ID MINY1_HUMAN Reviewed; 469 AA. AC Q8N5J2; B3KWP4; B3KWV8; B4DXF2; B4E1S4; D3DV09; J3KP53; Q5SZF0; Q9NUL9; AC Q9P2F7; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 160. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase MINDY-1 {ECO:0000303|PubMed:27292798}; DE EC=3.4.19.12 {ECO:0000269|PubMed:27292798}; DE AltName: Full=Deubiquitinating enzyme MINDY-1 {ECO:0000303|PubMed:27292798}; DE AltName: Full=Protein FAM63A; GN Name=MINDY1 {ECO:0000312|HGNC:HGNC:25648}; Synonyms=FAM63A, KIAA1390; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-385. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND RP VARIANT LYS-385. RC TISSUE=Placenta, Testis, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-385. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-385. RC TISSUE=Brain; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-441, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 110-384, X-RAY CRYSTALLOGRAPHY RP (2.65 ANGSTROMS) OF 110-384 IN COMPLEX WITH UBIQUITIN, FUNCTION, CATALYTIC RP ACTIVITY, MUTAGENESIS OF GLN-131; CYS-137; ASP-209; VAL-210; TRP-240; RP TYR-258; GLU-263; PHE-315; HIS-319 AND 415-LEU-ALA-416, AND GENE FAMILY. RX PubMed=27292798; DOI=10.1016/j.molcel.2016.05.009; RA Abdul Rehman S.A., Kristariyanto Y.A., Choi S.Y., Nkosi P.J., Weidlich S., RA Labib K., Hofmann K., Kulathu Y.; RT "MINDY-1 is a member of an evolutionarily conserved and structurally RT distinct new family of deubiquitinating enzymes."; RL Mol. Cell 63:146-155(2016). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 388-426 IN COMPLEX WITH RP UBIQUITIN, BINDING TO 'LYS-47' POLYUBIQUITIN CHAINS, AND MUTAGENESIS OF RP ALA-396; LEU-408; THR-411; ASP-412; LEU-413; GLU-414; LEU-415; ALA-416; RP GLN-418; LEU-419; GLN-420; GLN-421; GLU-422; GLU-423 AND TYR-424. RX PubMed=28082312; DOI=10.15252/embr.201643205; RA Kristariyanto Y.A., Abdul Rehman S.A., Weidlich S., Knebel A., Kulathu Y.; RT "A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin RT chains."; RL EMBO Rep. 18:392-402(2017). 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:0000269|PubMed:27292798, CC ECO:0000269|PubMed:28082312}. 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:0000269|PubMed:27292798}; CC -!- INTERACTION: CC Q8N5J2; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-372322, EBI-10172181; CC Q8N5J2-3; P55212: CASP6; NbExp=3; IntAct=EBI-12382151, EBI-718729; CC Q8N5J2-3; P36544: CHRNA7; NbExp=3; IntAct=EBI-12382151, EBI-79333; CC Q8N5J2-3; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12382151, EBI-724310; CC Q8N5J2-3; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-12382151, EBI-2548508; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8N5J2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N5J2-2; Sequence=VSP_034715; CC Name=3; CC IsoId=Q8N5J2-3; Sequence=VSP_037077; CC Name=4; CC IsoId=Q8N5J2-4; Sequence=VSP_037076; CC -!- SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA92628.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AB037811; BAA92628.1; ALT_INIT; mRNA. DR EMBL; AK002142; BAA92104.1; -; mRNA. DR EMBL; AK125493; BAG54206.1; -; mRNA. DR EMBL; AK125959; BAG54270.1; -; mRNA. DR EMBL; AK301946; BAG63364.1; -; mRNA. DR EMBL; AK303962; BAG64886.1; -; mRNA. DR EMBL; AL590133; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53491.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53492.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53493.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53495.1; -; Genomic_DNA. DR EMBL; BC032321; AAH32321.1; -; mRNA. DR CCDS; CCDS30854.1; -. [Q8N5J2-2] DR CCDS; CCDS55635.1; -. [Q8N5J2-4] DR CCDS; CCDS976.1; -. [Q8N5J2-1] DR RefSeq; NP_001035307.1; NM_001040217.2. [Q8N5J2-2] DR RefSeq; NP_001156730.1; NM_001163258.1. [Q8N5J2-1] DR RefSeq; NP_001156731.1; NM_001163259.1. [Q8N5J2-4] DR RefSeq; NP_001156732.1; NM_001163260.1. [Q8N5J2-2] DR RefSeq; NP_001306927.1; NM_001319998.1. [Q8N5J2-1] DR RefSeq; NP_060849.2; NM_018379.4. [Q8N5J2-1] DR RefSeq; XP_016857261.1; XM_017001772.1. DR RefSeq; XP_016857266.1; XM_017001777.1. [Q8N5J2-3] DR PDB; 5JKN; X-ray; 3.00 A; A=110-384. DR PDB; 5JQS; X-ray; 2.65 A; A=110-384. DR PDB; 5MN9; X-ray; 2.05 A; C=388-426. DR PDB; 6TUV; X-ray; 2.16 A; A=110-384. DR PDB; 6TXB; X-ray; 2.18 A; A=110-384. DR PDB; 6Y6R; X-ray; 3.32 A; A=110-384. DR PDB; 6YJG; X-ray; 3.28 A; A=97-384. DR PDB; 6Z90; X-ray; 3.59 A; A=110-384. DR PDBsum; 5JKN; -. DR PDBsum; 5JQS; -. DR PDBsum; 5MN9; -. DR PDBsum; 6TUV; -. DR PDBsum; 6TXB; -. DR PDBsum; 6Y6R; -. DR PDBsum; 6YJG; -. DR PDBsum; 6Z90; -. DR AlphaFoldDB; Q8N5J2; -. DR SMR; Q8N5J2; -. DR BioGRID; 120906; 41. DR IntAct; Q8N5J2; 15. DR STRING; 9606.ENSP00000354669; -. DR GlyGen; Q8N5J2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8N5J2; -. DR PhosphoSitePlus; Q8N5J2; -. DR BioMuta; MINDY1; -. DR DMDM; 311033379; -. DR EPD; Q8N5J2; -. DR jPOST; Q8N5J2; -. DR MassIVE; Q8N5J2; -. DR MaxQB; Q8N5J2; -. DR PaxDb; 9606-ENSP00000354669; -. DR PeptideAtlas; Q8N5J2; -. DR ProteomicsDB; 72065; -. [Q8N5J2-1] DR ProteomicsDB; 72066; -. [Q8N5J2-2] DR ProteomicsDB; 72067; -. [Q8N5J2-3] DR ProteomicsDB; 72068; -. [Q8N5J2-4] DR Pumba; Q8N5J2; -. DR TopDownProteomics; Q8N5J2-2; -. [Q8N5J2-2] DR Antibodypedia; 34043; 99 antibodies from 15 providers. DR DNASU; 55793; -. DR Ensembl; ENST00000312210.9; ENSP00000310923.5; ENSG00000143409.17. [Q8N5J2-2] DR Ensembl; ENST00000361738.12; ENSP00000354669.7; ENSG00000143409.17. [Q8N5J2-1] DR Ensembl; ENST00000361936.9; ENSP00000354814.5; ENSG00000143409.17. [Q8N5J2-1] DR Ensembl; ENST00000493834.2; ENSP00000437174.2; ENSG00000143409.17. [Q8N5J2-4] DR Ensembl; ENST00000683666.2; ENSP00000507359.1; ENSG00000143409.17. [Q8N5J2-1] DR GeneID; 55793; -. DR KEGG; hsa:55793; -. DR MANE-Select; ENST00000683666.2; ENSP00000507359.1; NM_001376665.1; NP_001363594.1. DR UCSC; uc001ewd.4; human. [Q8N5J2-1] DR AGR; HGNC:25648; -. DR CTD; 55793; -. DR DisGeNET; 55793; -. DR GeneCards; MINDY1; -. DR HGNC; HGNC:25648; MINDY1. DR HPA; ENSG00000143409; Low tissue specificity. DR MIM; 618407; gene. DR neXtProt; NX_Q8N5J2; -. DR OpenTargets; ENSG00000143409; -. DR PharmGKB; PA142671872; -. DR VEuPathDB; HostDB:ENSG00000143409; -. DR eggNOG; KOG2427; Eukaryota. DR GeneTree; ENSGT00390000016607; -. DR HOGENOM; CLU_022566_5_0_1; -. DR InParanoid; Q8N5J2; -. DR OMA; GVEMSIF; -. DR OrthoDB; 9158at2759; -. DR PhylomeDB; Q8N5J2; -. DR TreeFam; TF314589; -. DR PathwayCommons; Q8N5J2; -. DR SignaLink; Q8N5J2; -. DR BioGRID-ORCS; 55793; 70 hits in 1202 CRISPR screens. DR ChiTaRS; FAM63A; human. DR GenomeRNAi; 55793; -. DR Pharos; Q8N5J2; Tbio. DR PRO; PR:Q8N5J2; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8N5J2; Protein. DR Bgee; ENSG00000143409; Expressed in body of pancreas and 175 other cell types or tissues. DR ExpressionAtlas; Q8N5J2; baseline and differential. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IDA:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC. DR GO; GO:1990380; F:K48-linked deubiquitinase activity; IDA:UniProtKB. DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR InterPro; IPR007518; MINDY. DR InterPro; IPR033979; MINDY_domain. DR PANTHER; PTHR18063; NF-E2 INDUCIBLE PROTEIN; 1. DR PANTHER; PTHR18063:SF7; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE MINDY-1; 1. DR Pfam; PF04424; MINDY_DUB; 1. DR Genevisible; Q8N5J2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Hydrolase; Phosphoprotein; Protease; KW Reference proteome; Thiol protease; Ubl conjugation pathway. FT CHAIN 1..469 FT /note="Ubiquitin carboxyl-terminal hydrolase MINDY-1" FT /id="PRO_0000344037" FT REGION 1..85 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 388..426 FT /note="Ubiquitin-binding domain (UBD)" FT /evidence="ECO:0000305|PubMed:27292798" FT REGION 441..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 27..53 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 452..469 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 137 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:27292798" FT ACT_SITE 319 FT /note="Proton acceptor" FT /evidence="ECO:0000305|PubMed:27292798" FT SITE 412 FT /note="Ubiquitin-binding" FT /evidence="ECO:0000269|PubMed:28082312" FT SITE 415..416 FT /note="Ubiquitin-binding" FT /evidence="ECO:0000269|PubMed:28082312" FT SITE 419 FT /note="Ubiquitin-binding" FT /evidence="ECO:0000269|PubMed:28082312" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..142 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_034715" FT VAR_SEQ 1..95 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037076" FT VAR_SEQ 1 FT /note="M -> MLLGPPPFNESTKPSPSPCHSFASQAWLRQVPEVSKHLQCPSAKSLL FT TM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037077" FT VARIANT 385 FT /note="T -> K (in dbSNP:rs2925741)" FT /evidence="ECO:0000269|PubMed:10718198, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.4" FT /id="VAR_044541" FT MUTAGEN 131 FT /note="Q->A,E: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 137 FT /note="C->A: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 209 FT /note="D->A: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 210 FT /note="V->A: Greatly impairs ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 240 FT /note="W->A: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 258 FT /note="Y->A: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 263 FT /note="E->A: Greatly impairs ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 263 FT /note="E->R: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 315 FT /note="F->A: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 319 FT /note="H->A: Abolishes ubiquitin hydrolase activity." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 396 FT /note="A->G: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 408 FT /note="L->A: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 411 FT /note="T->A: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 412 FT /note="D->A: Loss of binding to 'Lys-48' tetraubiquitin FT chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 413 FT /note="L->A: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 414 FT /note="E->A: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 415..416 FT /note="LA->AG: Decreased association with 'Lys-48'-linked FT conjugated ubiquitin." FT /evidence="ECO:0000269|PubMed:27292798" FT MUTAGEN 415 FT /note="L->A: Loss of binding to 'Lys-48' tetraubiquitin FT chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 416 FT /note="A->G,D: Loss of binding to 'Lys-48' tetraubiquitin FT chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 416 FT /note="A->S: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 418 FT /note="Q->A,K: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 419 FT /note="L->A: Loss of binding to 'Lys-48' tetraubiquitin FT chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 420 FT /note="Q->A: Loss of binding to 'Lys-48' tetraubiquitin FT chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 421 FT /note="Q->E,R: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 422 FT /note="E->A: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 423 FT /note="E->A: Loss of binding to 'Lys-48' tetraubiquitin FT chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 423 FT /note="E->EA,EAAA,EAAAAAA,EAAAAAAA: Loss of binding to FT 'Lys-48' tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 423 FT /note="Missing: Loss of binding to 'Lys-48' tetraubiquitin FT chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 424 FT /note="Y->A,D,E: Decreased binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT MUTAGEN 424 FT /note="Y->F,W: No effect on binding to 'Lys-48' FT tetraubiquitin chains." FT /evidence="ECO:0000269|PubMed:28082312" FT CONFLICT 287 FT /note="L -> P (in Ref. 2; BAA92104)" FT /evidence="ECO:0000305" FT CONFLICT 367 FT /note="S -> R (in Ref. 2; BAA92104)" FT /evidence="ECO:0000305" FT STRAND 113..121 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 131..135 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 137..148 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 163..175 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 188..200 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 201..205 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 212..215 FT /evidence="ECO:0007829|PDB:6YJG" FT HELIX 224..231 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:5JKN" FT HELIX 247..253 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 258..269 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 274..289 FT /evidence="ECO:0007829|PDB:6TUV" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 296..305 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 311..315 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 320..326 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 329..333 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 347..350 FT /evidence="ECO:0007829|PDB:6TUV" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:6TUV" FT HELIX 411..425 FT /evidence="ECO:0007829|PDB:5MN9" FT CONFLICT Q8N5J2-3:44 FT /note="K -> E (in Ref. 2; BAG63364)" FT /evidence="ECO:0000305" SQ SEQUENCE 469 AA; 51778 MW; FEB658BAF8A878C6 CRC64; MEYHQPEDPA PGKAGTAEAV IPENHEVLAG PDEHPQDTDA RDADGEARER EPADQALLPS QCGDNLESPL PEASSAPPGP TLGTLPEVET IRACSMPQEL PQSPRTRQPE PDFYCVKWIP WKGEQTPIIT QSTNGPCPLL AIMNILFLQW KVKLPPQKEV ITSDELMAHL GNCLLSIKPQ EKSEGLQLNF QQNVDDAMTV LPKLATGLDV NVRFTGVSDF EYTPECSVFD LLGIPLYHGW LVDPQSPEAV RAVGKLSYNQ LVERIITCKH SSDTNLVTEG LIAEQFLETT AAQLTYHGLC ELTAAAKEGE LSVFFRNNHF STMTKHKSHL YLLVTDQGFL QEEQVVWESL HNVDGDSCFC DSDFHLSHSL GKGPGAEGGS GSPETQLQVD QDYLIALSLQ QQQPRGPLGL TDLELAQQLQ QEEYQQQQAA QPVRMRTRVL SLQGRGATSG RPAGERRQRP KHESDCILL //