RN215_HUMAN - dbPTM
RN215_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN215_HUMAN
UniProt AC Q9Y6U7
Protein Name RING finger protein 215
Gene Name RNF215
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MGPAARPALRSPPPPPPPPPSPLLLLLPLLPLWLGLAGPGAAADGSEPAAGAGRGGARAVRVDVRLPRQDALVLEGVRIGSEADPAPLLGGRLLLMDIVDAEQEAPVEGWIAVAYVGKEQAAQFHQENKGSGPQAYPKALVQQMRRALFLGASALLLLILNHNVVRELDISQLLLRPVIVLHYSSNVTKLLDALLQRTQATAEITSGESLSANIEWKLTLWTTCGLSKDGYGGWQDLVCLGGSRAQEQKPLQQLWNAILLVAMLLCTGLVVQAQRQASRQSQRELGGQVDLFKRRVVRRLASLKTRRCRLSRAAQGLPDPGAETCAVCLDYFCNKQWLRVLPCKHEFHRDCVDPWLMLQQTCPLCKFNVLGNRYSDD
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
11PhosphorylationAARPALRSPPPPPPP
CCCCCCCCCCCCCCC
42.4816094384
21PhosphorylationPPPPPPPSPLLLLLP
CCCCCCCCCHHHHHH
33.6716094384
129UbiquitinationAQFHQENKGSGPQAY
HHHHHHCCCCCCCCH
54.4229967540
138UbiquitinationSGPQAYPKALVQQMR
CCCCCHHHHHHHHHH
41.50-
186N-linked_GlycosylationIVLHYSSNVTKLLDA
EEEEECCCHHHHHHH
39.27UniProtKB CARBOHYD
222PhosphorylationEWKLTLWTTCGLSKD
EEEEEEEEECCCCCC
18.47-
267PhosphorylationLVAMLLCTGLVVQAQ
HHHHHHHHHHHHHHH
33.2622210691
278PhosphorylationVQAQRQASRQSQREL
HHHHHHHHHHHHHHH
23.6322210691
324PhosphorylationLPDPGAETCAVCLDY
CCCCCCCHHHHHHHH
12.77-

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 RN215_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN215_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 RN215_HUMAN !!

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

Oops, there are no PPI records of RN215_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 RN215_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-21, AND MASSSPECTROMETRY.

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