MINY1_HUMAN
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 03-AUG-2022, entry version 151.
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};
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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; CCDS53361.1; -. [Q8N5J2-1]
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; 38.
DR IntAct; Q8N5J2; 15.
DR STRING; 9606.ENSP00000354669; -.
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; Q8N5J2; -.
DR PeptideAtlas; Q8N5J2; -.
DR PRIDE; Q8N5J2; -.
DR ProteomicsDB; 72065; -. [Q8N5J2-1]
DR ProteomicsDB; 72066; -. [Q8N5J2-2]
DR ProteomicsDB; 72067; -. [Q8N5J2-3]
DR ProteomicsDB; 72068; -. [Q8N5J2-4]
DR TopDownProteomics; Q8N5J2-2; -. [Q8N5J2-2]
DR Antibodypedia; 34043; 93 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 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; NHEVPLG; -.
DR OrthoDB; 1601180at2759; -.
DR PhylomeDB; Q8N5J2; -.
DR TreeFam; TF314589; -.
DR PathwayCommons; Q8N5J2; -.
DR SignaLink; Q8N5J2; -.
DR BioGRID-ORCS; 55793; 52 hits in 1124 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 173 other tissues.
DR ExpressionAtlas; Q8N5J2; baseline and differential.
DR Genevisible; Q8N5J2; HS.
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:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
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 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
