Q14D04 · MELT_HUMAN

  • Protein
    Ventricular zone-expressed PH domain-containing protein homolog 1
  • Gene
    VEPH1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits dissociation of activated SMAD2 from TGFBR1, impeding its nuclear accumulation and resulting in impaired TGF-beta signaling. May also affect FOXO, Hippo and Wnt signaling.

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 Componentplasma membrane
Molecular Functionphosphatidylinositol-5-phosphate binding
Biological Processnegative regulation of SMAD protein signal transduction
Biological Processnegative regulation of transforming growth factor beta receptor signaling pathway
Biological Processregulation of signal transduction

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ventricular zone-expressed PH domain-containing protein homolog 1
  • Alternative names
    • Protein melted

Gene names

    • Name
      VEPH1
    • Synonyms
      KIAA1692, VEPH

Organism names

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

Accessions

  • Primary accession
    Q14D04
  • Secondary accessions
    • D3DNL0
    • F5GZ91
    • Q2TAA9
    • Q3MIX2
    • Q6PEL3

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Peripheral membrane protein

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_034692208in dbSNP:rs34559487
Natural variantVAR_034693263in dbSNP:rs1378796
Natural variantVAR_034694271in dbSNP:rs1378795
Natural variantVAR_034695319in dbSNP:rs11923380
Natural variantVAR_034696329in dbSNP:rs34823544
Natural variantVAR_034697365in dbSNP:rs16827563
Natural variantVAR_061683501in dbSNP:rs59504298
Natural variantVAR_034698522in dbSNP:rs11918974

Variants

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

The viewer provides 1,123 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002979551-833UniProtVentricular zone-expressed PH domain-containing protein homolog 1
Modified residue (large scale data)353PRIDEPhosphoserine
Modified residue (large scale data)380PRIDEPhosphoserine
Modified residue (large scale data)420PRIDEPhosphoserine
Modified residue (large scale data)422PRIDEPhosphothreonine
Modified residue (large scale data)425PRIDEPhosphoserine
Modified residue (large scale data)430PRIDEPhosphoserine
Modified residue (large scale data)449PRIDEPhosphoserine
Modified residue (large scale data)462PRIDEPhosphoserine
Modified residue (large scale data)529PRIDEPhosphoserine

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with TGFBR1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q14D04SCRIB Q141602EBI-1043669, EBI-357345

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region201-319Interaction with TGFBR1
Region458-505Disordered
Region663-833Interaction with TGFBR1
Domain716-819PH

Domain

The PH domain is required for membrane targeting.

Sequence similarities

Belongs to the MELT/VEPH family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

Q14D04-1

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
    833
  • Mass (Da)
    94,745
  • Last updated
    2006-08-22 v1
  • Checksum
    34995B4AB43474A4
MHQLFRLVLGQKDLSRAGDLFSLDDSEIEDSLTEALEQIKIISSSSDYQTNNNDQAVVEICITRITTAIRETESIEKHAKALVGLWDSCLEHNLRPFGKDEDTPHAKIASDIMSCILQNYNRPPVMALAIPIAVKFLHRGNKELCRNMSNYLSLAAITKADLLADHTEVIVKSILQGNTMLLRVLPAVYEKQPQPINRHLTELLALMSQLEQPEQYHLLRLLHVAAKKKQLEVVQKCIPFLIGHLKDSTHNDIILNILIEIAVYEPVALNSFLPMLKEIGERFPYLTGQMARIYGAVGHVDEERARSCLTYLVSQLANMEHSFHHILLLEIKSITDTFSSILGPQSRDIFRMSNSFTAIAKLLTRQLENTKAGSGRRKISTEIEFPEKLEETKLIVTENEDHEKLQVKIQAFEDKINAGSNTPGSIRRYSLGQVSKEERKNIRFNRSKSLAFHTMLTKGVGSDDGEDENRGDIPASISLSEIDPLGQGNDKLPFKTDTERSQLGESSVSYPNIIHIDSENLSETVKENSQEETPETTASPIEYQDKLYLHLKKNLSKVKAYAMEIGKKIPVPDQCTIEDTVRSCVAKLFFTCSLKGHYCLYSKSSFILISQEPQPWIQIMFLFQQSLFPEPLSIQSHSVQFLRALWEKTQAGGAHSFETAMMESTFPQQKDLDQVQLHLEEVRFFDVFGFSETAGAWQCFMCNNPEKATVVNQDGQPLIEGKLKEKQVRWKFIKRWKTRYFTLAGNQLLFQKGKSKDDPDDCPIELSKVQSVKAVAKKRRDRSLPRAFEIFTDNKTYVFKAKDEKNAEEWLQCINVAVAQAKERESREVTTYL

Q14D04-2

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

Q14D04-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 178-213: NTMLLRVLPAVYEKQPQPINRHLTELLALMSQLEQP → MVRKLSLGTCFGRYLKVFSSSIYGLWEARPRVLEAN
    • 214-833: Missing

Q14D04-4

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9IZY4C9IZY4_HUMANVEPH1120
C9J379C9J379_HUMANVEPH155
C9J4U8C9J4U8_HUMANVEPH162
F8WBD3F8WBD3_HUMANVEPH152
F8WBQ3F8WBQ3_HUMANVEPH169
C9JRT0C9JRT0_HUMANVEPH1165

Sequence caution

The sequence BAB14165.1 differs from that shown. Reason: Erroneous initiation
The sequence BAB21783.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_047655177in isoform 4
Alternative sequenceVSP_027431178-213in isoform 3
Alternative sequenceVSP_047656178-833in isoform 4
Alternative sequenceVSP_027432214-833in isoform 3
Sequence conflict259in Ref. 2; BAB55243
Alternative sequenceVSP_027433626-670in isoform 2
Sequence conflict808in Ref. 2; BAB55243

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB051479
EMBL· GenBank· DDBJ
BAB21783.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK022666
EMBL· GenBank· DDBJ
BAB14165.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK027625
EMBL· GenBank· DDBJ
BAB55243.1
EMBL· GenBank· DDBJ
mRNA
AL713656
EMBL· GenBank· DDBJ
CAD28465.2
EMBL· GenBank· DDBJ
mRNA
AC020630
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC092944
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471052
EMBL· GenBank· DDBJ
EAW78705.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471052
EMBL· GenBank· DDBJ
EAW78706.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471052
EMBL· GenBank· DDBJ
EAW78707.1
EMBL· GenBank· DDBJ
Genomic DNA
BC042159
EMBL· GenBank· DDBJ
AAH42159.1
EMBL· GenBank· DDBJ
mRNA
BC057999
EMBL· GenBank· DDBJ
AAH57999.1
EMBL· GenBank· DDBJ
mRNA
BC101660
EMBL· GenBank· DDBJ
AAI01661.1
EMBL· GenBank· DDBJ
mRNA
BC111017
EMBL· GenBank· DDBJ
AAI11018.1
EMBL· GenBank· DDBJ
mRNA
BC113555
EMBL· GenBank· DDBJ
AAI13556.1
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