CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008002
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
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MDAPKAGYAFEYubiquitination[1]
23TLNDSSHKKFFDVSKubiquitination[2]
24LNDSSHKKFFDVSKLubiquitination[1]
30KKFFDVSKLGTKYDVubiquitination[1]
34DVSKLGTKYDVLPYSubiquitination[1]
59NCDGFLMKKEDVMNIubiquitination[1]
60CDGFLMKKEDVMNILubiquitination[1]
70VMNILDWKTKQSNVEubiquitination[1]
72NILDWKTKQSNVEVPubiquitination[1, 3]
107AAMREAVKTLGGDPEubiquitination[1, 2, 4]
115TLGGDPEKVHPACPTubiquitination[1]
136SLQIDFSKCAIQNAPubiquitination[1]
152PGGGDLQKAGKLSPVubiquitination[1, 3]
160AGKLSPVKVQPKKLPubiquitination[3]
233RERLQFFKWSSRVFKubiquitination[1, 5]
240KWSSRVFKNVAVIPPubiquitination[1]
402LEHTGFSKAKLESMEubiquitination[1, 6]
404HTGFSKAKLESMETYubiquitination[1, 2]
413ESMETYLKAVKLFRNubiquitination[1, 2, 6]
416ETYLKAVKLFRNDQNubiquitination[1]
449VPSVSGPKRPQDRVAubiquitination[2, 4]
461RVAVTDMKSDFQACLubiquitination[1, 3, 6, 7, 8]
471FQACLNEKVGFKGFQubiquitination[1, 6, 8]
475LNEKVGFKGFQIAAEubiquitination[1, 2, 4, 6, 8]
483GFQIAAEKQKDIVSIubiquitination[1, 2, 6]
485QIAAEKQKDIVSIHYubiquitination[1]
611CGILSGNKNFEGRLCubiquitination[1, 3, 6, 7]
685HVILSMFKALKDKIEubiquitination[1]
696DKIEMGNKRWNSLEAubiquitination[2]
714VLFPWDLKSTYIRCPubiquitination[2, 4, 6, 7, 8]
726RCPSFFDKLTKEPIAubiquitination[1]
769ARNSAAAKYLTNRGLubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
803RGTFANIKLFNKFIGubiquitination[1, 2, 6, 8]
807ANIKLFNKFIGKPAPubiquitination[1, 5, 8]
811LFNKFIGKPAPKTIHubiquitination[1]
815FIGKPAPKTIHFPSGubiquitination[1]
847PLIILAGKKYGSGNSubiquitination[1, 2, 4, 6]
848LIILAGKKYGSGNSRubiquitination[1]
860NSRDWAAKGPYLLGVubiquitination[1, 2, 3, 4, 5, 7]
868GPYLLGVKAVLAESYubiquitination[1, 2, 4, 7]
877VLAESYEKIHKDHLIubiquitination[1, 2]
880ESYEKIHKDHLIGIGubiquitination[1, 2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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. 
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; Polymorphism; Reference proteome; RNA-binding; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 963 AA 
Protein Sequence
MDAPKAGYAF EYLIETLNDS SHKKFFDVSK LGTKYDVLPY SIRVLLEAAV RNCDGFLMKK 60
EDVMNILDWK TKQSNVEVPF FPARVLLQDF TGIPAMVDFA AMREAVKTLG GDPEKVHPAC 120
PTDLTVDHSL QIDFSKCAIQ NAPNPGGGDL QKAGKLSPVK VQPKKLPCRG QTTCRGSCDS 180
GELGRNSGTF SSQIENTPIL CPFHLQPVPE PETVLKNQEV EFGRNRERLQ FFKWSSRVFK 240
NVAVIPPGTG MAHQINLEYL SRVVFEEKDL LFPDSVVGTD SHITMVNGLG ILGWGVGGIE 300
TEAVMLGLPV SLTLPEVVGC ELTGSSNPFV TSIDVVLGIT KHLRQVGVAG KFVEFFGSGV 360
SQLSIVDRTT IANMCPEYGA ILSFFPVDNV TLKHLEHTGF SKAKLESMET YLKAVKLFRN 420
DQNSSGEPEY SQVIQINLNS IVPSVSGPKR PQDRVAVTDM KSDFQACLNE KVGFKGFQIA 480
AEKQKDIVSI HYEGSEYKLS HGSVVIAAVI SCTNNCNPSV MLAAGLLAKK AVEAGLRVKP 540
YIRTSLSPGS GMVTHYLSSS GVLPYLSKLG FEIVGYGCSI CVGNTAPLSD AVLNAVKQGD 600
LVTCGILSGN KNFEGRLCDC VRANYLASPP LVVAYAIAGT VNIDFQTEPL GTDPTGKNIY 660
LHDIWPSREE VHRVEEEHVI LSMFKALKDK IEMGNKRWNS LEAPDSVLFP WDLKSTYIRC 720
PSFFDKLTKE PIALQAIENA HVLLYLGDSV TTDHISPAGS IARNSAAAKY LTNRGLTPRE 780
FNSYGARRGN DAVMTRGTFA NIKLFNKFIG KPAPKTIHFP SGQTLDVFEA AELYQKEGIP 840
LIILAGKKYG SGNSRDWAAK GPYLLGVKAV LAESYEKIHK DHLIGIGIAP LQFLPGENAD 900
SLGLSGRETF SLTFPEELSP GITLNIQTST GKVFSVIASF EDDVEITLYK HGGLLNFVAR 960
KFS 963 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
 GO:0030350; F:iron-responsive element binding; TAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0007568; P:aging; IEA:Compara.
 GO:0006879; P:cellular iron ion homeostasis; IEA:Compara.
 GO:0071456; P:cellular response to hypoxia; IEA:Compara.
 GO:0034101; P:erythrocyte homeostasis; IEA:Compara.
 GO:0050892; P:intestinal absorption; IEA:Compara.
 GO:0006826; P:iron ion transport; TAS:UniProtKB.
 GO:0030316; P:osteoclast differentiation; IEA:Compara.
 GO:0009791; P:post-embryonic development; IEA:Compara.
 GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:Compara.
 GO:0006417; P:regulation of translation; IEA:Compara.
 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.