RNF43_HUMAN - dbPTM
RNF43_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF43_HUMAN
UniProt AC Q68DV7
Protein Name E3 ubiquitin-protein ligase RNF43
Gene Name RNF43
Organism Homo sapiens (Human).
Sequence Length 783
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Endoplasmic reticulum membrane
Single-pass type I membrane protein. Nucleus envelope. According to a report, may be secreted.
Protein Description E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination, endocytosis and subsequent degradation of Wnt receptor complex components Frizzled. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone..
Protein Sequence MSGGHQLQLAALWPWLLMATLQAGFGRTGLVLAAAVESERSAEQKAIIRVIPLKMDPTGKLNLTLEGVFAGVAEITPAEGKLMQSHPLYLCNASDDDNLEPGFISIVKLESPRRAPRPCLSLASKARMAGERGASAVLFDITEDRAAAEQLQQPLGLTWPVVLIWGNDAEKLMEFVYKNQKAHVRIELKEPPAWPDYDVWILMTVVGTIFVIILASVLRIRCRPRHSRPDPLQQRTAWAISQLATRRYQASCRQARGEWPDSGSSCSSAPVCAICLEEFSEGQELRVISCLHEFHRNCVDPWLHQHRTCPLCMFNITEGDSFSQSLGPSRSYQEPGRRLHLIRQHPGHAHYHLPAAYLLGPSRSAVARPPRPGPFLPSQEPGMGPRHHRFPRAAHPRAPGEQQRLAGAQHPYAQGWGLSHLQSTSQHPAACPVPLRRARPPDSSGSGESYCTERSGYLADGPASDSSSGPCHGSSSDSVVNCTDISLQGVHGSSSTFCSSLSSDFDPLVYCSPKGDPQRVDMQPSVTSRPRSLDSVVPTGETQVSSHVHYHRHRHHHYKKRFQWHGRKPGPETGVPQSRPPIPRTQPQPEPPSPDQQVTRSNSAAPSGRLSNPQCPRALPEPAPGPVDASSICPSTSSLFNLQKSSLSARHPQRKRRGGPSEPTPGSRPQDATVHPACQIFPHYTPSVAYPWSPEAHPLICGPPGLDKRLLPETPGPCYSNSQPVWLCLTPRQPLEPHPPGEGPSEWSSDTAEGRPCPYPHCQVLSAQPGSEEELEELCEQAV
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------MSGGHQLQL
------CCCHHHHHH
54.1824043423
20PhosphorylationWPWLLMATLQAGFGR
HHHHHHHHHHHCCCC
12.8724043423
62N-linked_GlycosylationMDPTGKLNLTLEGVF
CCCCCCCEEEEEEEE
34.17UniProtKB CARBOHYD
92N-linked_GlycosylationSHPLYLCNASDDDNL
CCCEEEECCCCCCCC
39.62UniProtKB CARBOHYD
105PhosphorylationNLEPGFISIVKLESP
CCCCCEEEEEECCCC
21.0424719451
121PhosphorylationRAPRPCLSLASKARM
CCCCCHHHHHHHHHH
28.7120860994
329PhosphorylationFSQSLGPSRSYQEPG
HHHHCCCCCCCCCCC
31.8724719451
364PhosphorylationYLLGPSRSAVARPPR
HHHCCCHHHCCCCCC
31.2822210691
585PhosphorylationSRPPIPRTQPQPEPP
CCCCCCCCCCCCCCC
38.97-
593PhosphorylationQPQPEPPSPDQQVTR
CCCCCCCCCCCCCCC
52.3928348404
667PhosphorylationPSEPTPGSRPQDATV
CCCCCCCCCCCCCEE
41.8323312004

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
-KUbiquitinationE3 ubiquitin ligaseRNF43Q68DV7
PMID:18313049

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF43_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 RNF43_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKP8L_HUMANAKAP8Lphysical
18313049
HECW1_HUMANHECW1physical
21108931
P53_HUMANTP53physical
21108931
SFPQ_HUMANSFPQphysical
18655028
NONO_HUMANNONOphysical
18655028
RSPO1_HUMANRSPO1physical
23756651
RNF43_HUMANRNF43physical
18313049
UB2D2_HUMANUBE2D2physical
18313049
UB2D3_HUMANUBE2D3physical
18313049
DVL2_HUMANDVL2physical
25891077
FZD5_HUMANFZD5physical
25825523
DVL2_HUMANDVL2physical
25825523
MYADM_HUMANMYADMphysical
28514442
KC1E_HUMANCSNK1Ephysical
28514442
CSK21_HUMANCSNK2A1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNF43_HUMAN

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Related Literatures of Post-Translational Modification

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