MINDY1 (1q21.3) , FAM63A, Deubikitinasien ryhmä Vi löytyi vuonna 2016 .

https://www.ncbi.nlm.nih.gov/gene/55793

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

1. 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
2. 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.
3. Genome-wide association study identifies genetic risk underlying primary rhegmatogenous retinal detachment. Kirin M, et al. Hum Mol Genet, 2013 Aug 1. PMID 23585552
4. New loci associated with kidney function and chronic kidney disease. Köttgen A, et al. Nat Genet, 2010 May. PMID 20383146, Free PMC Article
5. 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

See all (16) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

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