K2C79_MOUSE - dbPTM
K2C79_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C79_MOUSE
UniProt AC Q8VED5
Protein Name Keratin, type II cytoskeletal 79
Gene Name Krt79
Organism Mus musculus (Mouse).
Sequence Length 531
Subcellular Localization
Protein Description
Protein Sequence MRSSLSRQTFSTKGGFSSNSASGGGGSRMRTSYSSVTMSRGSGGGGGVRSGSSSGGFGSRSLYNLGGKNISVSMACGASSGRALGGFGSGAYVGLGASRQTFGPVCPPGGIQEVTVNQSLLTPLNVEIDPEIQRVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQSQNTGVARSLEPFFENYLSTLRRQLDTKQSERGRLDMELRNVQDNLEDFKNKYEDEINKRTALENEFVLLKKDVDAAYMGRMDLHGKVDSLTQEIDFLQQLFEMELSQVQTNVSDTNVILSMDNNRNLDLDSIIAEVKAQYELIAQKSRAEAESWYQTKYEELQVTAGKHGDSLRDTKNEIAELTRTTQRLQGEVDAAKKQCQQLQTAIAEAEQNGEMALKDAKKKLGDLDTALHQAKEDLARMLREYQDLVSVKLALDMEIATYRKLLESEESRMSGDCPSAISISVTGNSTSVCAGGTAGFGNGLSLGGAGGASKGGFGSSVSYGAAKGGQVSGGTSILRKTTTVKTSSRRY
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
3Phosphorylation-----MRSSLSRQTF
-----CCCCCCCCCC
34.0422324799
4Phosphorylation----MRSSLSRQTFS
----CCCCCCCCCCC
21.7223140645
6Phosphorylation--MRSSLSRQTFSTK
--CCCCCCCCCCCCC
25.0422324799
20PhosphorylationKGGFSSNSASGGGGS
CCCCCCCCCCCCCCC
26.2627087446
27PhosphorylationSASGGGGSRMRTSYS
CCCCCCCCCCCCEEC
26.61-
31PhosphorylationGGGSRMRTSYSSVTM
CCCCCCCCEECEEEE
23.7530635358
32PhosphorylationGGSRMRTSYSSVTMS
CCCCCCCEECEEEEC
16.8030635358
33PhosphorylationGSRMRTSYSSVTMSR
CCCCCCEECEEEECC
12.3530635358
34PhosphorylationSRMRTSYSSVTMSRG
CCCCCEECEEEECCC
20.3530635358
35PhosphorylationRMRTSYSSVTMSRGS
CCCCEECEEEECCCC
17.2430635358
37PhosphorylationRTSYSSVTMSRGSGG
CCEECEEEECCCCCC
16.0430635358
39PhosphorylationSYSSVTMSRGSGGGG
EECEEEECCCCCCCC
24.9130635358
40MethylationYSSVTMSRGSGGGGG
ECEEEECCCCCCCCC
32.2616289363
42PhosphorylationSVTMSRGSGGGGGVR
EEEECCCCCCCCCCC
32.9030635358
50PhosphorylationGGGGGVRSGSSSGGF
CCCCCCCCCCCCCCC
40.3929899451
52PhosphorylationGGGVRSGSSSGGFGS
CCCCCCCCCCCCCCC
23.6819367708
53PhosphorylationGGVRSGSSSGGFGSR
CCCCCCCCCCCCCCC
36.2119367708
54PhosphorylationGVRSGSSSGGFGSRS
CCCCCCCCCCCCCCC
44.6319367708
59PhosphorylationSSSGGFGSRSLYNLG
CCCCCCCCCCEEECC
19.2129899451
61PhosphorylationSGGFGSRSLYNLGGK
CCCCCCCCEEECCCC
36.5819060867
145PhosphorylationQEREQIKTLNNKFAS
HHHHHHHHHHHHHHH
36.0329899451
149UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH
41.03-
152PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH
26.3522817900
156UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH
30.4127667366
229AcetylationNLEDFKNKYEDEINK
HHHHHHHHHHHHHHH
51.08-
236AcetylationKYEDEINKRTALENE
HHHHHHHHHHHHHCE
57.71-
343PhosphorylationKYEELQVTAGKHGDS
HHHHCCHHCCCCCCC
19.4124719451
515PhosphorylationGGQVSGGTSILRKTT
CCCCCCCCCCCCCCE
19.0022817900

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 K2C79_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C79_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 K2C79_MOUSE !!

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

Oops, there are no PPI records of K2C79_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C79_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-20, AND MASSSPECTROMETRY.

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