Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00573
Entry Name
UniProt Accession
Theoretical PI
4.99
Molecular Weight
60752.98
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
E3 ubiquitin-protein ligase MGRN1
Protein Synonyms/Alias
6.3.2.-; Mahogunin RING finger protein 1; RING finger protein 156;
Gene Name
MGRN1
Gene Synonyms/Alias
KIAA0544; RNF156;
Created Date
25-JUL-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGSILSRRI
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[PMID:20213681]
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
Motif: 406 409 Required for TSG101-binding.
Modified residue: 411 411 Phosphotyrosine.
Modified residue: 524 524 Phosphoserine.
Protein Length
552 AA.
Protein Sequence
(Canonical)
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 GPPADIYLPA  540
LGPDSCSVGI DE                                                      552
FASTA
(Canonical)
>LipidDB-9606-00573|O60291
MGSILSRRIAGVEDIDIQANSAYRYPPKSGNYFASHFFMGGEKFDTPHPEGYLFGENMDL
NFLGSRPVQFPYVTPAPHEPVKTLRSLVNIRKDSLRLVRYKDDADSPTEDGDKPRVLYSL
EFTFDADARVAITIYCQASEEFLNGRAVYSPKSPSLQSETVHYKRGVSQQFSLPSFKIDF
SEWKDDELNFDLDRGVFPVVIQAVVDEGDVVEVTGHAHVLLAAFEKHMDGSFSVKPLKQK
QIVDRVSYLLQEIYGIENKNNQETKPSDDENSDNSNECVVCLSDLRDTLILPCRHLCLCT
SCADTLRYQANNCPICRLPFRALLQIRAVRKKPGALSPVSFSPVLAQSLEHDEHSCPFKK
SKPHPASLASKKPKRETNSDSVPPGYEPISLLEALNGLRAVSPAIPSAPLYEEITYSGIS
DGLSQASCPLAAIDHILDSSRQKGRPQSKAPDSTLRSPSSPIHEEDEEKLSEDVDAPPPL
GGAELALRESSSPESFITEEVDESSSPQQGTRAASIENVLQDSSPEHCGRGPPADIYLPA
LGPDSCSVGIDE
Gene Ontology
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005769; C:early endosome; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0016874; F:ligase activity; IEA:UniProtKB-KW
GO:0004842; F:ubiquitin-protein transferase 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:Ensembl
Interpro
InterPro; IPR001841; Znf_RING
InterPro; IPR013083; Znf_RING/FYVE/PHD
Pfam
SMART
SMART; SM00184; RING;
PROSITE
PROSITE; PS50089; ZF_RING_2;
PRINTS