLFGTFHVAHSS
HHCCCEEEEEECCCC		11.8430108239
399PhosphorylationGTFHVAHSSSLDDVD
EEEEECCCCCCHHCC		16.3430108239
400PhosphorylationTFHVAHSSSLDDVDH
EEEECCCCCCHHCCH		25.6730108239
401PhosphorylationFHVAHSSSLDDVDHK
EEECCCCCCHHCCHH		38.5430108239
413UbiquitinationDHKILTAKQALSEVT
CHHHHHHHHHHHHHH		30.762190698
420PhosphorylationKQALSEVTAALRERL
HHHHHHHHHHHHHHH		11.3622817900
486PhosphorylationDMDEEIVSPLSMQSP
CCCHHHCCCHHCCCH		26.2822817900
492PhosphorylationVSPLSMQSPSLQSSV
CCCHHCCCHHHHHHH		14.0722817900
498PhosphorylationQSPSLQSSVRQRLTE
CCHHHHHHHHHHHCC		14.3624275569
504PhosphorylationSSVRQRLTEPQHGLG
HHHHHHHCCCCCCCC		48.0524702127
512PhosphorylationEPQHGLGSQRDLTHS
CCCCCCCCCCCCCCC		27.3823401153
517PhosphorylationLGSQRDLTHSDSESS
CCCCCCCCCCCCCCC		24.5129255136
519PhosphorylationSQRDLTHSDSESSLH
CCCCCCCCCCCCCCC		37.2829255136
521PhosphorylationRDLTHSDSESSLHMS
CCCCCCCCCCCCCCC		42.2529255136
523PhosphorylationLTHSDSESSLHMSDR
CCCCCCCCCCCCCCC		42.0029255136
524PhosphorylationTHSDSESSLHMSDRQ
CCCCCCCCCCCCCCC		20.4529255136
527SulfoxidationDSESSLHMSDRQRVA
CCCCCCCCCCCCCCC		5.5921406390
528PhosphorylationSESSLHMSDRQRVAP
CCCCCCCCCCCCCCC		20.9223401153
541PhosphorylationAPKPPQMSRAADEAL
CCCCCCHHHHHHHHH		17.3326437602
551SulfoxidationADEALNAMTSNGSHR
HHHHHHHHCCCCCCC		4.0321406390
553PhosphorylationEALNAMTSNGSHRLI
HHHHHHCCCCCCCCE		26.5519881501
556PhosphorylationNAMTSNGSHRLIEGV
HHHCCCCCCCCEECC		15.08-
567PhosphorylationIEGVHPGSLVEKLPD
EECCCCCCHHHHCCC		33.4223927012
575PhosphorylationLVEKLPDSPALAKKA
HHHHCCCCHHHHHHH		15.3319664994
580AcetylationPDSPALAKKALLALN
CCCHHHHHHHHHHHH		39.1525953088
581UbiquitinationDSPALAKKALLALNH
CCHHHHHHHHHHHHC		38.36-
595PhosphorylationHGLDKAHSLMELSPS
CCHHHHHHHHHHCCC		33.9823401153
600PhosphorylationAHSLMELSPSAPPGG
HHHHHHHCCCCCCCC		11.9630266825
602PhosphorylationSLMELSPSAPPGGSP
HHHHHCCCCCCCCCC		50.4630266825
608PhosphorylationPSAPPGGSPHLDSSR
CCCCCCCCCCCCCCC		18.3029255136
613PhosphorylationGGSPHLDSSRSHSPS
CCCCCCCCCCCCCCC		33.7330266825
614PhosphorylationGSPHLDSSRSHSPSS
CCCCCCCCCCCCCCC		37.1530266825
616PhosphorylationPHLDSSRSHSPSSPD
CCCCCCCCCCCCCCC		30.2029255136
618PhosphorylationLDSSRSHSPSSPDPD
CCCCCCCCCCCCCCC		27.9429255136
620PhosphorylationSSRSHSPSSPDPDTP
CCCCCCCCCCCCCCC		58.4829255136
621PhosphorylationSRSHSPSSPDPDTPS
CCCCCCCCCCCCCCC		36.3822167270
626PhosphorylationPSSPDPDTPSPVGDS
CCCCCCCCCCCCCCH		30.9323927012
628PhosphorylationSPDPDTPSPVGDSRA
CCCCCCCCCCCCHHH		34.0223927012
633PhosphorylationTPSPVGDSRALQASR
CCCCCCCHHHHHHHC		17.3323927012
650AcetylationRIPHLAGKKAVAEED
CCCHHHCCCCEEECC		31.7725953088
660PhosphorylationVAEEDNGSIGEETDS
EEECCCCCCCCCCCC		33.4029255136
665PhosphorylationNGSIGEETDSSPGRK
CCCCCCCCCCCCCCC		36.5629255136
667PhosphorylationSIGEETDSSPGRKKF
CCCCCCCCCCCCCCC		45.9429255136
668PhosphorylationIGEETDSSPGRKKFP
CCCCCCCCCCCCCCC		33.9029255136
677UbiquitinationGRKKFPLKIFKKPLK
CCCCCCCCCCCCCCC		46.46-
680AcetylationKFPLKIFKKPLKK--
CCCCCCCCCCCCC--		57.8870559
681AcetylationFPLKIFKKPLKK---
CCCCCCCCCCCC---		44.857354891
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
257SPhosphorylationKinaseAMPKB1Q9Y478
PSP
257SPhosphorylationKinaseAMPKG2Q9UGJ0
PSP
257SPhosphorylationKinaseAMPKA1Q13131
PSP
361YPhosphorylationKinasePYK2Q14289
PSP
389TPhosphorylationKinasePKACAP17612
PSP
521SPhosphorylationKinaseAMPKB1Q9Y478
PSP
521SPhosphorylationKinaseAMPKG2Q9UGJ0
PSP
521SPhosphorylationKinaseAMPKA1Q13131
PSP
575SPhosphorylationKinaseMAPK1P28482
GPS
608SPhosphorylationKinaseMAPK1P28482
GPS
621SPhosphorylationKinaseMAPK1P28482
GPS
668SPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseXP03165
PMID:32235678
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STIM1_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 STIM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STIM2_HUMANSTIM2physical
11463338
MARE1_HUMANMAPRE1physical
23698468
EXOC5_HUMANEXOC5physical
27173435
Drug and Disease Associations
Kegg Disease
OMIM Disease
612783Immunodeficiency 10 (IMD10)
160565Myopathy, tubular aggregate, 1 (TAM1)
185070Stormorken syndrome (STRMK)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STIM1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171, AND MASSSPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-171.
"Stromal interaction molecule 1 (STIM1), a transmembrane protein withgrowth suppressor activity, contains an extracellular SAM domainmodified by N-linked glycosylation.";
Williams R.T., Senior P.V., van Stekelenburg L., Layton J.E.,Smith P.J., Dziadek M.A.;
Biochim. Biophys. Acta 1596:131-137(2002).
Cited for: SUBUNIT, AND GLYCOSYLATION AT ASN-131 AND ASN-171.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-660; THR-665AND SER-668, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-608; SER-660AND SER-668, AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND SER-608, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-420, AND MASSSPECTROMETRY.

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