dbPTM

PERM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PERM_HUMAN
UniProt AC	P05164
Protein Name	Myeloperoxidase
Gene Name	MPO
Organism	Homo sapiens (Human).
Sequence Length	745
Subcellular Localization	Lysosome.
Protein Description	Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity..
Protein Sequence	MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MGVPFFSSLRCMVDL CCCCCHHCCEEEEEC	18.06	24719451
90	Phosphorylation	SIKQRLRSGSASPME HHHHHHHCCCCCHHH	41.51	23532336
92	Phosphorylation	KQRLRSGSASPMELL HHHHHCCCCCHHHHH	27.16	28450419
94	Phosphorylation	RLRSGSASPMELLSY HHHCCCCCHHHHHHH	26.86	28857561
103	Acetylation	MELLSYFKQPVAATR HHHHHHHHCCHHCCH	45.52	61193
132	Phosphorylation	LLERKLRSLWRRPFN HHHHHHHHHHCCCCC	42.60	24719451
139	N-linked_Glycosylation	SLWRRPFNVTDVLTP HHHCCCCCHHHCCCH	38.16	16335952
172	Acetylation	VTCPEQDKYRTITGM CCCCCCCCCHHHHHH	36.00	26822725
187	Phosphorylation	CNNRRSPTLGASNRA CCCCCCCCCCCCCCH	38.79	23312004
191	Phosphorylation	RSPTLGASNRAFVRW CCCCCCCCCCHHEEE	25.67	23312004
231	Phosphorylation	VALARAVSNEIVRFP HHHHHHHHCCCCCCC	27.97	24247654
316	Sulfation	CIPFFRSCPACPGSN CCHHHHCCCCCCCCC	1.84	7840679
316	Oxidation	CIPFFRSCPACPGSN CCHHHHCCCCCCCCC	1.84	7840679
316	Cysteine sulfenic acid (-SOH)	CIPFFRSCPACPGSN CCHHHHCCCCCCCCC	1.84	-
322	O-linked_Glycosylation	SCPACPGSNITIRNQ CCCCCCCCCCCHHHH	15.36	28657654
323	N-linked_Glycosylation	CPACPGSNITIRNQI CCCCCCCCCCHHHHH	41.14	16740002
323	N-linked_Glycosylation	CPACPGSNITIRNQI CCCCCCCCCCHHHHH	41.14	20332087
355	N-linked_Glycosylation	PLARNLRNMSNQLGL HHHHHHHHHHHHHCH	41.21	1334087
355	N-linked_Glycosylation	PLARNLRNMSNQLGL HHHHHHHHHHHHHCH	41.21	1334087
357	Phosphorylation	ARNLRNMSNQLGLLA HHHHHHHHHHHCHHH	25.60	25278378
391	N-linked_Glycosylation	DDPCLLTNRSARIPC CCCCCCCCCCCCCCE	35.56	1334087
391	N-linked_Glycosylation	DDPCLLTNRSARIPC CCCCCCCCCCCCCCE	35.56	1334087
428	Phosphorylation	REHNRLATELKSLNP HHHHHHHHHHHHHCC	46.58	20736484
432	Phosphorylation	RLATELKSLNPRWDG HHHHHHHHHCCCCCH	46.10	-
470	Phosphorylation	LPLVLGPTAMRKYLP HHHHHCHHHHHHHCC	31.15	27499020
481	Phosphorylation	KYLPTYRSYNDSVDP HHCCCCCCCCCCCCH	20.20	23403867
482	Phosphorylation	YLPTYRSYNDSVDPR HCCCCCCCCCCCCHH	17.62	23403867
483	N-linked_Glycosylation	LPTYRSYNDSVDPRI CCCCCCCCCCCCHHH	36.01	16740002
500	Phosphorylation	VFTNAFRYGHTLIQP HHHHHHHHCCCCHHC	13.55	18083107
516	Phosphorylation	MFRLDNRYQPMEPNP HEECCCCCCCCCCCC	24.19	29083192
516	Nitrated tyrosine	MFRLDNRYQPMEPNP HEECCCCCCCCCCCC	24.19	-
528	Phosphorylation	PNPRVPLSRVFFASW CCCCCCHHHHHHHEH	21.96	-
625	Sumoylation	GTVLRNLKLARKLME HHHHHHHHHHHHHHH	43.58	-
625	Sumoylation	GTVLRNLKLARKLME HHHHHHHHHHHHHHH	43.58	-
687	Phosphorylation	WENEGVFSMQQRQAL CCCCCCCCHHHHHHH	17.18	29802988
698	Phosphorylation	RQALAQISLPRIICD HHHHHHCCCCEEECC	21.90	24719451
707	Phosphorylation	PRIICDNTGITTVSK CEEECCCCCCEEEEC	19.40	29978859
710	Phosphorylation	ICDNTGITTVSKNNI ECCCCCCEEEECCCE	23.61	29978859
711	Phosphorylation	CDNTGITTVSKNNIF CCCCCCEEEECCCEE	22.36	29978859
713	Phosphorylation	NTGITTVSKNNIFMS CCCCEEEECCCEECC	27.81	29978859
720	Phosphorylation	SKNNIFMSNSYPRDF ECCCEECCCCCCCCC	16.33	21552520
723	Phosphorylation	NIFMSNSYPRDFVNC CEECCCCCCCCCCCC	13.41	21552520
729	N-linked_Glycosylation	SYPRDFVNCSTLPAL CCCCCCCCCCCCCCC	17.64	20332087
729	N-linked_Glycosylation	SYPRDFVNCSTLPAL CCCCCCCCCCCCCCC	17.64	17623646

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 PERM_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
254600	Myeloperoxidase deficiency (MPOD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PERM_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-355 AND ASN-391, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry."; Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.; J. Proteome Res. 5:1493-1503(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483, AND MASSSPECTROMETRY.	16740002 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Glycosylation pattern of mature dimeric leukocyte and recombinantmonomeric myeloperoxidase: glycosylation is required for optimalenzymatic activity."; Van Antwerpen P., Slomianny M.C., Boudjeltia K.Z., Delporte C.,Faid V., Calay D., Rousseau A., Moguilevsky N., Raes M., Vanhamme L.,Furtmueller P.G., Obinger C., Vanhaeverbeek M., Neve J.,Michalski J.C.; J. Biol. Chem. 285:16351-16359(2010). Cited for: PROTEIN SEQUENCE OF 49-53, SUBUNIT, GLYCOSYLATION AT ASN-323; ASN-355;ASN-391; ASN-483 AND ASN-729, AND MASS SPECTROMETRY.	20332087 [Abstract]