MEPE_HUMAN - dbPTM
MEPE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEPE_HUMAN
UniProt AC Q9NQ76
Protein Name Matrix extracellular phosphoglycoprotein
Gene Name MEPE
Organism Homo sapiens (Human).
Sequence Length 525
Subcellular Localization Secreted, extracellular space, extracellular matrix.
Protein Description Promotes renal phosphate excretion and modulates mineralization..
Protein Sequence MRVFCVGLLLFSVTWAAPTFQPQTEKTKQSCVEEQRQEEKNKDNIGFHHLGKRINQELSSKENIVQERKKDLSLSEASENKGSSKSQNYFTNRQRLNKEYSISNKENTHNGLRMSIYPKSTGNKGFEDGDDAISKLHDQEEYGAALIRNNMQHIMGPVTAIKLLGEENKENTPRNVLNIIPASMNYAKAHSKDKKKPQRDSQAQKSPVKSKSTHRIQHNIDYLKHLSKVKKIPSDFEGSGYTDLQERGDNDISPFSGDGQPFKDIPGKGEATGPDLEGKDIQTGFAGPSEAESTHLDTKKPGYNEIPEREENGGNTIGTRDETAKEADAVDVSLVEGSNDIMGSTNFKELPGREGNRVDAGSQNAHQGKVEFHYPPAPSKEKRKEGSSDAAESTNYNEIPKNGKGSTRKGVDHSNRNQATLNEKQRFPSKGKSQGLPIPSRGLDNEIKNEMDSFNGPSHENIITHGRKYHYVPHRQNNSTRNKGMPQGKGSWGRQPHSNRRFSSRRRDDSSESSDSGSSSESDGD
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
2Phosphorylation------MRVFCVGLL
------CCCCHHHHH
30.1624719451
4Phosphorylation----MRVFCVGLLLF
----CCCCHHHHHHH
1.6524719451
8PhosphorylationMRVFCVGLLLFSVTW
CCCCHHHHHHHHHHH
1.5524719451
59PhosphorylationKRINQELSSKENIVQ
HHHHHHHHHHHHHHH
38.3124505115
60PhosphorylationRINQELSSKENIVQE
HHHHHHHHHHHHHHH
57.5224505115
73PhosphorylationQERKKDLSLSEASEN
HHHHHHCCHHHHHCC
39.7323532336
100PhosphorylationRQRLNKEYSISNKEN
HHHHCCHHCCCCCCC
16.9529978859
101PhosphorylationQRLNKEYSISNKENT
HHHCCHHCCCCCCCC
22.1929978859
103PhosphorylationLNKEYSISNKENTHN
HCCHHCCCCCCCCCC
35.5929978859
108PhosphorylationSISNKENTHNGLRMS
CCCCCCCCCCCEEEE
20.1529978859
115PhosphorylationTHNGLRMSIYPKSTG
CCCCEEEEEECCCCC
16.7324719451
117PhosphorylationNGLRMSIYPKSTGNK
CCEEEEEECCCCCCC
9.4124719451
121PhosphorylationMSIYPKSTGNKGFED
EEEECCCCCCCCCCC
51.4024719451
172PhosphorylationGEENKENTPRNVLNI
CCCCCCCCCCHHHHH
25.39-
477N-linked_GlycosylationHYVPHRQNNSTRNKG
ECCCCCCCCCCCCCC
44.36UniProtKB CARBOHYD
478N-linked_GlycosylationYVPHRQNNSTRNKGM
CCCCCCCCCCCCCCC
36.10UniProtKB CARBOHYD
498PhosphorylationSWGRQPHSNRRFSSR
CCCCCCCCCCCCCCC
38.42-
504PhosphorylationHSNRRFSSRRRDDSS
CCCCCCCCCCCCCCC
27.39-
514PhosphorylationRDDSSESSDSGSSSE
CCCCCCCCCCCCCCC
31.57-
516PhosphorylationDSSESSDSGSSSESD
CCCCCCCCCCCCCCC
42.39-
518PhosphorylationSESSDSGSSSESDGD
CCCCCCCCCCCCCCC
34.3424114839
519PhosphorylationESSDSGSSSESDGD-
CCCCCCCCCCCCCC-
41.4724114839
520PhosphorylationSSDSGSSSESDGD--
CCCCCCCCCCCCC--
42.7024114839
522PhosphorylationDSGSSSESDGD----
CCCCCCCCCCC----
49.1724114839

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 MEPE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEPE_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 MEPE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHK1_HUMANCHEK1physical
19808933
FINC_HUMANFN1physical
28514442
TOM34_HUMANTOMM34physical
28514442
LRP2_HUMANLRP2physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MEPE_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP