Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-binding protein RFXANK

Gene

RFXANK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates transcription from class II MHC promoters. Activation requires the activity of the MHC class II transactivator/CIITA. May regulate other genes in the cell. RFX binds the X1 box of MHC-II promoters (PubMed:9806546, PubMed:10072068, PubMed:10725724). May also potentiate the activation of RAF1 (By similarity).By similarity3 Publications
Isoform 2 is not involved in the positive regulation of MHC class II genes.1 Publication

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • transcription cofactor activity Source: ProtInc
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000064490-MONOMER.
SIGNORiO14593.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein RFXANK
Alternative name(s):
Ankyrin repeat family A protein 1
Regulatory factor X subunit B
Short name:
RFX-B
Regulatory factor X-associated ankyrin-containing protein
Gene namesi
Name:RFXANK
Synonyms:ANKRA1, RFXB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9987. RFXANK.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Bare lymphocyte syndrome 2 (BLS2)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe combined immunodeficiency disease with early onset. It is characterized by a profound defect in constitutive and interferon-gamma induced MHC II expression, absence of cellular and humoral T-cell response to antigen challenge, hypogammaglobulinemia and impaired antibody production. The consequence include extreme susceptibility to viral, bacterial and fungal infections.
See also OMIM:209920
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_009941195L → P in BLS2; loss of expression. 2 PublicationsCorresponds to variant rs751386365dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121D → V: Loss of expression. 1 Publication1
Mutagenesisi224Y → A: Loss of interaction with RFX5. 1 Publication1

Keywords - Diseasei

Disease mutation, SCID

Organism-specific databases

DisGeNETi8625.
MalaCardsiRFXANK.
MIMi209920. phenotype.
OpenTargetsiENSG00000064490.
Orphaneti572. Immunodeficiency by defective expression of HLA class 2.
PharmGKBiPA34357.

Polymorphism and mutation databases

BioMutaiRFXANK.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000670491 – 260DNA-binding protein RFXANKAdd BLAST260

Post-translational modificationi

Phosphorylated by RAF1.By similarity

Proteomic databases

MaxQBiO14593.
PaxDbiO14593.
PeptideAtlasiO14593.
PRIDEiO14593.

PTM databases

iPTMnetiO14593.
PhosphoSitePlusiO14593.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000064490.
CleanExiHS_RFXANK.
ExpressionAtlasiO14593. baseline and differential.
GenevisibleiO14593. HS.

Organism-specific databases

HPAiHPA049157.
HPA053330.

Interactioni

Subunit structurei

Forms homodimers (By similarity). The RFX heterotetrameric complex consists of 2 molecules of RFX5 and one each of RFXAP and RFX-B/RFXANK; with each subunit representing a separate complementation group. Interacts (via ankyrin repeats) with RFX5 (via PxLPxI/L motif); the interaction is direct. RFX forms cooperative DNA binding complexes with X2BP and CBF/NF-Y. RFX associates with CIITA to form an active transcriptional complex (PubMed:20732328, PubMed:22649097). Interacts with RAF1 (By similarity). Interacts (via ankyrin repeats) with RFX7 (via PxLPxI/L motif) (PubMed:25752541).By similarity3 PublicationsImported

Protein-protein interaction databases

BioGridi114180. 38 interactors.
STRINGi9606.ENSP00000305071.

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi94 – 99Combined sources6
Helixi103 – 110Combined sources8
Helixi115 – 118Combined sources4
Helixi127 – 133Combined sources7
Helixi137 – 146Combined sources10
Helixi160 – 166Combined sources7
Helixi170 – 177Combined sources8
Turni178 – 180Combined sources3
Helixi193 – 199Combined sources7
Helixi203 – 211Combined sources9
Helixi226 – 233Combined sources8
Helixi236 – 249Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UXGX-ray1.85A90-260[»]
3V30X-ray1.57A90-260[»]
4QQMX-ray1.78A/C90-260[»]
ProteinModelPortaliO14593.
SMRiO14593.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati89 – 118ANK 1Add BLAST30
Repeati123 – 152ANK 2Add BLAST30
Repeati156 – 185ANK 3Add BLAST30
Repeati189 – 218ANK 4Add BLAST30
Repeati222 – 251ANK 5Add BLAST30

Domaini

Interacts with RAF1 via its C-terminal ankyrin repeat domain. The same domain also mediates its homodimerization (By similarity). The third ankyrin repeat is required for association with the two other RFX subunits; RFX5 and RFXAP. The three central ANK repeats mediate binding to the PxLPxI/L motif of RFX5 (PubMed:20732328, PubMed:22649097).By similarity2 Publications

Sequence similaritiesi

Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0502. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00860000133759.
HOGENOMiHOG000294108.
HOVERGENiHBG017718.
InParanoidiO14593.
KOiK08062.
OMAiGADSGHM.
OrthoDBiEOG091G0BD5.
PhylomeDBiO14593.
TreeFamiTF333112.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017362. DNA-bd_RFXANK.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF13606. Ank_3. 1 hit.
[Graphical view]
PIRSFiPIRSF038034. DNA-binding_RFXANK. 1 hit.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14593-1) [UniParc]FASTAAdd to basket
Also known as: Long

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.

« Hide

        10         20         30         40         50
MELTQPAEDL IQTQQTPASE LGDPEDPGEE AADGSDTVVL SLFPCTPEPV
60 70 80 90 100
NPEPDASVSS PQAGSSLKHS TTLTNRQRGN EVSALPATLD SLSIHQLAAQ
110 120 130 140 150
GELDQLKEHL RKGDNLVNKP DERGFTPLIW ASAFGEIETV RFLLEWGADP
160 170 180 190 200
HILAKERESA LSLASTGGYT DIVGLLLERD VDINIYDWNG GTPLLYAVRG
210 220 230 240 250
NHVKCVEALL ARGADLTTEA DSGYTPMDLA VALGYRKVQQ VIENHILKLF
260
QSNLVPADPE
Length:260
Mass (Da):28,102
Last modified:July 15, 1999 - v2
Checksum:i6280B490F54816D2
GO
Isoform 2 (identifier: O14593-2) [UniParc]FASTAAdd to basket
Also known as: RFX-B-delta5

The sequence of this isoform differs from the canonical sequence as follows:
     63-63: Missing.
     91-113: SLSIHQLAAQGELDQLKEHLRKG → C
     159-172: Missing.

Show »
Length:223
Mass (Da):24,243
Checksum:iD0CC4523D656840B
GO
Isoform 3 (identifier: O14593-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     91-113: SLSIHQLAAQGELDQLKEHLRKG → C

Note: No experimental confirmation available.
Show »
Length:238
Mass (Da):25,652
Checksum:iCD46F8F674173B9E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04831148E → D.Corresponds to variant rs34282046dbSNPEnsembl.1
Natural variantiVAR_009941195L → P in BLS2; loss of expression. 2 PublicationsCorresponds to variant rs751386365dbSNPEnsembl.1
Natural variantiVAR_014472251Q → E.Corresponds to variant rs1802498dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00028363Missing in isoform 2. 1 Publication1
Alternative sequenceiVSP_00028491 – 113SLSIH…HLRKG → C in isoform 2 and isoform 3. 2 PublicationsAdd BLAST23
Alternative sequenceiVSP_054618159 – 172Missing in isoform 2. 1 PublicationAdd BLAST14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF094760 mRNA. Translation: AAC69883.1.
AF105427 mRNA. Translation: AAD17972.1.
AF105428 mRNA. Translation: AAD17973.1.
AF077196 mRNA. Translation: AAD26991.1.
CR542199 mRNA. Translation: CAG46996.1.
AC002126 Genomic DNA. No translation available.
AC003110 Genomic DNA. Translation: AAB86654.1.
CH471106 Genomic DNA. Translation: EAW84795.1.
BC114558 mRNA. Translation: AAI14559.1.
BC114563 mRNA. Translation: AAI14564.1.
CCDSiCCDS12395.1. [O14593-1]
CCDS62611.1. [O14593-3]
RefSeqiNP_001265656.1. NM_001278727.1. [O14593-3]
NP_001265657.1. NM_001278728.1.
NP_003712.1. NM_003721.3. [O14593-1]
NP_604389.1. NM_134440.2.
XP_005260191.1. XM_005260134.4. [O14593-1]
XP_005260192.1. XM_005260135.3. [O14593-1]
XP_016882904.1. XM_017027415.1. [O14593-1]
XP_016882905.1. XM_017027416.1. [O14593-3]
UniGeneiHs.153629.
Hs.296776.

Genome annotation databases

EnsembliENST00000303088; ENSP00000305071; ENSG00000064490. [O14593-1]
ENST00000407360; ENSP00000384572; ENSG00000064490. [O14593-1]
ENST00000456252; ENSP00000409138; ENSG00000064490. [O14593-3]
GeneIDi8625.
KEGGihsa:8625.
UCSCiuc002nls.4. human. [O14593-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

RFXANKbase

RFXANK mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF094760 mRNA. Translation: AAC69883.1.
AF105427 mRNA. Translation: AAD17972.1.
AF105428 mRNA. Translation: AAD17973.1.
AF077196 mRNA. Translation: AAD26991.1.
CR542199 mRNA. Translation: CAG46996.1.
AC002126 Genomic DNA. No translation available.
AC003110 Genomic DNA. Translation: AAB86654.1.
CH471106 Genomic DNA. Translation: EAW84795.1.
BC114558 mRNA. Translation: AAI14559.1.
BC114563 mRNA. Translation: AAI14564.1.
CCDSiCCDS12395.1. [O14593-1]
CCDS62611.1. [O14593-3]
RefSeqiNP_001265656.1. NM_001278727.1. [O14593-3]
NP_001265657.1. NM_001278728.1.
NP_003712.1. NM_003721.3. [O14593-1]
NP_604389.1. NM_134440.2.
XP_005260191.1. XM_005260134.4. [O14593-1]
XP_005260192.1. XM_005260135.3. [O14593-1]
XP_016882904.1. XM_017027415.1. [O14593-1]
XP_016882905.1. XM_017027416.1. [O14593-3]
UniGeneiHs.153629.
Hs.296776.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UXGX-ray1.85A90-260[»]
3V30X-ray1.57A90-260[»]
4QQMX-ray1.78A/C90-260[»]
ProteinModelPortaliO14593.
SMRiO14593.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114180. 38 interactors.
STRINGi9606.ENSP00000305071.

PTM databases

iPTMnetiO14593.
PhosphoSitePlusiO14593.

Polymorphism and mutation databases

BioMutaiRFXANK.

Proteomic databases

MaxQBiO14593.
PaxDbiO14593.
PeptideAtlasiO14593.
PRIDEiO14593.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303088; ENSP00000305071; ENSG00000064490. [O14593-1]
ENST00000407360; ENSP00000384572; ENSG00000064490. [O14593-1]
ENST00000456252; ENSP00000409138; ENSG00000064490. [O14593-3]
GeneIDi8625.
KEGGihsa:8625.
UCSCiuc002nls.4. human. [O14593-1]

Organism-specific databases

CTDi8625.
DisGeNETi8625.
GeneCardsiRFXANK.
HGNCiHGNC:9987. RFXANK.
HPAiHPA049157.
HPA053330.
MalaCardsiRFXANK.
MIMi209920. phenotype.
603200. gene.
neXtProtiNX_O14593.
OpenTargetsiENSG00000064490.
Orphaneti572. Immunodeficiency by defective expression of HLA class 2.
PharmGKBiPA34357.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0502. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00860000133759.
HOGENOMiHOG000294108.
HOVERGENiHBG017718.
InParanoidiO14593.
KOiK08062.
OMAiGADSGHM.
OrthoDBiEOG091G0BD5.
PhylomeDBiO14593.
TreeFamiTF333112.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000064490-MONOMER.
SIGNORiO14593.

Miscellaneous databases

GeneWikiiRFXANK.
GenomeRNAii8625.
PROiO14593.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000064490.
CleanExiHS_RFXANK.
ExpressionAtlasiO14593. baseline and differential.
GenevisibleiO14593. HS.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR017362. DNA-bd_RFXANK.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF13606. Ank_3. 1 hit.
[Graphical view]
PIRSFiPIRSF038034. DNA-binding_RFXANK. 1 hit.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRFXK_HUMAN
AccessioniPrimary (citable) accession number: O14593
Secondary accession number(s): O95839, Q24JQ1, Q6FGA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 30, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.