Q5T8P6 · RBM26_HUMAN

  • Protein
    RNA-binding protein 26
  • Gene
    RBM26
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

May be involved in the turnover of nuclear polyadenylated (pA+) RNA.

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 Componentnucleus
Molecular Functionmetal ion binding
Molecular FunctionRNA binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RNA-binding protein 26
  • Alternative names
    • CTCL tumor antigen se70-2
    • RNA-binding motif protein 26

Gene names

    • Name
      RBM26
    • Synonyms
      C13orf10
    • ORF names
      PRO1777

Organism names

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

Accessions

  • Primary accession
    Q5T8P6
  • Secondary accessions
    • B4DZE0
    • Q2NKM2
    • Q2NKQ2
    • Q5CZH8
    • Q5T8P5

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_030137718in dbSNP:rs10767

Variants

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

The viewer provides 1,039 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), cross-link, modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00002733761-1007UniProtRNA-binding protein 26
Modified residue (large scale data)90PRIDEPhosphoserine
Cross-link94UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link106UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link106UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue127UniProtPhosphoserine
Modified residue (large scale data)127PRIDEPhosphoserine
Modified residue (large scale data)131PRIDEPhosphoserine
Modified residue (large scale data)132PRIDEPhosphoserine
Modified residue (large scale data)133PRIDEPhosphoserine
Modified residue (large scale data)487PRIDEPhosphoserine
Modified residue496UniProtPhosphoserine
Modified residue (large scale data)496PRIDEPhosphoserine
Modified residue510UniProtN6-acetyllysine
Modified residue518UniProtPhosphoserine
Modified residue (large scale data)518PRIDEPhosphoserine
Modified residue (large scale data)588PRIDEPhosphoserine
Modified residue (large scale data)590PRIDEPhosphothreonine
Modified residue (large scale data)614PRIDEPhosphothreonine
Modified residue (large scale data)615PRIDEPhosphothreonine
Modified residue616UniProtPhosphoserine
Modified residue (large scale data)616PRIDEPhosphoserine
Modified residue (large scale data)795PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q5T8P6NCK2 O436393EBI-3232077, EBI-713635
View interactors in UniProtKB
View CPX-2750 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, zinc finger, domain, coiled coil.

TypeIDPosition(s)Description
Compositional bias106-124Basic and acidic residues
Region106-241Disordered
Compositional bias135-170Basic and acidic residues
Compositional bias183-226Basic and acidic residues
Zinc finger288-316C3H1-type
Compositional bias334-392Pro residues
Region334-404Disordered
Region460-519Disordered
Domain532-606RRM 1
Coiled coil719-795
Coiled coil823-847
Region853-884Disordered
Compositional bias861-877Basic residues
Domain891-960RRM 2
Region966-1007Disordered
Compositional bias969-999Acidic residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (6)
  • Sequence status
    Complete

This entry describes 6 isoforms produced by Alternative splicing.

Q5T8P6-1

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
    1,007
  • Mass (Da)
    113,597
  • Last updated
    2007-01-23 v3
  • Checksum
    DCA34DF4A9A42045
MVSKMIIENFEALKSWLSKTLEPICDADPSALAKYVLALVKKDKSEKELKALCIDQLDVFLQKETQIFVEKLFDAVNTKSYLPPPEQPSSGSLKVEFFPHQEKDIKKEEITKEEEREKKFSRRLNHSPPQSSSRYRENRSRDERKKDDRSRKRDYDRNPPRRDSYRDRYNRRRGRSRSYSRSRSRSWSKERLRERDRDRSRTRSRSRTRSRERDLVKPKYDLDRTDPLENNYTPVSSVPSISSGHYPVPTLSSTITVIAPTHHGNNTTESWSEFHEDQVDHNSYVRPPMPKKRCRDYDEKGFCMRGDMCPFDHGSDPVVVEDVNLPGMLPFPAQPPVVEGPPPPGLPPPPPILTPPPVNLRPPVPPPGPLPPSLPPVTGPPPPLPPLQPSGMDAPPNSATSSVPTVVTTGIHHQPPPAPPSLFTADTYDTDGYNPEAPSITNTSRPMYRHRVHAQRPNLIGLTSGDMDLPPREKPPNKSSMRIVVDSESRKRTIGSGEPGVPTKKTWFDKPNFNRTNSPGFQKKVQFGNENTKLELRKVPPELNNISKLNEHFSRFGTLVNLQVAYNGDPEGALIQFATYEEAKKAISSTEAVLNNRFIKVYWHREGSTQQLQTTSPKVMQPLVQQPILPVVKQSVKERLGPVPSSTIEPAEAQSASSDLPQNVTKLSVKDRLGFVSKPSVSATEKVLSTSTGLTKTVYNPAALKAAQKTLLVSTSAVDNNEAQKKKQEALKLQQDVRKRKQEILEKHIETQKMLISKLEKNKTMKSEDKAEIMKTLEVLTKNITKLKDEVKAASPGRCLPKSIKTKTQMQKELLDTELDLYKKMQAGEEVTELRRKYTELQLEAAKRGILSSGRGRGIHSRGRGAVHGRGRGRGRGRGVPGHAVVDHRPRALEISAFTESDREDLLPHFAQYGEIEDCQIDDSSLHAVITFKTRAEAEAAAVHGARFKGQDLKLAWNKPVTNISAVETEEVEPDEEEFQEESLVDDSLLQDDDEEEEDNESRSWRR

Q5T8P6-2

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

Q5T8P6-3

Q5T8P6-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q5T8P6-5

Q5T8P6-6

  • Name
    6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E2PSN0E2PSN0_HUMANRBM26171
A0A087X0H9A0A087X0H9_HUMANRBM261009

Sequence caution

The sequence AAG34912.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAB14933.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAB55125.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

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

TypeIDPosition(s)Description
Alternative sequenceVSP_0225281-446in isoform 4 and isoform 5
Sequence conflict12in Ref. 5; CAI56708
Sequence conflict66in Ref. 5; CAI56708
Compositional bias106-124Basic and acidic residues
Alternative sequenceVSP_022529110-120in isoform 6
Alternative sequenceVSP_022530121-1007in isoform 6
Compositional bias135-170Basic and acidic residues
Compositional bias183-226Basic and acidic residues
Compositional bias334-392Pro residues
Sequence conflict426in Ref. 5; CAI56708
Alternative sequenceVSP_022531619-621in isoform 3, isoform 4 and isoform 5
Alternative sequenceVSP_022532663-686in isoform 2, isoform 3 and isoform 5
Sequence conflict709in Ref. 1; BAB55046
Compositional bias861-877Basic residues
Sequence conflict900in Ref. 1; BAB55046/BAB55125
Sequence conflict959in Ref. 1; BAB14933
Compositional bias969-999Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK024610
EMBL· GenBank· DDBJ
BAB14933.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK027339
EMBL· GenBank· DDBJ
BAB55046.1
EMBL· GenBank· DDBJ
mRNA
AK027456
EMBL· GenBank· DDBJ
BAB55125.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK302871
EMBL· GenBank· DDBJ
BAG64052.1
EMBL· GenBank· DDBJ
mRNA
AF116667
EMBL· GenBank· DDBJ
AAF71087.1
EMBL· GenBank· DDBJ
mRNA
AL139006
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL159974
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC041655
EMBL· GenBank· DDBJ
AAH41655.1
EMBL· GenBank· DDBJ
mRNA
BC111697
EMBL· GenBank· DDBJ
AAI11698.1
EMBL· GenBank· DDBJ
mRNA
BC111739
EMBL· GenBank· DDBJ
AAI11740.1
EMBL· GenBank· DDBJ
mRNA
AL834343
EMBL· GenBank· DDBJ
CAD39009.3
EMBL· GenBank· DDBJ
mRNA
BX648672
EMBL· GenBank· DDBJ
CAI56708.1
EMBL· GenBank· DDBJ
mRNA
AF273052
EMBL· GenBank· DDBJ
AAG34912.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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