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Protein

Iron-responsive element-binding protein 2

Gene

IREB2

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

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

[4Fe-4S] clusterBy similarityNote: 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

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • iron-responsive element binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: UniProtKB
  • translation repressor activity Source: InterPro

GO - Biological processi

  • cellular iron ion homeostasis Source: InterPro
  • iron ion transport Source: UniProtKB
  • metabolic process Source: InterPro
Complete GO annotation...

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 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:6115. IREB2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29914.

Polymorphism and mutation databases

BioMutaiIREB2.
DMDMi308153591.

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

BgeeiP48200.
CleanExiHS_IREB2.
ExpressionAtlasiP48200. baseline and differential.
GenevisibleiP48200. HS.

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. 17 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.
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.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR006249. Aconitase/IRP2.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P48200-1) [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
MDAPKAGYAF EYLIETLNDS SHKKFFDVSK LGTKYDVLPY SIRVLLEAAV
60 70 80 90 100
RNCDGFLMKK EDVMNILDWK TKQSNVEVPF FPARVLLQDF TGIPAMVDFA
110 120 130 140 150
AMREAVKTLG GDPEKVHPAC PTDLTVDHSL QIDFSKCAIQ NAPNPGGGDL
160 170 180 190 200
QKAGKLSPVK VQPKKLPCRG QTTCRGSCDS GELGRNSGTF SSQIENTPIL
210 220 230 240 250
CPFHLQPVPE PETVLKNQEV EFGRNRERLQ FFKWSSRVFK NVAVIPPGTG
260 270 280 290 300
MAHQINLEYL SRVVFEEKDL LFPDSVVGTD SHITMVNGLG ILGWGVGGIE
310 320 330 340 350
TEAVMLGLPV SLTLPEVVGC ELTGSSNPFV TSIDVVLGIT KHLRQVGVAG
360 370 380 390 400
KFVEFFGSGV SQLSIVDRTT IANMCPEYGA ILSFFPVDNV TLKHLEHTGF
410 420 430 440 450
SKAKLESMET YLKAVKLFRN DQNSSGEPEY SQVIQINLNS IVPSVSGPKR
460 470 480 490 500
PQDRVAVTDM KSDFQACLNE KVGFKGFQIA AEKQKDIVSI HYEGSEYKLS
510 520 530 540 550
HGSVVIAAVI SCTNNCNPSV MLAAGLLAKK AVEAGLRVKP YIRTSLSPGS
560 570 580 590 600
GMVTHYLSSS GVLPYLSKLG FEIVGYGCSI CVGNTAPLSD AVLNAVKQGD
610 620 630 640 650
LVTCGILSGN KNFEGRLCDC VRANYLASPP LVVAYAIAGT VNIDFQTEPL
660 670 680 690 700
GTDPTGKNIY LHDIWPSREE VHRVEEEHVI LSMFKALKDK IEMGNKRWNS
710 720 730 740 750
LEAPDSVLFP WDLKSTYIRC PSFFDKLTKE PIALQAIENA HVLLYLGDSV
760 770 780 790 800
TTDHISPAGS IARNSAAAKY LTNRGLTPRE FNSYGARRGN DAVMTRGTFA
810 820 830 840 850
NIKLFNKFIG KPAPKTIHFP SGQTLDVFEA AELYQKEGIP LIILAGKKYG
860 870 880 890 900
SGNSRDWAAK GPYLLGVKAV LAESYEKIHK DHLIGIGIAP LQFLPGENAD
910 920 930 940 950
SLGLSGRETF SLTFPEELSP GITLNIQTST GKVFSVIASF EDDVEITLYK
960
HGGLLNFVAR KFS
Length:963
Mass (Da):105,045
Last modified:October 5, 2010 - v3
Checksum:iF3585B6BEA8DC9CA
GO
Isoform 2 (identifier: P48200-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     342-342: H → V
     343-962: Missing.

Show »
Length:343
Mass (Da):37,487
Checksum:i922D1072993318E5
GO

Sequence cautioni

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

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 BAF85681 (PubMed:14702039).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.9 Publications
Corresponds to variant rs2958720 [ dbSNP | Ensembl ].
VAR_058409
Natural varianti580 – 5801I → T.7 Publications
Corresponds to variant rs2230940 [ dbSNP | Ensembl ].
VAR_058410

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei342 – 3421H → V in isoform 2. 2 PublicationsVSP_056823
Alternative sequencei343 – 962620Missing in isoform 2. 2 PublicationsVSP_056824Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58511 mRNA. Translation: AAA69901.1.
AB586699 mRNA. Translation: BAJ19024.1.
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.
BC017880 mRNA. Translation: AAH17880.1.
BC117481 mRNA. Translation: AAI17482.1.
BC117483 mRNA. Translation: AAI17484.1.
U20180 mRNA. Translation: AAA79926.1. Frameshift.
AL133439 mRNA. Translation: CAB62825.1.
CCDSiCCDS10302.1. [P48200-1]
PIRiB57238.
RefSeqiNP_004127.1. NM_004136.2.
UniGeneiHs.436031.

Genome annotation databases

EnsembliENST00000560440; ENSP00000452938; ENSG00000136381.
GeneIDi3658.
KEGGihsa:3658.
UCSCiuc002bdq.3. human.
uc010unb.1. human. [P48200-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58511 mRNA. Translation: AAA69901.1.
AB586699 mRNA. Translation: BAJ19024.1.
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.
BC017880 mRNA. Translation: AAH17880.1.
BC117481 mRNA. Translation: AAI17482.1.
BC117483 mRNA. Translation: AAI17484.1.
U20180 mRNA. Translation: AAA79926.1. Frameshift.
AL133439 mRNA. Translation: CAB62825.1.
CCDSiCCDS10302.1. [P48200-1]
PIRiB57238.
RefSeqiNP_004127.1. NM_004136.2.
UniGeneiHs.436031.

3D structure databases

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

Protein-protein interaction databases

BioGridi109866. 17 interactions.
IntActiP48200. 2 interactions.
STRINGi9606.ENSP00000258886.

PTM databases

PhosphoSiteiP48200.

Polymorphism and mutation databases

BioMutaiIREB2.
DMDMi308153591.

Proteomic databases

MaxQBiP48200.
PaxDbiP48200.
PRIDEiP48200.

Protocols and materials databases

DNASUi3658.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000560440; ENSP00000452938; ENSG00000136381.
GeneIDi3658.
KEGGihsa:3658.
UCSCiuc002bdq.3. human.
uc010unb.1. human. [P48200-1]

Organism-specific databases

CTDi3658.
GeneCardsiGC15P078730.
HGNCiHGNC:6115. IREB2.
HPAiCAB032885.
MIMi147582. gene.
neXtProtiNX_P48200.
PharmGKBiPA29914.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiIREB2. human.
GenomeRNAii3658.
NextBioi14307.
PROiP48200.
SOURCEiSearch...

Gene expression databases

BgeeiP48200.
CleanExiHS_IREB2.
ExpressionAtlasiP48200. baseline and differential.
GenevisibleiP48200. HS.

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.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR006249. Aconitase/IRP2.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), FUNCTION, RNA-BINDING, VARIANTS LEU-159 AND THR-580.
  2. "IgA nephropathy-related gene."
    Ishiwata T., Sakurada M., Nishimura A., Nakagawa S., Nishi T., Kuga T., Sawada S., Takei M.
    Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-159.
  3. "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] (ISOFORM 1), VARIANTS LEU-159 AND THR-580.
    Tissue: Trachea.
  4. "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] (ISOFORM 1), VARIANTS LEU-159 AND THR-580.
    Tissue: Brain.
  5. NIEHS SNPs program
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-159 AND THR-580.
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LEU-159 AND THR-580.
  8. "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] (ISOFORMS 1 AND 2), VARIANTS LEU-159 AND THR-580.
    Tissue: Brain.
  9. "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.
  10. "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 (ISOFORM 1).
    Tissue: Brain.
  11. The European IMAGE consortium
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 847-963 (ISOFORM 1).
  12. "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.
  13. Cited for: UBIQUITINATION, INTERACTION WITH FBXL5.
  14. "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.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. 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
, E1CJT9, H0YKU0, Q13095, Q1HE21, Q59FQ7, Q8WVK6, Q9UF17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 5, 2010
Last modified: July 22, 2015
This is version 138 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

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.