K2C80_HUMAN - dbPTM
K2C80_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID K2C80_HUMAN
UniProt AC Q6KB66
Protein Name Keratin, type II cytoskeletal 80
Gene Name KRT80
Organism Homo sapiens (Human).
Sequence Length 452
Subcellular Localization
Protein Description
Protein Sequence MACRSCVVGFSSLSSCEVTPVGSPRPGTSGWDSCRAPGPGFSSRSLTGCWSAGTISKVTVNPGLLVPLDVKLDPAVQQLKNQEKEEMKALNDKFASLIGKVQALEQRNQLLETRWSFLQGQDSAIFDLGHLYEEYQGRLQEELRKVSQERGQLEANLLQVLEKVEEFRIRYEDEISKRTDMEFTFVQLKKDLDAECLHRTELETKLKSLESFVELMKTIYEQELKDLAAQVKDVSVTVGMDSRCHIDLSGIVEEVKAQYDAVAARSLEEAEAYSRSQLEEQAARSAEYGSSLQSSRSEIADLNVRIQKLRSQILSVKSHCLKLEENIKTAEEQGELAFQDAKTKLAQLEAALQQAKQDMARQLRKYQELMNVKLALDIEIATYRKLVEGEEGRMDSPSATVVSAVQSRCKTAASRSGLSKAPSRKKKGSKGPVIKITEMSEKYFSQESEVSE
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
5Phosphorylation---MACRSCVVGFSS
---CCCCCCEEECCC		15.9023312004
11PhosphorylationRSCVVGFSSLSSCEV
CCCEEECCCCCCCEE		25.1730576142
12PhosphorylationSCVVGFSSLSSCEVT
CCEEECCCCCCCEEE		29.9729083192
14PhosphorylationVVGFSSLSSCEVTPV
EEECCCCCCCEEECC		34.5830576142
15PhosphorylationVGFSSLSSCEVTPVG
EECCCCCCCEEECCC		21.4229083192
19PhosphorylationSLSSCEVTPVGSPRP
CCCCCEEECCCCCCC		7.0325394399
23PhosphorylationCEVTPVGSPRPGTSG
CEEECCCCCCCCCCC		20.2621712546
28PhosphorylationVGSPRPGTSGWDSCR
CCCCCCCCCCCCCCC		27.0923312004
29PhosphorylationGSPRPGTSGWDSCRA
CCCCCCCCCCCCCCC		43.7521712546
33PhosphorylationPGTSGWDSCRAPGPG
CCCCCCCCCCCCCCC		10.0523312004
45PhosphorylationGPGFSSRSLTGCWSA
CCCCCCCCCCCCCCC		32.0330183078
47PhosphorylationGFSSRSLTGCWSAGT
CCCCCCCCCCCCCCE		31.3821815630
51PhosphorylationRSLTGCWSAGTISKV
CCCCCCCCCCEEEEE		22.3922199227
54PhosphorylationTGCWSAGTISKVTVN
CCCCCCCEEEEEEEC		23.0722199227
59PhosphorylationAGTISKVTVNPGLLV
CCEEEEEEECCCCEE		20.5020860994
71 (in isoform 1)Ubiquitination-47.0021906983
71UbiquitinationLLVPLDVKLDPAVQQ
CEEEEECCCCHHHHH		47.0021906983
71 (in isoform 2)Ubiquitination-47.0021906983
71SumoylationLLVPLDVKLDPAVQQ
CEEEEECCCCHHHHH		47.00-
71SumoylationLLVPLDVKLDPAVQQ
CEEEEECCCCHHHHH		47.00-
80UbiquitinationDPAVQQLKNQEKEEM
CHHHHHHHHHHHHHH		52.8529967540
88SumoylationNQEKEEMKALNDKFA
HHHHHHHHHHHHHHH		53.66-
88SumoylationNQEKEEMKALNDKFA
HHHHHHHHHHHHHHH		53.66-
88UbiquitinationNQEKEEMKALNDKFA
HHHHHHHHHHHHHHH		53.6623503661
93SumoylationEMKALNDKFASLIGK
HHHHHHHHHHHHHHH		41.58-
93UbiquitinationEMKALNDKFASLIGK
HHHHHHHHHHHHHHH		41.5821987572
93 (in isoform 1)Ubiquitination-41.5821906983
93 (in isoform 2)Ubiquitination-41.5821906983
93SumoylationEMKALNDKFASLIGK
HHHHHHHHHHHHHHH		41.58-
96PhosphorylationALNDKFASLIGKVQA
HHHHHHHHHHHHHHH		24.5328555341
100UbiquitinationKFASLIGKVQALEQR
HHHHHHHHHHHHHHH		24.9521987572
100 (in isoform 2)Ubiquitination-24.95-
171PhosphorylationVEEFRIRYEDEISKR
HHHHCHHCHHHHHHC		25.9224114839
190UbiquitinationFTFVQLKKDLDAECL
EEEEEECCCCCHHHH		72.6029967540
205UbiquitinationHRTELETKLKSLESF
HHHHHHHHHHHHHHH		44.5429967540
225UbiquitinationTIYEQELKDLAAQVK
HHHHHHHHHHHHHCC		50.3629967540
235PhosphorylationAAQVKDVSVTVGMDS
HHHCCCEEEEECCCC		23.3928674419
242PhosphorylationSVTVGMDSRCHIDLS
EEEECCCCCCEEECC		28.1028674419
256UbiquitinationSGIVEEVKAQYDAVA
CHHHHHHHHHHCHHH		32.8129967540
259PhosphorylationVEEVKAQYDAVAARS
HHHHHHHHCHHHHHC		15.6628674419
266PhosphorylationYDAVAARSLEEAEAY
HCHHHHHCHHHHHHH		35.0921815630
273PhosphorylationSLEEAEAYSRSQLEE
CHHHHHHHCHHHHHH		8.9821406692
274PhosphorylationLEEAEAYSRSQLEEQ
HHHHHHHCHHHHHHH		32.2921406692
276PhosphorylationEAEAYSRSQLEEQAA
HHHHHCHHHHHHHHH		32.9328555341
288PhosphorylationQAARSAEYGSSLQSS
HHHHHHHHHHHHHHC		23.2528674419
315PhosphorylationKLRSQILSVKSHCLK
HHHHHHHHHHHHHHH		29.1824719451
317UbiquitinationRSQILSVKSHCLKLE
HHHHHHHHHHHHHHH		30.9829967540
322UbiquitinationSVKSHCLKLEENIKT
HHHHHHHHHHHHHHH		60.2829967540
328UbiquitinationLKLEENIKTAEEQGE
HHHHHHHHHHHHHHH		53.9529967540
342UbiquitinationELAFQDAKTKLAQLE
HHHHHHHHHHHHHHH		55.2529967540
344UbiquitinationAFQDAKTKLAQLEAA
HHHHHHHHHHHHHHH		40.9129967540
356SumoylationEAALQQAKQDMARQL
HHHHHHHHHHHHHHH		42.36-
356SumoylationEAALQQAKQDMARQL
HHHHHHHHHHHHHHH		42.36-
364MethylationQDMARQLRKYQELMN
HHHHHHHHHHHHHHC		27.57115387097
366PhosphorylationMARQLRKYQELMNVK
HHHHHHHHHHHHCHH		10.7720068231
396PhosphorylationGEEGRMDSPSATVVS
CCCCCCCCCHHHHHH		16.0621712546
398PhosphorylationEGRMDSPSATVVSAV
CCCCCCCHHHHHHHH		40.2921815630
400PhosphorylationRMDSPSATVVSAVQS
CCCCCHHHHHHHHHH		26.2721815630
403PhosphorylationSPSATVVSAVQSRCK
CCHHHHHHHHHHHHH		20.5622199227
407PhosphorylationTVVSAVQSRCKTAAS
HHHHHHHHHHHHHHH		32.8020068231
407 (in isoform 2)Phosphorylation-32.8020068231
414 (in isoform 2)Phosphorylation-25.23-
416PhosphorylationCKTAASRSGLSKAPS
HHHHHHHCCCCCCCC		41.4123911959
419PhosphorylationAASRSGLSKAPSRKK
HHHHCCCCCCCCCCC		30.2323911959
420UbiquitinationASRSGLSKAPSRKKK
HHHCCCCCCCCCCCC		70.1629967540
423PhosphorylationSGLSKAPSRKKKGSK
CCCCCCCCCCCCCCC		62.6923532336
429PhosphorylationPSRKKKGSKGPVIKI
CCCCCCCCCCCEEEH		43.2323911959
435SumoylationGSKGPVIKITEMSEK
CCCCCEEEHHHCCHH		43.75-
435SumoylationGSKGPVIKITEMSEK
CCCCCEEEHHHCCHH		43.75-
437PhosphorylationKGPVIKITEMSEKYF
CCCEEEHHHCCHHHH		22.19-
440PhosphorylationVIKITEMSEKYFSQE
EEEHHHCCHHHHCCC		25.3829396449
443PhosphorylationITEMSEKYFSQESEV
HHHCCHHHHCCCCCC		12.3829396449
445PhosphorylationEMSEKYFSQESEVSE
HCCHHHHCCCCCCCC		29.9228355574
448PhosphorylationEKYFSQESEVSE---
HHHHCCCCCCCC---		35.3429396449
451PhosphorylationFSQESEVSE------
HCCCCCCCC------		33.2728355574
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 K2C80_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of K2C80_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 K2C80_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of K2C80_HUMAN !!
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
There are no disease associations of PTM sites.
Regulatory Network of K2C80_HUMAN

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Related Literatures of Post-Translational Modification
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-45 AND SER-396, 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-396, AND MASSSPECTROMETRY.

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