Q9UMS5 · PHTF1_HUMAN

  • Protein
    Protein PHTF1
  • Gene
    PHTF1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

Caution

The PHTF domain was initially defined as an atypical homeodomain, suggesting that this protein could act as a transcription regulator (PubMed:10395808).
However, the protein is not found in the nucleus and mainly localizes in the endoplasmic reticulum membrane, suggesting that it does not act as a transcription factor (By similarity).

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 Componentcis-Golgi network membrane
Cellular Componentendoplasmic reticulum membrane

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein PHTF1

Gene names

    • Name
      PHTF1
    • Synonyms
      PHTF

Organism names

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

Accessions

  • Primary accession
    Q9UMS5
  • Secondary accessions
    • Q5VWP7
    • Q5VWP8
    • Q9BUP2
    • Q9H1X8

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum membrane
; Multi-pass membrane protein
Golgi apparatus, cis-Golgi network membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane77-97Helical
Transmembrane99-119Helical
Transmembrane121-141Helical
Transmembrane473-493Helical
Transmembrane512-532Helical
Transmembrane611-631Helical
Transmembrane645-665Helical
Transmembrane737-757Helical

Keywords

Disease & Variants

Variants

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

The viewer provides 880 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, glycosylation, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001274231-762UniProtProtein PHTF1
Glycosylation179UniProtN-linked (GlcNAc...) asparagine
Glycosylation180UniProtN-linked (GlcNAc...) asparagine
Modified residue272UniProtPhosphoserine
Modified residue (large scale data)272PRIDEPhosphoserine
Modified residue276UniProtPhosphoserine
Modified residue (large scale data)276PRIDEPhosphoserine
Modified residue277UniProtPhosphoserine
Modified residue (large scale data)277PRIDEPhosphoserine
Modified residue334UniProtPhosphoserine
Modified residue336UniProtPhosphoserine
Glycosylation363UniProtN-linked (GlcNAc...) asparagine
Glycosylation431UniProtN-linked (GlcNAc...) asparagine
Glycosylation674UniProtN-linked (GlcNAc...) asparagine
Glycosylation733UniProtN-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed with highest levels in testis.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with FEM1B.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain6-150PHTF
Region152-184Disordered
Compositional bias344-365Polar residues
Region344-380Disordered
Compositional bias366-380Basic and acidic residues
Compositional bias393-407Polar residues
Region393-415Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9UMS5-1

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
    762
  • Mass (Da)
    87,252
  • Last updated
    2005-07-19 v2
  • Checksum
    0813B7A668262DD9
MASNERDAISWYQKKIGAYDQQIWEKSIEQTQIKGLKNKPKKMGHIKPDLIDVDLIRGSTFAKAKPEIPWTSLTRKGLVRVVFFPLFSNWWIQVTSLRIFVWLLLLYFMQVIAIVLYLMMPIVNISEVLGPLCLMLLMGTVHCQIVSTQITRPSGNNGNRRRRKLRKTVNGDGSRENGNNSSDKVRGIETLESVPIIGGFWETIFGNRIKRVKLISNKGTETDNDPSCVHPIIKRRQCRPEIRMWQTREKAKFSDGEKCRREAFRRLGNGVSDDLSSEEDGEARTQMILLRRSVEGASSDNGCEVKNRKSILSRHLNSQVKKTTTRWCHIVRDSDSLAESEFESAAFSQGSRSGVSGGSRSLNMSRRDSESTRHDSETEDMLWDDLLHGPECRSSVTSDSEGAHVNTLHSGTKRDPKEDVFQQNHLFWLQNSSPSSDRVSAIIWEGNECKKMDMSVLEISGIIMSRVNAYQQGVGYQMLGNVVTIGLAFFPFLHRLFREKSLDQLKSISAEEILTLFCGAPPVTPIIVLSIINFFERLCLTWMFFFMMCVAERTYKQRFLFAKLFSHITSARKARKYEIPHFRLKKVENIKIWLSLRSYLKRRGPQRSVDVVVSSVFLLTLSIAFICCAQVLQGHKTFLNDAYNWEFLIWETALLLFLLRLASLGSETNKKYSNVSILLTEQINLYLKMEKKPNKKEQLTLVNNVLKLSTKLLKELDTPFRLYGLTMNPLIYNITRVVILSAVSGVISDLLGFNIRLWKIKS

Q9UMS5-2

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

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q5TCQ3Q5TCQ3_HUMANPHTF1709
Q5TCQ5Q5TCQ5_HUMANPHTF1717
H0Y825H0Y825_HUMANPHTF1331
F6T5D1F6T5D1_HUMANPHTF1105

Features

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

TypeIDPosition(s)Description
Sequence conflict245in Ref. 1; CAB51572
Sequence conflict251in Ref. 1; CAB51572
Compositional bias344-365Polar residues
Compositional bias366-380Basic and acidic residues
Compositional bias393-407Polar residues
Sequence conflict518in Ref. 1; CAB51572
Sequence conflict529in Ref. 1; CAB51572
Alternative sequenceVSP_002144632-637in isoform 2
Sequence conflict638in Ref. 1; CAB51572
Alternative sequenceVSP_002145638-762in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ011863
EMBL· GenBank· DDBJ
CAB51572.1
EMBL· GenBank· DDBJ
mRNA
AL365321
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL133517
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC002447
EMBL· GenBank· DDBJ
AAH02447.1
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.
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