dbPTM

PERE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PERE_HUMAN
UniProt AC	P11678
Protein Name	Eosinophil peroxidase
Gene Name	EPX
Organism	Homo sapiens (Human).
Sequence Length	715
Subcellular Localization	Cytoplasmic granule. Cytoplasmic granules of eosinophils.
Protein Description	Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis..
Protein Sequence	MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARKIMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPFMFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDELRDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLARKFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTKRQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	ALAGVLATLVLAQPC HHHHHHHHHHHHCCC	17.15	24043423
23	Phosphorylation	LAQPCEGTDPASPGA HHCCCCCCCCCCCCC	19.27	24043423
27	Phosphorylation	CEGTDPASPGAVETS CCCCCCCCCCCHHHH	29.29	24043423
33	Phosphorylation	ASPGAVETSVLRDCI CCCCCHHHHHHHHHH	19.96	24043423
34	Phosphorylation	SPGAVETSVLRDCIA CCCCHHHHHHHHHHH	12.97	24043423
52	N-linked_Glycosylation	LLVDAAYNWTQKSIK HHHHHHHHCCHHHHH	30.50	UniProtKB CARBOHYD
64	Phosphorylation	SIKQRLRSGSASPMD HHHHHHHCCCCCHHH	41.51	29083192
66	Phosphorylation	KQRLRSGSASPMDLL HHHHHCCCCCHHHHH	27.16	29083192
68	Phosphorylation	RLRSGSASPMDLLSY HHHCCCCCHHHHHHH	23.58	24719451
74	Phosphorylation	ASPMDLLSYFKQPVA CCHHHHHHHCCCCHH	35.50	29083192
75	Phosphorylation	SPMDLLSYFKQPVAA CHHHHHHHCCCCHHC	18.11	29083192
83	Phosphorylation	FKQPVAATRTVVRAA CCCCHHCCHHHHHHH	19.69	24719451
113	N-linked_Glycosylation	PQRSGPFNVTDVLTE CCCCCCCCHHHCCCH	38.62	UniProtKB CARBOHYD
149	Phosphorylation	SDKYRTITGRCNNKR CHHHHHHHCCCCCCC	20.26	27282143
175	Phosphorylation	ARWLPAEYEDGLSLP HHHCCCCCCCCCCCC	22.79	-
180	Phosphorylation	AEYEDGLSLPFGWTP CCCCCCCCCCCCCCC	39.25	-
320	Phosphorylation	MVYGSEVSLSLRLRN HHHCCCEEEEEEECC	14.27	17081983
322	Phosphorylation	YGSEVSLSLRLRNRT HCCCEEEEEEECCCC	12.16	17081983
327	N-linked_Glycosylation	SLSLRLRNRTNYLGL EEEEEECCCCCCEEE	60.77	UniProtKB CARBOHYD
363	N-linked_Glycosylation	DDPCLLTNRSARIPC CCCCCCCCCCCCCCE	35.56	17623646
363	N-linked_Glycosylation	DDPCLLTNRSARIPC CCCCCCCCCCCCCCE	35.56	UniProtKB CARBOHYD
370	S-nitrosylation	NRSARIPCFLAGDTR CCCCCCCEEECCCCC	3.98	25040305
376	Phosphorylation	PCFLAGDTRSTETPK CEEECCCCCCCCCHH	26.12	29083192
378	Phosphorylation	FLAGDTRSTETPKLA EECCCCCCCCCHHHH	32.46	29083192
379	Phosphorylation	LAGDTRSTETPKLAA ECCCCCCCCCHHHHH	40.36	29083192
431	Phosphorylation	AMVQIITYRDFLPLV HHHHHHHHHHHHHHH	9.58	19702290
451	Phosphorylation	ARRTLGHYRGYCSNV HHHHHCCCCCCCCCC	12.16	23312004
488	Nitrated tyrosine	MFRLDSQYRASAPNS HHHHCHHHCCCCCCC	16.46	-
488	Nitration	MFRLDSQYRASAPNS HHHHCHHHCCCCCCC	16.46	18694936
488	Nitration	MFRLDSQYRASAPNS HHHHCHHHCCCCCCC	16.46	18694936
491	Phosphorylation	LDSQYRASAPNSHVP HCHHHCCCCCCCCCC	34.95	21082442
500	Phosphorylation	PNSHVPLSSAFFASW CCCCCCHHHHHHHHE	17.35	21082442
581	Phosphorylation	WRRFCGLSQPRNLAQ HHHHHCCCCCCCHHH	24.34	24719451
594	Methylation	AQLSRVLKNQDLARK HHHHHHHHCHHHHHH	50.10	-
635	S-nitrosylation	RVGPLLACLFENQFR CHHHHHHHHHHCCHH	4.51	25040305
670	Phosphorylation	RKALSRISLSRIICD HHHHHHHCCHHHHCC	21.12	20068231
672	Phosphorylation	ALSRISLSRIICDNT HHHHHCCHHHHCCCC	18.03	29970186
700	N-linked_Glycosylation	IYPRGFVNCSRIPRL CCCCCCCCCCCCCCC	18.78	UniProtKB CARBOHYD
708	N-linked_Glycosylation	CSRIPRLNLSAWRGT CCCCCCCCCCCCCCC	32.98	UniProtKB CARBOHYD

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF41	Q9H4P4	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PERE_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 PERE_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PERE_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
261500	Eosinophil peroxidase deficiency (EPXD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PERE_HUMAN

Related Literatures of Post-Translational Modification

Nitration
Reference	PubMed
"Post-translational tyrosine nitration of eosinophil granule toxinsmediated by eosinophil peroxidase."; Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N.,Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H.,Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M.,Doering G.; J. Biol. Chem. 283:28629-28640(2008). Cited for: FUNCTION, AND NITRATION AT TYR-488.	18694936 [Abstract]