MINY1_MOUSE
ID MINY1_MOUSE Reviewed; 468 AA.
AC Q76LS9; Q3TEF4; Q52KE4; Q566I9; Q6PES4; Q80V14; Q8CB41; Q8CHR2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-1;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme MINDY-1;
DE AltName: Full=NF-E2 inducible protein;
DE AltName: Full=Protein FAM63A;
GN Name=Mindy1; Synonyms=Fam63a, Ni;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nagata Y., Oda M., Haruta H., Todokoro K.;
RT "NF-E2 inducible megakaryocyte specific novel gene.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-440, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked
CC conjugated ubiquitin from proteins. Has exodeubiquitinase activity and
CC has a preference for long polyubiquitin chains. May play a regulatory
CC role at the level of protein turnover. {ECO:0000250|UniProtKB:Q8N5J2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q8N5J2};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q76LS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76LS9-2; Sequence=VSP_034718;
CC Name=3;
CC IsoId=Q76LS9-3; Sequence=VSP_034716, VSP_034717;
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39762.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential vector sequence.; Evidence={ECO:0000305};
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DR EMBL; AB075603; BAD06451.1; -; mRNA.
DR EMBL; AK036838; BAC29601.1; -; mRNA.
DR EMBL; AK169673; BAE41294.1; -; mRNA.
DR EMBL; BC039762; AAH39762.1; ALT_SEQ; mRNA.
DR EMBL; BC051048; AAH51048.1; -; mRNA.
DR EMBL; BC057901; AAH57901.1; -; mRNA.
DR EMBL; BC093521; AAH93521.1; -; mRNA.
DR EMBL; BC094388; AAH94388.1; -; mRNA.
DR EMBL; BC132301; AAI32302.1; -; mRNA.
DR CCDS; CCDS17611.1; -. [Q76LS9-2]
DR CCDS; CCDS57233.1; -. [Q76LS9-1]
DR RefSeq; NP_598619.2; NM_133858.4. [Q76LS9-2]
DR RefSeq; NP_955769.1; NM_199475.1. [Q76LS9-1]
DR RefSeq; XP_006502282.1; XM_006502219.3. [Q76LS9-1]
DR RefSeq; XP_017175267.1; XM_017319778.1. [Q76LS9-1]
DR AlphaFoldDB; Q76LS9; -.
DR SMR; Q76LS9; -.
DR BioGRID; 217146; 1.
DR STRING; 10090.ENSMUSP00000102805; -.
DR iPTMnet; Q76LS9; -.
DR PhosphoSitePlus; Q76LS9; -.
DR EPD; Q76LS9; -.
DR jPOST; Q76LS9; -.
DR MaxQB; Q76LS9; -.
DR PaxDb; Q76LS9; -.
DR PeptideAtlas; Q76LS9; -.
DR PRIDE; Q76LS9; -.
DR ProteomicsDB; 290245; -. [Q76LS9-1]
DR ProteomicsDB; 290246; -. [Q76LS9-2]
DR ProteomicsDB; 290247; -. [Q76LS9-3]
DR Antibodypedia; 34043; 93 antibodies from 15 providers.
DR DNASU; 75007; -.
DR Ensembl; ENSMUST00000039537; ENSMUSP00000043910; ENSMUSG00000038712. [Q76LS9-2]
DR Ensembl; ENSMUST00000107187; ENSMUSP00000102805; ENSMUSG00000038712. [Q76LS9-1]
DR Ensembl; ENSMUST00000168223; ENSMUSP00000127839; ENSMUSG00000038712. [Q76LS9-2]
DR GeneID; 75007; -.
DR KEGG; mmu:75007; -.
DR UCSC; uc008qjd.2; mouse. [Q76LS9-2]
DR UCSC; uc008qje.2; mouse. [Q76LS9-1]
DR UCSC; uc008qjf.2; mouse. [Q76LS9-3]
DR CTD; 55793; -.
DR MGI; MGI:1922257; Mindy1.
DR VEuPathDB; HostDB:ENSMUSG00000038712; -.
DR eggNOG; KOG2427; Eukaryota.
DR GeneTree; ENSGT00390000016607; -.
DR HOGENOM; CLU_022566_5_1_1; -.
DR InParanoid; Q76LS9; -.
DR OMA; NHEVPLG; -.
DR PhylomeDB; Q76LS9; -.
DR TreeFam; TF314589; -.
DR BioGRID-ORCS; 75007; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fam63a; mouse.
DR PRO; PR:Q76LS9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q76LS9; protein.
DR Bgee; ENSMUSG00000038712; Expressed in primary oocyte and 252 other tissues.
DR ExpressionAtlas; Q76LS9; baseline and differential.
DR Genevisible; Q76LS9; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISO:MGI.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IBA:GO_Central.
DR InterPro; IPR007518; MINDY.
DR InterPro; IPR033979; MINDY_domain.
DR PANTHER; PTHR18063; PTHR18063; 1.
DR Pfam; PF04424; MINDY_DUB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..468
FT /note="Ubiquitin carboxyl-terminal hydrolase MINDY-1"
FT /id="PRO_0000344038"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..427
FT /note="Ubiquitin-binding domain (UBD)"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT REGION 423..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 413
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 416..417
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 420
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034716"
FT VAR_SEQ 170..191
FT /note="LGNCLLSIKPQEKSEGLQLNFQ -> MKHGMVGGREGRLDQPSCLFSH (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034717"
FT VAR_SEQ 392..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034718"
FT CONFLICT 61
FT /note="Q -> E (in Ref. 2; BAE41294)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="T -> A (in Ref. 3; AAH94388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 51226 MW; 1C52C022A3D5DBA9 CRC64;
MEQPQTENPA PSKATSAETV ESENHEALSG PEKHPQDKDG ADADGAAGEQ EPGDQTLPPA
QDGENLECPP PEASSSPPGP ACGTSPKVET AEVCSRPQEL PQSPRIQQPE LDFYCVKWIP
WKGERTPIIT QSTNGPCPLL AIMNILFLQW KVKLPPQKEV ITSDELLTHL GNCLLSIKPQ
EKSEGLQLNF QQNVDDAMTV LPKLATGLDV NVRFTGVSDF EYTPECSIFD LLGIPLYHGW
LVDPQSPEAV SAVGKLSYNQ LVEKIITCKH SSDSNLVTEG LVAEQFLETT AAQLTYHGLC
ELTAAATEDE LSVFFRNNHF STMTKHKSHL YLLVTDQGFL QEEQVVWESL HNVDGDSCFC
DSDFHLSHSL GKSHGAEGGG GSPEKQLQVD QDYLIALSLQ QQQQPQGTLG LSDLELAQQL
QQEEYQQQQA VQPVRTRAPS PQGRGATSGR PAGERRQRSK TESDCVLL
