CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000905
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase MGRN1 
Protein Synonyms/Alias
 Mahogunin RING finger protein 1; RING finger protein 156 
Gene Name
 MGRN1 
Gene Synonyms/Alias
 KIAA0544; RNF156 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82PAPHEPVKTLRSLVNubiquitination[1]
164QSETVHYKRGVSQQFubiquitination[1, 2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to- lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination. 
Sequence Annotation
 ZN_FING 278 317 RING-type.
 MOTIF 406 409 Required for TSG101-binding.
 MOD_RES 524 524 Phosphoserine.
 LIPID 2 2 N-myristoyl glycine.  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Endosome; Ligase; Lipoprotein; Membrane; Metal-binding; Myristate; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 552 AA 
Protein Sequence
MGSILSRRIA GVEDIDIQAN SAYRYPPKSG NYFASHFFMG GEKFDTPHPE GYLFGENMDL 60
NFLGSRPVQF PYVTPAPHEP VKTLRSLVNI RKDSLRLVRY KDDADSPTED GDKPRVLYSL 120
EFTFDADARV AITIYCQASE EFLNGRAVYS PKSPSLQSET VHYKRGVSQQ FSLPSFKIDF 180
SEWKDDELNF DLDRGVFPVV IQAVVDEGDV VEVTGHAHVL LAAFEKHMDG SFSVKPLKQK 240
QIVDRVSYLL QEIYGIENKN NQETKPSDDE NSDNSNECVV CLSDLRDTLI LPCRHLCLCT 300
SCADTLRYQA NNCPICRLPF RALLQIRAVR KKPGALSPVS FSPVLAQSLE HDEHSCPFKK 360
SKPHPASLAS KKPKRETNSD SVPPGYEPIS LLEALNGLRA VSPAIPSAPL YEEITYSGIS 420
DGLSQASCPL AAIDHILDSS RQKGRPQSKA PDSTLRSPSS PIHEEDEEKL SEDVDAPPPL 480
GGAELALRES SSPESFITEE VDESSSPQQG TRAASIENVL QDSSPEHCGR GPPADIYLPG 540
RPTSMETAHG LATTSPTWPP LGGPSPDPSA AELTPL 576 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
 GO:0043951; P:negative regulation of cAMP-mediated signaling; IDA:UniProtKB.
 GO:0045744; P:negative regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
 GO:0006513; P:protein monoubiquitination; IMP:UniProtKB.
 GO:0000209; P:protein polyubiquitination; IEA:Compara. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
  
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS