Format

Send to:

Choose Destination

RNF185 ring finger protein 185 [ Homo sapiens (human) ]

Gene ID: 91445, updated on 10-Oct-2019

Summary

Official Symbol
RNF185provided by HGNC
Official Full Name
ring finger protein 185provided by HGNC
Primary source
HGNC:HGNC:26783
See related
Ensembl:ENSG00000138942
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Expression
Ubiquitous expression in thyroid (RPKM 37.5), prostate (RPKM 19.7) and 25 other tissues See more
Orthologs

Genomic context

See RNF185 in Genome Data Viewer
Location:
22q12.2
Exon count:
8
Annotation release Status Assembly Chr Location
109.20190905 current GRCh38.p13 (GCF_000001405.39) 22 NC_000022.11 (31160182..31207019)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 22 NC_000022.10 (31556138..31603005)

Chromosome 22 - NC_000022.11Genomic Context describing neighboring genes Neighboring gene small nuclear ribonucleoprotein-associated protein N pseudogene Neighboring gene microRNA 3928 Neighboring gene origin of replication in RNF185 Neighboring gene LIM domain kinase 2 Neighboring gene RNA, U6 small nuclear 1128, pseudogene Neighboring gene protein phosphatase 1 regulatory inhibitor subunit 14B pseudogene 1

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

HIV-1 interactions

Protein interactions

Protein Gene Interaction Pubs
Tat tat HIV-1 Tat downregulates the expression of ring finger protein 185 (RNF185) in human primary T cells PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

  • ABC transporter disorders, organism-specific biosystem (from REACTOME)
    ABC transporter disorders, organism-specific biosystemThe ATP-binding cassette (ABC) transporters form a large family of transmembrane proteins that utilise the energy from the hydrolysis of ATP to facilitate the movement of a wide variety of substrates...
  • ABC-family proteins mediated transport, organism-specific biosystem (from REACTOME)
    ABC-family proteins mediated transport, organism-specific biosystemThe ATP-binding cassette (ABC) superfamily of active transporters involves a large number of functionally diverse transmembrane proteins. They transport a variety of compounds through membranes agai...
  • Asparagine N-linked glycosylation, organism-specific biosystem (from REACTOME)
    Asparagine N-linked glycosylation, organism-specific biosystemN-linked glycosylation is the most important form of post-translational modification for proteins synthesized and folded in the Endoplasmic Reticulum (Stanley et al. 2009). An early study in 1999 rev...
  • Calnexin/calreticulin cycle, organism-specific biosystem (from REACTOME)
    Calnexin/calreticulin cycle, organism-specific biosystemThe unfolded protein is recognized by a chaperon protein (calnexin or calreticulin) and the folding process starts. The binding of these protein requires a mono-glucosylated glycan (Caramelo JJ and P...
  • Defective CFTR causes cystic fibrosis, organism-specific biosystem (from REACTOME)
    Defective CFTR causes cystic fibrosis, organism-specific biosystemCystic fibrosis transmembrane conductance regulator (CFTR) is a low conductance chloride-selective channel that mediates the transport of chloride ions in human airway epithelial cells. Chloride ions...
  • Disease, organism-specific biosystem (from REACTOME)
    Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
  • Disorders of transmembrane transporters, organism-specific biosystem (from REACTOME)
    Disorders of transmembrane transporters, organism-specific biosystemProteins with transporting functions can be roughly classified into 3 categories: ATP hydrolysis-coupled pumps, ion channels, and transporters. Pumps utilize the energy released by ATP hydrolysis to ...
  • ER Quality Control Compartment (ERQC), organism-specific biosystem (from REACTOME)
    ER Quality Control Compartment (ERQC), organism-specific biosystemProteins that are released from the CNX or CRT complex with folding defects accumulate in a compartment of the ER called ERQC (Kamhi-Nesher et al. 2001). Here, the enzymes UGGG1 or UGGG2 are able to ...
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • N-glycan trimming in the ER and Calnexin/Calreticulin cycle, organism-specific biosystem (from REACTOME)
    N-glycan trimming in the ER and Calnexin/Calreticulin cycle, organism-specific biosystemAfter being synthesized in the ER membrane the 14-sugars lipid-linked oligosaccharide is co-translationally transferred to an unfolded protein, as described in the previous steps. After this point th...
  • Post-translational protein modification, organism-specific biosystem (from REACTOME)
    Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...
  • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Transmembrane transport of small molecules, organism-specific biosystem (from REACTOME)
    Transmembrane transport of small molecules, organism-specific biosystem
    Transmembrane transport of small molecules

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • FLJ38628

Gene Ontology Provided by GOA

Function Evidence Code Pubs
metal ion binding IEA
Inferred from Electronic Annotation
more info
 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein-containing complex binding IPI
Inferred from Physical Interaction
more info
PubMed 
ubiquitin binding IDA
Inferred from Direct Assay
more info
PubMed 
ubiquitin protein ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
ubiquitin protein ligase activity IDA
Inferred from Direct Assay
more info
PubMed 
ubiquitin protein ligase activity TAS
Traceable Author Statement
more info
 
ubiquitin-like protein conjugating enzyme binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
ubiquitin-like protein conjugating enzyme binding IPI
Inferred from Physical Interaction
more info
PubMed 
Process Evidence Code Pubs
ER-associated misfolded protein catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
ERAD pathway IGI
Inferred from Genetic Interaction
more info
PubMed 
autophagy IEA
Inferred from Electronic Annotation
more info
 
endoplasmic reticulum mannose trimming TAS
Traceable Author Statement
more info
 
positive regulation of ERAD pathway IMP
Inferred from Mutant Phenotype
more info
PubMed 
protein autoubiquitination IDA
Inferred from Direct Assay
more info
PubMed 
transmembrane transport TAS
Traceable Author Statement
more info
 
ubiquitin-dependent ERAD pathway IMP
Inferred from Mutant Phenotype
more info
PubMed 
ubiquitin-dependent protein catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
Component Evidence Code Pubs
endoplasmic reticulum IDA
Inferred from Direct Assay
more info
PubMed 
endoplasmic reticulum membrane NAS
Non-traceable Author Statement
more info
PubMed 
endoplasmic reticulum membrane TAS
Traceable Author Statement
more info
 
endoplasmic reticulum quality control compartment IEA
Inferred from Electronic Annotation
more info
 
integral component of membrane IEA
Inferred from Electronic Annotation
more info
 
mitochondrial outer membrane IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
E3 ubiquitin-protein ligase RNF185
Names
BSK65-MONO1
BSK65-MONO2
BSK65-PANC1
BSK65-PANC2
BSK65-TEST1
BSK65-TEST2
BSK65-TEST3
RING-type E3 ubiquitin transferase RNF185
NP_001129297.1
NP_689480.2

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001135825.2NP_001129297.1  E3 ubiquitin-protein ligase RNF185 isoform 2

    See identical proteins and their annotated locations for NP_001129297.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (3) is lacking two in-frame coding exons compared to transcript variant 1, resulting in a shorter isoform (2) missing a 56 aa protein segment compared to isoform 1.
    Source sequence(s)
    AA258379, DB134817, DQ296562
    Consensus CDS
    CCDS46689.1
    UniProtKB/Swiss-Prot
    Q96GF1
    UniProtKB/TrEMBL
    A0A024R1H4
    Related
    ENSP00000266252.7, ENST00000266252.8
    Conserved Domains (1) summary
    cl17238
    Location:3764
    RING_Ubox; The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain
  2. NM_152267.4NP_689480.2  E3 ubiquitin-protein ligase RNF185 isoform 1

    See identical proteins and their annotated locations for NP_689480.2

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) represents the predominant transcript and encodes the longer isoform (1).
    Source sequence(s)
    AA258379, BC033166, DB134817
    Consensus CDS
    CCDS13890.1
    UniProtKB/Swiss-Prot
    Q96GF1
    UniProtKB/TrEMBL
    A0A024R1F5
    Related
    ENSP00000320508.5, ENST00000326132.11
    Conserved Domains (1) summary
    cd16744
    Location:3880
    RING-HC_RNF185; RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins

RNA

  1. NR_024209.2 RNA Sequence

    Status: VALIDATED

    Description
    Transcript Variant: This variant (4) is missing an internal coding exon and contains an additional exon compared to transcript variant 1. This results in a frame-shift and premature translation termination, rendering the transcript susceptible to nonsense mediated mRNA decay (NMD). This transcript is sufficiently abundant to represent as a RefSeq record, however, the predicted protein is not represented because it is significantly truncated.
    Source sequence(s)
    AA258379, BC033166, BX648019, DB134817
  2. NR_024210.2 RNA Sequence

    Status: VALIDATED

    Description
    Transcript Variant: This variant (5) uses an alternate donor splice site at one of the coding exons compared to transcript variant 1. This results in a frame-shift and premature translation termination, rendering the transcript susceptible to nonsense mediated mRNA decay (NMD). This transcript is sufficiently abundant to represent as a RefSeq record, however, the predicted protein is not represented because it is truncated.
    Source sequence(s)
    AA258379, BC033166, DA498404, DB134817
    Related
    ENST00000426256.6
  3. NR_024211.2 RNA Sequence

    Status: VALIDATED

    Description
    Transcript Variant: This variant (6) is missing an internal coding exon compared to transcript variant 1. This results in a frame-shift and premature translation termination, rendering the transcript susceptible to nonsense mediated mRNA decay (NMD). This transcript is sufficiently abundant to represent as a RefSeq record, however, the predicted protein is not represented because it is significantly truncated.
    Source sequence(s)
    AA258379, BC033166, BX648019, DB134817
  4. NR_024212.2 RNA Sequence

    Status: VALIDATED

    Description
    Transcript Variant: This variant (7) is missing a coding exon (containing the translation start site) compared to transcript variant 1. This results in the use of a downstream AUG in a different frame, and a predicted protein that is severely truncated with no similarity to this gene product. However, this transcript is sufficiently abundant to represent as a RefSeq record.
    Source sequence(s)
    AA258379, BC033166, DB134817
    Related
    ENST00000471384.5

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109.20190905

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000022.11 Reference GRCh38.p13 Primary Assembly

    Range
    31160182..31207019
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_001135824.1: Suppressed sequence

    Description
    NM_001135824.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript.
Support Center