Q6P4R8 · NFRKB_HUMAN
- ProteinNuclear factor related to kappa-B-binding protein
- GeneNFRKB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1299 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'.
Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Modulates the deubiquitinase activity of UCHL5 in the INO80 complex.
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 | Ino80 complex | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | protease binding | |
Biological Process | chromatin remodeling | |
Biological Process | DNA recombination | |
Biological Process | DNA repair | |
Biological Process | positive regulation of DNA repair | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | positive regulation of telomere maintenance in response to DNA damage | |
Biological Process | regulation of cell cycle | |
Biological Process | regulation of chromosome organization | |
Biological Process | regulation of DNA repair | |
Biological Process | regulation of DNA replication | |
Biological Process | regulation of DNA strand elongation | |
Biological Process | regulation of embryonic development | |
Biological Process | telomere maintenance |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNuclear factor related to kappa-B-binding protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6P4R8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,525 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), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000227807 | 1-1299 | UniProt | Nuclear factor related to kappa-B-binding protein | |||
Sequence: MDSLDHMLTDPLELGPCGDGHGTRIMEDCLLGGTRVSLPEDLLEDPEIFFDVVSLSTWQEVLSDSQREHLQQFLPQFPEDSAEQQNELILALFSGENFRFGNPLHIAQKLFRDGHFNPEVVKYRQLCFKSQYKRYLNSQQQYFHRLLKQILASRSDLLEMARRSGPALPFRQKRPSPSRTPEEREWRTQQRYLKVLREVKEECGDTALSSDEEDLSSWLPSSPARSPSPAVPLRVVPTLSTTDMKTADKVELGDSDLKIMLKKHHEKRKHQPDHPDLLTGDLTLNDIMTRVNAGRKGSLAALYDLAVLKKKVKEKEEKKKKKIKTIKSEAEDLAEPLSSTEGVAPLSQAPSPLAIPAIKEEPLEDLKPCLGINEISSSFFSLLLEILLLESQASLPMLEERVLDWQSSPASSLNSWFSAAPNWAELVLPALQYLAGESRAVPSSFSPFVEFKEKTQQWKLLGQSQDNEKELAALFQLWLETKDQAFCKQENEDSSDATTPVPRVRTDYVVRPSTGEEKRVFQEQERYRYSQPHKAFTFRMHGFESVVGPVKGVFDKETSLNKAREHSLLRSDRPAYVTILSLVRDAAARLPNGEGTRAEICELLKDSQFLAPDVTSTQVNTVVSGALDRLHYEKDPCVKYDIGRKLWIYLHRDRSEEEFERIHQAQAAAAKARKALQQKPKPPSKVKSSSKESSIKVLSSGPSEQSQMSLSDSSMPPTPVTPVTPTTPALPAIPISPPPVSAVNKSGPSTVSEPAKSSSGVLLVSSPTMPHLGTMLSPASSQTAPSSQAAARVVSHSGSAGLSQVRVVAQPSLPAVPQQSGGPAQTLPQMPAGPQIRVPATATQTKVVPQTVMATVPVKAQTTAATVQRPGPGQTGLTVTSLPATASPVSKPATSSPGTSAPSASTAAVIQNVTGQNIIKQVAITGQLGVKPQTGNSIPLTATNFRIQGKDVLRLPPSSITTDAKGQTVLRITPDMMATLAKSQVTTVKLTQDLFGTGGNTTGKGISATLHVTSNPVHAADSPAKASSASAPSSTPTGTTVVKVTPDLKPTEASSSAFRLMPALGVSVADQKGKSTVASSEAKPAATIRIVQGLGVMPPKAGQTITVATHAKQGASVASGSGTVHTSAVSLPSMNAAVSKTVAVASGAASTPISISTGAPTVRQVPVSTTVVSTSQAGKLPTRITVPLSVISQPMKGKSVVTAPIIKGNLGANLSGLGRNIILTTMPAGTKLIAGNKPVSFLTAQQLQQLQQQGQATQVRIQTVPASHLQQGTASGSSKAVSTVVVTTAPSPKQAPEQQ | |||||||
Modified residue (large scale data) | 176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 228 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 228 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 298 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 327 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 328 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 351 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 351 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 469 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 488 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 488 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 495 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 799 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 887 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 899 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1022 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1022 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1034 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1035 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1237 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1288 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1291 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1291 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in thymus, brain, testes, spleen and liver.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the N-terminus of INO80. Interacts with UCHL5; NFRKB competes with ADRM1 for interaction with UCHL5.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6P4R8 | UCHL5 Q9Y5K5 | 14 | EBI-2511210, EBI-1051183 | |
BINARY | Q6P4R8 | UCHL5 Q9Y5K5-3 | 3 | EBI-2511210, EBI-11749875 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-156 | DEUBAD | ||||
Sequence: PEDLLEDPEIFFDVVSLSTWQEVLSDSQREHLQQFLPQFPEDSAEQQNELILALFSGENFRFGNPLHIAQKLFRDGHFNPEVVKYRQLCFKSQYKRYLNSQQQYFHRLLKQILASRSD | ||||||
Region | 163-187 | Disordered | ||||
Sequence: RSGPALPFRQKRPSPSRTPEEREWR | ||||||
Region | 204-232 | Disordered | ||||
Sequence: GDTALSSDEEDLSSWLPSSPARSPSPAVP | ||||||
Compositional bias | 210-224 | Polar residues | ||||
Sequence: SDEEDLSSWLPSSPA | ||||||
Region | 370-495 | Winged-helix like domain | ||||
Sequence: LGINEISSSFFSLLLEILLLESQASLPMLEERVLDWQSSPASSLNSWFSAAPNWAELVLPALQYLAGESRAVPSSFSPFVEFKEKTQQWKLLGQSQDNEKELAALFQLWLETKDQAFCKQENEDSS | ||||||
Region | 669-760 | Disordered | ||||
Sequence: AAKARKALQQKPKPPSKVKSSSKESSIKVLSSGPSEQSQMSLSDSSMPPTPVTPVTPTTPALPAIPISPPPVSAVNKSGPSTVSEPAKSSSG | ||||||
Compositional bias | 682-717 | Polar residues | ||||
Sequence: PPSKVKSSSKESSIKVLSSGPSEQSQMSLSDSSMPP | ||||||
Compositional bias | 718-738 | Pro residues | ||||
Sequence: TPVTPVTPTTPALPAIPISPP | ||||||
Compositional bias | 742-760 | Polar residues | ||||
Sequence: AVNKSGPSTVSEPAKSSSG | ||||||
Region | 882-902 | Disordered | ||||
Sequence: LPATASPVSKPATSSPGTSAP | ||||||
Region | 1017-1043 | Disordered | ||||
Sequence: VHAADSPAKASSASAPSSTPTGTTVVK | ||||||
Compositional bias | 1026-1043 | Polar residues | ||||
Sequence: ASSASAPSSTPTGTTVVK |
Domain
NFRKB seems to be mostly disordered. The wing-helix like domain doesn't bind DNA.
Sequence similarities
Belongs to the NFRKB family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6P4R8-1
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
- Length1,299
- Mass (Da)139,001
- Last updated2006-03-21 v2
- Checksum087B212E283C3820
Q6P4R8-2
- Name2
Q6P4R8-3
- Name3
- Differences from canonical
- 687-687: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_017592 | 1 | in isoform 2 | |||
Sequence: M → MHVFVQSTCGEETM | ||||||
Compositional bias | 210-224 | Polar residues | ||||
Sequence: SDEEDLSSWLPSSPA | ||||||
Alternative sequence | VSP_017593 | 213 | in isoform 2 | |||
Sequence: E → EATLDLQEQFSFE | ||||||
Compositional bias | 682-717 | Polar residues | ||||
Sequence: PPSKVKSSSKESSIKVLSSGPSEQSQMSLSDSSMPP | ||||||
Alternative sequence | VSP_017594 | 687 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 718-738 | Pro residues | ||||
Sequence: TPVTPVTPTTPALPAIPISPP | ||||||
Compositional bias | 742-760 | Polar residues | ||||
Sequence: AVNKSGPSTVSEPAKSSSG | ||||||
Compositional bias | 1026-1043 | Polar residues | ||||
Sequence: ASSASAPSSTPTGTTVVK | ||||||
Sequence conflict | 1178 | in Ref. 3; AAH63280 | ||||
Sequence: G → E | ||||||
Sequence conflict | 1213 | in Ref. 3; AAH63280 | ||||
Sequence: N → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U08191 EMBL· GenBank· DDBJ | AAA17871.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
X80878 EMBL· GenBank· DDBJ | CAA56846.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063280 EMBL· GenBank· DDBJ | AAH63280.1 EMBL· GenBank· DDBJ | mRNA | ||
AL512730 EMBL· GenBank· DDBJ | CAC21663.1 EMBL· GenBank· DDBJ | mRNA |