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Ubiquitin carboxyl-terminal hydrolase 13 (EC 3.4.19.12) (Deubiquitinating enzyme 13) (Isopeptidase T-3) (ISOT-3) (Ubiquitin thioesterase 13) (Ubiquitin-specific-processing protease 13)

 UBP13_HUMAN             Reviewed;         863 AA.
Q92995; A8K2S3; B4DYF3; D3DNS2; Q96B25;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 2.
27-SEP-2017, entry version 153.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 13;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 13;
AltName: Full=Isopeptidase T-3;
Short=ISOT-3;
AltName: Full=Ubiquitin thioesterase 13;
AltName: Full=Ubiquitin-specific-processing protease 13;
Name=USP13; Synonyms=ISOT3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9841226; DOI=10.1016/S0378-1119(98)00341-2;
Timms K.M., Ansari-Lari M.A., Morris W., Brown S.N., Gibbs R.A.;
"The genomic organization of Isopeptidase T-3 (ISOT-3), a new member
of the ubiquitin specific protease family (UBP).";
Gene 217:101-106(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
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).
[6]
FUNCTION.
PubMed=17653289; DOI=10.1371/journal.pone.0000679;
Catic A., Fiebiger E., Korbel G.A., Blom D., Galardy P.J.,
Ploegh H.L.;
"Screen for ISG15-crossreactive deubiquitinases.";
PLoS ONE 2:E679-E679(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND 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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-122, 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).
[9]
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).
[10]
FUNCTION, AND ENZYME REGULATION.
PubMed=21962518; DOI=10.1016/j.cell.2011.08.037;
Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V.,
Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y.,
Choi A., Ke H., Ma D., Yuan J.;
"Beclin1 controls the levels of p53 by regulating the deubiquitination
activity of USP10 and USP13.";
Cell 147:223-234(2011).
[11]
FUNCTION, INTERACTION WITH SIAH2, AND MUTAGENESIS OF TRP-221; LYS-233;
PHE-273; CYS-345; MET-664; MET-739; HIS-814 AND HIS-823.
PubMed=21659512; DOI=10.1074/jbc.M111.218214;
Scortegagna M., Subtil T., Qi J., Kim H., Zhao W., Gu W., Kluger H.,
Ronai Z.A.;
"USP13 enzyme regulates Siah2 ligase stability and activity via
noncatalytic ubiquitin-binding domains.";
J. Biol. Chem. 286:27333-27341(2011).
[12]
FUNCTION, AND MUTAGENESIS OF CYS-345.
PubMed=21811243; DOI=10.1038/ncomms1421;
Zhao X., Fiske B., Kawakami A., Li J., Fisher D.E.;
"Regulation of MITF stability by the USP13 deubiquitinase.";
Nat. Commun. 2:414-414(2011).
[13]
FUNCTION, AND INTERACTION WITH UFD1.
PubMed=21571647; DOI=10.1073/pnas.1100028108;
Chen M., Gutierrez G.J., Ronai Z.A.;
"Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum
(ER) stress response to cell cycle control.";
Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
FUNCTION, AND INTERACTION WITH AMFR; BAG6 AND UBL4A.
PubMed=24424410; DOI=10.7554/eLife.01369;
Liu Y., Soetandyo N., Lee J.G., Liu L., Xu Y., Clemons W.M. Jr.,
Ye Y.;
"USP13 antagonizes gp78 to maintain functionality of a chaperone in
ER-associated degradation.";
Elife 3:E01369-E01369(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-311 AND LYS-405, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
STRUCTURE BY NMR OF 188-301 AND 652-777, FUNCTION, DOMAIN, AND
UBIQUITIN-BINDING.
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).
-!- FUNCTION: Deubiquitinase that mediates deubiquitination of target
proteins such as BECN1, MITF, SKP2 and USP10 and is involved in
various processes such as autophagy and endoplasmic reticulum-
associated degradation (ERAD). Component of a regulatory loop that
controls autophagy and p53/TP53 levels: mediates deubiquitination
of BECN1, a key regulator of autophagy, leading to stabilize the
PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an
essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-
containing complexes regulate USP13 stability, suggesting the
existence of a regulatory system by which PIK3C3/VPS34-containing
complexes regulate p53/TP53 protein levels via USP10 and USP13.
Recruited by nuclear UFD1 and mediates deubiquitination of SKP2,
thereby regulating endoplasmic reticulum-associated degradation
(ERAD). Also regulates ERAD through the deubiquitination of UBL4A
a component of the BAG6/BAT3 complex. Mediates stabilization of
SIAH2 independently of deubiquitinase activity: binds
ubiquitinated SIAH2 and acts by impairing SIAH2
autoubiquitination. Has a weak deubiquitinase activity in vitro
and preferentially cleaves 'Lys-63'-linked polyubiquitin chains.
In contrast to USP5, it is not able to mediate unanchored
polyubiquitin disassembly. Able to cleave ISG15 in vitro; however,
additional experiments are required to confirm such data.
{ECO:0000269|PubMed:17653289, ECO:0000269|PubMed:21571647,
ECO:0000269|PubMed:21659512, ECO:0000269|PubMed:21811243,
ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:22216260,
ECO:0000269|PubMed:24424410}.
-!- 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).
-!- ENZYME REGULATION: Specifically inhibited by spautin-1 (specific
and potent autophagy inhibitor-1), a derivative of MBCQ that binds
to USP13 and inhibits deubiquitinase activity. Regulated by
PIK3C3/VPS34-containing complexes. The weak deubiquitinase
activity in vitro suggests the existence of some mechanism that
activates the enzyme. {ECO:0000269|PubMed:21962518}.
-!- SUBUNIT: Interacts with UFD1. Interacts (via UBA domains) with
SIAH2 (when ubiquitinated). Interacts with BAG6; the interaction
is direct and may mediate UBL4A deubiquitination
(PubMed:24424410). Interacts (via UBA 2 domain) with AMFR; the
interaction is direct (PubMed:24424410). Interacts with UBL4A; may
be indirect via BAG6 (PubMed:24424410).
{ECO:0000269|PubMed:21571647, ECO:0000269|PubMed:21659512,
ECO:0000269|PubMed:24424410}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92995-1; Sequence=Displayed;
Name=2;
IsoId=Q92995-2; Sequence=VSP_043954;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in ovary and testes.
-!- DOMAIN: The UBP-type zinc finger has lost its ability to bind
ubiquitin and USP13 is not activated by unanchored ubiquitin.
Swapping with the UBP-type zinc finger from USP5 restores ability
to bind unanchored ubiquitin and subsequent activation of the
protein (PubMed:22216260). {ECO:0000269|PubMed:22216260}.
-!- DOMAIN: The UBA domains mediate binding to ubiquitin.
{ECO:0000269|PubMed:22216260}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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EMBL; U75362; AAC63405.1; -; mRNA.
EMBL; AK290338; BAF83027.1; -; mRNA.
EMBL; AK302404; BAG63715.1; -; mRNA.
EMBL; AC007687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC125604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78383.1; -; Genomic_DNA.
EMBL; CH471052; EAW78384.1; -; Genomic_DNA.
EMBL; BC016146; AAH16146.1; -; mRNA.
CCDS; CCDS3235.1; -. [Q92995-1]
RefSeq; NP_003931.2; NM_003940.2. [Q92995-1]
UniGene; Hs.175322; -.
PDB; 2L80; NMR; -; A=188-301.
PDB; 2LBC; NMR; -; A=652-777.
PDBsum; 2L80; -.
PDBsum; 2LBC; -.
ProteinModelPortal; Q92995; -.
SMR; Q92995; -.
BioGrid; 114465; 53.
DIP; DIP-53511N; -.
IntAct; Q92995; 31.
MINT; MINT-1195142; -.
STRING; 9606.ENSP00000263966; -.
BindingDB; Q92995; -.
ChEMBL; CHEMBL3407324; -.
MEROPS; C19.012; -.
iPTMnet; Q92995; -.
PhosphoSitePlus; Q92995; -.
BioMuta; USP13; -.
DMDM; 209572692; -.
EPD; Q92995; -.
MaxQB; Q92995; -.
PaxDb; Q92995; -.
PeptideAtlas; Q92995; -.
PRIDE; Q92995; -.
DNASU; 8975; -.
Ensembl; ENST00000263966; ENSP00000263966; ENSG00000058056. [Q92995-1]
Ensembl; ENST00000496897; ENSP00000417146; ENSG00000058056. [Q92995-2]
GeneID; 8975; -.
KEGG; hsa:8975; -.
UCSC; uc003fkh.4; human. [Q92995-1]
CTD; 8975; -.
DisGeNET; 8975; -.
EuPathDB; HostDB:ENSG00000058056.8; -.
GeneCards; USP13; -.
H-InvDB; HIX0003883; -.
HGNC; HGNC:12611; USP13.
HPA; HPA004827; -.
MIM; 603591; gene.
neXtProt; NX_Q92995; -.
OpenTargets; ENSG00000058056; -.
PharmGKB; PA37237; -.
eggNOG; KOG0944; Eukaryota.
eggNOG; COG5207; LUCA.
GeneTree; ENSGT00390000000874; -.
HOGENOM; HOG000162311; -.
HOVERGEN; HBG002833; -.
InParanoid; Q92995; -.
KO; K11836; -.
OMA; MKEEHKP; -.
OrthoDB; EOG091G01W3; -.
PhylomeDB; Q92995; -.
TreeFam; TF300576; -.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
ChiTaRS; USP13; human.
GeneWiki; USP13; -.
GenomeRNAi; 8975; -.
PRO; PR:Q92995; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000058056; -.
CleanEx; HS_USP13; -.
ExpressionAtlas; Q92995; baseline and differential.
Genevisible; Q92995; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:1904288; F:BAT3 complex binding; IDA:ParkinsonsUK-UCL.
GO; GO:0051087; F:chaperone binding; IPI:ParkinsonsUK-UCL.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:ParkinsonsUK-UCL.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:1904454; F:ubiquitin-specific protease activity involved in positive regulation of ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0030318; P:melanocyte differentiation; TAS:UniProtKB.
GO; GO:1904294; P:positive regulation of ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0035523; P:protein K29-linked deubiquitination; IDA:MGI.
GO; GO:0044313; P:protein K6-linked deubiquitination; IDA:MGI.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like.
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.
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; Alternative splicing; Autophagy; Complete proteome;
Hydrolase; Isopeptide bond; Metal-binding; Phosphoprotein; Protease;
Reference proteome; Repeat; Thiol protease; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 863 Ubiquitin carboxyl-terminal hydrolase 13.
/FTId=PRO_0000080635.
DOMAIN 336 861 USP.
DOMAIN 652 693 UBA 1. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 727 767 UBA 2. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
ZN_FING 209 281 UBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00502}.
ACT_SITE 345 345 Nucleophile. {ECO:0000305}.
ACT_SITE 823 823 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
CROSSLNK 311 311 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 405 405 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 65 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043954.
MUTAGEN 221 221 W->A: Does not abolish ability to
stabilize SIAH2.
{ECO:0000269|PubMed:21659512}.
MUTAGEN 233 233 K->A: Does not abolish ability to
stabilize SIAH2.
{ECO:0000269|PubMed:21659512}.
MUTAGEN 273 273 F->A: Impairs ability to stabilize SIAH2.
{ECO:0000269|PubMed:21659512}.
MUTAGEN 345 345 C->A: Abolishes deubiquitinating
activity. Does not abolish ability to
stabilize SIAH2. Does not abolish ability
to stabilize SIAH2; when associated with
A-814 and A-823.
{ECO:0000269|PubMed:21659512,
ECO:0000269|PubMed:21811243}.
MUTAGEN 664 664 M->E: Impairs ability to stabilize SIAH2.
Abolishes ability to stabilize SIAH2;
when associated with E-739.
{ECO:0000269|PubMed:21659512}.
MUTAGEN 739 739 M->E: Impairs ability to stabilize SIAH2.
Abolishes ability to stabilize SIAH2;
when associated with E-664.
{ECO:0000269|PubMed:21659512}.
MUTAGEN 814 814 H->A: Does not abolish ability to
stabilize SIAH2; when associated with A-
345 and A-823.
{ECO:0000269|PubMed:21659512}.
MUTAGEN 823 823 H->A: Does not abolish ability to
stabilize SIAH2; when associated with A-
345 and A-814.
{ECO:0000269|PubMed:21659512}.
CONFLICT 96 96 V -> A (in Ref. 1; AAC63405).
{ECO:0000305}.
CONFLICT 293 293 I -> V (in Ref. 2; BAF83027).
{ECO:0000305}.
CONFLICT 305 305 L -> F (in Ref. 2; BAF83027).
{ECO:0000305}.
CONFLICT 325 325 T -> A (in Ref. 2; BAF83027).
{ECO:0000305}.
CONFLICT 338 338 L -> P (in Ref. 2; BAF83027).
{ECO:0000305}.
TURN 191 194 {ECO:0000244|PDB:2L80}.
STRAND 212 214 {ECO:0000244|PDB:2L80}.
STRAND 217 223 {ECO:0000244|PDB:2L80}.
TURN 224 226 {ECO:0000244|PDB:2L80}.
STRAND 229 231 {ECO:0000244|PDB:2L80}.
HELIX 244 251 {ECO:0000244|PDB:2L80}.
STRAND 256 260 {ECO:0000244|PDB:2L80}.
STRAND 269 272 {ECO:0000244|PDB:2L80}.
TURN 273 275 {ECO:0000244|PDB:2L80}.
STRAND 277 279 {ECO:0000244|PDB:2L80}.
HELIX 284 290 {ECO:0000244|PDB:2L80}.
HELIX 296 299 {ECO:0000244|PDB:2L80}.
HELIX 656 662 {ECO:0000244|PDB:2LBC}.
HELIX 669 678 {ECO:0000244|PDB:2LBC}.
HELIX 683 692 {ECO:0000244|PDB:2LBC}.
HELIX 693 695 {ECO:0000244|PDB:2LBC}.
STRAND 697 700 {ECO:0000244|PDB:2LBC}.
STRAND 710 714 {ECO:0000244|PDB:2LBC}.
HELIX 730 739 {ECO:0000244|PDB:2LBC}.
HELIX 743 753 {ECO:0000244|PDB:2LBC}.
HELIX 757 765 {ECO:0000244|PDB:2LBC}.
SEQUENCE 863 AA; 97327 MW; 988713ADF8C0B938 CRC64;
MQRRGALFGM PGGSGGRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA FSYDSPNSEG
GLYVCMNTFL AFGREHVERH FRKTGQSVYM HLKRHVREKV RGASGGALPK RRNSKIFLDL
DTDDDLNSDD YEYEDEAKLV IFPDHYEIAL PNIEELPALV TIACDAVLSS KSPYRKQDPD
TWENELPVSK YANNLTQLDN GVRIPPSGWK CARCDLRENL WLNLTDGSVL CGKWFFDSSG
GNGHALEHYR DMGYPLAVKL GTITPDGADV YSFQEEEPVL DPHLAKHLAH FGIDMLHMHG
TENGLQDNDI KLRVSEWEVI QESGTKLKPM YGPGYTGLKN LGNSCYLSSV MQAIFSIPEF
QRAYVGNLPR IFDYSPLDPT QDFNTQMTKL GHGLLSGQYS KPPVKSELIE QVMKEEHKPQ
QNGISPRMFK AFVSKSHPEF SSNRQQDAQE FFLHLVNLVE RNRIGSENPS DVFRFLVEER
IQCCQTRKVR YTERVDYLMQ LPVAMEAATN KDELIAYELT RREAEANRRP LPELVRAKIP
FSACLQAFSE PENVDDFWSS ALQAKSAGVK TSRFASFPEY LVVQIKKFTF GLDWVPKKFD
VSIDMPDLLD INHLRARGLQ PGEEELPDIS PPIVIPDDSK DRLMNQLIDP SDIDESSVMQ
LAEMGFPLEA CRKAVYFTGN MGAEVAFNWI IVHMEEPDFA EPLTMPGYGG AASAGASVFG
ASGLDNQPPE EIVAIITSMG FQRNQAIQAL RATNNNLERA LDWIFSHPEF EEDSDFVIEM
ENNANANIIS EAKPEGPRVK DGSGTYELFA FISHMGTSTM SGHYICHIKK EGRWVIYNDH
KVCASERPPK DLGYMYFYRR IPS


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