SYNEM_MOUSE - dbPTM
SYNEM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYNEM_MOUSE
UniProt AC Q70IV5
Protein Name Synemin {ECO:0000303|PubMed:15265691}
Gene Name Synm {ECO:0000312|MGI:MGI:2661187}
Organism Mus musculus (Mouse).
Sequence Length 1561
Subcellular Localization Cytoplasm, cytoskeleton . Cell junction, adherens junction . There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere.
Protein Description Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteropolymeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these heteropolymeric IFs to adherens-type junctions, such as to the costameres, neuromuscular junctions, and myotendinous junctions within striated muscle cells (By similarity)..
Protein Sequence MLSWRLQTGSEKAELQELNARLYDYVCRVRELERENLLLEEELRSRLSREDRWAEDQALYAEEARSLRQQLDELNWSTALAEGERDALRRELLELQREGVEAGTARSRLDAELGAQRRELEEALGARAALEALLGRLETERRDLDAAHERQVRDLRARAASLTMHFRARATSPAAPPPRLRDVHDSYALLVAESWRESVQLYEDEVRELEQALRRGQESRLQAEDEARLCAQEADALRNQALELEQLRARLEDELLRMREEYGMQAEERQRVIDSLEDEKEALTLAMADRLRDYQELLQVKTGLSLEVATYRALLEGESNPEILIWTENIENVPQEPRNTSYRYTNSVLQRKNEKNLFPRRKTPWAAVNHSSASYSNWPGHLDSQTTTAVGSAARRGLLTSRHSSSATTSGQQKPLEKTISSRANLRPVTPTHGFLRNTDAQMKTLPHRSKVEGTGDTHARRATESVITRESYRGHQGHVAAGAVSSTPSNERTVILGKKLEAQATKEQERDRSGVIRIKPEEKMFDSKEKASEERNLRWEELTKLDRDARKRESRHLRDEAREKEALKERSVKEREVPISLEVSRGSRAEVSTIHLQSPGRKDVSHSGGREAETKETRFRLDTQDTASSLQSDSTTETIAESIVTTILKQFTQSPGAEEEATSFPDTKVTYVDRKEFPGDGKTKTEIVVESKLTDVVDVSDEAGLDYLLSKDVKEVGLKGKSTETMIGEMINLGLKGREGRAKVVNVEIVEEPMSYIGGGKIDFSTPFQVEEVDDVSPSPKGFVEEEDGEGETHMAFSMRPHQTKQPQGTIPHVEEVTEAGDSEGEQSYFVSTPDEYPGGHDREDDGSVYGQIHIEEESTIRYSWQDEIAQGTWRRKMRGDVGGEKPVKVLEVPALSLGGAIGSAHLKEEASGELRAEPTVIEKEIKIPHEFHTSIKGVFSSEPRHQLVEVIGQLEETLPERMKEELSALTRQSQGESGSVSVDVKKVQSAAGGSVTLMAEVNLSQTVDADQLDLEQLSRDEAGEIERAVESVVRESLAKRSSPVPRSPDREDGEEVPAGGILFKRWATRELYSPSGERDDAGQVSPSSDQRVTQGPVSATVEVTSPTGFVQSHVLEDVSQSVRHVKLGPTEMWRTEQVTFGGPTAQVVEVSGDFSEAVSSEGASRSVRHITLGPHQSQVSTEVIFRGSVPTWQETGDTEKPGPVVLSVGADISGSGRMPGSERSHTEKEIRFQGPVSGTAQVGGNFATEESVGSQTFVRSLQLGPKEGFREEIQFIAPIPDKVGWGEEDSEHTKVSLERATSIQRIDIVPQRYLASKQMAPQTLEFRDSEDMVMVEGSAGTIQATHNFTSDREILQNKENTFQRVISGSPPDSVGDTGAEVTANVSRSFRHIQIGPTEEEPSEYFVTGRPVSKTFVLDGSVASPGLVGGADGGSTPCRIALGPKETSFTFQMDLSDTRAIRSWTRDTGSEVEAHGVSHRGGWRIAHSRDERVASTGSGASPGDAHQAPGEKGTEQAGFDKTVQLQRMVDQRSVASDEKKVALLYLDNEEEEEEEGEGWF
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
8PhosphorylationMLSWRLQTGSEKAEL
CCCCCCCCCCCHHHH		47.4728576409
10PhosphorylationSWRLQTGSEKAELQE
CCCCCCCCCHHHHHH		39.0328464351
12UbiquitinationRLQTGSEKAELQELN
CCCCCCCHHHHHHHH		49.1922790023
161PhosphorylationDLRARAASLTMHFRA
HHHHHHHHHHHEHHH		24.3224719451
163PhosphorylationRARAASLTMHFRARA
HHHHHHHHHEHHHHC		13.2028464351
171PhosphorylationMHFRARATSPAAPPP
HEHHHHCCCCCCCCC		29.6821454597
172PhosphorylationHFRARATSPAAPPPR
EHHHHCCCCCCCCCC		16.1426824392
198PhosphorylationVAESWRESVQLYEDE
HHHHHHHHCHHHHHH		13.4430635358
202PhosphorylationWRESVQLYEDEVREL
HHHHCHHHHHHHHHH		12.3030635358
347PhosphorylationTSYRYTNSVLQRKNE
CCHHHHHHHHHHHCC		19.1928464351
430PhosphorylationRANLRPVTPTHGFLR
CCCCCCCCCCCCHHC		25.7526824392
432PhosphorylationNLRPVTPTHGFLRNT
CCCCCCCCCCHHCCC		25.8426643407
464PhosphorylationDTHARRATESVITRE
CHHHHHHCEEEEEHH		27.2928464351
466PhosphorylationHARRATESVITRESY
HHHHHCEEEEEHHHH		17.9221183079
588PhosphorylationSLEVSRGSRAEVSTI
EEEECCCCCCEEEEE		27.4921454597
593PhosphorylationRGSRAEVSTIHLQSP
CCCCCEEEEEEECCC		17.1021454597
594PhosphorylationGSRAEVSTIHLQSPG
CCCCEEEEEEECCCC		20.0020415495
599PhosphorylationVSTIHLQSPGRKDVS
EEEEEECCCCCCCCC		35.3626824392
653PhosphorylationTTILKQFTQSPGAEE
HHHHHHHHCCCCCHH		26.1625521595
655PhosphorylationILKQFTQSPGAEEEA
HHHHHHCCCCCHHHH		23.4230372032
664PhosphorylationGAEEEATSFPDTKVT
CCHHHHCCCCCCEEE		41.6623375375
767PhosphorylationGGKIDFSTPFQVEEV
CCCCCCCCCCCEEEC		28.2827717184
778PhosphorylationVEEVDDVSPSPKGFV
EEECCCCCCCCCCEE		27.0124925903
780PhosphorylationEVDDVSPSPKGFVEE
ECCCCCCCCCCEEEE		31.5624925903
811PhosphorylationQTKQPQGTIPHVEEV
CCCCCCCCCCCEEEE		26.5322210690
819PhosphorylationIPHVEEVTEAGDSEG
CCCEEEEEECCCCCC		24.3322210690
824PhosphorylationEVTEAGDSEGEQSYF
EEEECCCCCCCEEEE		46.7322210690
829PhosphorylationGDSEGEQSYFVSTPD
CCCCCCEEEEEECCC		19.0822210690
830PhosphorylationDSEGEQSYFVSTPDE
CCCCCEEEEEECCCC		14.0122210690
849PhosphorylationHDREDDGSVYGQIHI
CCCCCCCCEEEEEEE		21.11-
861PhosphorylationIHIEEESTIRYSWQD
EEEEECEEECEEEHH		16.86-
936PhosphorylationIPHEFHTSIKGVFSS
CCHHCHHCCCCCCCC		17.4623375375
975PhosphorylationLSALTRQSQGESGSV
HHHHHHHHCCCCCCE		36.5428464351
1033PhosphorylationEIERAVESVVRESLA
HHHHHHHHHHHHHHH		21.2221183079
1043PhosphorylationRESLAKRSSPVPRSP
HHHHHCCCCCCCCCC		37.9829899451
1044PhosphorylationESLAKRSSPVPRSPD
HHHHCCCCCCCCCCC		33.6727742792
1049PhosphorylationRSSPVPRSPDREDGE
CCCCCCCCCCCCCCC		25.6925521595
1070PhosphorylationILFKRWATRELYSPS
EEEEEEEECCCCCCC		20.09-
1074PhosphorylationRWATRELYSPSGERD
EEEECCCCCCCCCCC		17.4926160508
1075PhosphorylationWATRELYSPSGERDD
EEECCCCCCCCCCCC		25.8027742792
1077PhosphorylationTRELYSPSGERDDAG
ECCCCCCCCCCCCCC		47.5526160508
1087PhosphorylationRDDAGQVSPSSDQRV
CCCCCCCCCCCCCCC		15.9225521595
1089PhosphorylationDAGQVSPSSDQRVTQ
CCCCCCCCCCCCCCC		38.7525521595
1090PhosphorylationAGQVSPSSDQRVTQG
CCCCCCCCCCCCCCC		40.9426160508
1107PhosphorylationSATVEVTSPTGFVQS
EEEEEECCCCCCCCH		26.1624719451
1109PhosphorylationTVEVTSPTGFVQSHV
EEEECCCCCCCCHHH		42.9128464351
1114PhosphorylationSPTGFVQSHVLEDVS
CCCCCCCHHHHCHHH		15.4029899451
1128UbiquitinationSQSVRHVKLGPTEMW
HHHCCCCCCCCCCCE		41.4222790023
1179PhosphorylationITLGPHQSQVSTEVI
EEECCCCHHCEEEEE		29.52-
1182PhosphorylationGPHQSQVSTEVIFRG
CCCCHHCEEEEEECC		15.94-
1298PhosphorylationDSEHTKVSLERATSI
CCCCCEECHHHCCCC		26.5224719451
1304PhosphorylationVSLERATSIQRIDIV
ECHHHCCCCEEEECC		18.7521454597
1363PhosphorylationILQNKENTFQRVISG
HHHCCCCCCHHHHCC		23.41-
1369PhosphorylationNTFQRVISGSPPDSV
CCCHHHHCCCCCCCC		30.2930352176
1371PhosphorylationFQRVISGSPPDSVGD
CHHHHCCCCCCCCCC		26.8626824392
1375PhosphorylationISGSPPDSVGDTGAE
HCCCCCCCCCCCCCE		33.5021454597
1379PhosphorylationPPDSVGDTGAEVTAN
CCCCCCCCCCEEEEE		32.1521454597
1399PhosphorylationRHIQIGPTEEEPSEY
CCEEECCCCCCCCCC		51.3023811945
1404PhosphorylationGPTEEEPSEYFVTGR
CCCCCCCCCCEECCC		48.4823811945
1406PhosphorylationTEEEPSEYFVTGRPV
CCCCCCCCEECCCCC		14.0023811945
1409PhosphorylationEPSEYFVTGRPVSKT
CCCCCEECCCCCCCE		19.9923811945
1414PhosphorylationFVTGRPVSKTFVLDG
EECCCCCCCEEEEEC		28.7623811945
1425PhosphorylationVLDGSVASPGLVGGA
EEECCCCCCCCCCCC		19.83-
1437PhosphorylationGGADGGSTPCRIALG
CCCCCCCCCCEEEEC		29.6824719451
1471PhosphorylationSWTRDTGSEVEAHGV
HEECCCCCCEEEECC		40.3328464351
1479PhosphorylationEVEAHGVSHRGGWRI
CEEEECCCCCCCEEE		16.4428464351
1481MethylationEAHGVSHRGGWRIAH
EEECCCCCCCEEEEE		37.5024129315
1485MethylationVSHRGGWRIAHSRDE
CCCCCCEEEEECCCC		21.35-
1496PhosphorylationSRDERVASTGSGASP
CCCCCCCCCCCCCCC		30.3726160508
1497PhosphorylationRDERVASTGSGASPG
CCCCCCCCCCCCCCC		26.1526160508
1499PhosphorylationERVASTGSGASPGDA
CCCCCCCCCCCCCCC		31.1326160508
1502PhosphorylationASTGSGASPGDAHQA
CCCCCCCCCCCCCCC		32.7026824392
1534PhosphorylationQRMVDQRSVASDEKK
HHHHHHCCCCCCCCE		19.1928464351
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 SYNEM_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYNEM_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 SYNEM_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SYNEM_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYNEM_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-599 AND SER-1049, ANDMASS SPECTROMETRY.

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