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Protein

Interferon regulatory factor 2-binding protein 2

Gene

IRF2BP2

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

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri506 – 55348RING-type; degenerateAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon regulatory factor 2-binding protein 2
Short name:
IRF-2-binding protein 2
Short name:
IRF-2BP2
Gene namesi
Name:IRF2BP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:21729. IRF2BP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134947294.

Polymorphism and mutation databases

BioMutaiIRF2BP2.
DMDMi229462882.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 587586Interferon regulatory factor 2-binding protein 2PRO_0000328734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei175 – 1751Phosphoserine3 Publications
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei318 – 3181Phosphoserine1 Publication
Modified residuei360 – 3601Phosphoserine4 Publications
Modified residuei455 – 4551Phosphoserine1 Publication
Modified residuei457 – 4571Phosphoserine3 Publications
Modified residuei460 – 4601Phosphoserine3 Publications

Post-translational modificationi

Phosphorylation at Ser-360 is required for nuclear targeting.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ7Z5L9.
PaxDbiQ7Z5L9.
PRIDEiQ7Z5L9.

PTM databases

PhosphoSiteiQ7Z5L9.

Expressioni

Gene expression databases

BgeeiQ7Z5L9.
CleanExiHS_IRF2BP2.
GenevisibleiQ7Z5L9. HS.

Organism-specific databases

HPAiHPA027815.

Interactioni

Subunit structurei

Interacts with IRF2. Part of a corepressor complex containing IRF2 and IRF2BP1. Interacts with VGLL4.2 Publications

Protein-protein interaction databases

BioGridi131797. 15 interactions.
IntActiQ7Z5L9. 2 interactions.
STRINGi9606.ENSP00000355568.

Structurei

3D structure databases

ProteinModelPortaliQ7Z5L9.
SMRiQ7Z5L9. Positions 498-577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni506 – 55045Cys-richAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi354 – 3618Nuclear localization signal1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi104 – 20097Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the IRF2BP family.Curated
Contains 1 RING-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri506 – 55348RING-type; degenerateAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG325224.
GeneTreeiENSGT00390000005089.
HOVERGENiHBG108364.
InParanoidiQ7Z5L9.
OMAiSESHKNR.
OrthoDBiEOG7673CH.
PhylomeDBiQ7Z5L9.
TreeFamiTF317075.

Family and domain databases

InterProiIPR022750. Interferon_reg_fac2-bd1_2_Znf.
[Graphical view]
PfamiPF11261. IRF-2BP1_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q7Z5L9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAAVAVAAA SRRQSCYLCD LPRMPWAMIW DFTEPVCRGC VNYEGADRVE
60 70 80 90 100
FVIETARQLK RAHGCFPEGR SPPGAAASAA AKPPPLSAKD ILLQQQQQLG
110 120 130 140 150
HGGPEAAPRA PQALERYPLA AAAERPPRLG SDFGSSRPAA SLAQPPTPQP
160 170 180 190 200
PPVNGILVPN GFSKLEEPPE LNRQSPNPRR GHAVPPTLVP LMNGSATPLP
210 220 230 240 250
TALGLGGRAA ASLAAVSGTA AASLGSAQPT DLGAHKRPAS VSSSAAVEHE
260 270 280 290 300
QREAAAKEKQ PPPPAHRGPA DSLSTAAGAA ELSAEGAGKS RGSGEQDWVN
310 320 330 340 350
RPKTVRDTLL ALHQHGHSGP FESKFKKEPA LTAGRLLGFE ANGANGSKAV
360 370 380 390 400
ARTARKRKPS PEPEGEVGPP KINGEAQPWL STSTEGLKIP MTPTSSFVSP
410 420 430 440 450
PPPTASPHSN RTTPPEAAQN GQSPMAALIL VADNAGGSHA SKDANQVHST
460 470 480 490 500
TRRNSNSPPS PSSMNQRRLG PREVGGQGAG NTGGLEPVHP ASLPDSSLAT
510 520 530 540 550
SAPLCCTLCH ERLEDTHFVQ CPSVPSHKFC FPCSRQSIKQ QGASGEVYCP
560 570 580
SGEKCPLVGS NVPWAFMQGE IATILAGDVK VKKERDS
Length:587
Mass (Da):61,025
Last modified:May 5, 2009 - v2
Checksum:i2B36B7EE2C3B96A6
GO
Isoform 2 (identifier: Q7Z5L9-2) [UniParc]FASTAAdd to basket

Also known as: IRF-2BP2B

The sequence of this isoform differs from the canonical sequence as follows:
     333-348: Missing.

Show »
Length:571
Mass (Da):59,481
Checksum:iCE45834F631B6E86
GO
Isoform 3 (identifier: Q7Z5L9-3) [UniParc]FASTAAdd to basket

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

Show »
Length:163
Mass (Da):17,139
Checksum:i9929F96A8CD66921
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771N → K in AAP78944 (PubMed:12799427).Curated
Sequence conflicti177 – 1771N → K in AAP78945 (PubMed:12799427).Curated
Sequence conflicti183 – 1831A → T in AAP78944 (PubMed:12799427).Curated
Sequence conflicti183 – 1831A → T in AAP78945 (PubMed:12799427).Curated
Sequence conflicti246 – 2461A → T in AAP78944 (PubMed:12799427).Curated
Sequence conflicti246 – 2461A → T in AAP78945 (PubMed:12799427).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti254 – 2541A → V.
Corresponds to variant rs11502 [ dbSNP | Ensembl ].
VAR_042503

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 424424Missing in isoform 3. 1 PublicationVSP_032769Add
BLAST
Alternative sequencei333 – 34816Missing in isoform 2. 1 PublicationVSP_032770Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1602.1. [Q7Z5L9-1]
CCDS41475.1. [Q7Z5L9-2]
RefSeqiNP_001070865.1. NM_001077397.1. [Q7Z5L9-2]
NP_892017.2. NM_182972.2. [Q7Z5L9-1]
UniGeneiHs.350268.

Genome annotation databases

EnsembliENST00000366609; ENSP00000355568; ENSG00000168264. [Q7Z5L9-1]
ENST00000366610; ENSP00000355569; ENSG00000168264. [Q7Z5L9-2]
GeneIDi359948.
KEGGihsa:359948.
UCSCiuc001hwf.3. human. [Q7Z5L9-2]
uc001hwg.3. human. [Q7Z5L9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1602.1. [Q7Z5L9-1]
CCDS41475.1. [Q7Z5L9-2]
RefSeqiNP_001070865.1. NM_001077397.1. [Q7Z5L9-2]
NP_892017.2. NM_182972.2. [Q7Z5L9-1]
UniGeneiHs.350268.

3D structure databases

ProteinModelPortaliQ7Z5L9.
SMRiQ7Z5L9. Positions 498-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131797. 15 interactions.
IntActiQ7Z5L9. 2 interactions.
STRINGi9606.ENSP00000355568.

PTM databases

PhosphoSiteiQ7Z5L9.

Polymorphism and mutation databases

BioMutaiIRF2BP2.
DMDMi229462882.

Proteomic databases

MaxQBiQ7Z5L9.
PaxDbiQ7Z5L9.
PRIDEiQ7Z5L9.

Protocols and materials databases

DNASUi359948.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366609; ENSP00000355568; ENSG00000168264. [Q7Z5L9-1]
ENST00000366610; ENSP00000355569; ENSG00000168264. [Q7Z5L9-2]
GeneIDi359948.
KEGGihsa:359948.
UCSCiuc001hwf.3. human. [Q7Z5L9-2]
uc001hwg.3. human. [Q7Z5L9-1]

Organism-specific databases

CTDi359948.
GeneCardsiGC01M234740.
H-InvDBHIX0023152.
HGNCiHGNC:21729. IRF2BP2.
HPAiHPA027815.
MIMi615332. gene.
neXtProtiNX_Q7Z5L9.
PharmGKBiPA134947294.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG325224.
GeneTreeiENSGT00390000005089.
HOVERGENiHBG108364.
InParanoidiQ7Z5L9.
OMAiSESHKNR.
OrthoDBiEOG7673CH.
PhylomeDBiQ7Z5L9.
TreeFamiTF317075.

Miscellaneous databases

ChiTaRSiIRF2BP2. human.
GenomeRNAii359948.
NextBioi99975.
PROiQ7Z5L9.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z5L9.
CleanExiHS_IRF2BP2.
GenevisibleiQ7Z5L9. HS.

Family and domain databases

InterProiIPR022750. Interferon_reg_fac2-bd1_2_Znf.
[Graphical view]
PfamiPF11261. IRF-2BP1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-175 AND SER-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiI2BP2_HUMAN
AccessioniPrimary (citable) accession number: Q7Z5L9
Secondary accession number(s): B1AM35
, B1AM36, Q6P083, Q7Z5L8, Q8N351, Q8WUH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 5, 2009
Last modified: June 24, 2015
This is version 96 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 1
    Human chromosome 1: 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. 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.