RNF26_HUMAN - dbPTM
RNF26_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF26_HUMAN
UniProt AC Q9BY78
Protein Name E3 ubiquitin-protein ligase RNF26 {ECO:0000305}
Gene Name RNF26 {ECO:0000312|HGNC:HGNC:14646}
Organism Homo sapiens (Human).
Sequence Length 433
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud. [PubMed: 27368102 Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1]
Protein Sequence MEAVYLVVNGLGLVLDVLTLVLDLNFLLVSSLLASLAWLLAFVYNLPHTVLTSLLHLGRGVLLSLLALIEAVVRFTCGGLQALCTLLYSCCSGLESLKLLGHLASHGALRSREILHRGVLNVVSSGHALLRQACDICAIAMSLVAYVINSLVNICLIGTQNLFSLVLALWDAVTGPLWRMTDVVAAFLAHISSSAVAMAILLWTPCQLALELLASAARLLASFVLVNLTGLVLLACVLAVTVTVLHPDFTLRLATQALSQLHARPSYHRLREDVMRLSRLALGSEAWRRVWSRSLQLASWPNRGGAPGAPQGDPMRVFSVRTRRQDTLPEAGRRSEAEEEEARTIRVTPVRGRERLNEEEPPGGQDPWKLLKEQEERKKCVICQDQSKTVLLLPCRHLCLCQACTEILMRHPVYHRNCPLCRRGILQTLNVYL
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
88PhosphorylationQALCTLLYSCCSGLE
HHHHHHHHHHCCCHH
11.63-
250PhosphorylationTVLHPDFTLRLATQA
HHHCCCHHHHHHHHH
20.5324719451
255PhosphorylationDFTLRLATQALSQLH
CHHHHHHHHHHHHHH
20.9723312004
259PhosphorylationRLATQALSQLHARPS
HHHHHHHHHHHCCCC
33.4423312004
266PhosphorylationSQLHARPSYHRLRED
HHHHCCCCHHHHHHH
28.1923312004
267PhosphorylationQLHARPSYHRLREDV
HHHCCCCHHHHHHHH
8.1423312004
299PhosphorylationSRSLQLASWPNRGGA
HHHCHHHCCCCCCCC
52.2229449344
327PhosphorylationVRTRRQDTLPEAGRR
EEEECCCCCCCCCCC
35.5528348404
348PhosphorylationEARTIRVTPVRGRER
HHHCCEEECCCCCCC
13.2523898821
369UbiquitinationPGGQDPWKLLKEQEE
CCCCCHHHHHHHHHH
49.70-
372UbiquitinationQDPWKLLKEQEERKK
CCHHHHHHHHHHHCC
68.7233845483
378AcetylationLKEQEERKKCVICQD
HHHHHHHCCCEEECC
54.5319813539
379AcetylationKEQEERKKCVICQDQ
HHHHHHCCCEEECCC
39.7019813547
432PhosphorylationILQTLNVYL------
HHHHHCCCC------
12.9616497976

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 RNF26_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF26_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 RNF26_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN143_HUMANZNF143physical
26186194
RBM26_HUMANRBM26physical
26186194
PSME1_HUMANPSME1physical
26186194
CUED2_HUMANCUEDC2physical
26186194
NB5R3_HUMANCYB5R3physical
26186194
FACE1_HUMANZMPSTE24physical
26186194
STOM_HUMANSTOMphysical
26186194
RAB1B_HUMANRAB1Bphysical
26186194
RAB6A_HUMANRAB6Aphysical
26186194
IF2B_HUMANEIF2S2physical
26186194
EF1A2_HUMANEEF1A2physical
26186194
ERF1_HUMANETF1physical
26186194
ARF5_HUMANARF5physical
26186194
RAB2A_HUMANRAB2Aphysical
26186194
STING_HUMANTMEM173physical
25254379
ZN143_HUMANZNF143physical
28514442
CUED2_HUMANCUEDC2physical
28514442
FACE1_HUMANZMPSTE24physical
28514442
PSME2_HUMANPSME2physical
28514442
PSME1_HUMANPSME1physical
28514442
ERF1_HUMANETF1physical
28514442
NAA50_HUMANNAA50physical
28514442
TAXB1_HUMANTAX1BP1physical
27368102
SQSTM_HUMANSQSTM1physical
27368102
EPS15_HUMANEPS15physical
27368102
TOLIP_HUMANTOLLIPphysical
27368102
UBP15_HUMANUSP15physical
27368102

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 RNF26_HUMAN

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Related Literatures of Post-Translational Modification

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