K2C1_MOUSE - dbPTM
K2C1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C1_MOUSE
UniProt AC P04104
Protein Name Keratin, type II cytoskeletal 1
Gene Name Krt1
Organism Mus musculus (Mouse).
Sequence Length 637
Subcellular Localization Cell membrane.
Protein Description May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK (By similarity)..
Protein Sequence MSLQCSSRSLCRGGGGSRNFSSGSAGLVSFQRRSTSSSMRRSGGGGGGRFSGGGFCGSSGSGFGSKSLMNLGGGRSISKSVAGGGGSFCGGFGGGSYGGGGFGGGSYGGGGFGGGSFGGGGFGGSGFGGGLGGGGGFGSGGGFGGGRFGSMGPVCPPGGIQEVTINQSLLQPLNVEVDPQIQKVKSQEREQIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQVDTTTRTQNLDPFFENYISILRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALYQMEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSICQRSKAEAETFYQSKYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRGEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTKLALDMEIATYKKLLEGEEIRMSGECTPNVSVSVSTSHTSMSGSSSRGGGSGGGRYGGGGSYGGGSGGGSYGGSSGGGGSGGSYGGGSGGGSYGGGSGGGSSGSHRGGSGGGGGSSGGSYGGSSGGGRGGSSSGGGGVKSSGSSTVKFVSTSYSRGTK
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
12MethylationCSSRSLCRGGGGSRN
CCCCCCCCCCCCCCC		52.6824129315
18Asymmetric dimethylarginineCRGGGGSRNFSSGSA
CCCCCCCCCCCCCCC		52.03-
21PhosphorylationGGGSRNFSSGSAGLV
CCCCCCCCCCCCCEE		37.0222817900
22PhosphorylationGGSRNFSSGSAGLVS
CCCCCCCCCCCCEEE		32.4119060867
24PhosphorylationSRNFSSGSAGLVSFQ
CCCCCCCCCCEEEEE		22.5522817900
34PhosphorylationLVSFQRRSTSSSMRR
EEEEEECCCCCCCCC		34.5319367708
35PhosphorylationVSFQRRSTSSSMRRS
EEEEECCCCCCCCCC		30.7128576409
36PhosphorylationSFQRRSTSSSMRRSG
EEEECCCCCCCCCCC		22.97-
37PhosphorylationFQRRSTSSSMRRSGG
EEECCCCCCCCCCCC		28.3922871156
38PhosphorylationQRRSTSSSMRRSGGG
EECCCCCCCCCCCCC		18.97-
49MethylationSGGGGGGRFSGGGFC
CCCCCCCCCCCCCCC		26.3224129315
51PhosphorylationGGGGGRFSGGGFCGS
CCCCCCCCCCCCCCC		34.8622817900
59PhosphorylationGGGFCGSSGSGFGSK
CCCCCCCCCCCCCCC		23.4322817900
61PhosphorylationGFCGSSGSGFGSKSL
CCCCCCCCCCCCCCC		32.6622817900
65PhosphorylationSSGSGFGSKSLMNLG
CCCCCCCCCCCEECC		19.4621183079
67PhosphorylationGSGFGSKSLMNLGGG
CCCCCCCCCEECCCC		34.2522817900
106PhosphorylationGGGFGGGSYGGGGFG
CCCCCCCCCCCCCCC		24.71-
125PhosphorylationGGGGFGGSGFGGGLG
CCCCCCCCCCCCCCC		31.18-
186PhosphorylationPQIQKVKSQEREQIK
HHHHHHHHHHHHHHH		40.0219367708
198MalonylationQIKSLNDKFASFIDK
HHHHHHHHHHHHHHH		41.5826320211
201PhosphorylationSLNDKFASFIDKVRF
HHHHHHHHHHHHHHH		26.3529472430
205UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.4127667366
205AcetylationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.4123201123
252PhosphorylationILRRKVDSLKSDQSR
HHHHHHHHHHHCHHH		40.4623737553
276PhosphorylationDLVEEYRTKYEDEIN
HHHHHHHHHHHHHHH		36.7628576409
284"N6,N6-dimethyllysine"KYEDEINKRTNAENE
HHHHHHHHCCCCCCC		67.28-
284MethylationKYEDEINKRTNAENE
HHHHHHHHCCCCCCC		67.28-
301PhosphorylationTIKKDVDSAYMTKVE
EEEHHCCHHCEEHHH		22.5823375375
306AcetylationVDSAYMTKVELQAKA
CCHHCEEHHHHHHHH		19.7212650331
352PhosphorylationLSMDNNRSLDLDGII
EEECCCCEECHHHHH		28.4923737553
360PhosphorylationLDLDGIISEVKAQYD
ECHHHHHHHHHHHHH		34.1223737553
368PhosphorylationEVKAQYDSICQRSKA
HHHHHHHHHHHHHHH		21.9623375375
373PhosphorylationYDSICQRSKAEAETF
HHHHHHHHHHHHHHH		15.4423375375
383PhosphorylationEAETFYQSKYEELQI
HHHHHHHHHHHHHEE		26.3123375375
398PhosphorylationTAGKHGDSVRNTKME
CCCCCCHHHHHHHHH		27.8023375375
428PhosphorylationDGCKKQISQIQQNIN
HHHHHHHHHHHHHHH		20.8023375375
526MethylationSMSGSSSRGGGSGGG
CCCCCCCCCCCCCCC		50.1224129315
530PhosphorylationSSSRGGGSGGGRYGG
CCCCCCCCCCCCCCC		37.22-
530O-linked_GlycosylationSSSRGGGSGGGRYGG
CCCCCCCCCCCCCCC		37.2255472655
535PhosphorylationGGSGGGRYGGGGSYG
CCCCCCCCCCCCCCC		24.3226239621
581PhosphorylationGGSGGGSSGSHRGGS
CCCCCCCCCCCCCCC		47.8126239621
583PhosphorylationSGGGSSGSHRGGSGG
CCCCCCCCCCCCCCC		16.3826239621
585MethylationGGSSGSHRGGSGGGG
CCCCCCCCCCCCCCC		53.5224129315
588PhosphorylationSGSHRGGSGGGGGSS
CCCCCCCCCCCCCCC		36.7722817900
594PhosphorylationGSGGGGGSSGGSYGG
CCCCCCCCCCCCCCC		29.1422817900
595PhosphorylationSGGGGGSSGGSYGGS
CCCCCCCCCCCCCCC		50.9122817900
598PhosphorylationGGGSSGGSYGGSSGG
CCCCCCCCCCCCCCC		24.9120139300
599PhosphorylationGGSSGGSYGGSSGGG
CCCCCCCCCCCCCCC		28.8720139300
602PhosphorylationSGGSYGGSSGGGRGG
CCCCCCCCCCCCCCC		22.8019367708
603PhosphorylationGGSYGGSSGGGRGGS
CCCCCCCCCCCCCCC		44.7422817900
607MethylationGGSSGGGRGGSSSGG
CCCCCCCCCCCCCCC		49.9624129315
610PhosphorylationSGGGRGGSSSGGGGV
CCCCCCCCCCCCCCC		24.9320139300
622PhosphorylationGGVKSSGSSTVKFVS
CCCCCCCCCCEEEEE		25.4523375375
623PhosphorylationGVKSSGSSTVKFVST
CCCCCCCCCEEEEEE		40.5223375375
629PhosphorylationSSTVKFVSTSYSRGT
CCCEEEEEECCCCCC		18.1223375375
631PhosphorylationTVKFVSTSYSRGTK-
CEEEEEECCCCCCC-		17.3823375375
633PhosphorylationKFVSTSYSRGTK---
EEEEECCCCCCC---		24.8123375375
634MethylationFVSTSYSRGTK----
EEEECCCCCCC----		48.8758858103
636PhosphorylationSTSYSRGTK------
EECCCCCCC------		32.2523375375
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 K2C1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C1_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 K2C1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of K2C1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C1_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-24 AND SER-352, AND MASSSPECTROMETRY.

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