MINY2_MOUSE
ID MINY2_MOUSE Reviewed; 601 AA.
AC Q6PDI6; Q571N1; Q6NSV8; Q7TML6; Q8BK25; Q8BL22; Q8BL47; Q8BZC1;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-2;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme MINDY-2;
DE AltName: Full=Protein FAM63B;
GN Name=Mindy2; Synonyms=Fam63b, Kiaa1164;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-589 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Cerebellum, and Corpora quadrigemina;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-590 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC 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 remove 'Lys-48'-linked conjugated
CC ubiquitin from proteins. Can also bind to polyubiquitin chains of
CC different linkage types, including 'Lys-6', 'Lys-11', 'Lys-29', 'Lys-
CC 33' and 'Lys-63'. May play a regulatory role at the level of protein
CC turnover. {ECO:0000250|UniProtKB:Q8NBR6}.
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:Q8NBR6};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PDI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PDI6-2; Sequence=VSP_034720;
CC Name=3;
CC IsoId=Q6PDI6-3; Sequence=VSP_034721, VSP_034722;
CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69845.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC32709.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90344.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK035930; BAC29246.1; -; mRNA.
DR EMBL; AK046403; BAC32709.1; ALT_FRAME; mRNA.
DR EMBL; AK046623; BAC32810.1; -; mRNA.
DR EMBL; AK077470; BAC36815.1; -; mRNA.
DR EMBL; BC055816; AAH55816.1; -; mRNA.
DR EMBL; BC058683; AAH58683.1; -; mRNA.
DR EMBL; BC069845; AAH69845.1; ALT_SEQ; mRNA.
DR EMBL; AK220158; BAD90344.1; ALT_INIT; mRNA.
DR CCDS; CCDS40681.1; -. [Q6PDI6-1]
DR RefSeq; NP_766360.2; NM_172772.2. [Q6PDI6-1]
DR AlphaFoldDB; Q6PDI6; -.
DR SMR; Q6PDI6; -.
DR STRING; 10090.ENSMUSP00000037035; -.
DR iPTMnet; Q6PDI6; -.
DR PhosphoSitePlus; Q6PDI6; -.
DR EPD; Q6PDI6; -.
DR jPOST; Q6PDI6; -.
DR MaxQB; Q6PDI6; -.
DR PaxDb; Q6PDI6; -.
DR PeptideAtlas; Q6PDI6; -.
DR PRIDE; Q6PDI6; -.
DR ProteomicsDB; 290248; -. [Q6PDI6-1]
DR ProteomicsDB; 290249; -. [Q6PDI6-2]
DR ProteomicsDB; 290250; -. [Q6PDI6-3]
DR Antibodypedia; 63975; 60 antibodies from 12 providers.
DR Ensembl; ENSMUST00000049031; ENSMUSP00000037035; ENSMUSG00000042444. [Q6PDI6-1]
DR GeneID; 235461; -.
DR KEGG; mmu:235461; -.
DR UCSC; uc009qon.1; mouse. [Q6PDI6-1]
DR UCSC; uc009qoq.1; mouse. [Q6PDI6-3]
DR CTD; 54629; -.
DR MGI; MGI:2443086; Mindy2.
DR VEuPathDB; HostDB:ENSMUSG00000042444; -.
DR eggNOG; KOG2427; Eukaryota.
DR GeneTree; ENSGT00390000016607; -.
DR HOGENOM; CLU_022566_3_1_1; -.
DR InParanoid; Q6PDI6; -.
DR OMA; THLCPDN; -.
DR OrthoDB; 1601180at2759; -.
DR PhylomeDB; Q6PDI6; -.
DR TreeFam; TF314589; -.
DR BioGRID-ORCS; 235461; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Mindy2; mouse.
DR PRO; PR:Q6PDI6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6PDI6; protein.
DR Bgee; ENSMUSG00000042444; Expressed in cerebellar vermis and 231 other tissues.
DR ExpressionAtlas; Q6PDI6; baseline and differential.
DR Genevisible; Q6PDI6; MM.
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:0071795; F:K11-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0071796; F:K6-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0070530; F:K63-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..601
FT /note="Ubiquitin carboxyl-terminal hydrolase MINDY-2"
FT /id="PRO_0000344043"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..537
FT /note="Ubiquitin-binding domain (UBD)"
FT /evidence="ECO:0000250|UniProtKB:Q8NBR6"
FT REGION 534..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 520
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 523..524
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT SITE 527
FT /note="Ubiquitin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8N5J2"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBR6"
FT VAR_SEQ 1..263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034720"
FT VAR_SEQ 388
FT /note="F -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034721"
FT VAR_SEQ 389..601
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034722"
FT CONFLICT 78
FT /note="G -> S (in Ref. 2; AAH55816)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> T (in Ref. 2; AAH55816)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="L -> F (in Ref. 2; AAH69845 and 3; BAD90344)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="E -> G (in Ref. 1; BAC29246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 65637 MW; D1094C08F6DFB10B CRC64;
MENSPDSPQP LELGVAAGRV SPPEGRRRGG REAEDGPAGR AVDSGGQGAA AAAARSSLGD
PTSPSQLGCG AGSDLKDGAS SSPAASEVPS RGQHKVTASP ELAEAAAGRG SGPVGDTGTC
RVEQAAEEPS STGAPSSSCS EPSPPGDSPS LDSLESFSNL HSFPSSSEFN SEEGAETRVP
EDVEEGAAGP PRAAPLCKEE EEDPAQVLAA SKERFPGQSV YHIKWIQWKE ENTPIITQNE
NGPCPLLAIL NVLLLAWKVK LPPMMEIITA EQLMEYLGDY MLEAKPKEIS EIQRVNYEQN
MSDAMAILHK LQTGLDVNVR FTGVRVFEYT PECIVFDLLD IPLYHGWLVD PQIDDIVKAV
GNCSYNQLVE KIISCKQSDN SQLVSEGFVA EQFLNNTATQ LTYHGLCELT STVQEGELCV
FFRNNHFSTM TKYKGQLYLL VTDQGFLTEE KIVWESLHNV DGDGNFCDSE FHLRPPSDPE
TVYKGQQDQI DQDYLMALSL QQEQQSQEIN WEQIPEGISD LELAKKLQEE EDRRASQYYQ
EQEQAQAVVT TTTPSTQAQQ GQPAQASPSS IKQPGNSERK RKEPREKDKE KEKEKNSCVI
L
