CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023865
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase ARIH1 
Protein Synonyms/Alias
 H7-AP2; HHARI; Monocyte protein 6; MOP-6; Protein ariadne-1 homolog; ARI-1; UbcH7-binding protein; UbcM4-interacting protein; Ubiquitin-conjugating enzyme E2-binding protein 1 
Gene Name
 ARIH1 
Gene Synonyms/Alias
 ARI; MOP6; UBCH7BP; HUSSY-27 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
142LSHFNWDKEKLMERYacetylation[1]
142LSHFNWDKEKLMERYubiquitination[2, 3, 4, 5]
144HFNWDKEKLMERYFDubiquitination[3, 4, 5, 6, 7, 8]
156YFDGNLEKLFAECHVubiquitination[5, 6, 8]
253MRLITDSKVKLKYQHubiquitination[2, 5, 7]
255LITDSKVKLKYQHLIubiquitination[5]
257TDSKVKLKYQHLITNubiquitination[5]
274VECNRLLKWCPAPDCubiquitination[5]
286PDCHHVVKVQYPDAKubiquitination[5, 6, 8]
293KVQYPDAKPVRCKCGubiquitination[2, 5, 7]
316ENWHDPVKCKWLKKWubiquitination[2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
326WLKKWIKKCDDDSETubiquitination[2, 5, 11]
346ANTKECPKCHVTIEKubiquitination[11]
368VCRNQNCKAEFCWVCubiquitination[3, 9]
398RYNEDDAKAARDAQEubiquitination[2, 7, 11]
439HKLYAQVKQKMEEMQubiquitination[2]
484VFAFYLKKNNQSIIFubiquitination[2]
522QDSLQDIKQKVQDKYubiquitination[2, 5, 7]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [9] 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]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [11] 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
 E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation. 
Sequence Annotation
 ZN_FING 186 236 RING-type 1; atypical.
 ZN_FING 256 317 IBR-type.
 ZN_FING 344 375 RING-type 2.
 REGION 186 254 Interaction with UBE2L3.
 METAL 344 344 Zinc.
 METAL 347 347 Zinc.
 METAL 362 362 Zinc.
 METAL 367 367 Zinc.  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 557 AA 
Protein Sequence
MDSDEGYNYE FDEDEECSEE DSGAEEEEDE DDDEPDDDTL DLGEVELVEP GLGVGGERDG 60
LLCGETGGGG GSALGPGGGG GGGGGGGGGG PGHEQEEDYR YEVLTAEQIL QHMVECIREV 120
NEVIQNPATI TRILLSHFNW DKEKLMERYF DGNLEKLFAE CHVINPSKKS RTRQMNTRSS 180
AQDMPCQICY LNYPNSYFTG LECGHKFCMQ CWSEYLTTKI MEEGMGQTIS CPAHGCDILV 240
DDNTVMRLIT DSKVKLKYQH LITNSFVECN RLLKWCPAPD CHHVVKVQYP DAKPVRCKCG 300
RQFCFNCGEN WHDPVKCKWL KKWIKKCDDD SETSNWIAAN TKECPKCHVT IEKDGGCNHM 360
VCRNQNCKAE FCWVCLGPWE PHGSAWYNCN RYNEDDAKAA RDAQERSRAA LQRYLFYCNR 420
YMNHMQSLRF EHKLYAQVKQ KMEEMQQHNM SWIEVQFLKK AVDVLCQCRA TLMYTYVFAF 480
YLKKNNQSII FENNQADLEN ATEVLSGYLE RDISQDSLQD IKQKVQDKYR YCESRRRVLL 540
QHVHEGYEKD LWEYIED 557 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000151; C:ubiquitin ligase complex; TAS:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:UniProtKB. 
Interpro
 IPR002867; Znf_C6HC.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01485; IBR 
SMART
 SM00647; IBR
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS