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Q7Z5L9 (I2BP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon regulatory factor 2-binding protein 2

Short name=IRF-2-binding protein 2
Short name=IRF-2BP2
Gene names
Name:IRF2BP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional corepressor in a IRF2-dependent manner; this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscle. Ref.1 Ref.10 Ref.13

Subunit structure

Interacts with IRF2. Part of a corepressor complex containing IRF2 and IRF2BP1. Interacts with VGLL4. Ref.1 Ref.10

Subcellular location

Cytoplasm. Nucleus Ref.1 Ref.10 Ref.14.

Domain

The C-terminal RING-type zinc finger domain is sufficient for interaction with IRF2.

Post-translational modification

Phosphorylation at Ser-360 is required for nuclear targeting.

Sequence similarities

Belongs to the IRF2BP family.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z5L9-1)

Also known as: IRF-2BP2A;

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.
Isoform 2 (identifier: Q7Z5L9-2)

Also known as: IRF-2BP2B;

The sequence of this isoform differs from the canonical sequence as follows:
     333-348: Missing.
Isoform 3 (identifier: Q7Z5L9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-424: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 587586Interferon regulatory factor 2-binding protein 2
PRO_0000328734

Regions

Zinc finger506 – 55348RING-type; degenerate
Region506 – 55045Cys-rich
Motif354 – 3618Nuclear localization signal Ref.14
Compositional bias104 – 20097Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.16
Modified residue1751Phosphoserine Ref.4 Ref.11
Modified residue2401Phosphoserine By similarity
Modified residue3601Phosphoserine Ref.4 Ref.9 Ref.11 Ref.14
Modified residue4551Phosphoserine Ref.7
Modified residue4571Phosphoserine Ref.7 Ref.11 Ref.15
Modified residue4601Phosphoserine Ref.7 Ref.11 Ref.15

Natural variations

Alternative sequence1 – 424424Missing in isoform 3.
VSP_032769
Alternative sequence333 – 34816Missing in isoform 2.
VSP_032770
Natural variant2541A → V.
Corresponds to variant rs11502 [ dbSNP | Ensembl ].
VAR_042503

Experimental info

Sequence conflict1771N → K in AAP78944. Ref.1
Sequence conflict1771N → K in AAP78945. Ref.1
Sequence conflict1831A → T in AAP78944. Ref.1
Sequence conflict1831A → T in AAP78945. Ref.1
Sequence conflict2461A → T in AAP78944. Ref.1
Sequence conflict2461A → T in AAP78945. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IRF-2BP2A) [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 2B36B7EE2C3B96A6

FASTA58761,025
        10         20         30         40         50         60 
MAAAVAVAAA SRRQSCYLCD LPRMPWAMIW DFTEPVCRGC VNYEGADRVE FVIETARQLK 

        70         80         90        100        110        120 
RAHGCFPEGR SPPGAAASAA AKPPPLSAKD ILLQQQQQLG HGGPEAAPRA PQALERYPLA 

       130        140        150        160        170        180 
AAAERPPRLG SDFGSSRPAA SLAQPPTPQP PPVNGILVPN GFSKLEEPPE LNRQSPNPRR 

       190        200        210        220        230        240 
GHAVPPTLVP LMNGSATPLP TALGLGGRAA ASLAAVSGTA AASLGSAQPT DLGAHKRPAS 

       250        260        270        280        290        300 
VSSSAAVEHE QREAAAKEKQ PPPPAHRGPA DSLSTAAGAA ELSAEGAGKS RGSGEQDWVN 

       310        320        330        340        350        360 
RPKTVRDTLL ALHQHGHSGP FESKFKKEPA LTAGRLLGFE ANGANGSKAV ARTARKRKPS 

       370        380        390        400        410        420 
PEPEGEVGPP KINGEAQPWL STSTEGLKIP MTPTSSFVSP PPPTASPHSN RTTPPEAAQN 

       430        440        450        460        470        480 
GQSPMAALIL VADNAGGSHA SKDANQVHST TRRNSNSPPS PSSMNQRRLG PREVGGQGAG 

       490        500        510        520        530        540 
NTGGLEPVHP ASLPDSSLAT SAPLCCTLCH ERLEDTHFVQ CPSVPSHKFC FPCSRQSIKQ 

       550        560        570        580 
QGASGEVYCP SGEKCPLVGS NVPWAFMQGE IATILAGDVK VKKERDS 

« Hide

Isoform 2 (IRF-2BP2B) [UniParc].

Checksum: CE45834F631B6E86
Show »

FASTA57159,481
Isoform 3 [UniParc].

Checksum: 9929F96A8CD66921
Show »

FASTA16317,139

References

« Hide 'large scale' references
[1]"Identification of novel co-repressor molecules for interferon regulatory factor-2."
Childs K.S., Goodbourn S.
Nucleic Acids Res. 31:3016-3026(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH IRF2, SUBCELLULAR LOCATION.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-587 (ISOFORMS 1/2).
Tissue: Lung.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-457 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"IRF2BP2 is a skeletal and cardiac muscle-enriched ischemia-inducible activator of VEGFA expression."
Teng A.C., Kuraitis D., Deeke S.A., Ahmadi A., Dugan S.G., Cheng B.L., Crowson M.G., Burgon P.G., Suuronen E.J., Chen H.H., Stewart A.F.
FASEB J. 24:4825-4834(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VGLL4, SUBCELLULAR LOCATION.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-360; SER-457 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Interferon regulatory factor 2 binding protein 2 is a new NFAT1 partner and represses its transcriptional activity."
Carneiro F.R., Ramalho-Oliveira R., Mognol G.P., Viola J.P.
Mol. Cell. Biol. 31:2889-2901(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Identification of a phosphorylation-dependent nuclear localization motif in interferon regulatory factor 2 binding protein 2."
Teng A.C., Al-Montashiri N.A., Cheng B.L., Lou P., Ozmizrak P., Chen H.H., Stewart A.F.
PLoS ONE 6:E24100-E24100(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, PHOSPHORYLATION AT SER-360.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY278023 mRNA. Translation: AAP78944.1.
AY278024 mRNA. Translation: AAP78945.1.
AL160408 Genomic DNA. Translation: CAI22767.1.
AL160408 Genomic DNA. Translation: CAI22768.1.
BC020516 mRNA. Translation: AAH20516.1.
BC065759 mRNA. Translation: AAH65759.1.
CCDSCCDS1602.1. [Q7Z5L9-1]
CCDS41475.1. [Q7Z5L9-2]
RefSeqNP_001070865.1. NM_001077397.1. [Q7Z5L9-2]
NP_892017.2. NM_182972.2. [Q7Z5L9-1]
UniGeneHs.350268.

3D structure databases

ProteinModelPortalQ7Z5L9.
SMRQ7Z5L9. Positions 498-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid131797. 12 interactions.
IntActQ7Z5L9. 2 interactions.
STRING9606.ENSP00000355568.

PTM databases

PhosphoSiteQ7Z5L9.

Polymorphism databases

DMDM229462882.

Proteomic databases

MaxQBQ7Z5L9.
PaxDbQ7Z5L9.
PRIDEQ7Z5L9.

Protocols and materials databases

DNASU359948.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366609; ENSP00000355568; ENSG00000168264. [Q7Z5L9-1]
ENST00000366610; ENSP00000355569; ENSG00000168264. [Q7Z5L9-2]
GeneID359948.
KEGGhsa:359948.
UCSCuc001hwf.3. human. [Q7Z5L9-2]
uc001hwg.3. human. [Q7Z5L9-1]

Organism-specific databases

CTD359948.
GeneCardsGC01M234740.
H-InvDBHIX0023152.
HGNCHGNC:21729. IRF2BP2.
HPAHPA027815.
MIM615332. gene.
neXtProtNX_Q7Z5L9.
PharmGKBPA134947294.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325224.
HOVERGENHBG108364.
InParanoidQ7Z5L9.
OMASIPLCCT.
OrthoDBEOG7673CH.
PhylomeDBQ7Z5L9.
TreeFamTF317075.

Gene expression databases

ArrayExpressQ7Z5L9.
BgeeQ7Z5L9.
CleanExHS_IRF2BP2.
GenevestigatorQ7Z5L9.

Family and domain databases

InterProIPR022750. Interferon_reg_fac2-bd1_2_Znf.
[Graphical view]
PfamPF11261. IRF-2BP1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIRF2BP2. human.
GenomeRNAi359948.
NextBio99975.
PROQ7Z5L9.
SOURCESearch...

Entry information

Entry nameI2BP2_HUMAN
AccessionPrimary (citable) accession number: Q7Z5L9
Secondary accession number(s): B1AM35 expand/collapse secondary AC list , B1AM36, Q6P083, Q7Z5L8, Q8N351, Q8WUH8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM