CPVL_HUMAN - dbPTM
CPVL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPVL_HUMAN
UniProt AC Q9H3G5
Protein Name Probable serine carboxypeptidase CPVL
Gene Name CPVL
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization
Protein Description May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation..
Protein Sequence MVGAMWKVIVSLVLLMPGPCDGLFRSLYRSVSMPPKGDSGQPLFLTPYIEAGKIQKGRELSLVGPFPGLNMKSYAGFLTVNKTYNSNLFFWFFPAQIQPEDAPVVLWLQGGPGGSSMFGLFVEHGPYVVTSNMTLRDRDFPWTTTLSMLYIDNPVGTGFSFTDDTHGYAVNEDDVARDLYSALIQFFQIFPEYKNNDFYVTGESYAGKYVPAIAHLIHSLNPVREVKINLNGIAIGDGYSDPESIIGGYAEFLYQIGLLDEKQKKYFQKQCHECIEHIRKQNWFEAFEILDKLLDGDLTSDPSYFQNVTGCSNYYNFLRCTEPEDQLYYVKFLSLPEVRQAIHVGNQTFNDGTIVEKYLREDTVQSVKPWLTEIMNNYKVLIYNGQLDIIVAAALTERSLMGMDWKGSQEYKKAEKKVWKIFKSDSEVAGYIRQAGDFHQVIIRGGGHILPYDQPLRAFDMINRFIYGKGWDPYVG
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
26PhosphorylationPCDGLFRSLYRSVSM
CCCHHHHHHHHHCCC
23.5530622161
28PhosphorylationDGLFRSLYRSVSMPP
CHHHHHHHHHCCCCC
11.3330622161
30PhosphorylationLFRSLYRSVSMPPKG
HHHHHHHHCCCCCCC
12.6530622161
32PhosphorylationRSLYRSVSMPPKGDS
HHHHHHCCCCCCCCC
27.1530622161
39PhosphorylationSMPPKGDSGQPLFLT
CCCCCCCCCCCCEEE
48.2530622161
46PhosphorylationSGQPLFLTPYIEAGK
CCCCCEEECEEECCC
13.5030622161
48PhosphorylationQPLFLTPYIEAGKIQ
CCCEEECEEECCCCC
13.2230622161
53UbiquitinationTPYIEAGKIQKGREL
ECEEECCCCCCCCEE
49.35-
73PhosphorylationFPGLNMKSYAGFLTV
CCCCCCCCEEEEEEE
14.94-
74PhosphorylationPGLNMKSYAGFLTVN
CCCCCCCEEEEEEEC
12.77-
79PhosphorylationKSYAGFLTVNKTYNS
CCEEEEEEECCCCCC
21.55-
81N-linked_GlycosylationYAGFLTVNKTYNSNL
EEEEEEECCCCCCCE
26.2220068230
81N-linked_GlycosylationYAGFLTVNKTYNSNL
EEEEEEECCCCCCCE
26.2219159218
127PhosphorylationLFVEHGPYVVTSNMT
EEECCCCEEEECCCC
16.4927732954
130PhosphorylationEHGPYVVTSNMTLRD
CCCCEEEECCCCCCC
12.3527732954
131PhosphorylationHGPYVVTSNMTLRDR
CCCEEEECCCCCCCC
17.0027732954
132N-linked_GlycosylationGPYVVTSNMTLRDRD
CCEEEECCCCCCCCC
20.3519159218
134PhosphorylationYVVTSNMTLRDRDFP
EEEECCCCCCCCCCC
23.9227732954
269UbiquitinationKQKKYFQKQCHECIE
HHHHHHHHHHHHHHH
45.02-
280UbiquitinationECIEHIRKQNWFEAF
HHHHHHHHCCHHHHH
47.5921890473
280UbiquitinationECIEHIRKQNWFEAF
HHHHHHHHCCHHHHH
47.5921890473
307N-linked_GlycosylationSDPSYFQNVTGCSNY
CCCHHHHCCCCCCCC
24.34UniProtKB CARBOHYD
320GlutathionylationNYYNFLRCTEPEDQL
CCCCCCCCCCCCCCE
5.7122555962
331UbiquitinationEDQLYYVKFLSLPEV
CCCEEEEEECCCHHH
25.1921890473
331UbiquitinationEDQLYYVKFLSLPEV
CCCEEEEEECCCHHH
25.1921890473
346N-linked_GlycosylationRQAIHVGNQTFNDGT
HHHHCCCCCCCCCCC
36.3119159218
348O-linked_GlycosylationAIHVGNQTFNDGTIV
HHCCCCCCCCCCCCC
28.5330059200
383PhosphorylationNNYKVLIYNGQLDII
HCEEEEEECCCHHHH
14.74-
406UbiquitinationSLMGMDWKGSQEYKK
HHCCCCCCCCHHHHH
44.41-
411PhosphorylationDWKGSQEYKKAEKKV
CCCCCHHHHHHHHHH
15.34-
423UbiquitinationKKVWKIFKSDSEVAG
HHHHHHHCCHHHHHH
57.7521890473
423UbiquitinationKKVWKIFKSDSEVAG
HHHHHHHCCHHHHHH
57.7521890473
469UbiquitinationINRFIYGKGWDPYVG
HHHHHHCCCCCCCCC
39.60-

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 CPVL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPVL_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 CPVL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NB5R3_HUMANCYB5R3physical
26186194
5NT3A_HUMANNT5C3Aphysical
26186194
F162A_HUMANFAM162Aphysical
26186194
QSOX2_HUMANQSOX2physical
26186194
OCAD1_HUMANOCIAD1physical
26186194
TM177_HUMANTMEM177physical
26186194
MANEA_HUMANMANEAphysical
26186194
MICU1_HUMANMICU1physical
26186194
NAT14_HUMANNAT14physical
26186194
NB5R3_HUMANCYB5R3physical
28514442
NAT14_HUMANNAT14physical
28514442
ABD12_HUMANABHD12physical
28514442
5NT3A_HUMANNT5C3Aphysical
28514442
OCAD1_HUMANOCIAD1physical
28514442
TM177_HUMANTMEM177physical
28514442

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 CPVL_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-81; ASN-132 AND ASN-346,AND MASS SPECTROMETRY.

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