STIM2_HUMAN - dbPTM
STIM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STIM2_HUMAN
UniProt AC Q9P246
Protein Name Stromal interaction molecule 2
Gene Name STIM2
Organism Homo sapiens (Human).
Sequence Length 746
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein . Dynamically translocates from a uniform endoplasmic reticulum distribution to punctual endoplasmic reticulum-plasma membrane junctions in response to decrease in endoplasmic retic
Protein Description Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx..
Protein Sequence MLVLGLLVAGAADGCELVPRHLRGRRATGSAATAASSPAAAAGDSPALMTDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVEESDEFIREDMKYKDATNKHSHLHREDKHITIEDLWKRWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHEPSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTVSIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRNVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVSQFPGTMAKPPGSLARSSSLCRSRRSIVPSSPQPQRAQLAPHAPHPSHPRHPHHPQHTPHSLPSPDPDILSVSSCPALYRNEEEEEAIYFSAEKQWEVPDTASECDSLNSSIGRKQSPPLSLEIYQTLSPRKISRDEVSLEDSSRGDSPVTVDVSWGSPDCVGLTETKSMIFSPASKVYNGILEKSCSMNQLSSGIPVPKPRHTSCSSAGNDSKPVQEAPSVARISSIPHDLCHNGEKSKKPSKIKSLFKKKSK
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
24 (in isoform 2)Phosphorylation-29.7730257219
28PhosphorylationHLRGRRATGSAATAA
HHCCCCCCCCCHHHH
29.8328122231
30PhosphorylationRGRRATGSAATAASS
CCCCCCCCCHHHHCC
15.4628122231
33PhosphorylationRATGSAATAASSPAA
CCCCCCHHHHCCHHH
23.6028122231
36PhosphorylationGSAATAASSPAAAAG
CCCHHHHCCHHHHCC
34.1028122231
37PhosphorylationSAATAASSPAAAAGD
CCHHHHCCHHHHCCC
17.5228122231
45PhosphorylationPAAAAGDSPALMTDP
HHHHCCCCCCCCCCC
15.9128122231
50PhosphorylationGDSPALMTDPCMSLS
CCCCCCCCCCCCCCC
37.3328122231
55O-linked_GlycosylationLMTDPCMSLSPPCFT
CCCCCCCCCCCCCCC
32.20OGP
55PhosphorylationLMTDPCMSLSPPCFT
CCCCCCCCCCCCCCC
32.2028122231
57PhosphorylationTDPCMSLSPPCFTEE
CCCCCCCCCCCCCHH
21.3528122231
62PhosphorylationSLSPPCFTEEDRFSL
CCCCCCCCHHHHCCH
45.2228122231
135N-linked_GlycosylationWKTSEVHNWTLEDTL
HHCCCCCCCCHHHHH
38.31UniProtKB CARBOHYD
164UbiquitinationNFRDNNVKGTTLPRI
HCCCCCCCCCCCCEE
53.30-
181PhosphorylationHEPSFMISQLKISDR
CCCCCEEEEECCCCC
20.0624719451
254PhosphorylationKMMKDLESLQTAEQS
HHHHHHHHHHHHHHH
32.8329083192
257PhosphorylationKDLESLQTAEQSLMD
HHHHHHHHHHHHHHH
37.1429083192
261PhosphorylationSLQTAEQSLMDLQER
HHHHHHHHHHHHHHH
19.7126657352
283UbiquitinationNRNVAVEKQNLERKM
HHHHHHHHHHHHHHH
37.582190698
289UbiquitinationEKQNLERKMMDEINY
HHHHHHHHHHHHHHH
29.24-
320PhosphorylationCELSRRQYAEQELEQ
CCHHHHHHHHHHHHH
15.4220736484
343PhosphorylationEKEFELRSSWSVPDA
HHHHHHCCCCCCCHH
49.1028857561
344PhosphorylationKEFELRSSWSVPDAL
HHHHHCCCCCCCHHH
19.5528857561
346PhosphorylationFELRSSWSVPDALQK
HHHCCCCCCCHHHHH
26.2230576142
370UbiquitinationVQYYNIKRQNAEMQL
EEEEEHHHCCHHHHH
31.0521906983
370UbiquitinationVQYYNIKRQNAEMQL
EEEEEHHHCCHHHHH
31.0521906983
392PhosphorylationEKIKKKRSTVFGTLH
HHHHHHHCHHHHHHH
37.4929449344
393PhosphorylationKIKKKRSTVFGTLHV
HHHHHHCHHHHHHHH
24.7229449344
397PhosphorylationKRSTVFGTLHVAHSS
HHCHHHHHHHHHCCC
11.3929449344
453PhosphorylationAHNSGLPSLTSSLYS
HCCCCCCCHHCHHCC
49.6928348404
455PhosphorylationNSGLPSLTSSLYSDH
CCCCCCHHCHHCCCC
22.1728348404
456PhosphorylationSGLPSLTSSLYSDHS
CCCCCHHCHHCCCCC
24.5228348404
457PhosphorylationGLPSLTSSLYSDHSW
CCCCHHCHHCCCCCE
26.5428348404
460PhosphorylationSLTSSLYSDHSWVVM
CHHCHHCCCCCEEEE
33.8528348404
463PhosphorylationSSLYSDHSWVVMPRV
CHHCCCCCEEEEECC
26.9324719451
471PhosphorylationWVVMPRVSIPPYPIA
EEEEECCCCCCCCCC
30.5624719451
518PhosphorylationSLCRSRRSIVPSSPQ
HHHHCCCCCCCCCCC
27.1630266825
522PhosphorylationSRRSIVPSSPQPQRA
CCCCCCCCCCCCCHH
43.7030266825
523PhosphorylationRRSIVPSSPQPQRAQ
CCCCCCCCCCCCHHC
22.8329255136
526PhosphorylationIVPSSPQPQRAQLAP
CCCCCCCCCHHCCCC
29.0724719451
530PhosphorylationSPQPQRAQLAPHAPH
CCCCCHHCCCCCCCC
40.1024719451
531PhosphorylationPQPQRAQLAPHAPHP
CCCCHHCCCCCCCCC
8.5924719451
539PhosphorylationAPHAPHPSHPRHPHH
CCCCCCCCCCCCCCC
42.9923312004
556PhosphorylationHTPHSLPSPDPDILS
CCCCCCCCCCCCCEE
47.4226657352
563PhosphorylationSPDPDILSVSSCPAL
CCCCCCEECCCCCCE
21.9326657352
566PhosphorylationPDILSVSSCPALYRN
CCCEECCCCCCEECC
23.20-
581PhosphorylationEEEEEAIYFSAEKQW
HHHHHHEEEECCCCC
9.8728796482
583PhosphorylationEEEAIYFSAEKQWEV
HHHHEEEECCCCCCC
20.6728796482
593PhosphorylationKQWEVPDTASECDSL
CCCCCCCCHHHHHHC
26.4723403867
595PhosphorylationWEVPDTASECDSLNS
CCCCCCHHHHHHCCC
40.6323403867
599PhosphorylationDTASECDSLNSSIGR
CCHHHHHHCCCCCCC
40.9023403867
602PhosphorylationSECDSLNSSIGRKQS
HHHHHCCCCCCCCCC
28.7325159151
603PhosphorylationECDSLNSSIGRKQSP
HHHHCCCCCCCCCCC
28.1723927012
609PhosphorylationSSIGRKQSPPLSLEI
CCCCCCCCCCCEEEE
31.3630266825
610PhosphorylationSIGRKQSPPLSLEIY
CCCCCCCCCCEEEEE
31.2124719451
611PhosphorylationIGRKQSPPLSLEIYQ
CCCCCCCCCEEEEEE
39.5727251275
613PhosphorylationRKQSPPLSLEIYQTL
CCCCCCCEEEEEECC
29.7230266825
617PhosphorylationPPLSLEIYQTLSPRK
CCCEEEEEECCCCCC
6.0030266825
619PhosphorylationLSLEIYQTLSPRKIS
CEEEEEECCCCCCCC
16.5425159151
621PhosphorylationLEIYQTLSPRKISRD
EEEEECCCCCCCCCC
26.5025159151
626PhosphorylationTLSPRKISRDEVSLE
CCCCCCCCCCCCCCC
36.3923401153
627PhosphorylationLSPRKISRDEVSLED
CCCCCCCCCCCCCCC
47.8127251275
629PhosphorylationPRKISRDEVSLEDSS
CCCCCCCCCCCCCCC
32.6624719451
631PhosphorylationKISRDEVSLEDSSRG
CCCCCCCCCCCCCCC
24.8029255136
634PhosphorylationRDEVSLEDSSRGDSP
CCCCCCCCCCCCCCC
58.1524719451
635PhosphorylationDEVSLEDSSRGDSPV
CCCCCCCCCCCCCCE
16.7421815630
636PhosphorylationEVSLEDSSRGDSPVT
CCCCCCCCCCCCCEE
53.2423927012
639PhosphorylationLEDSSRGDSPVTVDV
CCCCCCCCCCEEEEE
48.9724719451
640PhosphorylationEDSSRGDSPVTVDVS
CCCCCCCCCEEEEEC
24.8825159151
643PhosphorylationSRGDSPVTVDVSWGS
CCCCCCEEEEECCCC
17.8627732954
650PhosphorylationTVDVSWGSPDCVGLT
EEEECCCCCCCCCCC
16.00-
659PhosphorylationDCVGLTETKSMIFSP
CCCCCCCCCCCCCCH
24.1626074081
661PhosphorylationVGLTETKSMIFSPAS
CCCCCCCCCCCCHHH
25.2423401153
665PhosphorylationETKSMIFSPASKVYN
CCCCCCCCHHHHHHH
14.5030266825
668PhosphorylationSMIFSPASKVYNGIL
CCCCCHHHHHHHHHH
26.4923403867
669PhosphorylationMIFSPASKVYNGILE
CCCCHHHHHHHHHHH
51.3427251275
671PhosphorylationFSPASKVYNGILEKS
CCHHHHHHHHHHHHC
16.0626074081
678PhosphorylationYNGILEKSCSMNQLS
HHHHHHHCCCHHHHC
11.3123927012
680PhosphorylationGILEKSCSMNQLSSG
HHHHHCCCHHHHCCC
28.0525159151
685PhosphorylationSCSMNQLSSGIPVPK
CCCHHHHCCCCCCCC
19.4323927012
686PhosphorylationCSMNQLSSGIPVPKP
CCHHHHCCCCCCCCC
49.7023927012
688PhosphorylationMNQLSSGIPVPKPRH
HHHHCCCCCCCCCCC
3.1624719451
696PhosphorylationPVPKPRHTSCSSAGN
CCCCCCCCCCCCCCC
32.4822617229
697PhosphorylationVPKPRHTSCSSAGND
CCCCCCCCCCCCCCC
13.0823401153
699PhosphorylationKPRHTSCSSAGNDSK
CCCCCCCCCCCCCCC
24.0025159151
700PhosphorylationPRHTSCSSAGNDSKP
CCCCCCCCCCCCCCC
44.5223911959
704PhosphorylationSCSSAGNDSKPVQEA
CCCCCCCCCCCCCCC
58.0624719451
705PhosphorylationCSSAGNDSKPVQEAP
CCCCCCCCCCCCCCC
42.7423663014
707PhosphorylationSAGNDSKPVQEAPSV
CCCCCCCCCCCCCCE
36.6624719451
708PhosphorylationAGNDSKPVQEAPSVA
CCCCCCCCCCCCCEE
10.3727251275
713PhosphorylationKPVQEAPSVARISSI
CCCCCCCCEEEHHHC
35.1426552605
718PhosphorylationAPSVARISSIPHDLC
CCCEEEHHHCCCHHC
19.3623401153
719PhosphorylationPSVARISSIPHDLCH
CCEEEHHHCCCHHCC
37.4523401153
726PhosphorylationSIPHDLCHNGEKSKK
HCCCHHCCCCCCCCC
53.2624719451
739PhosphorylationKKPSKIKSLFKKKSK
CCHHHHHHHHHHCCC
42.3824719451
742MethylationSKIKSLFKKKSK---
HHHHHHHHHCCC---
65.66-
747PhosphorylationLFKKKSK--------
HHHHCCC--------
24719451

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 STIM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STIM2_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 STIM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STIM1_HUMANSTIM1physical
11463338
STIM1_HUMANSTIM1physical
28514442
BRNP3_HUMANBRINP3physical
28514442
AAPK1_HUMANPRKAA1physical
28514442
AAKG2_HUMANPRKAG2physical
28514442
AAKG1_HUMANPRKAG1physical
28514442
AAKB1_HUMANPRKAB1physical
28514442
AAKB2_HUMANPRKAB2physical
28514442
AAPK2_HUMANPRKAA2physical
28514442
MSRB3_HUMANMSRB3physical
28514442
SUMF1_HUMANSUMF1physical
28514442
CISD2_HUMANCISD2physical
28514442
TMLH_HUMANTMLHEphysical
28514442
HMOX1_HUMANHMOX1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STIM2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-609; SER-621; SER-661AND SER-680, AND MASS SPECTROMETRY.

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