KRT84_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KRT84_HUMAN
• UniProt AC: Q9NSB2
• Protein Name: Keratin, type II cuticular Hb4
• Gene Name: KRT84
• Organism: Homo sapiens (Human).
• Sequence Length: 600
• Protein Sequence: MSCRSYRVSSGHRVGNFSSCSAMTPQNLNRFRANSVSCWSGPGFRGLGSFGSRSVITFGSYSPRIAAVGSRPIHCGVRFGAGCGMGFGDGRGVGLGPRADSCVGLGFGAGSGIGYGFGGPGFGYRVGGVGVPAAPSITAVTVNKSLLTPLNLEIDPNAQRVKKDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCIRSNLEPLFESYITNLRRQLEVLVSDQARLQAERNHLQDVLEGFKKKYEEEVVCRANAENEFVALKKDVDAAFMNKSDLEANVDTLTQEIDFLKTLYMEEIQLLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVARRSRADAEAWYQTKYEEMQVTAGQHCDNLRNIRNEINELTRLIQRLKAEIEHAKAQRAKLEAAVAEAEQQGEATLSDAKCKLADLECALQQAKQDMARQLCEYQELMNAKLGLDIEIATYRRLLEGEESRLCEGVGPVNISVSSSRGGLVCGPEPLVAGSTLSRGGVTFSGSSSVCATSGVLASCGPSLGGARVAPATGDLLSTGTRSGSMLISEACVPSVPCPLPTQGGFSSCSGGRSSSVRFVSTTTSCRTKY

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
2	Phosphorylation	------MSCRSYRVS ------CCCCEEEEC	20.45	-
60	Phosphorylation	RSVITFGSYSPRIAA CEEEEECCCCCCEEE	20.46	20860994
62	Phosphorylation	VITFGSYSPRIAAVG EEEECCCCCCEEEEC	14.92	24719451
70	Phosphorylation	PRIAAVGSRPIHCGV CCEEEECCCCCCCCC	28.43	20860994
138	Phosphorylation	VPAAPSITAVTVNKS CCCCCCEEEEEECCH	21.29	28674151
141	Phosphorylation	APSITAVTVNKSLLT CCCEEEEEECCHHHC	18.85	28674151
163	Ubiquitination	PNAQRVKKDEKEQIK CCCCCCCCCHHHHHH	69.16	-
166	Ubiquitination	QRVKKDEKEQIKTLN CCCCCCHHHHHHHHH	66.12	22817900
170	Ubiquitination	KDEKEQIKTLNNKFA CCHHHHHHHHHHHHH	46.80	21906983
171	Phosphorylation	DEKEQIKTLNNKFAS CHHHHHHHHHHHHHH	36.03	24719451
175	Ubiquitination	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	21963094
175	Sumoylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	-
175	Neddylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	32015554
175	Methylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	133015
175	Acetylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	133015
175	Sumoylation	QIKTLNNKFASFIDK HHHHHHHHHHHHHHH	41.03	-
178	Phosphorylation	TLNNKFASFIDKVRF HHHHHHHHHHHHHHH	26.35	28355574
182	Ubiquitination	KFASFIDKVRFLEQQ HHHHHHHHHHHHHHH	30.41	21906983
182	Acetylation	KFASFIDKVRFLEQQ HHHHHHHHHHHHHHH	30.41	7706145
191	Ubiquitination	RFLEQQNKLLETKWS HHHHHHHHHHHHHHH	50.54	22817900
196	Ubiquitination	QNKLLETKWSFLQEQ HHHHHHHHHHHHHHH	31.31	22817900
341	Phosphorylation	IAEVKAQYEEVARRS HHHHHHHHHHHHHHH	20.93	26437602
360	Phosphorylation	EAWYQTKYEEMQVTA HHHHHHHHHHEEECC	22.10	-
438	Sumoylation	ECALQQAKQDMARQL HHHHHHHHHHHHHHH	42.36	-
438	Sumoylation	ECALQQAKQDMARQL HHHHHHHHHHHHHHH	42.36	-
455	Methylation	YQELMNAKLGLDIEI HHHHHHHHCCCCEEH	37.78	-
455	"N6,N6-dimethyllysine"	YQELMNAKLGLDIEI HHHHHHHHCCCCEEH	37.78	-
474	Phosphorylation	RLLEGEESRLCEGVG HHHCCCHHHCCCCCC	26.67	21815630
586	Phosphorylation	CSGGRSSSVRFVSTT CCCCCCCCEEEEEEC	20.68	30576142
592	Phosphorylation	SSVRFVSTTTSCRTK CCEEEEEECCCCCCC	28.88	25690035
595	Phosphorylation	RFVSTTTSCRTKY-- EEEEECCCCCCCC--	10.25	30576142

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of KRT84_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KRT84_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KRT84_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of KRT84_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.

Related Literatures of Post-Translational Modification

Acetylation

"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-182, AND MASS SPECTROMETRY.
PubMed: 19608861