RN167_HUMAN - dbPTM
RN167_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN167_HUMAN
UniProt AC Q9H6Y7
Protein Name E3 ubiquitin-protein ligase RNF167
Gene Name RNF167
Organism Homo sapiens (Human).
Sequence Length 350
Subcellular Localization Endomembrane system
Single-pass membrane protein . Targeted to cytoplasmic membranes.
Protein Description May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition..
Protein Sequence MHPAAFPLPVVVAAVLWGAAPTRGLIRATSDHNASMDFADLPALFGATLSQEGLQGFLVEAHPDNACSPIAPPPPAPVNGSVFIALLRRFDCNFDLKVLNAQKAGYGAAVVHNVNSNELLNMVWNSEEIQQQIWIPSVFIGERSSEYLRALFVYEKGARVLLVPDNTFPLGYYLIPFTGIVGLLVLAMGAVMIARCIQHRKRLQRNRLTKEQLKQIPTHDYQKGDQYDVCAICLDEYEDGDKLRVLPCAHAYHSRCVDPWLTQTRKTCPICKQPVHRGPGDEDQEEETQGQEEGDEGEPRDHPASERTPLLGSSPTLPTSFGSLAPAPLVFPGPSTDPPLSPPSSPVILV
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
79N-linked_GlycosylationPPPPAPVNGSVFIAL
CCCCCCCCHHHHHHH
35.64UniProtKB CARBOHYD
97UbiquitinationFDCNFDLKVLNAQKA
CCCCCEEEECCHHHC
46.6621890473
1562-HydroxyisobutyrylationRALFVYEKGARVLLV
HHHEEEECCCEEEEC
39.94-
156UbiquitinationRALFVYEKGARVLLV
HHHEEEECCCEEEEC
39.9421890473
210UbiquitinationLQRNRLTKEQLKQIP
HHHCCCCHHHHHCCC
48.3221890473
214UbiquitinationRLTKEQLKQIPTHDY
CCCHHHHHCCCCCCC
45.9721890473
223UbiquitinationIPTHDYQKGDQYDVC
CCCCCCCCCCCCCEE
59.22-
237PhosphorylationCAICLDEYEDGDKLR
EEEEEEECCCCCEEE
20.98-
242UbiquitinationDEYEDGDKLRVLPCA
EECCCCCEEEEEECH
43.66-
266UbiquitinationPWLTQTRKTCPICKQ
HHHCCCCCCCCCCCC
58.84-
272UbiquitinationRKTCPICKQPVHRGP
CCCCCCCCCCCCCCC
59.3621890473
277MethylationICKQPVHRGPGDEDQ
CCCCCCCCCCCCCCH
53.92115491395
288PhosphorylationDEDQEEETQGQEEGD
CCCHHHHHCCCCCCC
41.08-
305PhosphorylationEPRDHPASERTPLLG
CCCCCCCHHCCCCCC
31.8720068231
308PhosphorylationDHPASERTPLLGSSP
CCCCHHCCCCCCCCC
17.7820873877
313PhosphorylationERTPLLGSSPTLPTS
HCCCCCCCCCCCCCC
32.8720068231
314PhosphorylationRTPLLGSSPTLPTSF
CCCCCCCCCCCCCCC
21.8020068231
316PhosphorylationPLLGSSPTLPTSFGS
CCCCCCCCCCCCCCC
47.5220873877
319PhosphorylationGSSPTLPTSFGSLAP
CCCCCCCCCCCCCCC
39.5420873877
320PhosphorylationSSPTLPTSFGSLAPA
CCCCCCCCCCCCCCC
26.1820068231
323PhosphorylationTLPTSFGSLAPAPLV
CCCCCCCCCCCCCEE
21.2428348404
335PhosphorylationPLVFPGPSTDPPLSP
CEECCCCCCCCCCCC
51.8920873877
336PhosphorylationLVFPGPSTDPPLSPP
EECCCCCCCCCCCCC
56.5120068231
341PhosphorylationPSTDPPLSPPSSPVI
CCCCCCCCCCCCCEE
40.3020068231
344PhosphorylationDPPLSPPSSPVILV-
CCCCCCCCCCEEEC-
51.1320873877
345PhosphorylationPPLSPPSSPVILV--
CCCCCCCCCEEEC--
29.0320873877

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 RN167_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN167_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 RN167_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAP26_HUMANCCDC59physical
17353931
RN167_HUMANRNF167physical
16314844
UB2D1_HUMANUBE2D1physical
16314844
UB2E1_HUMANUBE2E1physical
16314844
S22AI_HUMANSLC22A18physical
16314844
RN167_HUMANRNF167physical
24387786

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 RN167_HUMAN

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Related Literatures of Post-Translational Modification

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