RNLS_HUMAN - dbPTM
RNLS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNLS_HUMAN
UniProt AC Q5VYX0
Protein Name Renalase {ECO:0000303|PubMed:15841207}
Gene Name RNLS
Organism Homo sapiens (Human).
Sequence Length 342
Subcellular Localization Secreted .
Protein Description Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis..
Protein Sequence MAQVLIVGAGMTGSLCAALLRRQTSGPLYLAVWDKAEDSGGRMTTACSPHNPQCTADLGAQYITCTPHYAKKHQRFYDELLAYGVLRPLSSPIEGMVMKEGDCNFVAPQGISSIIKHYLKESGAEVYFRHRVTQINLRDDKWEVSKQTGSPEQFDLIVLTMPVPEILQLQGDITTLISECQRQQLEAVSYSSRYALGLFYEAGTKIDVPWAGQYITSNPCIRFVSIDNKKRNIESSEIGPSLVIHTTVPFGVTYLEHSIEDVQELVFQQLENILPGLPQPIATKCQKWRHSQVTNAAANCPGQMTLHHKPFLACGGDGFTQSNFDGCITSALCVLEALKNYI
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
12PhosphorylationLIVGAGMTGSLCAAL
EEECCCHHHHHHHHH
23.7724043423
14PhosphorylationVGAGMTGSLCAALLR
ECCCHHHHHHHHHHH
15.8824043423
44PhosphorylationEDSGGRMTTACSPHN
CCCCCCCCCCCCCCC
15.1824043423
45PhosphorylationDSGGRMTTACSPHNP
CCCCCCCCCCCCCCC
19.1424043423
48PhosphorylationGRMTTACSPHNPQCT
CCCCCCCCCCCCCCC
27.0824043423
55PhosphorylationSPHNPQCTADLGAQY
CCCCCCCCCCCCCEE
20.2624043423
62PhosphorylationTADLGAQYITCTPHY
CCCCCCEEEECCHHH
9.5422817900
64PhosphorylationDLGAQYITCTPHYAK
CCCCEEEECCHHHHH
12.8524043423
66PhosphorylationGAQYITCTPHYAKKH
CCEEEECCHHHHHHH
12.4024043423
69PhosphorylationYITCTPHYAKKHQRF
EEECCHHHHHHHHHH
22.7124043423
113PhosphorylationVAPQGISSIIKHYLK
ECCCCHHHHHHHHHH
26.8124719451
189PhosphorylationRQQLEAVSYSSRYAL
HHHHHHCCHHHHHHH
26.75-
190PhosphorylationQQLEAVSYSSRYALG
HHHHHCCHHHHHHHH
12.22-
191PhosphorylationQLEAVSYSSRYALGL
HHHHCCHHHHHHHHH
10.79-
192PhosphorylationLEAVSYSSRYALGLF
HHHCCHHHHHHHHHH
22.52-
216PhosphorylationPWAGQYITSNPCIRF
CCCHHCCCCCCEEEE
19.9529449344
217PhosphorylationWAGQYITSNPCIRFV
CCHHCCCCCCEEEEE
29.2629449344
225PhosphorylationNPCIRFVSIDNKKRN
CCEEEEEEECCCCCC
22.8529449344

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 RNLS_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNLS_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 RNLS_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RNLS_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 RNLS_HUMAN

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Related Literatures of Post-Translational Modification

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