Q5T8P6 · RBM26_HUMAN
- ProteinRNA-binding protein 26
- GeneRBM26
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1007 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA-binding protein 26
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5T8P6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_030137 | 718 | in dbSNP:rs10767 | |||
Sequence: V → D |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), cross-link, modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000273376 | 1-1007 | UniProt | RNA-binding protein 26 | |||
Sequence: MVSKMIIENFEALKSWLSKTLEPICDADPSALAKYVLALVKKDKSEKELKALCIDQLDVFLQKETQIFVEKLFDAVNTKSYLPPPEQPSSGSLKVEFFPHQEKDIKKEEITKEEEREKKFSRRLNHSPPQSSSRYRENRSRDERKKDDRSRKRDYDRNPPRRDSYRDRYNRRRGRSRSYSRSRSRSWSKERLRERDRDRSRTRSRSRTRSRERDLVKPKYDLDRTDPLENNYTPVSSVPSISSGHYPVPTLSSTITVIAPTHHGNNTTESWSEFHEDQVDHNSYVRPPMPKKRCRDYDEKGFCMRGDMCPFDHGSDPVVVEDVNLPGMLPFPAQPPVVEGPPPPGLPPPPPILTPPPVNLRPPVPPPGPLPPSLPPVTGPPPPLPPLQPSGMDAPPNSATSSVPTVVTTGIHHQPPPAPPSLFTADTYDTDGYNPEAPSITNTSRPMYRHRVHAQRPNLIGLTSGDMDLPPREKPPNKSSMRIVVDSESRKRTIGSGEPGVPTKKTWFDKPNFNRTNSPGFQKKVQFGNENTKLELRKVPPELNNISKLNEHFSRFGTLVNLQVAYNGDPEGALIQFATYEEAKKAISSTEAVLNNRFIKVYWHREGSTQQLQTTSPKVMQPLVQQPILPVVKQSVKERLGPVPSSTIEPAEAQSASSDLPQNVTKLSVKDRLGFVSKPSVSATEKVLSTSTGLTKTVYNPAALKAAQKTLLVSTSAVDNNEAQKKKQEALKLQQDVRKRKQEILEKHIETQKMLISKLEKNKTMKSEDKAEIMKTLEVLTKNITKLKDEVKAASPGRCLPKSIKTKTQMQKELLDTELDLYKKMQAGEEVTELRRKYTELQLEAAKRGILSSGRGRGIHSRGRGAVHGRGRGRGRGRGVPGHAVVDHRPRALEISAFTESDREDLLPHFAQYGEIEDCQIDDSSLHAVITFKTRAEAEAAAVHGARFKGQDLKLAWNKPVTNISAVETEEVEPDEEEFQEESLVDDSLLQDDDEEEEDNESRSWRR | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 94 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 106 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 106 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 127 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 127 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 131 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 132 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 133 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 487 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 496 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 496 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 510 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 518 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 590 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 615 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 616 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 616 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 795 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5T8P6 | NCK2 O43639 | 3 | EBI-3232077, EBI-713635 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, zinc finger, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 106-124 | Basic and acidic residues | ||||
Sequence: KKEEITKEEEREKKFSRRL | ||||||
Region | 106-241 | Disordered | ||||
Sequence: KKEEITKEEEREKKFSRRLNHSPPQSSSRYRENRSRDERKKDDRSRKRDYDRNPPRRDSYRDRYNRRRGRSRSYSRSRSRSWSKERLRERDRDRSRTRSRSRTRSRERDLVKPKYDLDRTDPLENNYTPVSSVPSI | ||||||
Compositional bias | 135-170 | Basic and acidic residues | ||||
Sequence: YRENRSRDERKKDDRSRKRDYDRNPPRRDSYRDRYN | ||||||
Compositional bias | 183-226 | Basic and acidic residues | ||||
Sequence: RSRSWSKERLRERDRDRSRTRSRSRTRSRERDLVKPKYDLDRTD | ||||||
Zinc finger | 288-316 | C3H1-type | ||||
Sequence: PMPKKRCRDYDEKGFCMRGDMCPFDHGSD | ||||||
Compositional bias | 334-392 | Pro residues | ||||
Sequence: QPPVVEGPPPPGLPPPPPILTPPPVNLRPPVPPPGPLPPSLPPVTGPPPPLPPLQPSGM | ||||||
Region | 334-404 | Disordered | ||||
Sequence: QPPVVEGPPPPGLPPPPPILTPPPVNLRPPVPPPGPLPPSLPPVTGPPPPLPPLQPSGMDAPPNSATSSVP | ||||||
Region | 460-519 | Disordered | ||||
Sequence: IGLTSGDMDLPPREKPPNKSSMRIVVDSESRKRTIGSGEPGVPTKKTWFDKPNFNRTNSP | ||||||
Domain | 532-606 | RRM 1 | ||||
Sequence: TKLELRKVPPELNNISKLNEHFSRFGTLVNLQVAYNGDPEGALIQFATYEEAKKAISSTEAVLNNRFIKVYWHRE | ||||||
Coiled coil | 719-795 | |||||
Sequence: DNNEAQKKKQEALKLQQDVRKRKQEILEKHIETQKMLISKLEKNKTMKSEDKAEIMKTLEVLTKNITKLKDEVKAAS | ||||||
Coiled coil | 823-847 | |||||
Sequence: KKMQAGEEVTELRRKYTELQLEAAK | ||||||
Region | 853-884 | Disordered | ||||
Sequence: SGRGRGIHSRGRGAVHGRGRGRGRGRGVPGHA | ||||||
Compositional bias | 861-877 | Basic residues | ||||
Sequence: SRGRGAVHGRGRGRGRG | ||||||
Domain | 891-960 | RRM 2 | ||||
Sequence: RALEISAFTESDREDLLPHFAQYGEIEDCQIDDSSLHAVITFKTRAEAEAAAVHGARFKGQDLKLAWNKP | ||||||
Region | 966-1007 | Disordered | ||||
Sequence: AVETEEVEPDEEEFQEESLVDDSLLQDDDEEEEDNESRSWRR | ||||||
Compositional bias | 969-999 | Acidic residues | ||||
Sequence: TEEVEPDEEEFQEESLVDDSLLQDDDEEEED |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length1,007
- Mass (Da)113,597
- Last updated2007-01-23 v3
- ChecksumDCA34DF4A9A42045
Q5T8P6-2
- Name2
- Differences from canonical
- 663-686: Missing
Q5T8P6-3
- Name3
Q5T8P6-4
- Name4
Q5T8P6-5
- Name5
Q5T8P6-6
- Name6
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E2PSN0 | E2PSN0_HUMAN | RBM26 | 171 | ||
A0A087X0H9 | A0A087X0H9_HUMAN | RBM26 | 1009 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_022528 | 1-446 | in isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 12 | in Ref. 5; CAI56708 | ||||
Sequence: A → T | ||||||
Sequence conflict | 66 | in Ref. 5; CAI56708 | ||||
Sequence: Q → H | ||||||
Compositional bias | 106-124 | Basic and acidic residues | ||||
Sequence: KKEEITKEEEREKKFSRRL | ||||||
Alternative sequence | VSP_022529 | 110-120 | in isoform 6 | |||
Sequence: ITKEEEREKKF → VTICVNTLQVI | ||||||
Alternative sequence | VSP_022530 | 121-1007 | in isoform 6 | |||
Sequence: Missing | ||||||
Compositional bias | 135-170 | Basic and acidic residues | ||||
Sequence: YRENRSRDERKKDDRSRKRDYDRNPPRRDSYRDRYN | ||||||
Compositional bias | 183-226 | Basic and acidic residues | ||||
Sequence: RSRSWSKERLRERDRDRSRTRSRSRTRSRERDLVKPKYDLDRTD | ||||||
Compositional bias | 334-392 | Pro residues | ||||
Sequence: QPPVVEGPPPPGLPPPPPILTPPPVNLRPPVPPPGPLPPSLPPVTGPPPPLPPLQPSGM | ||||||
Sequence conflict | 426 | in Ref. 5; CAI56708 | ||||
Sequence: D → A | ||||||
Alternative sequence | VSP_022531 | 619-621 | in isoform 3, isoform 4 and isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022532 | 663-686 | in isoform 2, isoform 3 and isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 709 | in Ref. 1; BAB55046 | ||||
Sequence: K → E | ||||||
Compositional bias | 861-877 | Basic residues | ||||
Sequence: SRGRGAVHGRGRGRGRG | ||||||
Sequence conflict | 900 | in Ref. 1; BAB55046/BAB55125 | ||||
Sequence: E → G | ||||||
Sequence conflict | 959 | in Ref. 1; BAB14933 | ||||
Sequence: K → E | ||||||
Compositional bias | 969-999 | Acidic residues | ||||
Sequence: TEEVEPDEEEFQEESLVDDSLLQDDDEEEED |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |