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Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.4.19.12) (Deubiquitinating enzyme 5) (Isopeptidase T) (Ubiquitin thioesterase 5) (Ubiquitin-specific-processing protease 5)

 UBP5_HUMAN              Reviewed;         858 AA.
P45974; D3DUS7; D3DUS8; Q96J22;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
10-OCT-2018, entry version 189.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 5;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 5;
AltName: Full=Isopeptidase T;
AltName: Full=Ubiquitin thioesterase 5;
AltName: Full=Ubiquitin-specific-processing protease 5;
Name=USP5; Synonyms=ISOT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=7498549; DOI=10.1016/0014-5793(95)01287-7;
Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K.,
Jaton J.-C.;
"cDNA cloning of a human 100 kDa de-ubiquitinating enzyme: the 100 kDa
human de-ubiquitinase belongs to the ubiquitin C-terminal hydrolase
family 2 (UCH2).";
FEBS Lett. 376:233-237(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8723724; DOI=10.1101/gr.6.4.314;
Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S.,
Malley T., Gibbs R.A.;
"A gene-rich cluster between the CD4 and triosephosphate isomerase
genes at human chromosome 12p13.";
Genome Res. 6:314-326(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9074930; DOI=10.1101/gr.7.3.268;
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
"Large-scale sequencing in human chromosome 12p13: experimental and
computational gene structure determination.";
Genome Res. 7:268-280(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Tashayev V.L., O'Connor L.B., Larsen C.N., Kasperek E., Pickart C.M.;
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
TISSUE=Kidney, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CHARACTERIZATION.
PubMed=7851534; DOI=10.1016/0014-5793(94)01451-6;
Falquet L., Paquet N., Frutiger S., Hughes G.J., Hoang-Van K.,
Jaton J.-C.;
"A human de-ubiquitinating enzyme with both isopeptidase and peptidase
activities in vitro.";
FEBS Lett. 359:73-77(1995).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
MUTAGENESIS OF ARG-221; CYS-335; ASP-435; MET-666 AND MET-734, AND
POLYUBIQUITIN BINDING.
PubMed=18482987; DOI=10.1074/jbc.M800947200;
Reyes-Turcu F.E., Shanks J.R., Komander D., Wilkinson K.D.;
"Recognition of polyubiquitin isoforms by the multiple ubiquitin
binding modules of isopeptidase T.";
J. Biol. Chem. 283:19581-19592(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
FUNCTION.
PubMed=19098288; DOI=10.1074/jbc.M805871200;
Dayal S., Sparks A., Jacob J., Allende-Vega N., Lane D.P.,
Saville M.K.;
"Suppression of the deubiquitinating enzyme USP5 causes the
accumulation of unanchored polyubiquitin and the activation of p53.";
J. Biol. Chem. 284:5030-5041(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
MUTAGENESIS OF 221-ARG--TYR-223 AND TYR-261.
PubMed=22216260; DOI=10.1371/journal.pone.0029362;
Zhang Y.H., Zhou C.J., Zhou Z.R., Song A.X., Hu H.Y.;
"Domain analysis reveals that a deubiquitinating enzyme USP13 performs
non-activating catalysis for Lys63-linked polyubiquitin.";
PLoS ONE 6:E29362-E29362(2011).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292; SER-779; SER-783
AND SER-785, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 163-291 IN COMPLEX WITH
UBIQUITIN, ZINC-BINDING, AND MUTAGENESIS OF CYS-199; CYS-202; CYS-219
AND HIS-232.
PubMed=16564012; DOI=10.1016/j.cell.2006.02.038;
Reyes-Turcu F.E., Horton J.R., Mullally J.E., Heroux A., Cheng X.,
Wilkinson K.D.;
"The ubiquitin binding domain ZnF UBP recognizes the C-terminal
diglycine motif of unanchored ubiquitin.";
Cell 124:1197-1208(2006).
[22]
STRUCTURE BY NMR OF 655-772.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first and second UBA domains in the human
ubiquitin specific protease 5 (isopeptidase 5).";
Submitted (JUN-2006) to the PDB data bank.
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-858 IN COMPLEX WITH
UBIQUITIN, DISULFIDE BOND, AND ZINC-BINDING.
Walker J.R., Avvakumov G.V., Xue S., Butler-Cole C., Weigelt J.,
Bountra C., Arrowsmith C.H., Edwards A.M., Bochkarev A.,
Dhe-Paganon S.;
"Covalent ubiquitin-USP5 complex.";
Submitted (DEC-2009) to the PDB data bank.
-!- FUNCTION: Cleaves linear and branched multiubiquitin polymers with
a marked preference for branched polymers. Involved in unanchored
'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-
63'-linked polyubiquitin with a lower affinity. Knock-down of USP5
causes the accumulation of p53/TP53 and an increase in p53/TP53
transcriptional activity because the unanchored polyubiquitin that
accumulates is able to compete with ubiquitinated p53/TP53 but not
with MDM2 for proteasomal recognition.
{ECO:0000269|PubMed:19098288}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: Interacts with TRIML1. {ECO:0000250}.
-!- INTERACTION:
Q15038:DAZAP2; NbExp=3; IntAct=EBI-741277, EBI-724310;
P54727:RAD23B; NbExp=2; IntAct=EBI-741277, EBI-954531;
O75528:TADA3; NbExp=2; IntAct=EBI-741277, EBI-473249;
Q8WW34:TMEM239; NbExp=3; IntAct=EBI-741277, EBI-9675724;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P45974-1; Sequence=Displayed;
Name=Short;
IsoId=P45974-2; Sequence=VSP_005259;
-!- DOMAIN: The UBP-type zinc finger domain interacts selectively with
an unmodified C-terminus of the proximal ubiquitin. Both UBA
domains are involved in polyubiquitin recognition.
-!- MISCELLANEOUS: The UBP-type zinc finger domain crystallizes as a
dimer linked by a disulfide bond between the Cys-195 residues of
both molecules, but there is no evidence that the full-length USP5
exists as a dimer.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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EMBL; X91349; CAA62690.1; -; mRNA.
EMBL; U47927; AAC50465.1; -; mRNA.
EMBL; U47924; AAB51314.1; -; Genomic_DNA.
EMBL; U47924; AAB51315.1; -; Genomic_DNA.
EMBL; U35116; AAA78934.1; -; mRNA.
EMBL; CH471116; EAW88724.1; -; Genomic_DNA.
EMBL; CH471116; EAW88725.1; -; Genomic_DNA.
EMBL; CH471116; EAW88726.1; -; Genomic_DNA.
EMBL; CH471116; EAW88727.1; -; Genomic_DNA.
EMBL; BC004889; AAH04889.1; -; mRNA.
EMBL; BC005139; AAH05139.1; -; mRNA.
CCDS; CCDS31733.1; -. [P45974-2]
CCDS; CCDS41743.1; -. [P45974-1]
PIR; S68227; S68227.
RefSeq; NP_001092006.1; NM_001098536.1. [P45974-1]
RefSeq; NP_003472.2; NM_003481.2. [P45974-2]
UniGene; Hs.631661; -.
PDB; 2DAG; NMR; -; A=655-715.
PDB; 2DAK; NMR; -; A=723-772.
PDB; 2G43; X-ray; 2.09 A; A/B=163-291.
PDB; 2G45; X-ray; 1.99 A; A/D=163-291.
PDB; 3IHP; X-ray; 2.80 A; A/B=1-858.
PDB; 6DXH; X-ray; 2.00 A; A=171-290.
PDB; 6DXT; X-ray; 1.95 A; A/B=171-290.
PDBsum; 2DAG; -.
PDBsum; 2DAK; -.
PDBsum; 2G43; -.
PDBsum; 2G45; -.
PDBsum; 3IHP; -.
PDBsum; 6DXH; -.
PDBsum; 6DXT; -.
ProteinModelPortal; P45974; -.
SMR; P45974; -.
BioGrid; 113751; 83.
DIP; DIP-34459N; -.
IntAct; P45974; 13.
MINT; P45974; -.
STRING; 9606.ENSP00000229268; -.
BindingDB; P45974; -.
ChEMBL; CHEMBL6158; -.
GuidetoPHARMACOLOGY; 2431; -.
MEROPS; C19.001; -.
iPTMnet; P45974; -.
PhosphoSitePlus; P45974; -.
SwissPalm; P45974; -.
BioMuta; USP5; -.
DMDM; 1717869; -.
REPRODUCTION-2DPAGE; IPI00375145; -.
EPD; P45974; -.
MaxQB; P45974; -.
PaxDb; P45974; -.
PeptideAtlas; P45974; -.
PRIDE; P45974; -.
ProteomicsDB; 55692; -.
ProteomicsDB; 55693; -. [P45974-2]
DNASU; 8078; -.
Ensembl; ENST00000229268; ENSP00000229268; ENSG00000111667. [P45974-1]
Ensembl; ENST00000389231; ENSP00000373883; ENSG00000111667. [P45974-2]
GeneID; 8078; -.
KEGG; hsa:8078; -.
UCSC; uc001qrh.5; human. [P45974-1]
CTD; 8078; -.
DisGeNET; 8078; -.
EuPathDB; HostDB:ENSG00000111667.13; -.
GeneCards; USP5; -.
HGNC; HGNC:12628; USP5.
HPA; HPA006756; -.
MIM; 601447; gene.
neXtProt; NX_P45974; -.
OpenTargets; ENSG00000111667; -.
PharmGKB; PA37253; -.
eggNOG; KOG0944; Eukaryota.
eggNOG; COG5207; LUCA.
GeneTree; ENSGT00390000000874; -.
HOGENOM; HOG000162311; -.
HOVERGEN; HBG002833; -.
InParanoid; P45974; -.
KO; K11836; -.
OMA; QYVERHY; -.
OrthoDB; EOG091G01W3; -.
PhylomeDB; P45974; -.
TreeFam; TF300576; -.
BRENDA; 3.4.19.12; 2681.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
ChiTaRS; USP5; human.
EvolutionaryTrace; P45974; -.
GeneWiki; USP5; -.
GenomeRNAi; 8078; -.
PMAP-CutDB; P45974; -.
PRO; PR:P45974; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111667; Expressed in 217 organ(s), highest expression level in frontal cortex.
CleanEx; HS_USP5; -.
ExpressionAtlas; P45974; baseline and differential.
Genevisible; P45974; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:ParkinsonsUK-UCL.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0043130; F:ubiquitin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0071108; P:protein K48-linked deubiquitination; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR016652; Ubiquitinyl_hydrolase.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR001607; Znf_UBP.
Pfam; PF00627; UBA; 2.
Pfam; PF00443; UCH; 1.
Pfam; PF02148; zf-UBP; 1.
PIRSF; PIRSF016308; UBP; 1.
SMART; SM00165; UBA; 2.
SMART; SM00290; ZnF_UBP; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54001; SSF54001; 4.
PROSITE; PS50030; UBA; 2.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
PROSITE; PS50271; ZF_UBP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 858 Ubiquitin carboxyl-terminal hydrolase 5.
/FTId=PRO_0000080623.
DOMAIN 326 856 USP.
DOMAIN 654 695 UBA 1. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 722 762 UBA 2. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
ZN_FING 197 269 UBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00502}.
REGION 221 224 Substrate binding.
ACT_SITE 335 335 Nucleophile.
ACT_SITE 818 818 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
METAL 199 199 Zinc.
METAL 202 202 Zinc.
METAL 219 219 Zinc.
METAL 232 232 Zinc.
BINDING 209 209 Substrate.
BINDING 259 259 Substrate.
BINDING 261 261 Substrate; via carbonyl oxygen.
BINDING 264 264 Substrate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 292 292 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 623 623 Phosphothreonine.
{ECO:0000250|UniProtKB:P56399}.
MOD_RES 779 779 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
DISULFID 195 816 {ECO:0000269|Ref.23}.
VAR_SEQ 629 652 GSLGFYGNEDEDSFCSPHFSSPTS -> A (in isoform
Short). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_005259.
MUTAGEN 199 199 C->A: Decreased rate of activity and
decreased zinc binding.
{ECO:0000269|PubMed:16564012}.
MUTAGEN 202 202 C->A: Decreased rate of activity.
{ECO:0000269|PubMed:16564012}.
MUTAGEN 219 219 C->A: Decreased rate of activity.
{ECO:0000269|PubMed:16564012}.
MUTAGEN 221 223 RRY->KWF: Loss of polyubiquitin binding
and subsequent activation.
{ECO:0000269|PubMed:22216260}.
MUTAGEN 221 221 R->A: Loss of polyubiquitin hydrolysis.
Loss of ubiquitin binding; when
associated with A-335.
{ECO:0000269|PubMed:18482987}.
MUTAGEN 232 232 H->A: Decreased rate of activity.
{ECO:0000269|PubMed:16564012}.
MUTAGEN 261 261 Y->F: Loss of polyubiquitin binding.
{ECO:0000269|PubMed:22216260}.
MUTAGEN 335 335 C->A: Loss of activity. Loss of ubiquitin
binding; when associated with A-221.
Lower affinity for triubiquitin and
tetraubiquitin, but no effect on affinity
for diubiquitin; when associated with E-
666. Lower affinity for diubiquitin,
triubiquitin and tetraubiquitin; when
associated with E-734.
{ECO:0000269|PubMed:18482987}.
MUTAGEN 435 435 D->A: Loss of polyubiquitin binding and
hydrolysis.
{ECO:0000269|PubMed:18482987}.
MUTAGEN 666 666 M->E: Lower affinity for triubiquitin and
tetraubiquitin, but no effect on affinity
for diubiquitin; when associated with A-
335. No effect on activity; when
associated with E-734.
{ECO:0000269|PubMed:18482987}.
MUTAGEN 734 734 M->E: Lower affinity for diubiquitin,
triubiquitin and tetraubiquitin; when
associated with A-335. No effect on
activity; when associated with E-666.
{ECO:0000269|PubMed:18482987}.
CONFLICT 3 4 EL -> DV (in Ref. 1; CAA62690).
{ECO:0000305}.
CONFLICT 45 45 I -> V (in Ref. 1; CAA62690).
{ECO:0000305}.
CONFLICT 468 468 K -> R (in Ref. 4; AAA78934).
{ECO:0000305}.
CONFLICT 681 681 G -> D (in Ref. 4; AAA78934).
{ECO:0000305}.
HELIX 5 11 {ECO:0000244|PDB:3IHP}.
HELIX 12 15 {ECO:0000244|PDB:3IHP}.
STRAND 31 34 {ECO:0000244|PDB:3IHP}.
STRAND 43 46 {ECO:0000244|PDB:3IHP}.
TURN 47 49 {ECO:0000244|PDB:3IHP}.
TURN 55 57 {ECO:0000244|PDB:3IHP}.
HELIX 58 65 {ECO:0000244|PDB:3IHP}.
STRAND 69 75 {ECO:0000244|PDB:3IHP}.
STRAND 118 124 {ECO:0000244|PDB:3IHP}.
TURN 125 128 {ECO:0000244|PDB:3IHP}.
STRAND 129 131 {ECO:0000244|PDB:3IHP}.
HELIX 141 154 {ECO:0000244|PDB:3IHP}.
TURN 178 182 {ECO:0000244|PDB:2G45}.
STRAND 200 203 {ECO:0000244|PDB:2G45}.
STRAND 206 211 {ECO:0000244|PDB:2G45}.
TURN 212 214 {ECO:0000244|PDB:2G45}.
STRAND 217 219 {ECO:0000244|PDB:2G45}.
HELIX 232 240 {ECO:0000244|PDB:2G45}.
STRAND 244 247 {ECO:0000244|PDB:2G45}.
STRAND 258 260 {ECO:0000244|PDB:2G45}.
TURN 261 264 {ECO:0000244|PDB:2G45}.
STRAND 265 268 {ECO:0000244|PDB:2G45}.
HELIX 272 277 {ECO:0000244|PDB:2G45}.
TURN 278 280 {ECO:0000244|PDB:2G45}.
TURN 283 285 {ECO:0000244|PDB:2G45}.
HELIX 335 344 {ECO:0000244|PDB:3IHP}.
HELIX 348 354 {ECO:0000244|PDB:3IHP}.
TURN 355 357 {ECO:0000244|PDB:3IHP}.
HELIX 358 364 {ECO:0000244|PDB:3IHP}.
HELIX 369 371 {ECO:0000244|PDB:3IHP}.
HELIX 373 385 {ECO:0000244|PDB:3IHP}.
HELIX 415 421 {ECO:0000244|PDB:3IHP}.
TURN 422 424 {ECO:0000244|PDB:3IHP}.
TURN 426 429 {ECO:0000244|PDB:3IHP}.
STRAND 430 432 {ECO:0000244|PDB:3IHP}.
HELIX 436 449 {ECO:0000244|PDB:3IHP}.
HELIX 457 460 {ECO:0000244|PDB:3IHP}.
STRAND 463 471 {ECO:0000244|PDB:3IHP}.
TURN 472 475 {ECO:0000244|PDB:3IHP}.
STRAND 476 489 {ECO:0000244|PDB:3IHP}.
HELIX 493 495 {ECO:0000244|PDB:3IHP}.
HELIX 499 514 {ECO:0000244|PDB:3IHP}.
HELIX 529 537 {ECO:0000244|PDB:3IHP}.
STRAND 540 547 {ECO:0000244|PDB:3IHP}.
TURN 548 551 {ECO:0000244|PDB:3IHP}.
STRAND 552 564 {ECO:0000244|PDB:3IHP}.
STRAND 567 573 {ECO:0000244|PDB:3IHP}.
STRAND 576 578 {ECO:0000244|PDB:3IHP}.
HELIX 580 582 {ECO:0000244|PDB:3IHP}.
STRAND 584 586 {ECO:0000244|PDB:3IHP}.
STRAND 595 598 {ECO:0000244|PDB:3IHP}.
HELIX 600 602 {ECO:0000244|PDB:3IHP}.
HELIX 658 666 {ECO:0000244|PDB:3IHP}.
HELIX 670 679 {ECO:0000244|PDB:3IHP}.
HELIX 685 695 {ECO:0000244|PDB:3IHP}.
HELIX 700 702 {ECO:0000244|PDB:3IHP}.
HELIX 725 732 {ECO:0000244|PDB:3IHP}.
TURN 733 735 {ECO:0000244|PDB:3IHP}.
HELIX 738 747 {ECO:0000244|PDB:3IHP}.
TURN 748 750 {ECO:0000244|PDB:3IHP}.
HELIX 752 770 {ECO:0000244|PDB:3IHP}.
STRAND 799 812 {ECO:0000244|PDB:3IHP}.
STRAND 818 825 {ECO:0000244|PDB:3IHP}.
STRAND 828 833 {ECO:0000244|PDB:3IHP}.
STRAND 836 839 {ECO:0000244|PDB:3IHP}.
STRAND 849 855 {ECO:0000244|PDB:3IHP}.
SEQUENCE 858 AA; 95786 MW; E99CB7CDFA682C65 CRC64;
MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF LGFGKQYVER
HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA IGVEGGFDLS EEKFELDEDV
KIVILPDYLE IARDGLGGLP DIVRDRVTSA VEALLSADSA SRKQEVQAWD GEVRQVSKHA
FSLKQLDNPA RIPPCGWKCS KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET
GYPLAVKLGT ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM
NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF QRKYVDKLEK
IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE RVPEQKEVQD GIAPRMFKAL
IGKGHPEFST NRQQDAQEFF LHLINMVERN CRSSENPNEV FRFLVEEKIK CLATEKVKYT
QRVDYIMQLP VPMDAALNKE ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE
QVDDFWSTAL QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS
QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP TSPMLDESVI
IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD FANPLILPGS SGPGSTSAAA
DPPPEDCVTT IVSMGFSRDQ ALKALRATNN SLERAVDWIF SHIDDLDAEA AMDISEGRSA
ADSISESVPV GPKVRDGPGK YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS
EKPPKDLGYI YFYQRVAS


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