SRCA_MOUSE - dbPTM
SRCA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRCA_MOUSE
UniProt AC Q7TQ48
Protein Name Sarcalumenin
Gene Name Srl
Organism Mus musculus (Mouse).
Sequence Length 910
Subcellular Localization Sarcoplasmic reticulum lumen. Associated through calcium with the membrane..
Protein Description May be involved in the regulation of calcium transport..
Protein Sequence MKALLLLCCFLASLLLSGQAELQVSASGGTEDVGNLLENHFSAGDASLEEKERALYADAAPGDKNLLLHYPDGREAESLEQTPAGAPSTANGQGSETEASLSNTSAAESAPPGDVEGPGEEEEGPHAAGTLPPGGIEGPEEERPQFSSGKEPGQEEAGVGVPTEGAASMEAEVQEGSSGVPEELQGLLGDGPMNEAAGTAESVVTQSSPPIEGKEAEGEGNTGSDHQSTELDGTQDAIPAGDESEAREGAEDKPQDYSLQSEDTATPGPDHQPTDLHAASDTASSGVEAEEGAEESKAEVDTESGEKVEDQGEPRPSLDAGSAIEANKQSEYTQARETENDSPEGQVSGMSEEGLAEASSEEEGGEEDGSENGEVPFKEESGEDSGDGASSEEEGSTPGEAGEPQKTPGATGHEEEGPQLDVEDLNTGFEGSKTQDIEAEASEERQQERGNPVIAQWEEVEDASEEAPLRDRSHIDKTLMLNEDKPADDYSAVLQRLRKIYHTSIKPLEQSYKYNELRQHEITDGEITSKPMVLFLGPWSVGKSTMINYLLGLEDTRYQLYTGAEPTTSEFTVLMHGPKLKTIEGIVMAADSARSFSPLEKFGQNFLEKLIGIEVPHKLLERVTFVDTPGIIENRKQQERGYPFNDVCQWFIDRADLIFVVFDPTKLDVGLELEMLFRQLKGRESQIRIILNKADNLATQMLMRVYGALFWSLAPLINVTEPPRVYVSSFWPQDYKPDTHRELFLKEEISLLEDLNQVIENRLENKIAFIRQHAIRVRIHALLVDRYLQTYKDKMTFFSDGELVFKDIVEDPDKFYIFKTILAKTNVSKFDLPNREAYKDFFGINPISNFKLLSQQCSYMGGCFLEKIERAITQELPSLLGSIGLGKNPGAPNCDKTGCGETPKNRYKKH
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
47PhosphorylationHFSAGDASLEEKERA
CCCCCCCCHHHHHHH
40.8421082442
56PhosphorylationEEKERALYADAAPGD
HHHHHHHHHCCCCCC
11.0528464351
64UbiquitinationADAAPGDKNLLLHYP
HCCCCCCCCEEEECC
56.2422790023
70PhosphorylationDKNLLLHYPDGREAE
CCCEEEECCCCHHCC
11.7328464351
103 (in isoform 1)N-linked_Glycosylation-43.26-
222PhosphorylationEAEGEGNTGSDHQST
CCCCCCCCCCCCCCC
49.2522210690
224PhosphorylationEGEGNTGSDHQSTEL
CCCCCCCCCCCCCCC
29.8522210690
228PhosphorylationNTGSDHQSTELDGTQ
CCCCCCCCCCCCCCC
22.0419060867
229PhosphorylationTGSDHQSTELDGTQD
CCCCCCCCCCCCCCC
33.7217242355
234PhosphorylationQSTELDGTQDAIPAG
CCCCCCCCCCCCCCC
23.9622210690
244PhosphorylationAIPAGDESEAREGAE
CCCCCCHHHHHCCCC
41.1022210690
257PhosphorylationAEDKPQDYSLQSEDT
CCCCCCCCCCCCCCC
13.16-
258PhosphorylationEDKPQDYSLQSEDTA
CCCCCCCCCCCCCCC
28.37-
280N-linked_GlycosylationPTDLHAASDTASSGV
CCCCCCCCCCHHCCC
35.96-
302PhosphorylationESKAEVDTESGEKVE
HHCCEECCCCCCCCC
36.9127742792
304 (in isoform 1)Phosphorylation-55.1121183079
304PhosphorylationKAEVDTESGEKVEDQ
CCEECCCCCCCCCCC
55.1125521595
317PhosphorylationDQGEPRPSLDAGSAI
CCCCCCCCCCHHHHH
39.9127742792
322PhosphorylationRPSLDAGSAIEANKQ
CCCCCHHHHHHHHHH
28.0027742792
333PhosphorylationANKQSEYTQARETEN
HHHHCCCCCCHHCCC
16.2328542873
381PhosphorylationEVPFKEESGEDSGDG
CCCCCCCCCCCCCCC
48.8823737553
385PhosphorylationKEESGEDSGDGASSE
CCCCCCCCCCCCCCC
34.1923737553
388N-linked_GlycosylationSGEDSGDGASSEEEG
CCCCCCCCCCCCCCC
30.77-
390PhosphorylationEDSGDGASSEEEGST
CCCCCCCCCCCCCCC
43.7623737553
391PhosphorylationDSGDGASSEEEGSTP
CCCCCCCCCCCCCCC
48.7923737553
396PhosphorylationASSEEEGSTPGEAGE
CCCCCCCCCCCCCCC
34.4123737553
397PhosphorylationSSEEEGSTPGEAGEP
CCCCCCCCCCCCCCC
46.2823737553
407PhosphorylationEAGEPQKTPGATGHE
CCCCCCCCCCCCCCC
23.0027742792
411PhosphorylationPQKTPGATGHEEEGP
CCCCCCCCCCCCCCC
45.0127742792
427PhosphorylationLDVEDLNTGFEGSKT
CCHHHHCCCCCCCCH
51.0128464351
432PhosphorylationLNTGFEGSKTQDIEA
HCCCCCCCCHHCHHH
25.9022210690
434PhosphorylationTGFEGSKTQDIEAEA
CCCCCCCHHCHHHHH
32.9222210690
442PhosphorylationQDIEAEASEERQQER
HCHHHHHHHHHHHHH
31.3427742792
464PhosphorylationWEEVEDASEEAPLRD
HEECCCCCCCCCCCC
48.5728978645
477UbiquitinationRDRSHIDKTLMLNED
CCHHHCCCEEECCCC
42.8522790023
485UbiquitinationTLMLNEDKPADDYSA
EEECCCCCCCCHHHH
35.6122790023
490PhosphorylationEDKPADDYSAVLQRL
CCCCCCHHHHHHHHH
10.0828542873
491PhosphorylationDKPADDYSAVLQRLR
CCCCCHHHHHHHHHH
20.9228542873
503PhosphorylationRLRKIYHTSIKPLEQ
HHHHHHHCCCHHHHH
18.38-
506UbiquitinationKIYHTSIKPLEQSYK
HHHHCCCHHHHHHHC
43.2322790023
528PhosphorylationEITDGEITSKPMVLF
CCCCCCCCCCCEEEE
26.7928464351
529PhosphorylationITDGEITSKPMVLFL
CCCCCCCCCCEEEEE
40.1828464351
558PhosphorylationLGLEDTRYQLYTGAE
HCCCCCEEEEECCCC
12.6428464351
562PhosphorylationDTRYQLYTGAEPTTS
CCEEEEECCCCCCCC
38.2128542873
567PhosphorylationLYTGAEPTTSEFTVL
EECCCCCCCCEEEEE
34.1623737553
568PhosphorylationYTGAEPTTSEFTVLM
ECCCCCCCCEEEEEE
36.6523737553
569PhosphorylationTGAEPTTSEFTVLMH
CCCCCCCCEEEEEEC
32.9423737553
592PhosphorylationGIVMAADSARSFSPL
EEEHHCHHCCCCCCH
22.3628464351
595PhosphorylationMAADSARSFSPLEKF
HHCHHCCCCCCHHHH
29.7728542873
597PhosphorylationADSARSFSPLEKFGQ
CHHCCCCCCHHHHHH
29.8028542873
601UbiquitinationRSFSPLEKFGQNFLE
CCCCCHHHHHHHHHH
63.5822790023
609AcetylationFGQNFLEKLIGIEVP
HHHHHHHHHHCCCCC
47.7721728379
618UbiquitinationIGIEVPHKLLERVTF
HCCCCCHHHHHHCEE
49.0122790023
628PhosphorylationERVTFVDTPGIIENR
HHCEEECCCCHHCCH
20.36-
648S-nitrosocysteineGYPFNDVCQWFIDRA
CCCHHHHHHHHHHCC
3.10-
648S-nitrosylationGYPFNDVCQWFIDRA
CCCHHHHHHHHHHCC
3.1021278135
699PhosphorylationNKADNLATQMLMRVY
HHHCHHHHHHHHHHH
20.0628464351
750PhosphorylationLFLKEEISLLEDLNQ
HHHHHHHHHHHHHHH
30.1322210690
787PhosphorylationHALLVDRYLQTYKDK
HHHHHHHHHHHCHHC
9.9428576409
790PhosphorylationLVDRYLQTYKDKMTF
HHHHHHHHCHHCCEE
29.9128576409
791PhosphorylationVDRYLQTYKDKMTFF
HHHHHHHCHHCCEEE
12.2928576409
792SuccinylationDRYLQTYKDKMTFFS
HHHHHHCHHCCEEEC
55.0223954790
799PhosphorylationKDKMTFFSDGELVFK
HHCCEEECCCCEEEE
40.2828507225
816PhosphorylationVEDPDKFYIFKTILA
HCCCCCEEEEEEHHH
15.9323737553
848PhosphorylationFFGINPISNFKLLSQ
HHCCCCCCCHHHHHC
37.1523737553
854PhosphorylationISNFKLLSQQCSYMG
CCCHHHHHCCCCCCC
28.7428464351
858PhosphorylationKLLSQQCSYMGGCFL
HHHHCCCCCCCCHHH
17.5128464351
859PhosphorylationLLSQQCSYMGGCFLE
HHHCCCCCCCCHHHH
13.8628464351
878PhosphorylationAITQELPSLLGSIGL
HHHHHHHHHHHHHCC
49.1823737553
882PhosphorylationELPSLLGSIGLGKNP
HHHHHHHHHCCCCCC
17.2922210690
897PhosphorylationGAPNCDKTGCGETPK
CCCCCCCCCCCCCCC
25.1828542873
902PhosphorylationDKTGCGETPKNRYKK
CCCCCCCCCCCCCCC
25.5028542873

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 SRCA_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRCA_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 SRCA_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SRCA_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-442, AND MASSSPECTROMETRY.
"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 SER-304 AND SER-442, ANDMASS SPECTROMETRY.
"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 THR-229, AND MASSSPECTROMETRY.

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