dbPTM

PERL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PERL_HUMAN
UniProt AC	P22079
Protein Name	Lactoperoxidase
Gene Name	LPO
Organism	Homo sapiens (Human).
Sequence Length	712
Subcellular Localization	Secreted .
Protein Description	Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN) (By similarity). May contribute to airway host defense against infection..
Protein Sequence	MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAMSSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTTARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAFVQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDENYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQPTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGLYGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDSLQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	HLPALLASLILLQAA HHHHHHHHHHHHHHH	18.86	24043423
22	Phosphorylation	ILLQAAASTTRAQTT HHHHHHHHCCCHHHH	26.11	24043423
35	Phosphorylation	TTRTSAISDTVSQAK HHCHHHHHHHHHHHH	27.26	21712546
39	Phosphorylation	SAISDTVSQAKVQVN HHHHHHHHHHHHHHH	26.89	21712546
58	Phosphorylation	DSRTRLKTAMSSETP HHHHHHHHHHCCCCC	31.98	29978859
61	Phosphorylation	TRLKTAMSSETPTSR HHHHHHHCCCCCCHH	23.66	21299198
62	Phosphorylation	RLKTAMSSETPTSRQ HHHHHHCCCCCCHHH	32.19	29978859
64	Phosphorylation	KTAMSSETPTSRQLS HHHHCCCCCCHHHHH	33.54	21299198
66	Phosphorylation	AMSSETPTSRQLSEY HHCCCCCCHHHHHHH	43.92	21299198
67	Phosphorylation	MSSETPTSRQLSEYL HCCCCCCHHHHHHHH	21.16	21299198
71	Phosphorylation	TPTSRQLSEYLKHAK CCCHHHHHHHHHHCC	18.83	29978859
73	Phosphorylation	TSRQLSEYLKHAKGR CHHHHHHHHHHCCCC	20.06	23532336
106	N-linked_Glycosylation	RQKASLTNVTDPSLD HHHHCCCCCCCCCCC	39.73	17623646
106	N-linked_Glycosylation	RQKASLTNVTDPSLD HHHHCCCCCCCCCCC	39.73	UniProtKB CARBOHYD
168	Phosphorylation	ARWLPAEYEDGLSLP HHHCCCCCCCCCCCC	22.79	-
173	Phosphorylation	AEYEDGLSLPFGWTP CCCCCCCCCCCCCCC	39.25	-
212	N-linked_Glycosylation	EEGVLDQNRSLLFMQ CCCCCCCCCEEEEEE	34.86	17623646
212	N-linked_Glycosylation	EEGVLDQNRSLLFMQ CCCCCCCCCEEEEEE	34.86	16740002
315	Phosphorylation	FVYSSEPSLASRLRN HHHCCCHHHHHHHHH	32.30	-
322	N-linked_Glycosylation	SLASRLRNLSSPLGL HHHHHHHHCCCCCCE	49.19	UniProtKB CARBOHYD
324	Phosphorylation	ASRLRNLSSPLGLMA HHHHHHCCCCCCEEE	33.20	26074081
325	Phosphorylation	SRLRNLSSPLGLMAV HHHHHCCCCCCEEEC	27.58	26074081
337	Phosphorylation	MAVNQEVSDHGLPYL EECCCCHHHCCCCCC	24.12	26074081
343	Phosphorylation	VSDHGLPYLPYDSKK HHHCCCCCCCCCCCC	25.92	26074081
346	Phosphorylation	HGLPYLPYDSKKPSP CCCCCCCCCCCCCCC	30.19	26074081
348	Phosphorylation	LPYLPYDSKKPSPCE CCCCCCCCCCCCCCC	36.41	26074081
358	N-linked_Glycosylation	PSPCEFINTTARVPC CCCCCCCCCCCCCCE	36.38	16740002
358	N-linked_Glycosylation	PSPCEFINTTARVPC CCCCCCCCCCCCCCE	36.38	18780401
374	Phosphorylation	LAGDSRASEHILLAT ECCCCCHHHHHHHHH	28.70	-
384	Phosphorylation	ILLATSHTLFLREHN HHHHHCHHHHHHHHH	20.97	-
451	Phosphorylation	PYQGYSESVDPRISN CCCCCCCCCCHHHHH	26.36	-
461	Phosphorylation	PRISNVFTFAFRFGH HHHHHHEEEEECCCC	15.12	-
482	Nitration	MFRLDENYQPWGPEP HEEECCCCCCCCCCC	17.57	-
521	Phosphorylation	RGLLAKKSKLMKQNK HHHHHHHHHHHHHCC	30.25	-
537	Acetylation	MTGELRNKLFQPTHR CCHHHHHHHCCCCCC	44.22	11794753
677	Phosphorylation	VCDNTRITKVPRDPF ECCCCCCEECCCCCC	23.77	27174698
705	Phosphorylation	AIDKLDLSPWASVKN HHCCCCCCCCCCCCC	20.33	-

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 PERL_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

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

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry."; Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; Proteomics 8:3833-3847(2008). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-358, AND MASSSPECTROMETRY.	18780401 [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-212 AND ASN-358, AND MASSSPECTROMETRY.	16740002 [Abstract]