K2C1B_MOUSE - dbPTM
K2C1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C1B_MOUSE
UniProt AC Q6IFZ6
Protein Name Keratin, type II cytoskeletal 1b
Gene Name Krt77
Organism Mus musculus (Mouse).
Sequence Length 572
Subcellular Localization
Protein Description
Protein Sequence MSRQFSSQSAFSSRSRRAYSSRSSSGFGGGRQALVSVSQSRRYGGDYGGGFSSRSLYSLGGSKSIFGNLVGRSASGFCQSRGPGGGFGGGIGGGIGGGRGFGGGGFGGGYGGGGRFGGGFGGAGFGFGGFGPSYPPGGIHEVTINQSLLEPLHLEVDPEIQRVKTQEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQVNTSTRTSSLEPVFEEFISQLQRQVDVLTTEQLRQNTEIRNMQDVVEDYKNKYEDEINKRTNAENDFVVLKKDVDAAFMGKSDLQSKVDTLYGEINFLKYLFDTELSQIQTHVSDTNVILSMDNNRSLDLDSIIDAVRAQYEIIAQKSKDEAEALYQTKYQELQITAGKHGDDLKNSKMEISELNRNIQRLRAEIANIKKQVEGMHGLISDAEERGERALQNAKQKLQDMEEALQQAKEDLAKLLRDYQAMLGAKLSLDVEIATYRQLLEGEESRMSGALQSQVSISVQSSQVTIGGGGGGSGSYSGSSRGGGGGGGGTGSRGGGGGGGGSSYVSSSRSATKYGSGGGSSRTQILQTSTHSSRRHVVE
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
9PhosphorylationSRQFSSQSAFSSRSR
CCCCCCHHCCCCCCC		32.9822817900
12PhosphorylationFSSQSAFSSRSRRAY
CCCHHCCCCCCCHHH		25.2622817900
13PhosphorylationSSQSAFSSRSRRAYS
CCHHCCCCCCCHHHH		28.0221183079
14MethylationSQSAFSSRSRRAYSS
CHHCCCCCCCHHHHC		32.7458858175
19PhosphorylationSSRSRRAYSSRSSSG
CCCCCHHHHCCCCCC		12.8422817900
20PhosphorylationSRSRRAYSSRSSSGF
CCCCHHHHCCCCCCC		20.4922817900
21PhosphorylationRSRRAYSSRSSSGFG
CCCHHHHCCCCCCCC		24.4122817900
47PhosphorylationSRRYGGDYGGGFSSR
CCCCCCCCCCCCCCC		22.4221183079
52PhosphorylationGDYGGGFSSRSLYSL
CCCCCCCCCCCCHHC		28.2822817900
55PhosphorylationGGGFSSRSLYSLGGS
CCCCCCCCCHHCCCC		33.3422817900
57PhosphorylationGFSSRSLYSLGGSKS
CCCCCCCHHCCCCHH		11.7721183079
58PhosphorylationFSSRSLYSLGGSKSI
CCCCCCHHCCCCHHH		26.3222817900
62PhosphorylationSLYSLGGSKSIFGNL
CCHHCCCCHHHHCCH		22.7921082442
64PhosphorylationYSLGGSKSIFGNLVG
HHCCCCHHHHCCHHC		25.5019131326
72MethylationIFGNLVGRSASGFCQ
HHCCHHCCCCCCCCC		22.9058858169
73PhosphorylationFGNLVGRSASGFCQS
HCCHHCCCCCCCCCC		22.3619131326
75PhosphorylationNLVGRSASGFCQSRG
CHHCCCCCCCCCCCC		33.3819131326
81MethylationASGFCQSRGPGGGFG
CCCCCCCCCCCCCCC		29.4624129315
99MethylationGGGIGGGRGFGGGGF
CCCCCCCCCCCCCCC		40.3124129315
115MethylationGGYGGGGRFGGGFGG
CCCCCCCCCCCCCCC		30.2558858163
173PhosphorylationQEREQIKTLNNKFAS
HHHHHHHHHHHHHHH		36.0329899451
177UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03-
180PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH		26.3522817900
184UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.41-
253PhosphorylationMQDVVEDYKNKYEDE
HHHHHHHHHHHHHHH		11.7117203969
256AcetylationVVEDYKNKYEDEINK
HHHHHHHHHHHHHHH		45.9555169339
263AcetylationKYEDEINKRTNAEND
HHHHHHHHCCCCCCC		67.28-
294PhosphorylationDLQSKVDTLYGEINF
HHHHHHHHHHHHHHH		25.5225777480
296PhosphorylationQSKVDTLYGEINFLK
HHHHHHHHHHHHHHH		18.1425777480
304PhosphorylationGEINFLKYLFDTELS
HHHHHHHHHHHHCHH		18.1025777480
308PhosphorylationFLKYLFDTELSQIQT
HHHHHHHHCHHHHHH		31.3425777480
311PhosphorylationYLFDTELSQIQTHVS
HHHHHCHHHHHHHCC		21.0025777480
315PhosphorylationTELSQIQTHVSDTNV
HCHHHHHHHCCCCCE		26.3525777480
318PhosphorylationSQIQTHVSDTNVILS
HHHHHHCCCCCEEEE		30.9825777480
320PhosphorylationIQTHVSDTNVILSMD
HHHHCCCCCEEEEEC		24.7125777480
325PhosphorylationSDTNVILSMDNNRSL
CCCCEEEEECCCCCC		16.9925777480
331PhosphorylationLSMDNNRSLDLDSII
EEECCCCCCCHHHHH		28.4919854140
478PhosphorylationQLLEGEESRMSGALQ
HHHCCCHHHHCCCCC		29.0528066266
523PhosphorylationGGGGGGGTGSRGGGG
CCCCCCCCCCCCCCC		34.9523140645
525PhosphorylationGGGGGTGSRGGGGGG
CCCCCCCCCCCCCCC		27.8223140645
526MethylationGGGGTGSRGGGGGGG
CCCCCCCCCCCCCCC		49.4724129315
535PhosphorylationGGGGGGGSSYVSSSR
CCCCCCCCCCCCCCC		23.0523140645
536PhosphorylationGGGGGGSSYVSSSRS
CCCCCCCCCCCCCCC		32.5923140645
537PhosphorylationGGGGGSSYVSSSRSA
CCCCCCCCCCCCCCC		13.1723140645
539PhosphorylationGGGSSYVSSSRSATK
CCCCCCCCCCCCCCC		17.8623140645
540PhosphorylationGGSSYVSSSRSATKY
CCCCCCCCCCCCCCC		21.5223140645
541PhosphorylationGSSYVSSSRSATKYG
CCCCCCCCCCCCCCC		23.8123140645
542MethylationSSYVSSSRSATKYGS
CCCCCCCCCCCCCCC		32.0524129315
543PhosphorylationSYVSSSRSATKYGSG
CCCCCCCCCCCCCCC		42.0923140645
545PhosphorylationVSSSRSATKYGSGGG
CCCCCCCCCCCCCCC		26.5023140645
547PhosphorylationSSRSATKYGSGGGSS
CCCCCCCCCCCCCCC		16.5118779572
549PhosphorylationRSATKYGSGGGSSRT
CCCCCCCCCCCCCCC		31.0418779572
554PhosphorylationYGSGGGSSRTQILQT
CCCCCCCCCCEEEEC		42.4918779572
555MethylationGSGGGSSRTQILQTS
CCCCCCCCCEEEECC		32.1458858157
556PhosphorylationSGGGSSRTQILQTST
CCCCCCCCEEEECCC		23.1630635358
561PhosphorylationSRTQILQTSTHSSRR
CCCEEEECCCCCCCC		31.9530635358
562PhosphorylationRTQILQTSTHSSRRH
CCEEEECCCCCCCCC		15.9130635358
563PhosphorylationTQILQTSTHSSRRHV
CEEEECCCCCCCCCC		29.2130635358
565PhosphorylationILQTSTHSSRRHVVE
EEECCCCCCCCCCCC		26.1530635358
566PhosphorylationLQTSTHSSRRHVVE-
EECCCCCCCCCCCC-		26.2330635358
567MethylationQTSTHSSRRHVVE--
ECCCCCCCCCCCC--		35.4258858193
568MethylationTSTHSSRRHVVE---
CCCCCCCCCCCC---		28.9758858187
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 K2C1B_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C1B_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 K2C1B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of K2C1B_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C1B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-73 AND SER-75,AND MASS SPECTROMETRY.
"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 TYR-253, AND MASSSPECTROMETRY.

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