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Q7Z5L9

- I2BP2_HUMAN

UniProt

Q7Z5L9 - I2BP2_HUMAN

Protein

Interferon regulatory factor 2-binding protein 2

Gene

IRF2BP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    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

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:21729. IRF2BP2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134947294.

    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 residuei175 – 1751Phosphoserine2 Publications
    Modified residuei240 – 2401PhosphoserineBy similarity
    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.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z5L9.
    PaxDbiQ7Z5L9.
    PRIDEiQ7Z5L9.

    PTM databases

    PhosphoSiteiQ7Z5L9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ7Z5L9.
    BgeeiQ7Z5L9.
    CleanExiHS_IRF2BP2.
    GenevestigatoriQ7Z5L9.

    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. 13 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.
    HOVERGENiHBG108364.
    InParanoidiQ7Z5L9.
    OMAiSIPLCCT.
    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. Align

    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

    MAAAVAVAAA SRRQSCYLCD LPRMPWAMIW DFTEPVCRGC VNYEGADRVE    50
    FVIETARQLK RAHGCFPEGR SPPGAAASAA AKPPPLSAKD ILLQQQQQLG 100
    HGGPEAAPRA PQALERYPLA AAAERPPRLG SDFGSSRPAA SLAQPPTPQP 150
    PPVNGILVPN GFSKLEEPPE LNRQSPNPRR GHAVPPTLVP LMNGSATPLP 200
    TALGLGGRAA ASLAAVSGTA AASLGSAQPT DLGAHKRPAS VSSSAAVEHE 250
    QREAAAKEKQ PPPPAHRGPA DSLSTAAGAA ELSAEGAGKS RGSGEQDWVN 300
    RPKTVRDTLL ALHQHGHSGP FESKFKKEPA LTAGRLLGFE ANGANGSKAV 350
    ARTARKRKPS PEPEGEVGPP KINGEAQPWL STSTEGLKIP MTPTSSFVSP 400
    PPPTASPHSN RTTPPEAAQN GQSPMAALIL VADNAGGSHA SKDANQVHST 450
    TRRNSNSPPS PSSMNQRRLG PREVGGQGAG NTGGLEPVHP ASLPDSSLAT 500
    SAPLCCTLCH ERLEDTHFVQ CPSVPSHKFC FPCSRQSIKQ QGASGEVYCP 550
    SGEKCPLVGS NVPWAFMQGE IATILAGDVK VKKERDS 587
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi229462882.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1602.1. [Q7Z5L9-1 ]
    CCDS41475.1. [Q7Z5L9-2 ]
    RefSeqi NP_001070865.1. NM_001077397.1. [Q7Z5L9-2 ]
    NP_892017.2. NM_182972.2. [Q7Z5L9-1 ]
    UniGenei Hs.350268.

    3D structure databases

    ProteinModelPortali Q7Z5L9.
    SMRi Q7Z5L9. Positions 498-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 131797. 13 interactions.
    IntActi Q7Z5L9. 2 interactions.
    STRINGi 9606.ENSP00000355568.

    PTM databases

    PhosphoSitei Q7Z5L9.

    Polymorphism databases

    DMDMi 229462882.

    Proteomic databases

    MaxQBi Q7Z5L9.
    PaxDbi Q7Z5L9.
    PRIDEi Q7Z5L9.

    Protocols and materials databases

    DNASUi 359948.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366609 ; ENSP00000355568 ; ENSG00000168264 . [Q7Z5L9-1 ]
    ENST00000366610 ; ENSP00000355569 ; ENSG00000168264 . [Q7Z5L9-2 ]
    GeneIDi 359948.
    KEGGi hsa:359948.
    UCSCi uc001hwf.3. human. [Q7Z5L9-2 ]
    uc001hwg.3. human. [Q7Z5L9-1 ]

    Organism-specific databases

    CTDi 359948.
    GeneCardsi GC01M234740.
    H-InvDB HIX0023152.
    HGNCi HGNC:21729. IRF2BP2.
    HPAi HPA027815.
    MIMi 615332. gene.
    neXtProti NX_Q7Z5L9.
    PharmGKBi PA134947294.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325224.
    HOVERGENi HBG108364.
    InParanoidi Q7Z5L9.
    OMAi SIPLCCT.
    OrthoDBi EOG7673CH.
    PhylomeDBi Q7Z5L9.
    TreeFami TF317075.

    Miscellaneous databases

    ChiTaRSi IRF2BP2. human.
    GenomeRNAii 359948.
    NextBioi 99975.
    PROi Q7Z5L9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z5L9.
    Bgeei Q7Z5L9.
    CleanExi HS_IRF2BP2.
    Genevestigatori Q7Z5L9.

    Family and domain databases

    InterProi IPR022750. Interferon_reg_fac2-bd1_2_Znf.
    [Graphical view ]
    Pfami PF11261. IRF-2BP1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].

    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: October 1, 2014
    This is version 89 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