Protein detail

RHDF2

Inactive rhomboid protein 2 (iRhom2) (Rhomboid 5 homolog 2) (Rhomboid family member 2) (Rhomboid veinlet-like protein 5) (Rhomboid veinlet-like protein 6)

Entry name
RHDF2
UniProt ID
EVMP confidence score
0.38
Supporting publications (n)
6
Transmembrane count
7
Protein classification
Disease related genesEnzymesPotential drug targetsPredicted intracellular proteinsPredicted membrane proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information13
Protein Names
Inactive rhomboid protein 2 (iRhom2) (Rhomboid 5 homolog 2) (Rhomboid family member 2) (Rhomboid veinlet-like protein 5) (Rhomboid veinlet-like protein 6)
Protein Class (5)
Disease related genesEnzymesPotential drug targetsPredicted intracellular proteinsPredicted membrane proteins
Protein Function (5)
  • Predicted intracellular proteins
  • Potential drug targets
  • Peptidases:Serine-type peptidases
  • Enzymes
  • Disease related genes
Transmembrane
410..430; Helical; 661..681; Helical; 693..713; Helical; 716..736; Helical; 748..768; Helical; 774..794; Helical; 803..823; Helical
Transmembrane Count
7
Entrez Gene Symbol
Gene Synonym (6)
FLJ22341iRhom2RHBDL5RHBDL6TOCTOCG
Gene Description
Rhomboid 5 homolog 2
Chromosome
17
Position
76470891-76501790
Supporting publications (n)
6
EVMP confidence score
0.38
Fluorescence & Localization4
Tissue Specificchoroid plexusBrain Regional Specificchoroid plexusCell SpecificBergmann gliaSingle-Nuclei Brain Specificchoroid plexus epithelial cell
Function & Pathway7
Relations & Evidence26

Ligand-Receptor Signaling (20)

20 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorCellTalkDBNoYesNoYesNo
receptorreceptorOmniPathNoYesNoYesNo
intracellularintracellularGO_IntercellNoNoNoYesNo
intracellularintracellularUniProt_locationNoNoNoYesNo
intracellularintracellularOmniPathNoNoNoYesNo
growth_factor_binderligand_regulatorUniProt_keywordYesNoNoYesNo
ligand_regulatorligand_regulatorOmniPathYesNoNoYesNo
transmembranetransmembraneUniProt_locationNoNoNoYesNo
transmembranetransmembraneUniProt_topologyNoNoNoYesNo
transmembranetransmembraneUniProt_keywordNoNoNoYesNo
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Protein Complex Composition (5)

5 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
CYP26C1DDOSTEPB42NOS3RHBDF2RTN3SACM1LSLC22A5SURF4SV2ATMED10TMED7TMED9UBCZMPSTE24O15260O75844O76082O95197P0CG48P16452P29474P39656P49755Q6PJF5Q6V0L0Q7L0J3Q9BVK6Q9NTJ5Q9Y3B31:1:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC5481
ATP13A1CEPT1LMAN2RHBDF2SEC23ASURF4TMED10TMED2TMED4TMED5TMED7TMED9UBCO15260P0CG48P49755Q12907Q15363Q15436Q6PJF5Q7Z7H5Q9BVK6Q9HD20Q9Y3A6Q9Y3B3Q9Y6K01:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC5483
CPDAD1DDOSTMAGT1RHBDF2RPN2SEC61A2SEC61BSEC61GSEC62SEC63STT3BUBCZDHHC6P00450P04844P0CG48P39656P60059P60468P61803Q6PJF5Q8TCJ2Q99442Q9H0U3Q9H6R6Q9H9S3Q9UGP81:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8314
CERS6DAD1DDOSTMAGT1RHBDF2RPN2SEC61A2SEC61BSEC61GSEC62SEC63STT3BTMEM258UBCP04844P0CG48P39656P60059P60468P61165P61803Q6PJF5Q6ZMG9Q8TCJ2Q99442Q9H0U3Q9H9S3Q9UGP81:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8855
DAD1DDOSTRHBDF2RPN2SEC61A2SEC61BSEC61GSEC62SEC63SPCS1SPCS2STT3BTRAM1UBCP04844P0CG48P39656P60059P60468P61803Q15005Q15629Q6PJF5Q8TCJ2Q99442Q9H9S3Q9UGP8Q9Y6A91:1:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC9530

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyMass spectrometryMass spectrometry [LTQ-FT Ultra]Mass spectrometry [QTOF]Western blotting3328418943279541429689087
Sequence, Structure & Domains13

Sequences

Length
856
Mass
96,686
Sequence
MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLTFVHVIITLLVICTYGIAPVGFAQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLSLFLHAGVVHCLVSVVFQMTILRDLEKLAGWHRIAIIFILSGITGNLASAIFLPYRAEVGPAGSQFGLLACLFVELFQSWPLLERPWKAFLNLSAIVLFLFICGLLPWIDNIAHIFGFLSGLLLAFAFLPYITFGTSDKYRKRALILVSLLAFAGLFAALVLWLYIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6PJF5-1; Sequence=Displayed; Name=2; IsoId=Q6PJF5-2; Sequence=VSP_034368
Alternative Sequence
51..79; Missing (in isoform 2)

3D Structural Models

Turn
518..520; 528..530; 553..555; 589..591; 843..850
Helix
373..377; 388..395; 403..422; 463..469; 474..477; 481..495; 513..515; 563..565; 571..573; 613..618; 630..632; 635..640; 656..659; 660..662; 667..688; 690..711; 721..737; 739..741; 745..763; 770..787; 795..824; 832..837
Beta Strand
429..440; 442..454; 457..460; 498..504; 508..511; 521..524; 540..542; 556..558; 578..580; 598..601; 603..606; 608..611; 742..744; 852..854
3D Structure
Electron microscopy (5)

Domain & Motif Annotations

Compositional Bias
94..106; Basic and acidic residues
Region
1..115; Disordered; 165..184; Disordered; 191..271; Involved in interaction with FRMD8; 531..553; Disordered
Protein Families
Peptidase S54 family
Sequence Similarities
Belongs to the peptidase S54 family.
Clinical Relevance5
Disease Involvement (2)
Disease variantPalmoplantar keratoderma
Biomarker
Investigative
Antibody
Supporting Publications6
PMIDTitleAbstract
34265469Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.
38576002Therapy-induced senescent tumor cell-derived extracellular vesicles promote colorectal cancer progression through SERPINE1-mediated NF-κB p65 nuclear translocation.No abstract available
39195200Analysis of Cytotoxic Granules and Constitutively Produced Extracellular Vesicles from Large Granular Lymphocytic Leukemia Cell Lines.No abstract available
39408670Proteomic Characterization of Corneal Epithelial and Stromal Cell-Derived Extracellular Vesicles.No abstract available
39948040Quantitative proteomics identifies possible flow of metastatic cues between progressive stages of colorectal cancer via transfer of ceramide-dependent exosomal cargoes.No abstract available
40689422Defining the Ovarian Cancer Precancerous Landscape through Modeling Fallopian Tube Epithelium Reprogramming Driven by Extracellular Vesicles.No abstract available