Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P48200

- IREB2_HUMAN

UniProt

P48200 - IREB2_HUMAN

Protein

Iron-responsive element-binding protein 2

Gene

IREB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.1 Publication

    Cofactori

    Binds 1 4Fe-4S cluster per subunit. 4Fe-4S-binding affects RNA-binding activity, thereby inhibiting activity of the protein.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi512 – 5121Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi578 – 5781Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi581 – 5811Iron-sulfur (4Fe-4S)By similarity

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. iron-responsive element binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. cellular iron ion homeostasis Source: Ensembl
    3. cellular response to hypoxia Source: Ensembl
    4. erythrocyte homeostasis Source: Ensembl
    5. intestinal absorption Source: Ensembl
    6. iron ion transport Source: UniProtKB
    7. osteoclast differentiation Source: Ensembl
    8. post-embryonic development Source: Ensembl
    9. protoporphyrinogen IX biosynthetic process Source: Ensembl
    10. regulation of translation Source: Ensembl
    11. response to iron(II) ion Source: Ensembl
    12. response to retinoic acid Source: Ensembl

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Iron-responsive element-binding protein 2
    Short name:
    IRE-BP 2
    Alternative name(s):
    Iron regulatory protein 2
    Short name:
    IRP2
    Gene namesi
    Name:IREB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:6115. IREB2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Ensembl
    3. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29914.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 963963Iron-responsive element-binding protein 2PRO_0000076684Add
    BLAST

    Post-translational modificationi

    Ubiquitinated and degraded by the proteasome in presence of high level of iron and oxygen. Ubiquitinated by a SCF complex containing FBXL5. Upon iron and oxygen depletion FBXL5 is degraded, preventing ubiquitination and allowing its RNA-binding activity.3 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP48200.
    PaxDbiP48200.
    PRIDEiP48200.

    PTM databases

    PhosphoSiteiP48200.

    Expressioni

    Gene expression databases

    ArrayExpressiP48200.
    BgeeiP48200.
    CleanExiHS_IREB2.
    GenevestigatoriP48200.

    Organism-specific databases

    HPAiCAB032885.

    Interactioni

    Subunit structurei

    Interacts with RBCK1 isoform 1 and isoform 2 only in iron-rich conditions. Interacts (when associated with the 4Fe-4S) with FBXL5.3 Publications

    Protein-protein interaction databases

    BioGridi109866. 12 interactions.
    IntActiP48200. 2 interactions.
    STRINGi9606.ENSP00000258886.

    Structurei

    3D structure databases

    ProteinModelPortaliP48200.
    SMRiP48200. Positions 10-129, 220-963.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aconitase/IPM isomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG1048.
    HOGENOMiHOG000025704.
    HOVERGENiHBG052147.
    InParanoidiP48200.
    OMAiPCRGQTT.
    OrthoDBiEOG7CG6Z7.
    PhylomeDBiP48200.
    TreeFamiTF313476.

    Family and domain databases

    Gene3Di3.20.19.10. 1 hit.
    3.30.499.10. 4 hits.
    3.40.1060.10. 1 hit.
    InterProiIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
    IPR015937. Acoase/IPM_deHydtase.
    IPR001030. Acoase/IPM_deHydtase_lsu_aba.
    IPR015928. Aconitase/3IPM_dehydase_swvl.
    IPR006249. Aconitase/Fe_reg_2.
    IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
    IPR018136. Aconitase_4Fe-4S_BS.
    IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
    IPR029755. IRE-BP2.
    [Graphical view]
    PANTHERiPTHR11670. PTHR11670. 1 hit.
    PTHR11670:SF31. PTHR11670:SF31. 1 hit.
    PfamiPF00330. Aconitase. 2 hits.
    PF00694. Aconitase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00415. ACONITASE.
    SUPFAMiSSF52016. SSF52016. 1 hit.
    SSF53732. SSF53732. 2 hits.
    TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
    PROSITEiPS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48200-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDAPKAGYAF EYLIETLNDS SHKKFFDVSK LGTKYDVLPY SIRVLLEAAV    50
    RNCDGFLMKK EDVMNILDWK TKQSNVEVPF FPARVLLQDF TGIPAMVDFA 100
    AMREAVKTLG GDPEKVHPAC PTDLTVDHSL QIDFSKCAIQ NAPNPGGGDL 150
    QKAGKLSPVK VQPKKLPCRG QTTCRGSCDS GELGRNSGTF SSQIENTPIL 200
    CPFHLQPVPE PETVLKNQEV EFGRNRERLQ FFKWSSRVFK NVAVIPPGTG 250
    MAHQINLEYL SRVVFEEKDL LFPDSVVGTD SHITMVNGLG ILGWGVGGIE 300
    TEAVMLGLPV SLTLPEVVGC ELTGSSNPFV TSIDVVLGIT KHLRQVGVAG 350
    KFVEFFGSGV SQLSIVDRTT IANMCPEYGA ILSFFPVDNV TLKHLEHTGF 400
    SKAKLESMET YLKAVKLFRN DQNSSGEPEY SQVIQINLNS IVPSVSGPKR 450
    PQDRVAVTDM KSDFQACLNE KVGFKGFQIA AEKQKDIVSI HYEGSEYKLS 500
    HGSVVIAAVI SCTNNCNPSV MLAAGLLAKK AVEAGLRVKP YIRTSLSPGS 550
    GMVTHYLSSS GVLPYLSKLG FEIVGYGCSI CVGNTAPLSD AVLNAVKQGD 600
    LVTCGILSGN KNFEGRLCDC VRANYLASPP LVVAYAIAGT VNIDFQTEPL 650
    GTDPTGKNIY LHDIWPSREE VHRVEEEHVI LSMFKALKDK IEMGNKRWNS 700
    LEAPDSVLFP WDLKSTYIRC PSFFDKLTKE PIALQAIENA HVLLYLGDSV 750
    TTDHISPAGS IARNSAAAKY LTNRGLTPRE FNSYGARRGN DAVMTRGTFA 800
    NIKLFNKFIG KPAPKTIHFP SGQTLDVFEA AELYQKEGIP LIILAGKKYG 850
    SGNSRDWAAK GPYLLGVKAV LAESYEKIHK DHLIGIGIAP LQFLPGENAD 900
    SLGLSGRETF SLTFPEELSP GITLNIQTST GKVFSVIASF EDDVEITLYK 950
    HGGLLNFVAR KFS 963
    Length:963
    Mass (Da):105,045
    Last modified:October 5, 2010 - v3
    Checksum:iF3585B6BEA8DC9CA
    GO

    Sequence cautioni

    The sequence AAA79926.1 differs from that shown. Reason: Frameshift at positions 605 and 611.
    The sequence BAD92640.1 differs from that shown. Reason: Frameshift at position 727.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti195 – 1951E → G in BAF85681. (PubMed:14702039)Curated
    Sequence conflicti239 – 2391F → L in AAA69901. (PubMed:7983023)Curated
    Sequence conflicti239 – 2391F → L in AAA79926. (PubMed:7622457)Curated
    Sequence conflicti452 – 4521Q → R in AAA79926. (PubMed:7622457)Curated
    Sequence conflicti458 – 4581T → P in BAF85681. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti159 – 1591V → L.8 Publications
    Corresponds to variant rs2958720 [ dbSNP | Ensembl ].
    VAR_058409
    Natural varianti580 – 5801I → T.7 Publications
    Corresponds to variant rs2230940 [ dbSNP | Ensembl ].
    VAR_058410

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58511 mRNA. Translation: AAA69901.1.
    AK292992 mRNA. Translation: BAF85681.1.
    AB209403 mRNA. Translation: BAD92640.1. Frameshift.
    DQ496102 Genomic DNA. Translation: ABF47091.1.
    AC011270 Genomic DNA. No translation available.
    AC027228 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99169.1.
    BC117481 mRNA. Translation: AAI17482.1.
    BC117483 mRNA. Translation: AAI17484.1.
    U20180 mRNA. Translation: AAA79926.1. Frameshift.
    AL133439 mRNA. Translation: CAB62825.1.
    CCDSiCCDS10302.1.
    PIRiB57238.
    RefSeqiNP_004127.1. NM_004136.2.
    UniGeneiHs.436031.

    Genome annotation databases

    EnsembliENST00000258886; ENSP00000258886; ENSG00000136381.
    GeneIDi3658.
    KEGGihsa:3658.
    UCSCiuc010unb.1. human.

    Polymorphism databases

    DMDMi308153591.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M58511 mRNA. Translation: AAA69901.1 .
    AK292992 mRNA. Translation: BAF85681.1 .
    AB209403 mRNA. Translation: BAD92640.1 . Frameshift.
    DQ496102 Genomic DNA. Translation: ABF47091.1 .
    AC011270 Genomic DNA. No translation available.
    AC027228 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99169.1 .
    BC117481 mRNA. Translation: AAI17482.1 .
    BC117483 mRNA. Translation: AAI17484.1 .
    U20180 mRNA. Translation: AAA79926.1 . Frameshift.
    AL133439 mRNA. Translation: CAB62825.1 .
    CCDSi CCDS10302.1.
    PIRi B57238.
    RefSeqi NP_004127.1. NM_004136.2.
    UniGenei Hs.436031.

    3D structure databases

    ProteinModelPortali P48200.
    SMRi P48200. Positions 10-129, 220-963.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109866. 12 interactions.
    IntActi P48200. 2 interactions.
    STRINGi 9606.ENSP00000258886.

    PTM databases

    PhosphoSitei P48200.

    Polymorphism databases

    DMDMi 308153591.

    Proteomic databases

    MaxQBi P48200.
    PaxDbi P48200.
    PRIDEi P48200.

    Protocols and materials databases

    DNASUi 3658.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258886 ; ENSP00000258886 ; ENSG00000136381 .
    GeneIDi 3658.
    KEGGi hsa:3658.
    UCSCi uc010unb.1. human.

    Organism-specific databases

    CTDi 3658.
    GeneCardsi GC15P078730.
    HGNCi HGNC:6115. IREB2.
    HPAi CAB032885.
    MIMi 147582. gene.
    neXtProti NX_P48200.
    PharmGKBi PA29914.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1048.
    HOGENOMi HOG000025704.
    HOVERGENi HBG052147.
    InParanoidi P48200.
    OMAi PCRGQTT.
    OrthoDBi EOG7CG6Z7.
    PhylomeDBi P48200.
    TreeFami TF313476.

    Miscellaneous databases

    ChiTaRSi IREB2. human.
    GenomeRNAii 3658.
    NextBioi 14307.
    PROi P48200.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48200.
    Bgeei P48200.
    CleanExi HS_IREB2.
    Genevestigatori P48200.

    Family and domain databases

    Gene3Di 3.20.19.10. 1 hit.
    3.30.499.10. 4 hits.
    3.40.1060.10. 1 hit.
    InterProi IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
    IPR015937. Acoase/IPM_deHydtase.
    IPR001030. Acoase/IPM_deHydtase_lsu_aba.
    IPR015928. Aconitase/3IPM_dehydase_swvl.
    IPR006249. Aconitase/Fe_reg_2.
    IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
    IPR018136. Aconitase_4Fe-4S_BS.
    IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
    IPR029755. IRE-BP2.
    [Graphical view ]
    PANTHERi PTHR11670. PTHR11670. 1 hit.
    PTHR11670:SF31. PTHR11670:SF31. 1 hit.
    Pfami PF00330. Aconitase. 2 hits.
    PF00694. Aconitase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00415. ACONITASE.
    SUPFAMi SSF52016. SSF52016. 1 hit.
    SSF53732. SSF53732. 2 hits.
    TIGRFAMsi TIGR01341. aconitase_1. 1 hit.
    PROSITEi PS00450. ACONITASE_1. 1 hit.
    PS01244. ACONITASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation."
      Samaniego F., Chin J., Iwai K., Rouault T.A., Klausner R.D.
      J. Biol. Chem. 269:30904-30910(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, RNA-BINDING, VARIANTS LEU-159 AND THR-580.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-159 AND THR-580.
      Tissue: Trachea.
    3. "Homo sapiens protein coding cDNA."
      Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-159 AND THR-580.
      Tissue: Brain.
    4. NIEHS SNPs program
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-159 AND THR-580.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LEU-159 AND THR-580.
    7. "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], VARIANTS LEU-159 AND THR-580.
      Tissue: Brain.
    8. "Cloning of the cDNA encoding an RNA regulatory protein -- the human iron-responsive element-binding protein."
      Rouault T.A., Tang C.K., Kaptain S., Burgess W.H., Haile D.J., Samaniego F., McBride O.W., Harford J.B., Klausner R.D.
      Proc. Natl. Acad. Sci. U.S.A. 87:7958-7962(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-159 AND THR-580.
    9. "Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels."
      Guo B., Brown F.M., Phillips J.D., Yu Y., Leibold E.A.
      J. Biol. Chem. 270:16529-16535(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-963.
      Tissue: Brain.
    10. The European IMAGE consortium
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 847-963.
    11. "Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2."
      Yamanaka K., Ishikawa H., Megumi Y., Tokunaga F., Kanie M., Rouault T.A., Morishima I., Minato N., Ishimori K., Iwai K.
      Nat. Cell Biol. 5:336-340(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH RBCK1.
    12. Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
    13. "An E3 ligase possessing an iron responsive hemerythrin domain is a regulator of iron homeostasis."
      Salahudeen A.A., Thompson J.W., Ruiz J.C., Ma H.-W., Kinch L.N., Li Q., Grishin N.V., Bruick R.K.
      Science 326:722-726(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiIREB2_HUMAN
    AccessioniPrimary (citable) accession number: P48200
    Secondary accession number(s): A8KAC7
    , Q13095, Q1HE21, Q59FQ7, Q9UF17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 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 15
      Human chromosome 15: 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