Q6PJF5 · RHDF2_HUMAN

  • Protein
    Inactive rhomboid protein 2
  • Gene
    RHBDF2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular ComponentGolgi lumen
Cellular Componentplasma membrane
Molecular Functiongrowth factor binding
Molecular Functionprotein transporter activity
Biological Processnegative regulation of inflammatory response to antigenic stimulus
Biological Processnegative regulation of protein secretion
Biological Processprotein localization to plasma membrane
Biological Processprotein transport
Biological Processregulation of epidermal growth factor receptor signaling pathway
Biological Processregulation of protein secretion

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Inactive rhomboid protein 2
  • Short names
    iRhom2
  • Alternative names
    • Rhomboid 5 homolog 2
    • Rhomboid family member 2
    • Rhomboid veinlet-like protein 5
    • Rhomboid veinlet-like protein 6

Gene names

    • Name
      RHBDF2
    • Synonyms
      IRHOM2, RHBDL5, RHBDL6

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q6PJF5
  • Secondary accessions
    • A6NEM3
    • A8K801
    • Q5U607
    • Q5YGQ8
    • Q9H6E9

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-409Cytoplasmic
Transmembrane410-430Helical
Topological domain431-660Lumenal
Transmembrane661-681Helical
Topological domain682-692Cytoplasmic
Transmembrane693-713Helical
Topological domain714-715Lumenal
Transmembrane716-736Helical
Topological domain737-747Cytoplasmic
Transmembrane748-768Helical
Topological domain769-773Lumenal
Transmembrane774-794Helical
Topological domain795-802Cytoplasmic
Transmembrane803-823Helical
Topological domain824-856Lumenal

Keywords

Disease & Variants

Involvement in disease

Tylosis with esophageal cancer (TOC)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal dominant syndrome characterized by focal non-epidermolytic palmoplantar keratoderma, oral leukokeratosis, and a high lifetime risk of developing esophageal squamous cell carcinoma.
  • See also
    MIM:148500
Natural variants in TOC
Variant IDPosition(s)ChangeDescription
VAR_067827186I>Tin TOC; likely pathogenic; dbSNP:rs387907129
VAR_089310188D>Nin TOC; likely pathogenic
VAR_089311188D>Yin TOC; likely pathogenic
VAR_067828189P>Lin TOC; likely pathogenic; dbSNP:rs387907130

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_067827186in TOC; likely pathogenic; dbSNP:rs387907129
Natural variantVAR_089310188in TOC; likely pathogenic
Natural variantVAR_089311188in TOC; likely pathogenic
Natural variantVAR_067828189in TOC; likely pathogenic; dbSNP:rs387907130
Natural variantVAR_044125208in dbSNP:rs3744045
Natural variantVAR_044126249in dbSNP:rs34814954
Natural variantVAR_044127528in dbSNP:rs11553545

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 933 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00003419381-856UniProtInactive rhomboid protein 2
Modified residue (large scale data)10PRIDEPhosphoserine
Modified residue90UniProtPhosphoserine
Modified residue (large scale data)90PRIDEPhosphoserine
Modified residue (large scale data)102PRIDEPhosphoserine
Modified residue113UniProtPhosphoserine
Modified residue (large scale data)113PRIDEPhosphoserine
Modified residue (large scale data)115PRIDEPhosphoserine
Modified residue117UniProtPhosphoserine
Modified residue (large scale data)117PRIDEPhosphoserine
Modified residue (large scale data)129PRIDEPhosphoserine
Modified residue (large scale data)166PRIDEPhosphoserine
Modified residue (large scale data)171PRIDEPhosphoserine
Modified residue (large scale data)175PRIDEPhosphothreonine
Modified residue (large scale data)177PRIDEPhosphoserine
Modified residue (large scale data)227PRIDEPhosphoserine
Modified residue (large scale data)239PRIDEPhosphoserine
Modified residue (large scale data)309PRIDEPhosphoserine
Modified residue (large scale data)313PRIDEPhosphoserine
Modified residue323UniProtPhosphoserine
Modified residue (large scale data)323PRIDEPhosphoserine
Modified residue325UniProtPhosphoserine
Modified residue (large scale data)325PRIDEPhosphoserine
Modified residue328UniProtPhosphoserine
Modified residue (large scale data)328PRIDEPhosphoserine
Modified residue (large scale data)385PRIDEPhosphoserine
Modified residue (large scale data)387PRIDEPhosphoserine
Modified residue (large scale data)388PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Found in the epidermis and esophageal epithelium.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with EGF (By similarity).
Interacts (via cytoplasmic N-terminus) with FRMD8/iTAP; this interaction leads to mutual protein stabilization (PubMed:29897333, PubMed:29897336).
Interacts with ADAM17/TACE (PubMed:29897333, PubMed:29897336).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-26Polar residues
Region1-115Disordered
Region165-184Disordered
Region191-271Involved in interaction with FRMD8
Region531-553Disordered

Sequence similarities

Belongs to the peptidase S54 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q6PJF5-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    856
  • Mass (Da)
    96,686
  • Last updated
    2008-07-01 v2
  • Checksum
    69C40A21EBDBDDC0
MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLTFVHVIITLLVICTYGIAPVGFAQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLSLFLHAGVVHCLVSVVFQMTILRDLEKLAGWHRIAIIFILSGITGNLASAIFLPYRAEVGPAGSQFGLLACLFVELFQSWPLLERPWKAFLNLSAIVLFLFICGLLPWIDNIAHIFGFLSGLLLAFAFLPYITFGTSDKYRKRALILVSLLAFAGLFAALVLWLYIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH

Q6PJF5-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 10 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
K7EJD6K7EJD6_HUMANRHBDF213
K7EIY3K7EIY3_HUMANRHBDF274
K7EJ10K7EJ10_HUMANRHBDF228
K7EKI1K7EKI1_HUMANRHBDF2112
K7EKA3K7EKA3_HUMANRHBDF273
K7ELA9K7ELA9_HUMANRHBDF226
K7EQ53K7EQ53_HUMANRHBDF289
K7EPV3K7EPV3_HUMANRHBDF2185
K7EPN8K7EPN8_HUMANRHBDF286
K7EQT5K7EQT5_HUMANRHBDF247

Sequence caution

The sequence AAH35829.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence BAB15310.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-26Polar residues
Alternative sequenceVSP_03436851-79in isoform 2
Sequence conflict67in Ref. 2; BAF84824 and 4; AAH16034
Sequence conflict705in Ref. 2; BAF84855
Sequence conflict852in Ref. 2; BAF84855

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY500247
EMBL· GenBank· DDBJ
AAS77567.1
EMBL· GenBank· DDBJ
mRNA
AK025994
EMBL· GenBank· DDBJ
BAB15310.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK292135
EMBL· GenBank· DDBJ
BAF84824.1
EMBL· GenBank· DDBJ
mRNA
AK292166
EMBL· GenBank· DDBJ
BAF84855.1
EMBL· GenBank· DDBJ
mRNA
AC015802
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC035829
EMBL· GenBank· DDBJ
AAH35829.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC016034
EMBL· GenBank· DDBJ
AAH16034.2
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp