K2C1_HUMAN - dbPTM
K2C1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C1_HUMAN
UniProt AC P04264
Protein Name Keratin, type II cytoskeletal 1
Gene Name KRT1
Organism Homo sapiens (Human).
Sequence Length 644
Subcellular Localization Cell membrane . Located on plasma membrane of neuroblastoma NMB7 cells.
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..
Protein Sequence MSRQFSSRSGYRSGGGFSSGSAGIINYQRRTTSSSTRRSGGGGGRFSSCGGGGGSFGAGGGFGSRSLVNLGGSKSISISVARGGGRGSGFGGGYGGGGFGGGGFGGGGFGGGGIGGGGFGGFGSGGGGFGGGGFGGGGYGGGYGPVCPPGGIQEVTINQSLLQPLNVEIDPEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQAELSQMQTQISETNVILSMDNNRSLDLDSIIAEVKAQYEDIAQKSKAEAESLYQSKYEELQITAGRHGDSVRNSKIEISELNRVIQRLRSEIDNVKKQISNLQQSISDAEQRGENALKDAKNKLNDLEDALQQAKEDLARLLRDYQELMNTKLALDLEIATYRTLLEGEESRMSGECAPNVSVSVSTSHTTISGGGSRGGGGGGYGSGGSSYGSGGGSYGSGGGGGGGRGSYGSGGSSYGSGGGSYGSGGGGGGHGSYGSGSSSGGYRGGSGGGGGGSSGGRGSGGGSSGGSIGGRGSSSGGVKSSGGSSSVKFVSTTYSGVTR
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
12MethylationFSSRSGYRSGGGFSS
CCCCCCCCCCCCCCC		32.14-
13PhosphorylationSSRSGYRSGGGFSSG
CCCCCCCCCCCCCCC		33.0520071362
18PhosphorylationYRSGGGFSSGSAGII
CCCCCCCCCCCCEEE		36.7420071362
19PhosphorylationRSGGGFSSGSAGIIN
CCCCCCCCCCCEEEE		34.2121955146
21PhosphorylationGGGFSSGSAGIINYQ
CCCCCCCCCEEEEEE		25.8521955146
27PhosphorylationGSAGIINYQRRTTSS
CCCEEEEEEEECCCC		7.93-
31PhosphorylationIINYQRRTTSSSTRR
EEEEEEECCCCCCCC		32.97-
33O-linked_GlycosylationNYQRRTTSSSTRRSG
EEEEECCCCCCCCCC		22.9828510447
39PhosphorylationTSSSTRRSGGGGGRF
CCCCCCCCCCCCCCC		38.2028111955
45MethylationRSGGGGGRFSSCGGG
CCCCCCCCCCCCCCC		31.39-
47PhosphorylationGGGGGRFSSCGGGGG
CCCCCCCCCCCCCCC		24.2928111955
48PhosphorylationGGGGRFSSCGGGGGS
CCCCCCCCCCCCCCC		17.6728111955
49GlutathionylationGGGRFSSCGGGGGSF
CCCCCCCCCCCCCCC		5.9424333276
55PhosphorylationSCGGGGGSFGAGGGF
CCCCCCCCCCCCCCC		24.6328111955
64PhosphorylationGAGGGFGSRSLVNLG
CCCCCCCCCCEEECC		19.2128111955
66PhosphorylationGGGFGSRSLVNLGGS
CCCCCCCCEEECCCC		38.0628731282
73PhosphorylationSLVNLGGSKSISISV
CEEECCCCCEEEEEE		22.7928111955
82MethylationSISISVARGGGRGSG
EEEEEEECCCCCCCC		41.9854556925
193PhosphorylationSLNNQFASFIDKVRF
HHHHHHHHHHHHHHH		24.8328355574
197AcetylationQFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.417705623
197UbiquitinationQFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.4122817900
211MethylationQNQVLQTKWELLQQV
HHHHHHHHHHHHHHC		26.22115971597
233PhosphorylationNLEPYFESFINNLRR
CCHHHHHHHHHHHHH		22.87-
246AcetylationRRRVDQLKSDQSRLD
HHHHHHHHHHHHHHH		46.4826051181
247PhosphorylationRRVDQLKSDQSRLDS
HHHHHHHHHHHHHHH		49.8526074081
250PhosphorylationDQLKSDQSRLDSELK
HHHHHHHHHHHHHHH		39.5426074081
254PhosphorylationSDQSRLDSELKNMQD
HHHHHHHHHHHHHHH		49.7926074081
269MethylationMVEDYRNKYEDEINK
HHHHHHHHHHHHHHH		40.81-
269NeddylationMVEDYRNKYEDEINK
HHHHHHHHHHHHHHH		40.8132015554
269UbiquitinationMVEDYRNKYEDEINK
HHHHHHHHHHHHHHH		40.8133845483
270PhosphorylationVEDYRNKYEDEINKR
HHHHHHHHHHHHHHC		31.96-
276"N6,N6-dimethyllysine"KYEDEINKRTNAENE
HHHHHHHHCCCCCCC		67.28-
276MethylationKYEDEINKRTNAENE
HHHHHHHHCCCCCCC		67.2823161681
276UbiquitinationKYEDEINKRTNAENE
HHHHHHHHCCCCCCC		67.2833845483
295PhosphorylationKKDVDGAYMTKVDLQ
EECCCCCEECCCHHH		15.7317924679
297PhosphorylationDVDGAYMTKVDLQAK
CCCCCEECCCHHHHH		18.4217924679
298AcetylationVDGAYMTKVDLQAKL
CCCCEECCCHHHHHH		19.7412650327
344PhosphorylationLSMDNNRSLDLDSII
EEECCCCCCCHHHHH		28.4921082442
349PhosphorylationNRSLDLDSIIAEVKA
CCCCCHHHHHHHHHH		24.1626546556
355UbiquitinationDSIIAEVKAQYEDIA
HHHHHHHHHHHHHHH		22.6822817900
358PhosphorylationIAEVKAQYEDIAQKS
HHHHHHHHHHHHHHH		22.0428796482
364UbiquitinationQYEDIAQKSKAEAES
HHHHHHHHHHHHHHH		44.9229967540
366UbiquitinationEDIAQKSKAEAESLY
HHHHHHHHHHHHHHH		58.2329967540
371PhosphorylationKSKAEAESLYQSKYE
HHHHHHHHHHHHHHH		39.1528060719
373PhosphorylationKAEAESLYQSKYEEL
HHHHHHHHHHHHHHH		21.7328060719
375PhosphorylationEAESLYQSKYEELQI
HHHHHHHHHHHHHHC		24.5321082442
376AcetylationAESLYQSKYEELQIT
HHHHHHHHHHHHHCC		40.9526210075
377PhosphorylationESLYQSKYEELQITA
HHHHHHHHHHHHCCC		21.6322817900
383PhosphorylationKYEELQITAGRHGDS
HHHHHHCCCCCCCCC		15.3120860994
394PhosphorylationHGDSVRNSKIEISEL
CCCCHHCCCEEHHHH		25.1720068231
395UbiquitinationGDSVRNSKIEISELN
CCCHHCCCEEHHHHH		48.1629967540
399PhosphorylationRNSKIEISELNRVIQ
HCCCEEHHHHHHHHH		24.2020068231
417UbiquitinationSEIDNVKKQISNLQQ
HHHHHHHHHHHHHHH		48.8929967540
427PhosphorylationSNLQQSISDAEQRGE
HHHHHHHHHHHHHHH		35.69-
443UbiquitinationALKDAKNKLNDLEDA
HHHHHHHHHHHHHHH		48.2121853274
465PhosphorylationLARLLRDYQELMNTK
HHHHHHHHHHHHHHH		9.4622210691
471PhosphorylationDYQELMNTKLALDLE
HHHHHHHHHHHHHHH		17.3022210691
472UbiquitinationYQELMNTKLALDLEI
HHHHHHHHHHHHHHH		27.1033845483
491PhosphorylationTLLEGEESRMSGECA
HHHCCCHHHCCCCCC		29.0521815630
494PhosphorylationEGEESRMSGECAPNV
CCCHHHCCCCCCCCE		30.2619060867
502PhosphorylationGECAPNVSVSVSTSH
CCCCCCEEEEEEECC		18.4722817900
507PhosphorylationNVSVSVSTSHTTISG
CEEEEEEECCCEEEC		23.5222817900
517PhosphorylationTTISGGGSRGGGGGG
CEEECCCCCCCCCCC		30.90-
518MethylationTISGGGSRGGGGGGY
EEECCCCCCCCCCCC		51.5658858093
527O-linked_GlycosylationGGGGGYGSGGSSYGS
CCCCCCCCCCCCCCC		31.3428510447
530PhosphorylationGGYGSGGSSYGSGGG
CCCCCCCCCCCCCCC		24.74-
532PhosphorylationYGSGGSSYGSGGGSY
CCCCCCCCCCCCCCC		19.60-
534PhosphorylationSGGSSYGSGGGSYGS
CCCCCCCCCCCCCCC		26.49-
538O-linked_GlycosylationSYGSGGGSYGSGGGG
CCCCCCCCCCCCCCC		29.6028510447
539PhosphorylationYGSGGGSYGSGGGGG
CCCCCCCCCCCCCCC		20.7022817900
541PhosphorylationSGGGSYGSGGGGGGG
CCCCCCCCCCCCCCC		26.49-
551PhosphorylationGGGGGRGSYGSGGSS
CCCCCCCCCCCCCCC		25.5923286773
552PhosphorylationGGGGRGSYGSGGSSY
CCCCCCCCCCCCCCC		20.3823286773
554PhosphorylationGGRGSYGSGGSSYGS
CCCCCCCCCCCCCCC		31.5723286773
557PhosphorylationGSYGSGGSSYGSGGG
CCCCCCCCCCCCCCC		24.7423286773
558PhosphorylationSYGSGGSSYGSGGGS
CCCCCCCCCCCCCCC		36.4723286773
559PhosphorylationYGSGGSSYGSGGGSY
CCCCCCCCCCCCCCC		19.60-
561PhosphorylationSGGSSYGSGGGSYGS
CCCCCCCCCCCCCCC		26.4925022875
565PhosphorylationSYGSGGGSYGSGGGG
CCCCCCCCCCCCCCC		29.6021082442
566PhosphorylationYGSGGGSYGSGGGGG
CCCCCCCCCCCCCCC		20.7018083107
568PhosphorylationSGGGSYGSGGGGGGH
CCCCCCCCCCCCCCC		26.49-
577PhosphorylationGGGGGHGSYGSGSSS
CCCCCCCCCCCCCCC		22.2025022875
578PhosphorylationGGGGHGSYGSGSSSG
CCCCCCCCCCCCCCC		21.6530576142
580PhosphorylationGGHGSYGSGSSSGGY
CCCCCCCCCCCCCCC		27.5425022875
582PhosphorylationHGSYGSGSSSGGYRG
CCCCCCCCCCCCCCC		24.0323286773
583PhosphorylationGSYGSGSSSGGYRGG
CCCCCCCCCCCCCCC		36.2123286773
584PhosphorylationSYGSGSSSGGYRGGS
CCCCCCCCCCCCCCC		37.6223286773
587PhosphorylationSGSSSGGYRGGSGGG
CCCCCCCCCCCCCCC		15.0330576142
588MethylationGSSSGGYRGGSGGGG
CCCCCCCCCCCCCCC		46.39-
591PhosphorylationSGGYRGGSGGGGGGS
CCCCCCCCCCCCCCC		36.7723312004
598PhosphorylationSGGGGGGSSGGRGSG
CCCCCCCCCCCCCCC		29.1423312004
599PhosphorylationGGGGGGSSGGRGSGG
CCCCCCCCCCCCCCC		48.8423312004
602MethylationGGGSSGGRGSGGGSS
CCCCCCCCCCCCCCC		39.3697770661
604PhosphorylationGSSGGRGSGGGSSGG
CCCCCCCCCCCCCCC		32.6723312004
608PhosphorylationGRGSGGGSSGGSIGG
CCCCCCCCCCCCCCC		29.1420068231
609PhosphorylationRGSGGGSSGGSIGGR
CCCCCCCCCCCCCCC		50.9121955146
612PhosphorylationGGGSSGGSIGGRGSS
CCCCCCCCCCCCCCC		22.9120068231
616MethylationSGGSIGGRGSSSGGV
CCCCCCCCCCCCCCC		36.2982954615
618PhosphorylationGSIGGRGSSSGGVKS
CCCCCCCCCCCCCCC		21.7029396449
619PhosphorylationSIGGRGSSSGGVKSS
CCCCCCCCCCCCCCC		35.5129396449
620PhosphorylationIGGRGSSSGGVKSSG
CCCCCCCCCCCCCCC		41.0623403867
625PhosphorylationSSSGGVKSSGGSSSV
CCCCCCCCCCCCCCE		31.6329396449
626PhosphorylationSSGGVKSSGGSSSVK
CCCCCCCCCCCCCEE		41.2629396449
629PhosphorylationGVKSSGGSSSVKFVS
CCCCCCCCCCEEEEE		23.9829396449
636PhosphorylationSSSVKFVSTTYSGVT
CCCEEEEEECCCCCC		20.4020068231
637PhosphorylationSSVKFVSTTYSGVTR
CCEEEEEECCCCCCC		25.1728796482
638PhosphorylationSVKFVSTTYSGVTR-
CEEEEEECCCCCCC-		14.2628796482
639PhosphorylationVKFVSTTYSGVTR--
EEEEEECCCCCCC--		11.9728796482
640PhosphorylationKFVSTTYSGVTR---
EEEEECCCCCCC---		25.3728796482
643PhosphorylationSTTYSGVTR------
EECCCCCCC------		33.9028796482
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C1_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MBL2_HUMANMBL2physical
11549596
LORI_HUMANLORphysical
8999895
KNG1_HUMANKNG1physical
10066772
CCNA2_HUMANCCNA2physical
17361108
K1C10_HUMANKRT10physical
26344197
K22E_HUMANKRT2physical
26344197
K2C5_HUMANKRT5physical
26344197
K2C1B_HUMANKRT77physical
26344197
TRY1_HUMANPRSS1physical
26344197
Drug and Disease Associations
Kegg Disease
H00691 Epidermolytic hyperkeratosis (EHK); Bullous congenital ichthyosiform erythroderma (BCIE)
H00707 Ichthyosis hystrix, Curth-Macklin type
H00717 Striate palmoplantar keratoderma
H00722 Epidermolytic palmoplantar keratoderma (EPPK)
OMIM Disease
113800Epidermolytic hyperkeratosis (EHK)
146590Ichthyosis hystrix, Curth-Macklin type (IHCM)
600962Keratoderma, palmoplantar, non-epidermolytic (NEPPK)
607602Ichthyosis annular epidermolytic (AEI)
607654Keratoderma, palmoplantar, striate 3 (SPPK3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of K2C1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-66, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-295 AND THR-297, ANDMASS SPECTROMETRY.

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