GELS_MOUSE - dbPTM
GELS_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GELS_MOUSE
UniProt AC P13020
Protein Name Gelsolin
Gene Name Gsn
Organism Mus musculus (Mouse).
Sequence Length 780
Subcellular Localization Isoform 2: Cytoplasm, cytoskeleton.
Isoform 1: Secreted.
Protein Description Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis..
Protein Sequence MAPYRSSLLCALLLLALCALSPSHAATTSRGRAQERAPQSRVSEARPSTMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESSTFSGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWDSFNNGDCFILDLGNNIYQWCGSGSNKFERLKATQVSKGIRDNERSGRAQVHVSEEGGEPEAMLQVLGPKPALPEGTEDTAKEDAANRRLAKLYKVSNGAGSMSVSLVADENPFAQGALRSEDCFILDHGRDGKIFVWKGKQANMEERKAALKTASDFISKMQYPRQTQVSVLPEGGETPLFKQFFKNWRDPDQTDGPGLGYLSSHIANVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSRDGGQTAPASIRLFQVRASSSGATRAVEVMPKSGALNSNDAFVLKTPSAAYLWVGAGASEAEKTGAQELLKVLRSQHVQVEEGSEPDAFWEALGGKTAYRTSPRLKDKKMDAHPPRLFACSNRIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANRDRRTPITVVRQGFEPPSFVGWFLGWDDNYWSVDPLDRALAELAA
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
1 (in isoform 2)Acetylation-8.38-
84PhosphorylationVPVPPNLYGDFFTGD
ECCCCCCCCCCCCCC		22.68-
152PhosphorylationREVQGFESSTFSGYF
EECCCCCCCEECEEE		32.2025338131
175UbiquitinationGGVASGFKHVVPNEV
CCCCCCCCCCCCCHH		38.73-
191AcetylationVQRLFQVKGRRVVRA
HEEEEEECCCEEEEE		35.6022826441
191UbiquitinationVQRLFQVKGRRVVRA
HEEEEEECCCEEEEE		35.60-
243UbiquitinationLKATQVSKGIRDNER
HHHHEECCCCCCCCC		60.54-
251PhosphorylationGIRDNERSGRAQVHV
CCCCCCCCCCCEEEE		26.8429899451
282PhosphorylationKPALPEGTEDTAKED
CCCCCCCCCCHHHHH		29.0929550500
302PhosphorylationLAKLYKVSNGAGSMS
HHHHHHCCCCCCCCE		25.9520415495
307PhosphorylationKVSNGAGSMSVSLVA
HCCCCCCCCEEEEEE		13.8322817900
309PhosphorylationSNGAGSMSVSLVADE
CCCCCCCEEEEEECC		15.3923649490
311PhosphorylationGAGSMSVSLVADENP
CCCCCEEEEEECCCC		15.1523649490
358UbiquitinationEERKAALKTASDFIS
HHHHHHHHHHHHHHH		37.00-
359PhosphorylationERKAALKTASDFISK
HHHHHHHHHHHHHHH		32.04-
366AcetylationTASDFISKMQYPRQT
HHHHHHHHCCCCCCC		25.8023236377
366UbiquitinationTASDFISKMQYPRQT
HHHHHHHHCCCCCCC		25.80-
373PhosphorylationKMQYPRQTQVSVLPE
HCCCCCCCCEEECCC		32.0225777480
376PhosphorylationYPRQTQVSVLPEGGE
CCCCCCEEECCCCCC		14.2326824392
384PhosphorylationVLPEGGETPLFKQFF
ECCCCCCCHHHHHHH		28.6826824392
392AcetylationPLFKQFFKNWRDPDQ
HHHHHHHHCCCCCCC		57.8123236377
407PhosphorylationTDGPGLGYLSSHIAN
CCCCCHHHHHHHEEC		14.41-
463PhosphorylationVPVDPATYGQFYGGD
CCCCHHHCEEEECCC		15.84-
504PhosphorylationTQDEVAASAILTAQL
CCHHHHHHHHHHHHH		13.2023649490
540AcetylationLMSLFGGKPMIIYKG
HHHHHCCCCEEEEEC		31.6223806337
546AcetylationGKPMIIYKGGTSRDG
CCCEEEEECCCCCCC		40.2222826441
549PhosphorylationMIIYKGGTSRDGGQT
EEEEECCCCCCCCCC		29.2923684622
550PhosphorylationIIYKGGTSRDGGQTA
EEEECCCCCCCCCCC		31.4823684622
556PhosphorylationTSRDGGQTAPASIRL
CCCCCCCCCCCEEEE		37.5723684622
560PhosphorylationGGQTAPASIRLFQVR
CCCCCCCEEEEEEEE		13.7426824392
582UbiquitinationRAVEVMPKSGALNSN
EEEEECCCCCCCCCC		43.35-
582AcetylationRAVEVMPKSGALNSN
EEEEECCCCCCCCCC		43.3523806337
595UbiquitinationSNDAFVLKTPSAAYL
CCCEEEEECCCCEEE		53.76-
601PhosphorylationLKTPSAAYLWVGAGA
EECCCCEEEEECCCC		10.79-
621AcetylationTGAQELLKVLRSQHV
HHHHHHHHHHHHCCC		52.4223806337
634PhosphorylationHVQVEEGSEPDAFWE
CCEEECCCCCHHHHH		49.5926525534
649PhosphorylationALGGKTAYRTSPRLK
HCCCCCCCCCCCCCC		21.47-
651PhosphorylationGGKTAYRTSPRLKDK
CCCCCCCCCCCCCCC		30.3327681418
652PhosphorylationGKTAYRTSPRLKDKK
CCCCCCCCCCCCCCC		10.0629899451
671PhosphorylationPPRLFACSNRIGRFV
CCCEEEECCCCEEEE		26.2229176673
740PhosphorylationPANRDRRTPITVVRQ
CCCCCCCCCEEEEEC		21.6729176673
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 GELS_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GELS_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 GELS_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P3C2A_MOUSEPik3c2aphysical
10684249
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GELS_MOUSE

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Related Literatures of Post-Translational Modification

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