K2C7_HUMAN - dbPTM
K2C7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C7_HUMAN
UniProt AC P08729
Protein Name Keratin, type II cytoskeletal 7
Gene Name KRT7
Organism Homo sapiens (Human).
Sequence Length 469
Subcellular Localization Cytoplasm .
Protein Description Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7)..
Protein Sequence MSIHFSSPVFTSRSAAFSGRGAQVRLSSARPGGLGSSSLYGLGASRPRVAVRSAYGGPVGAGIREVTINQSLLAPLRLDADPSLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIFEAQIAGLRGQLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINHRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTLNETELTELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEMAKCSRAEAEAWYQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAALQRGKQDMARQLREYQELMSVKLALDIEIATYRKLLEGEESRLAGDGVGAVNISVMNSTGGSSSGGGIGLTLGGTMGSNALSFSSSAGPGLLKAYSIRTASASRRSARD
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
2Acetylation------MSIHFSSPV
------CCCCCCCCC		25.4419007248
2Phosphorylation------MSIHFSSPV
------CCCCCCCCC		25.4428355574
6Phosphorylation--MSIHFSSPVFTSR
--CCCCCCCCCCCCC		21.4128355574
7Phosphorylation-MSIHFSSPVFTSRS
-CCCCCCCCCCCCCC		24.9228355574
11PhosphorylationHFSSPVFTSRSAAFS
CCCCCCCCCCCHHHC		24.3820860994
12PhosphorylationFSSPVFTSRSAAFSG
CCCCCCCCCCHHHCC		16.8723186163
14PhosphorylationSPVFTSRSAAFSGRG
CCCCCCCCHHHCCCC		24.5823927012
18PhosphorylationTSRSAAFSGRGAQVR
CCCCHHHCCCCCEEE		23.8924719451
20DimethylationRSAAFSGRGAQVRLS
CCHHHCCCCCEEEEC		35.76-
20MethylationRSAAFSGRGAQVRLS
CCHHHCCCCCEEEEC		35.7612017827
25MethylationSGRGAQVRLSSARPG
CCCCCEEEECCCCCC		19.4416288061
27PhosphorylationRGAQVRLSSARPGGL
CCCEEEECCCCCCCC		16.0420201521
28PhosphorylationGAQVRLSSARPGGLG
CCEEEECCCCCCCCC		32.6528355574
31UbiquitinationVRLSSARPGGLGSSS
EEECCCCCCCCCCCH		40.7023503661
36PhosphorylationARPGGLGSSSLYGLG
CCCCCCCCCHHCCCC		23.0723927012
37PhosphorylationRPGGLGSSSLYGLGA
CCCCCCCCHHCCCCC		23.6728355574
37UbiquitinationRPGGLGSSSLYGLGA
CCCCCCCCHHCCCCC		23.6721963094
38PhosphorylationPGGLGSSSLYGLGAS
CCCCCCCHHCCCCCC		27.5828355574
40PhosphorylationGLGSSSLYGLGASRP
CCCCCHHCCCCCCCC		16.5627273156
45PhosphorylationSLYGLGASRPRVAVR
HHCCCCCCCCEEEEE		40.8123927012
46MethylationLYGLGASRPRVAVRS
HCCCCCCCCEEEEEC		23.6254556941
48MethylationGLGASRPRVAVRSAY
CCCCCCCEEEEECCC		28.1054556949
53PhosphorylationRPRVAVRSAYGGPVG
CCEEEEECCCCCCCC		21.1728355574
55PhosphorylationRVAVRSAYGGPVGAG
EEEEECCCCCCCCCC		24.7019534553
67PhosphorylationGAGIREVTINQSLLA
CCCEEEEEECCHHHH		14.9524732914
71PhosphorylationREVTINQSLLAPLRL
EEEEECCHHHHCCCC		22.3624732914
83PhosphorylationLRLDADPSLQRVRQE
CCCCCCHHHHHHHHH		37.3721815630
88UbiquitinationDPSLQRVRQEESEQI
CHHHHHHHHHHHHHH		40.1421987572
92PhosphorylationQRVRQEESEQIKTLN
HHHHHHHHHHHHHHH		33.7728355574
96UbiquitinationQEESEQIKTLNNKFA
HHHHHHHHHHHHHHH		46.8021963094
97PhosphorylationEESEQIKTLNNKFAS
HHHHHHHHHHHHHHH		36.0323186163
101SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03-
101AcetylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03133007
101MethylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03133007
101NeddylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0332015554
101SumoylationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.03-
101UbiquitinationQIKTLNNKFASFIDK
HHHHHHHHHHHHHHH		41.0321963094
104PhosphorylationTLNNKFASFIDKVRF
HHHHHHHHHHHHHHH		26.3528355574
108AcetylationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.417705645
108UbiquitinationKFASFIDKVRFLEQQ
HHHHHHHHHHHHHHH		30.4121963094
109UbiquitinationFASFIDKVRFLEQQN
HHHHHHHHHHHHHHH		4.6721963094
117UbiquitinationRFLEQQNKLLETKWT
HHHHHHHHHHHHHHH		50.5421963094
119UbiquitinationLEQQNKLLETKWTLL
HHHHHHHHHHHHHHH		9.3121963094
122UbiquitinationQNKLLETKWTLLQEQ
HHHHHHHHHHHHHHH		28.8921963094
130SumoylationWTLLQEQKSAKSSRL
HHHHHHHHHHHHCCC		52.18-
130SumoylationWTLLQEQKSAKSSRL
HHHHHHHHHHHHCCC		52.1828112733
130UbiquitinationWTLLQEQKSAKSSRL
HHHHHHHHHHHHCCC		52.1821963094
133UbiquitinationLQEQKSAKSSRLPDI
HHHHHHHHHCCCCHH		56.9322817900
134PhosphorylationQEQKSAKSSRLPDIF
HHHHHHHHCCCCHHH		22.0230087585
135PhosphorylationEQKSAKSSRLPDIFE
HHHHHHHCCCCHHHH		36.8127251275
149UbiquitinationEAQIAGLRGQLEALQ
HHHHHHHHHHEEEEE		29.8721963094
154UbiquitinationGLRGQLEALQVDGGR
HHHHHEEEEEECCCH		16.3421963094
168PhosphorylationRLEAELRSMQDVVED
HHHHHHHHHHHHHHH		33.1628355574
171UbiquitinationAELRSMQDVVEDFKN
HHHHHHHHHHHHHHH		37.4821963094
176UbiquitinationMQDVVEDFKNKYEDE
HHHHHHHHHHHHHHH		6.2622817900
177UbiquitinationQDVVEDFKNKYEDEI
HHHHHHHHHHHHHHC		65.9233845483
179AcetylationVVEDFKNKYEDEINH
HHHHHHHHHHHHCHH		51.0819608861
179UbiquitinationVVEDFKNKYEDEINH
HHHHHHHHHHHHCHH		51.0833845483
180PhosphorylationVEDFKNKYEDEINHR
HHHHHHHHHHHCHHC		37.70-
198UbiquitinationENEFVVLKKDVDAAY
CCEEEEEECCCCHHH		35.0033845483
199AcetylationNEFVVLKKDVDAAYM
CEEEEEECCCCHHHH		59.8419608861
199UbiquitinationNEFVVLKKDVDAAYM
CEEEEEECCCCHHHH		59.8433845483
205PhosphorylationKKDVDAAYMSKVELE
ECCCCHHHHCCCCHH		12.0226356563
207PhosphorylationDVDAAYMSKVELEAK
CCCHHHHCCCCHHHH		22.3726356563
208UbiquitinationVDAAYMSKVELEAKV
CCHHHHCCCCHHHHH		24.1733845483
214UbiquitinationSKVELEAKVDALNDE
CCCCHHHHHHHHHHH		31.1321963094
217UbiquitinationELEAKVDALNDEINF
CHHHHHHHHHHHHHH		15.9722053931
227PhosphorylationDEINFLRTLNETELT
HHHHHHHHCCHHHHH		35.7620044836
231PhosphorylationFLRTLNETELTELQS
HHHHCCHHHHHHHHH		34.9118452278
234PhosphorylationTLNETELTELQSQIS
HCCHHHHHHHHHHHC		28.5420044836
238PhosphorylationTELTELQSQISDTSV
HHHHHHHHHHCCCEE		41.9521815630
241PhosphorylationTELQSQISDTSVVLS
HHHHHHHCCCEEEEE		27.4826657352
243PhosphorylationLQSQISDTSVVLSMD
HHHHHCCCEEEEEEC		19.3424732914
244PhosphorylationQSQISDTSVVLSMDN
HHHHCCCEEEEEECC		18.4121955146
248PhosphorylationSDTSVVLSMDNSRSL
CCCEEEEEECCCCCC		16.6926657352
249SulfoxidationDTSVVLSMDNSRSLD
CCEEEEEECCCCCCC		5.0328183972
252PhosphorylationVVLSMDNSRSLDLDG
EEEEECCCCCCCCCH		20.9821955146
254PhosphorylationLSMDNSRSLDLDGII
EEECCCCCCCCCHHH		26.5128355574
265SumoylationDGIIAEVKAQYEEMA
CHHHHHHHHHHHHHH		22.6828112733
265UbiquitinationDGIIAEVKAQYEEMA
CHHHHHHHHHHHHHH		22.6833845483
268PhosphorylationIAEVKAQYEEMAKCS
HHHHHHHHHHHHHCC		20.7926356563
273UbiquitinationAQYEEMAKCSRAEAE
HHHHHHHHCCHHHHH		31.2821963094
275PhosphorylationYEEMAKCSRAEAEAW
HHHHHHCCHHHHHHH		33.5427251275
283PhosphorylationRAEAEAWYQTKFETL
HHHHHHHHHHHHHHH		17.2226356563
285PhosphorylationEAEAWYQTKFETLQA
HHHHHHHHHHHHHHH		23.2321082442
286SumoylationAEAWYQTKFETLQAQ
HHHHHHHHHHHHHHH		26.1928112733
286UbiquitinationAEAWYQTKFETLQAQ
HHHHHHHHHHHHHHH		26.1921963094
289PhosphorylationWYQTKFETLQAQAGK
HHHHHHHHHHHHCCC		27.5728355574
296AcetylationTLQAQAGKHGDDLRN
HHHHHCCCCHHHHHH		47.6421466224
296SumoylationTLQAQAGKHGDDLRN
HHHHHCCCCHHHHHH		47.6428112733
296UbiquitinationTLQAQAGKHGDDLRN
HHHHHCCCCHHHHHH		47.6421963094
326SumoylationQAEIDNIKNQRAKLE
HHHHHHHHHHHHHHH		53.97-
326UbiquitinationQAEIDNIKNQRAKLE
HHHHHHHHHHHHHHH		53.9721963094
331SumoylationNIKNQRAKLEAAIAE
HHHHHHHHHHHHHHH		49.3928112733
331UbiquitinationNIKNQRAKLEAAIAE
HHHHHHHHHHHHHHH		49.3921963094
348UbiquitinationERGELALKDARAKQE
HHHHHHHHHHHHHHH		43.6721963094
353UbiquitinationALKDARAKQEELEAA
HHHHHHHHHHHHHHH		53.3322817900
365UbiquitinationEAALQRGKQDMARQL
HHHHHHCHHHHHHHH		45.3633845483
375PhosphorylationMARQLREYQELMSVK
HHHHHHHHHHHHHHH		10.8020068231
380PhosphorylationREYQELMSVKLALDI
HHHHHHHHHHHHHHH		28.8220068231
392PhosphorylationLDIEIATYRKLLEGE
HHHHHHHHHHHHCCC		9.2018083107
394SumoylationIEIATYRKLLEGEES
HHHHHHHHHHCCCCH		47.19-
394AcetylationIEIATYRKLLEGEES
HHHHHHHHHHCCCCH		47.1922631317
394NeddylationIEIATYRKLLEGEES
HHHHHHHHHHCCCCH		47.1932015554
394SumoylationIEIATYRKLLEGEES
HHHHHHHHHHCCCCH		47.19-
394UbiquitinationIEIATYRKLLEGEES
HHHHHHHHHHCCCCH		47.1921906983
401PhosphorylationKLLEGEESRLAGDGV
HHHCCCCHHHCCCCC		28.4321815630
414PhosphorylationGVGAVNISVMNSTGG
CCCEEEEEEEECCCC		15.3122210691
419PhosphorylationNISVMNSTGGSSSGG
EEEEEECCCCCCCCC		40.3222210691
423PhosphorylationMNSTGGSSSGGGIGL
EECCCCCCCCCCCEE		35.9628857561
424PhosphorylationNSTGGSSSGGGIGLT
ECCCCCCCCCCCEEE		43.0628857561
435PhosphorylationIGLTLGGTMGSNALS
CEEECCCCCCCCCCC		19.3022210691
438PhosphorylationTLGGTMGSNALSFSS
ECCCCCCCCCCCCCC		14.2222210691
456PhosphorylationPGLLKAYSIRTASAS
CCHHHHHHHHCHHHH		15.5122210691
459PhosphorylationLKAYSIRTASASRRS
HHHHHHHCHHHHHHH		24.2421712546
461PhosphorylationAYSIRTASASRRSAR
HHHHHCHHHHHHHCC		26.6026329039
463PhosphorylationSIRTASASRRSARD-
HHHCHHHHHHHCCC-		26.2326329039
466PhosphorylationTASASRRSARD----
CHHHHHHHCCC----		26.9227282143
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 K2C7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
20RMethylation


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 K2C7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
AP3S1_HUMANAP3S1physical
22863883
COG3_HUMANCOG3physical
22863883
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01087Primaquine
Regulatory Network of K2C7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-296, AND MASSSPECTROMETRY.
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-20, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-254, ANDMASS SPECTROMETRY.
"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-7, 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-7; SER-36; SER-38 ANDSER-53, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND TYR-40, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-375 AND SER-380, ANDMASS SPECTROMETRY.
"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 SER-45, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40 AND TYR-55, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-205, AND MASSSPECTROMETRY.

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