Q6PJF5 · RHDF2_HUMAN
- ProteinInactive rhomboid protein 2
- GeneRHBDF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids856 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi lumen | |
Cellular Component | plasma membrane | |
Molecular Function | growth factor binding | |
Molecular Function | protein transporter activity | |
Biological Process | negative regulation of inflammatory response to antigenic stimulus | |
Biological Process | negative regulation of protein secretion | |
Biological Process | protein localization to plasma membrane | |
Biological Process | protein transport | |
Biological Process | regulation of epidermal growth factor receptor signaling pathway | |
Biological Process | regulation of protein secretion |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameInactive rhomboid protein 2
- Short namesiRhom2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6PJF5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-409 | Cytoplasmic | ||||
Sequence: MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLT | ||||||
Transmembrane | 410-430 | Helical | ||||
Sequence: FVHVIITLLVICTYGIAPVGF | ||||||
Topological domain | 431-660 | Lumenal | ||||
Sequence: AQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLS | ||||||
Transmembrane | 661-681 | Helical | ||||
Sequence: LFLHAGVVHCLVSVVFQMTIL | ||||||
Topological domain | 682-692 | Cytoplasmic | ||||
Sequence: RDLEKLAGWHR | ||||||
Transmembrane | 693-713 | Helical | ||||
Sequence: IAIIFILSGITGNLASAIFLP | ||||||
Topological domain | 714-715 | Lumenal | ||||
Sequence: YR | ||||||
Transmembrane | 716-736 | Helical | ||||
Sequence: AEVGPAGSQFGLLACLFVELF | ||||||
Topological domain | 737-747 | Cytoplasmic | ||||
Sequence: QSWPLLERPWK | ||||||
Transmembrane | 748-768 | Helical | ||||
Sequence: AFLNLSAIVLFLFICGLLPWI | ||||||
Topological domain | 769-773 | Lumenal | ||||
Sequence: DNIAH | ||||||
Transmembrane | 774-794 | Helical | ||||
Sequence: IFGFLSGLLLAFAFLPYITFG | ||||||
Topological domain | 795-802 | Cytoplasmic | ||||
Sequence: TSDKYRKR | ||||||
Transmembrane | 803-823 | Helical | ||||
Sequence: ALILVSLLAFAGLFAALVLWL | ||||||
Topological domain | 824-856 | Lumenal | ||||
Sequence: YIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Tylosis with esophageal cancer (TOC)
- Note
- DescriptionAn autosomal dominant syndrome characterized by focal non-epidermolytic palmoplantar keratoderma, oral leukokeratosis, and a high lifetime risk of developing esophageal squamous cell carcinoma.
- See alsoMIM:148500
Natural variants in TOC
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067827 | 186 | I>T | in TOC; likely pathogenic; dbSNP:rs387907129 | |
VAR_089310 | 188 | D>N | in TOC; likely pathogenic | |
VAR_089311 | 188 | D>Y | in TOC; likely pathogenic | |
VAR_067828 | 189 | P>L | in TOC; likely pathogenic; dbSNP:rs387907130 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067827 | 186 | in TOC; likely pathogenic; dbSNP:rs387907129 | |||
Sequence: I → T | ||||||
Natural variant | VAR_089310 | 188 | in TOC; likely pathogenic | |||
Sequence: D → N | ||||||
Natural variant | VAR_089311 | 188 | in TOC; likely pathogenic | |||
Sequence: D → Y | ||||||
Natural variant | VAR_067828 | 189 | in TOC; likely pathogenic; dbSNP:rs387907130 | |||
Sequence: P → L | ||||||
Natural variant | VAR_044125 | 208 | in dbSNP:rs3744045 | |||
Sequence: P → L | ||||||
Natural variant | VAR_044126 | 249 | in dbSNP:rs34814954 | |||
Sequence: A → T | ||||||
Natural variant | VAR_044127 | 528 | in dbSNP:rs11553545 | |||
Sequence: D → Y |
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.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000341938 | 1-856 | UniProt | Inactive rhomboid protein 2 | |||
Sequence: MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLTFVHVIITLLVICTYGIAPVGFAQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLSLFLHAGVVHCLVSVVFQMTILRDLEKLAGWHRIAIIFILSGITGNLASAIFLPYRAEVGPAGSQFGLLACLFVELFQSWPLLERPWKAFLNLSAIVLFLFICGLLPWIDNIAHIFGFLSGLLLAFAFLPYITFGTSDKYRKRALILVSLLAFAGLFAALVLWLYIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 90 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 113 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 113 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 115 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 117 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 117 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 129 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 171 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 177 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 313 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 323 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 325 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 325 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 328 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 387 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 388 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
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
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Polar residues | ||||
Sequence: MASADKNGGSVSSVSSSRLQSRKPPN | ||||||
Region | 1-115 | Disordered | ||||
Sequence: MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLS | ||||||
Region | 165-184 | Disordered | ||||
Sequence: PSQEAPSFQGTESPKPCKMP | ||||||
Region | 191-271 | Involved in interaction with FRMD8 | ||||
Sequence: ARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRS | ||||||
Region | 531-553 | Disordered | ||||
Sequence: GPPMDKSDLGQKRTSGAVCHQDP |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length856
- Mass (Da)96,686
- Last updated2008-07-01 v2
- Checksum69C40A21EBDBDDC0
Q6PJF5-2
- Name2
- Differences from canonical
- 51-79: Missing
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Polar residues | ||||
Sequence: MASADKNGGSVSSVSSSRLQSRKPPN | ||||||
Alternative sequence | VSP_034368 | 51-79 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 67 | in Ref. 2; BAF84824 and 4; AAH16034 | ||||
Sequence: A → S | ||||||
Sequence conflict | 705 | in Ref. 2; BAF84855 | ||||
Sequence: N → D | ||||||
Sequence conflict | 852 | in Ref. 2; BAF84855 | ||||
Sequence: D → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |