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Protein

NF-kappa-B-repressing factor

Gene

NKRF

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

Functioni

Interacts with a specific negative regulatory element (NRE) 5'-AATTCCTCTGA-3' to mediate transcriptional repression of certain NK-kappa-B responsive genes. Involved in the constitutive silencing of the interferon beta promoter, independently of the virus-induced signals, and in the inhibition of the basal and cytokine-induced iNOS promoter activity. Also involved in the regulation of IL-8 transcription.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi296 – 38893Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of transcription, DNA-templated Source: UniProtKB
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
NF-kappa-B-repressing factor
Short name:
NFkB-repressing factor
Alternative name(s):
Protein ITBA4
Transcription factor NRF
Gene namesi
Name:NKRF
Synonyms:ITBA4, NRF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:19374. NKRF.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: HPA
  2. nucleolus Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134990602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 690690NF-kappa-B-repressing factorPRO_0000096869Add
BLAST

Proteomic databases

MaxQBiO15226.
PaxDbiO15226.
PeptideAtlasiO15226.
PRIDEiO15226.

2D gel databases

SWISS-2DPAGEO15226.

PTM databases

PhosphoSiteiO15226.

Expressioni

Tissue specificityi

Widely and constitutively expressed. Expressed at lower level in colon, peripheral blood lymphocytes, lung and kidney.

Gene expression databases

BgeeiO15226.
CleanExiHS_NKRF.
ExpressionAtlasiO15226. baseline and differential.
GenevestigatoriO15226.

Interactioni

Subunit structurei

Interacts with NF-kappa-B.

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX58Q96C102EBI-766011,EBI-744193

Protein-protein interaction databases

BioGridi121002. 24 interactions.
DIPiDIP-34570N.
IntActiO15226. 9 interactions.
MINTiMINT-4728497.
STRINGi9606.ENSP00000304803.

Structurei

3D structure databases

ProteinModelPortaliO15226.
SMRiO15226. Positions 437-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini551 – 59646G-patchPROSITE-ProRule annotationAdd
BLAST
Domaini600 – 66465R3HPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 296296Active repression domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi25 – 4521Nuclear localization signalAdd
BLAST

Sequence similaritiesi

Contains 1 G-patch domain.PROSITE-ProRule annotation
Contains 1 R3H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG123689.
GeneTreeiENSGT00530000063234.
HOGENOMiHOG000230930.
HOVERGENiHBG052630.
InParanoidiO15226.
OMAiWRYSHES.
OrthoDBiEOG7XWPN1.
PhylomeDBiO15226.
TreeFamiTF326321.

Family and domain databases

Gene3Di3.30.1370.50. 1 hit.
3.30.160.20. 1 hit.
InterProiIPR014720. dsRNA-bd_dom.
IPR000467. G_patch_dom.
IPR001374. R3H_ss-bd.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
PF01424. R3H. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 2 hits.
SM00443. G_patch. 1 hit.
SM00393. R3H. 1 hit.
[Graphical view]
SUPFAMiSSF82708. SSF82708. 1 hit.
PROSITEiPS50174. G_PATCH. 1 hit.
PS51061. R3H. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15226-1) [UniParc]FASTAAdd to Basket

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
MEKILQMAEG IDIGEMPSYD LVLSKPSKGQ KRHLSTCDGQ NPPKKQAGSK
60 70 80 90 100
FHARPRFEPV HFVASSSKDE RQEDPYGPQT KEVNEQTHFA SMPRDIYQDY
110 120 130 140 150
TQDSFSIQDG NSQYCDSSGF ILTKDQPVTA NMYFDSGNPA PSTTSQQANS
160 170 180 190 200
QSTPEPSPSQ TFPESVVAEK QYFIEKLTAT IWKNLSNPEM TSGSDKINYT
210 220 230 240 250
YMLTRCIQAC KTNPEYIYAP LKEIPPADIP KNKKLLTDGY ACEVRCQNIY
260 270 280 290 300
LTTGYAGSKN GSRDRATELA VKLLQKRIEV RVVRRKFKHT FGEDLVVCQI
310 320 330 340 350
GMSSYEFPPA LKPPEDLVVL GKDASGQPIF NASAKHWTNF VITENANDAI
360 370 380 390 400
GILNNSASFN KMSIEYKYEM MPNRTWRCRV FLQDHCLAEG YGTKKTSKHA
410 420 430 440 450
AADEALKILQ KTQPTYPSVK SSQCHTGSSP RGSGKKKDIK DLVVYENSSN
460 470 480 490 500
PVCTLNDTAQ FNRMTVEYVY ERMTGLRWKC KVILESEVIA EAVGVKKTVK
510 520 530 540 550
YEAAGEAVKT LKKTQPTVIN NLKKGAVEDV ISRNEIQGRS AEEAYKQQIK
560 570 580 590 600
EDNIGNQLLR KMGWTGGGLG KSGEGIREPI SVKEQHKREG LGLDVERVNK
610 620 630 640 650
IAKRDIEQII RNYARSESHT DLTFSRELTN DERKQIHQIA QKYGLKSKSH
660 670 680 690
GVGHDRYLVV GRKRRKEDLL DQLKQEGQVG HYELVMPQAN
Length:690
Mass (Da):77,673
Last modified:August 15, 2003 - v2
Checksum:i3067A52671A7AE8F
GO
Isoform 2 (identifier: O15226-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGFMLPLIFRYSPRLM

Note: No experimental confirmation available.

Show »
Length:705
Mass (Da):79,496
Checksum:i48B245E4929BD14B
GO

Sequence cautioni

The sequence AL539002 differs from that shown.Probable cloning artifact.Curated
The sequence CAB56459.1 differs from that shown. Reason: Frameshift at positions 378, 405, 410, 441, 502, 516, 588, 599, 601 and 681. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711R → G in CAB56459. (PubMed:10562553)Curated
Sequence conflicti453 – 4531C → G in CAA68976. (PubMed:9224902)Curated
Sequence conflicti614 – 6152AR → ES in CAB56459. (PubMed:10562553)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGFMLPLIFRYSPRLM in isoform 2. 1 PublicationVSP_047377

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011812 mRNA. Translation: CAB56459.1. Frameshift.
AY208891 mRNA. Translation: AAP43025.1.
AC004913 Genomic DNA. No translation available.
CH471161 Genomic DNA. Translation: EAW89859.1.
BC040379 mRNA. Translation: AAH40379.1.
BC047878 mRNA. Translation: AAH47878.1.
AL539002 mRNA. No translation available.
Y07707 mRNA. Translation: CAA68976.1.
CCDSiCCDS35375.1. [O15226-1]
CCDS55486.1. [O15226-2]
RefSeqiNP_001166958.1. NM_001173487.1. [O15226-2]
NP_001166959.1. NM_001173488.1. [O15226-1]
NP_060014.2. NM_017544.3. [O15226-1]
XP_005262500.1. XM_005262443.2. [O15226-2]
UniGeneiHs.437084.

Genome annotation databases

EnsembliENST00000304449; ENSP00000304803; ENSG00000186416. [O15226-1]
ENST00000371527; ENSP00000360582; ENSG00000186416. [O15226-1]
ENST00000542113; ENSP00000442308; ENSG00000186416. [O15226-2]
GeneIDi55922.
KEGGihsa:55922.
UCSCiuc004erq.3. human. [O15226-1]
uc022cdk.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011812 mRNA. Translation: CAB56459.1. Frameshift.
AY208891 mRNA. Translation: AAP43025.1.
AC004913 Genomic DNA. No translation available.
CH471161 Genomic DNA. Translation: EAW89859.1.
BC040379 mRNA. Translation: AAH40379.1.
BC047878 mRNA. Translation: AAH47878.1.
AL539002 mRNA. No translation available.
Y07707 mRNA. Translation: CAA68976.1.
CCDSiCCDS35375.1. [O15226-1]
CCDS55486.1. [O15226-2]
RefSeqiNP_001166958.1. NM_001173487.1. [O15226-2]
NP_001166959.1. NM_001173488.1. [O15226-1]
NP_060014.2. NM_017544.3. [O15226-1]
XP_005262500.1. XM_005262443.2. [O15226-2]
UniGeneiHs.437084.

3D structure databases

ProteinModelPortaliO15226.
SMRiO15226. Positions 437-514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121002. 24 interactions.
DIPiDIP-34570N.
IntActiO15226. 9 interactions.
MINTiMINT-4728497.
STRINGi9606.ENSP00000304803.

Chemistry

ChEMBLiCHEMBL3163.

PTM databases

PhosphoSiteiO15226.

2D gel databases

SWISS-2DPAGEO15226.

Proteomic databases

MaxQBiO15226.
PaxDbiO15226.
PeptideAtlasiO15226.
PRIDEiO15226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304449; ENSP00000304803; ENSG00000186416. [O15226-1]
ENST00000371527; ENSP00000360582; ENSG00000186416. [O15226-1]
ENST00000542113; ENSP00000442308; ENSG00000186416. [O15226-2]
GeneIDi55922.
KEGGihsa:55922.
UCSCiuc004erq.3. human. [O15226-1]
uc022cdk.1. human.

Organism-specific databases

CTDi55922.
GeneCardsiGC0XM118722.
HGNCiHGNC:19374. NKRF.
MIMi300440. gene.
neXtProtiNX_O15226.
PharmGKBiPA134990602.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG123689.
GeneTreeiENSGT00530000063234.
HOGENOMiHOG000230930.
HOVERGENiHBG052630.
InParanoidiO15226.
OMAiWRYSHES.
OrthoDBiEOG7XWPN1.
PhylomeDBiO15226.
TreeFamiTF326321.

Miscellaneous databases

GeneWikiiNKRF_(gene).
GenomeRNAii55922.
NextBioi61327.
PROiO15226.
SOURCEiSearch...

Gene expression databases

BgeeiO15226.
CleanExiHS_NKRF.
ExpressionAtlasiO15226. baseline and differential.
GenevestigatoriO15226.

Family and domain databases

Gene3Di3.30.1370.50. 1 hit.
3.30.160.20. 1 hit.
InterProiIPR014720. dsRNA-bd_dom.
IPR000467. G_patch_dom.
IPR001374. R3H_ss-bd.
[Graphical view]
PfamiPF01585. G-patch. 1 hit.
PF01424. R3H. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 2 hits.
SM00443. G_patch. 1 hit.
SM00393. R3H. 1 hit.
[Graphical view]
SUPFAMiSSF82708. SSF82708. 1 hit.
PROSITEiPS50174. G_PATCH. 1 hit.
PS51061. R3H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Constitutive silencing of IFN-beta promoter is mediated by NRF (NF-kB-repressing factor), a nuclear inhibitor of NF-kB."
    Nourbakhsh M., Hauser H.
    EMBO J. 18:6415-6425(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cervix carcinoma.
  2. "Cloning and identification of human transcription factor NRF complete cDNA."
    Mao Y., Xie Y., Dai J.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pancreas and Skin.
  6. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-258 (ISOFORM 2).
    Tissue: Fetal brain.
  7. "Identification of a new member (ZNF183) of the Ring finger gene family in Xq24-25."
    Frattini A., Faranda S., Bagnasco L., Patrosso C., Nulli P., Zucchi I., Vezzoni P.
    Gene 192:291-298(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 453-690 (ISOFORM 1/2).
    Tissue: Brain.
  8. "Identification of a negative response element in the human inducible nitric-oxide synthase (hiNOS) promoter: the role of NF-kappa B-repressing factor (NRF) in basal repression of the hiNOS gene."
    Feng X., Guo Z., Nourbakhsh M., Hauser H., Ganster R., Shao L., Geller D.A.
    Proc. Natl. Acad. Sci. U.S.A. 99:14212-14217(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNKRF_HUMAN
AccessioniPrimary (citable) accession number: O15226
Secondary accession number(s): G3V1N1, Q4VC41, Q9UJ91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 15, 2003
Last modified: February 4, 2015
This is version 147 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.