CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016140
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Iron-responsive element-binding protein 2 
Protein Synonyms/Alias
 IRE-BP 2; Iron regulatory protein 2; IRP2 
Gene Name
 Ireb2 
Gene Synonyms/Alias
 Irp2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
483GFQVAAEKQSDTVSVubiquitination[1]
714VLFPWDVKSTYIRCPubiquitination[1]
726RCPSFFDKLTKEPAAubiquitination[1]
769ARSSAAAKYLTNRGLubiquitination[1]
803RGTFANIKLFNKFIGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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 (By similarity). 
Sequence Annotation
 METAL 512 512 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 578 578 Iron-sulfur (4Fe-4S) (By similarity).
 METAL 581 581 Iron-sulfur (4Fe-4S) (By similarity).  
Keyword
 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome; RNA-binding; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 963 AA 
Protein Sequence
MDSPSAGYTF EYLIETLNGN SQKKFFNVPK LGGTKYDILP YSIRVLLEAA VRNCDGFLMK 60
KEDVMNILDW KTKQSNVEVP FFPARVVLQD FTGIPAMVDF AAMREAVKTL GGDPKKVHPA 120
CPTDLTVDHS LQIDFSKCAI QNAPNPGGGD LQKAGKLSPL KVQSKKLPCR GQTTCRGSCD 180
SGELSRNSGT FSSQIENTPV LCPFHLQPVP EPETVLKNQE VEFGRNRERL QFFKWSSGAF 240
KNVAVIPPGT GMAHQVNLEY LSRVVFEETD LLFPDSVVGT DSHITMVNGL GILGWGVGGI 300
ETEAVMLGLP VTLTLPEVVG CELTGSSNAF VTSIDIVLGI TKHLRQVGVA GKFVEFFGSG 360
VSQLSIVDRT TIANMCPEYG AILSFFPVDN VTLRHLEHTG FDKTKLESME KYLKAVKLFR 420
NDENSSEPEY SQVIQINLNS IVASVSGPKR PQDRVAVTDM KSDFQACLNE KVGFKGFQVA 480
AEKQSDTVSV RYDGSEYKLS HGSVVIAAVI SCTNNCNPSV MLAAGLLAKK AVEIGLRVKP 540
YIRTSLSPGS GMVTHYLSSS GVLPYLSKLG FDIVGYGCST CVGNTAPLSE AVLNAVKQGD 600
LVTCGVLSGN KHFEGRLCDC VRANYLASPP LVVAYAIAGT VNIDFQTEPL GTDSTGKEIY 660
LHDIWPSREE VHQMEEEHVI LSMFKTLKEK VEMGNKRWNS LEAPDSVLFP WDVKSTYIRC 720
PSFFDKLTKE PAASQPIENA HVLLYLGDSV TTDHISPAGS IARSSAAAKY LTNRGLTPRE 780
FNSYGARRGN DAVMTRGTFA NIKLFNKFIG KPAPKTIHFP SGQTLDVFEA AELYQKEGIP 840
LIILAGKKYG SGNSRDWAAK GPYLLGVKAV LAESYEKIHK DHLIGIGIAP LEFLPGENAD 900
SLGLSGREVF SLSFPEELFP GITLNIKTST GKEFSVIASF ANDVEITLYK HGGLLNFVAR 960
KFL 963 
Gene Ontology
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0030350; F:iron-responsive element binding; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0030371; F:translation repressor activity; TAS:MGI.
 GO:0007568; P:aging; IEA:Compara.
 GO:0006879; P:cellular iron ion homeostasis; IDA:MGI.
 GO:0071456; P:cellular response to hypoxia; IEA:Compara.
 GO:0034101; P:erythrocyte homeostasis; IMP:MGI.
 GO:0050892; P:intestinal absorption; IGI:MGI.
 GO:0030316; P:osteoclast differentiation; IEP:DFLAT.
 GO:0009791; P:post-embryonic development; IGI:MGI.
 GO:0006782; P:protoporphyrinogen IX biosynthetic process; IMP:MGI.
 GO:0010040; P:response to iron(II) ion; IEA:Compara.
 GO:0032526; P:response to retinoic acid; IEA:Compara. 
Interpro
 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_prot_2.
 IPR015934; Aconitase/Fe_reg_prot_2/AcnD.
 IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
 IPR018136; Aconitase_4Fe-4S_BS.
 IPR000573; AconitaseA/IPMdHydase_ssu_swvl. 
Pfam
 PF00330; Aconitase
 PF00694; Aconitase_C 
SMART
  
PROSITE
 PS00450; ACONITASE_1
 PS01244; ACONITASE_2 
PRINTS
 PR00415; ACONITASE.