Search by BoMiProt ID - Bomi10231


Primary Information

BoMiProt ID Bomi10231
Protein Name Ubiquitin carboxyl-terminal hydrolase MINDY-2/Deubiquitinating enzyme MINDY-2/Protein FAM63B
Organism Bos taurus
Uniprot IDQ2KI23
Milk FractionWhey
Ref Sequence ID NP_001039740.1
Aminoacid Length 630
Molecular Weight 68118
FASTA Sequence Download
Gene Name MINDY2/FAM63B
Gene ID 524749
Protein Existence Status reviewed

Secondary Information

Protein Function deubiquitinase activity.removes 'Lys-48'-linked conjugated ubiquitin from proteins.
Biochemical Properties The catalytic domain of MINDY1/2 has five distinct Ub binding sites. Cys loop regulate DUB activity,Non-canonical catalytic triad composed of Cys-His-Thr,
PTMs Phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q2KI23|MINY2_BOVIN Ubiquitin carboxyl-terminal hydrolase MINDY-2 OS=Bos taurus OX=9913 GN=MINDY2 PE=2 SV=1 MESGPESLQPLEHGVAAGPAPGTGSPQEGQQETRLAAGDGPGVWAAESSGGKGQGAAAGG RSLSDSASPAGSPQVLVPCSSLPRLDLKESDLES*94PAAQKEPVRGQHKVTASPETAEAGAD HGLGPEGDGGARPDPAGTCQEESAAAGSSEPSSGGGLSSSCSDPSPPGESPSLDSLESFS NLHSFPSSSEFNSEEGAENRVPEEEEGAAVLPGAVPLCGEEEVEEEEAQVLAASKERFPG QSVYHIKWIQWKEENTPIITQNENGPCPLLAILNVLLLAWKVKLPPMMEIITAEQLMEYL GDYMLDTKPKEISEIQRLNYEQNMSDAMAVLHKLQTGLDVNVKFTGVRVFEYTPECIVFD LLDIPLYHGWLVDPQIDDIVKAVGNCSYNQLVEKIISCKQSENSELVSEGFVAEQFLNNT ATQLTYHGLCELTSTVQEGELCVFFRNNHFSTMTKYKGLLYLLVTDQGFLTEEKVVWESL HNVDGDGNFCDSEFHLRPPSDPETVYRGQQDQIDQDYLMALSLQQEQQSQEINWEQIPEG ISDLELAKKLQEEEDRRASQYYQEQEQAAAAAASASASASASASTQAPQSQPVQASPSSG RQSGNSERKRKEPREKDKEKEKEKNSCVIL
Predicted Disorder Regions 3 disordered segments; (1-213), (233-236), (502-510)
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography Abdul Rehman SA, Armstrong LA, Lange SM, Kristariyanto YA, Gräwert TW, Knebel A, Svergun DI, Kulathu Y. Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2. Mol Cell. 2021 Oct 21;81(20):4176-4190.e6. doi: 10.1016/j.molcel.2021.08.024. Epub 2021 Sep 15. PMID: 34529927; PMCID: PMC8550791.