- Official Symbol
- MINDY1provided by HGNC
- Official Full Name
- MINDY lysine 48 deubiquitinase 1provided by HGNC
- Also known as
- FAM63A; MINDY-1
- Expression
- Ubiquitous expression in thyroid (RPKM 17.7), testis (RPKM 8.4) and 25 other tissues See more
- Orthologs mouse all
Related articles in PubMed
- MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes. Abdul Rehman SA, et al. Mol Cell, 2016 Jul 7. PMID 27292798, Free PMC Article Abstract
- A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains. Kristariyanto YA, et al. EMBO Rep, 2017 Mar. PMID 28082312, Free PMC ArticleTHe eight different types of ubiquitin (Ub) chains that can be formed play important roles in diverse cellular processes. Linkage-selective recognition of Ub chains by Ub-binding domain (UBD)-containing proteins is central to coupling different Ub signals to specific cellular responses. The motif interacting with ubiquitin (MIU) is a small UBD that has been characterized for its binding to monoUb. The recently discovered deubiquitinase MINDY-1/FAM63A contains a tandem MIU repeat (tMIU) that is highly selective at binding to K48-linked polyUb. We here identify that this linkage-selective binding is mediated by a single MIU motif (MIU2) in MINDY-1. The crystal structure of MIU2 in complex with K48-linked polyubiquitin chains reveals that MIU2 on its own binds to all three Ub moieties in an open conformation that can only be accommodated by K48-linked triUb. The weak Ub binder MIU1 increases overall affinity of the tMIU for polyUb chains without affecting its linkage selectivity. Our analyses reveal new concepts for linkage selectivity and polyUb recognition by UBDs.
- Genome-wide association study identifies genetic risk underlying primary rhegmatogenous retinal detachment. Kirin M, et al. Hum Mol Genet, 2013 Aug 1. PMID 23585552
- New loci associated with kidney function and chronic kidney disease. Köttgen A, et al. Nat Genet, 2010 May. PMID 20383146, Free PMC Article
- Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability. Kwasna D, et al. Mol Cell, 2018 Apr 5. PMID 29576527, Free PMC Article
- Preferred Names
- ubiquitin carboxyl-terminal hydrolase MINDY-1
- Names
- MINDY deubiquitinase 1
- MIU-containing novel DUB family member 1
- deubiquitinating enzyme MINDY-1
- family with sequence similarity 63 member A
- motif interacting with Ub-containing novel DUB
- protein FAM63A
ORIGIN 1 mnilflqwkv klppqkevit sdelmahlgn cllsikpqek seglqlnfqq nvddamtvlp 61 klatgldvnv rftgvsdfey tpecsvfdll giplyhgwlv dpqspeavra vgklsynqlv 121 eriitckhss dtnlvtegli aeqflettaa qltyhglcel taaakegels vffrnnhfst 181 mtkhkshlyl lvtdqgflqe eqvvweslhn vdgdscfcds dfhlshslgk gpgaeggsgs 241 petqlqvdqd ylialslqqq qprgplgltd lelaqqlqqe eyqqqqaaqp vrmrtrvlsl 301 qgrgatsgrp agerrqrpkh esdcill
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