ID ZRAN1_HUMAN Reviewed; 708 AA.
AC Q9UGI0; B4DZ98; D3DRF4; Q5SQP6; Q69YK3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Ubiquitin thioesterase ZRANB1 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:33637724};
DE AltName: Full=TRAF-binding domain-containing protein {ECO:0000303|PubMed:11463333};
DE Short=hTrabid {ECO:0000303|PubMed:11463333};
DE AltName: Full=Zinc finger Ran-binding domain-containing protein 1 {ECO:0000303|PubMed:21834987};
GN Name=ZRANB1 {ECO:0000303|PubMed:21834987, ECO:0000312|HGNC:HGNC:18224};
GN Synonyms=TRABID {ECO:0000303|PubMed:11463333};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH TRAF6.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=11463333; DOI=10.1042/0264-6021:3570617;
RA Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R.,
RA Kilshaw P.J.;
RT "Isolation and characterization of two novel A20-like proteins.";
RL Biochem. J. 357:617-623(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] OF 151-708.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APC, DOMAIN, AND
RP MUTAGENESIS OF CYS-10; 14-THR-TYR-15; CYS-90; 94-THR-TYR-95; CYS-155;
RP 159-THR-TYR-160 AND CYS-443.
RX PubMed=18281465; DOI=10.1101/gad.463208;
RA Tran H., Hamada F., Schwarz-Romond T., Bienz M.;
RT "Trabid, a new positive regulator of Wnt-induced transcription with
RT preference for binding and cleaving K63-linked ubiquitin chains.";
RL Genes Dev. 22:528-542(2008).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M.,
RA Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and enable
RT ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF TYR-12; THR-14;
RP TYR-14; GLU-16; THR-25; MET-26 AND CYS-443.
RX PubMed=25752573; DOI=10.1016/j.molcel.2015.01.041;
RA Kristariyanto Y.A., Abdul Rehman S.A., Campbell D.G., Morrice N.A.,
RA Johnson C., Toth R., Kulathu Y.;
RT "K29-selective ubiquitin binding domain reveals structural basis of
RT specificity and heterotypic nature of K29 polyubiquitin.";
RL Mol. Cell 58:83-94(2015).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33637724; DOI=10.1038/s41467-021-21715-1;
RA Chen Y.H., Huang T.Y., Lin Y.T., Lin S.Y., Li W.H., Hsiao H.J., Yan R.L.,
RA Tang H.W., Shen Z.Q., Chen G.C., Wu K.P., Tsai T.F., Chen R.H.;
RT "VPS34 K29/K48 branched ubiquitination governed by UBE3C and TRABID
RT regulates autophagy, proteostasis and liver metabolism.";
RL Nat. Commun. 12:1322-1322(2021).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 245-697, FUNCTION, LINKAGE
RP SPECIFICITY, ACTIVE SITE, AND DOMAIN ANK REPEATS.
RX PubMed=22157957; DOI=10.1038/nsmb.2169;
RA Licchesi J.D., Mieszczanek J., Mevissen T.E., Rutherford T.J., Akutsu M.,
RA Virdee S., El Oualid F., Chin J.W., Ovaa H., Bienz M., Komander D.;
RT "An ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity
RT for atypical ubiquitin chains.";
RL Nat. Struct. Mol. Biol. 19:62-71(2012).
RN [12] {ECO:0007744|PDB:5AF6}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 1-33 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
RP OF TYR-15; TRP-18; SER-20; THR-25 AND CYS-443.
RX PubMed=25752577; DOI=10.1016/j.molcel.2015.01.042;
RA Michel M.A., Elliott P.R., Swatek K.N., Simicek M., Pruneda J.N.,
RA Wagstaff J.L., Freund S.M., Komander D.;
RT "Assembly and specific recognition of K29- and K33-linked polyubiquitin.";
RL Mol. Cell 58:95-109(2015).
CC -!- FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-
CC 29'-linked and 'Lys-33'-linked diubiquitin (PubMed:22157957,
CC PubMed:23827681, PubMed:25752573, PubMed:25752577). Also cleaves 'Lys-
CC 63'-linked chains, but with 40-fold less efficiency compared to 'Lys-
CC 29'-linked ones (PubMed:18281465). Positive regulator of the Wnt
CC signaling pathway that deubiquitinates APC protein, a negative
CC regulator of Wnt-mediated transcription (PubMed:18281465). Acts as a
CC regulator of autophagy by mediating deubiquitination of PIK3C3/VPS34,
CC thereby promoting autophagosome maturation (PubMed:33637724). Plays a
CC role in the regulation of cell morphology and cytoskeletal organization
CC (PubMed:21834987). Required in the stress fiber dynamics and cell
CC migration (PubMed:21834987). {ECO:0000269|PubMed:18281465,
CC ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:22157957,
CC ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:25752573,
CC ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:33637724}.
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:23827681,
CC ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577,
CC ECO:0000269|PubMed:33637724};
CC -!- SUBUNIT: Interacts with TRAF6 (PubMed:11463333). Interacts with APC
CC (PubMed:18281465). {ECO:0000269|PubMed:11463333,
CC ECO:0000269|PubMed:18281465}.
CC -!- INTERACTION:
CC Q9UGI0; X5D778: ANKRD11; NbExp=3; IntAct=EBI-527853, EBI-17183751;
CC Q9UGI0; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-527853, EBI-541426;
CC Q9UGI0; Q12774: ARHGEF5; NbExp=3; IntAct=EBI-527853, EBI-602199;
CC Q9UGI0; Q8TBH0: ARRDC2; NbExp=3; IntAct=EBI-527853, EBI-12191751;
CC Q9UGI0; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-527853, EBI-2875665;
CC Q9UGI0; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-527853, EBI-745689;
CC Q9UGI0; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-527853, EBI-742750;
CC Q9UGI0; O95696: BRD1; NbExp=3; IntAct=EBI-527853, EBI-714754;
CC Q9UGI0; Q13895: BYSL; NbExp=3; IntAct=EBI-527853, EBI-358049;
CC Q9UGI0; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-527853, EBI-11530605;
CC Q9UGI0; O95931: CBX7; NbExp=3; IntAct=EBI-527853, EBI-3923843;
CC Q9UGI0; Q9HC52: CBX8; NbExp=3; IntAct=EBI-527853, EBI-712912;
CC Q9UGI0; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-527853, EBI-744556;
CC Q9UGI0; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-527853, EBI-10961312;
CC Q9UGI0; Q8N715: CCDC185; NbExp=3; IntAct=EBI-527853, EBI-740814;
CC Q9UGI0; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-527853, EBI-2836773;
CC Q9UGI0; O75419: CDC45; NbExp=3; IntAct=EBI-527853, EBI-374969;
CC Q9UGI0; Q99459: CDC5L; NbExp=3; IntAct=EBI-527853, EBI-374880;
CC Q9UGI0; Q07002: CDK18; NbExp=3; IntAct=EBI-527853, EBI-746238;
CC Q9UGI0; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-527853, EBI-3919850;
CC Q9UGI0; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-527853, EBI-741032;
CC Q9UGI0; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-527853, EBI-12012272;
CC Q9UGI0; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-527853, EBI-5453285;
CC Q9UGI0; O43602-2: DCX; NbExp=3; IntAct=EBI-527853, EBI-14148644;
CC Q9UGI0; P26196: DDX6; NbExp=3; IntAct=EBI-527853, EBI-351257;
CC Q9UGI0; P59910: DNAJB13; NbExp=3; IntAct=EBI-527853, EBI-11514233;
CC Q9UGI0; O60941-5: DTNB; NbExp=3; IntAct=EBI-527853, EBI-11984733;
CC Q9UGI0; Q9UII6: DUSP13B; NbExp=3; IntAct=EBI-527853, EBI-749800;
CC Q9UGI0; Q08426: EHHADH; NbExp=3; IntAct=EBI-527853, EBI-2339219;
CC Q9UGI0; O15371: EIF3D; NbExp=3; IntAct=EBI-527853, EBI-353818;
CC Q9UGI0; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-527853, EBI-744099;
CC Q9UGI0; P50548: ERF; NbExp=3; IntAct=EBI-527853, EBI-8465203;
CC Q9UGI0; Q9NVQ4-2: FAIM; NbExp=3; IntAct=EBI-527853, EBI-12039347;
CC Q9UGI0; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-527853, EBI-11986315;
CC Q9UGI0; Q3B820: FAM161A; NbExp=3; IntAct=EBI-527853, EBI-719941;
CC Q9UGI0; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-527853, EBI-7225287;
CC Q9UGI0; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-527853, EBI-742802;
CC Q9UGI0; O95363: FARS2; NbExp=3; IntAct=EBI-527853, EBI-2513774;
CC Q9UGI0; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-527853, EBI-744935;
CC Q9UGI0; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-527853, EBI-372506;
CC Q9UGI0; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-527853, EBI-7960826;
CC Q9UGI0; P55040: GEM; NbExp=3; IntAct=EBI-527853, EBI-744104;
CC Q9UGI0; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-527853, EBI-7251368;
CC Q9UGI0; O95872: GPANK1; NbExp=3; IntAct=EBI-527853, EBI-751540;
CC Q9UGI0; Q92917: GPKOW; NbExp=3; IntAct=EBI-527853, EBI-746309;
CC Q9UGI0; P09067: HOXB5; NbExp=3; IntAct=EBI-527853, EBI-3893317;
CC Q9UGI0; P31273: HOXC8; NbExp=3; IntAct=EBI-527853, EBI-1752118;
CC Q9UGI0; Q14005-2: IL16; NbExp=3; IntAct=EBI-527853, EBI-17178971;
CC Q9UGI0; Q9C086: INO80B; NbExp=3; IntAct=EBI-527853, EBI-715611;
CC Q9UGI0; Q96PC2: IP6K3; NbExp=3; IntAct=EBI-527853, EBI-10990676;
CC Q9UGI0; Q8NA54: IQUB; NbExp=3; IntAct=EBI-527853, EBI-10220600;
CC Q9UGI0; O75564-2: JRK; NbExp=3; IntAct=EBI-527853, EBI-17181882;
CC Q9UGI0; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-527853, EBI-2556193;
CC Q9UGI0; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-527853, EBI-8472129;
CC Q9UGI0; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-527853, EBI-14069005;
CC Q9UGI0; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-527853, EBI-726510;
CC Q9UGI0; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-527853, EBI-11742507;
CC Q9UGI0; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-527853, EBI-739832;
CC Q9UGI0; O15481: MAGEB4; NbExp=3; IntAct=EBI-527853, EBI-751857;
CC Q9UGI0; P61326: MAGOH; NbExp=3; IntAct=EBI-527853, EBI-299134;
CC Q9UGI0; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-527853, EBI-348259;
CC Q9UGI0; P53582: METAP1; NbExp=4; IntAct=EBI-527853, EBI-1051435;
CC Q9UGI0; Q8WXB1: METTL21A; NbExp=3; IntAct=EBI-527853, EBI-8652459;
CC Q9UGI0; P55081: MFAP1; NbExp=3; IntAct=EBI-527853, EBI-1048159;
CC Q9UGI0; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-527853, EBI-14086479;
CC Q9UGI0; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-527853, EBI-10172526;
CC Q9UGI0; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-527853, EBI-742459;
CC Q9UGI0; O15442-2: MPPED1; NbExp=3; IntAct=EBI-527853, EBI-12183511;
CC Q9UGI0; Q9P2K5-2: MYEF2; NbExp=3; IntAct=EBI-527853, EBI-10318831;
CC Q9UGI0; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-527853, EBI-11750983;
CC Q9UGI0; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-527853, EBI-2949792;
CC Q9UGI0; O43809: NUDT21; NbExp=3; IntAct=EBI-527853, EBI-355720;
CC Q9UGI0; P30039: PBLD; NbExp=4; IntAct=EBI-527853, EBI-750589;
CC Q9UGI0; O43189: PHF1; NbExp=3; IntAct=EBI-527853, EBI-530034;
CC Q9UGI0; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-527853, EBI-2339674;
CC Q9UGI0; Q16512: PKN1; NbExp=3; IntAct=EBI-527853, EBI-602382;
CC Q9UGI0; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-527853, EBI-12014286;
CC Q9UGI0; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-527853, EBI-10171633;
CC Q9UGI0; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-527853, EBI-10276663;
CC Q9UGI0; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-527853, EBI-10320765;
CC Q9UGI0; O15160: POLR1C; NbExp=3; IntAct=EBI-527853, EBI-1055079;
CC Q9UGI0; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-527853, EBI-2557469;
CC Q9UGI0; Q99633: PRPF18; NbExp=3; IntAct=EBI-527853, EBI-2798416;
CC Q9UGI0; O43395: PRPF3; NbExp=3; IntAct=EBI-527853, EBI-744322;
CC Q9UGI0; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-527853, EBI-1567797;
CC Q9UGI0; Q8WXF1-2: PSPC1; NbExp=3; IntAct=EBI-527853, EBI-12135327;
CC Q9UGI0; P47897: QARS1; NbExp=3; IntAct=EBI-527853, EBI-347462;
CC Q9UGI0; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-527853, EBI-3437896;
CC Q9UGI0; O94955: RHOBTB3; NbExp=3; IntAct=EBI-527853, EBI-2367123;
CC Q9UGI0; Q15287: RNPS1; NbExp=3; IntAct=EBI-527853, EBI-395959;
CC Q9UGI0; O00560: SDCBP; NbExp=3; IntAct=EBI-527853, EBI-727004;
CC Q9UGI0; Q96FJ0: STAMBPL1; NbExp=3; IntAct=EBI-527853, EBI-745021;
CC Q9UGI0; B7ZLI8: STK19; NbExp=3; IntAct=EBI-527853, EBI-10176124;
CC Q9UGI0; O43463: SUV39H1; NbExp=3; IntAct=EBI-527853, EBI-349968;
CC Q9UGI0; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-527853, EBI-745392;
CC Q9UGI0; Q96C24: SYTL4; NbExp=3; IntAct=EBI-527853, EBI-747142;
CC Q9UGI0; Q9Y2I9-2: TBC1D30; NbExp=3; IntAct=EBI-527853, EBI-17455779;
CC Q9UGI0; A6NER0: TBC1D3F; NbExp=3; IntAct=EBI-527853, EBI-18393978;
CC Q9UGI0; Q6DHY5: TBC1D3G; NbExp=6; IntAct=EBI-527853, EBI-13092532;
CC Q9UGI0; Q15560: TCEA2; NbExp=3; IntAct=EBI-527853, EBI-710310;
CC Q9UGI0; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-527853, EBI-11955057;
CC Q9UGI0; Q9BT49: THAP7; NbExp=3; IntAct=EBI-527853, EBI-741350;
CC Q9UGI0; P35590: TIE1; NbExp=3; IntAct=EBI-527853, EBI-2256865;
CC Q9UGI0; Q08117-2: TLE5; NbExp=3; IntAct=EBI-527853, EBI-11741437;
CC Q9UGI0; Q8IZW8: TNS4; NbExp=3; IntAct=EBI-527853, EBI-7543499;
CC Q9UGI0; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-527853, EBI-74615;
CC Q9UGI0; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-527853, EBI-765817;
CC Q9UGI0; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-527853, EBI-3650647;
CC Q9UGI0; Q9Y4K3: TRAF6; NbExp=4; IntAct=EBI-527853, EBI-359276;
CC Q9UGI0; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-527853, EBI-11961968;
CC Q9UGI0; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-527853, EBI-10241197;
CC Q9UGI0; Q9UJ04: TSPYL4; NbExp=3; IntAct=EBI-527853, EBI-308511;
CC Q9UGI0; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-527853, EBI-8994397;
CC Q9UGI0; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-527853, EBI-7353612;
CC Q9UGI0; P0CG48: UBC; NbExp=2; IntAct=EBI-527853, EBI-3390054;
CC Q9UGI0; O75604: USP2; NbExp=3; IntAct=EBI-527853, EBI-743272;
CC Q9UGI0; Q9UKW4: VAV3; NbExp=3; IntAct=EBI-527853, EBI-297568;
CC Q9UGI0; Q14119: VEZF1; NbExp=3; IntAct=EBI-527853, EBI-11980193;
CC Q9UGI0; P19544-6: WT1; NbExp=3; IntAct=EBI-527853, EBI-11745701;
CC Q9UGI0; P13010: XRCC5; NbExp=3; IntAct=EBI-527853, EBI-357997;
CC Q9UGI0; O43167: ZBTB24; NbExp=3; IntAct=EBI-527853, EBI-744471;
CC Q9UGI0; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-527853, EBI-7781767;
CC Q9UGI0; Q15973: ZNF124; NbExp=3; IntAct=EBI-527853, EBI-2555767;
CC Q9UGI0; P17021: ZNF17; NbExp=3; IntAct=EBI-527853, EBI-1105334;
CC Q9UGI0; P15622-3: ZNF250; NbExp=3; IntAct=EBI-527853, EBI-10177272;
CC Q9UGI0; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-527853, EBI-347633;
CC Q9UGI0; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-527853, EBI-740727;
CC Q9UGI0; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-527853, EBI-11962468;
CC Q9UGI0; Q9ULM2: ZNF490; NbExp=3; IntAct=EBI-527853, EBI-1105370;
CC Q9UGI0; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-527853, EBI-10486136;
CC Q9UGI0; Q9H707: ZNF552; NbExp=3; IntAct=EBI-527853, EBI-2555731;
CC Q9UGI0; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-527853, EBI-14069183;
CC Q9UGI0; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-527853, EBI-745520;
CC Q9UGI0; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-527853, EBI-6427977;
CC Q9UGI0; Q96NL3: ZNF599; NbExp=3; IntAct=EBI-527853, EBI-8653994;
CC Q9UGI0; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-527853, EBI-9977294;
CC Q9UGI0; Q5T619: ZNF648; NbExp=3; IntAct=EBI-527853, EBI-11985915;
CC Q9UGI0; Q96H86: ZNF764; NbExp=3; IntAct=EBI-527853, EBI-745775;
CC Q9UGI0; Q96BV0: ZNF775; NbExp=3; IntAct=EBI-527853, EBI-7149881;
CC Q9UGI0; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-527853, EBI-10240849;
CC Q9UGI0; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-527853, EBI-11962574;
CC Q9UGI0; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-527853, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18281465,
CC ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:25752577}. Nucleus
CC {ECO:0000269|PubMed:11463333, ECO:0000269|PubMed:18281465,
CC ECO:0000269|PubMed:25752577}. Note=Enriched in punctate localization in
CC the cytoplasm. {ECO:0000269|PubMed:18281465,
CC ECO:0000269|PubMed:25752577}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11463333}.
CC -!- DOMAIN: The RanBP2-type zinc fingers, also called NZFs, mediate the
CC interaction with ubiquitin and determine linkage specificity
CC (PubMed:25752577). RanBP2-type zinc fingers 1 and 2 (also named NZF1
CC and NZF2) specifically recognize and bind 'Lys-29'- and 'Lys-33'-linked
CC ubiquitin (PubMed:25752573, PubMed:25752577). RanBP2-type zinc finger 3
CC (also named NZF3) binds 'Lys-33'-linked ubiquitin and shows weak
CC binding to 'Lys-6'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin chains but
CC it does not interact with 'Lys-29'-linked chains (PubMed:25752573).
CC {ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577}.
CC -!- DOMAIN: The OTU domain mediates the deubiquitinating activity.
CC {ECO:0000269|PubMed:18281465, ECO:0000269|PubMed:22157957}.
CC -!- DOMAIN: The second ankyrin repeat ANK 2 is termed AnkUBD, it interacts
CC with ubiquitin hydrophobic patch and contributes to linkage
CC specificity. {ECO:0000269|PubMed:22157957}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG64010.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ252060; CAB64449.1; -; mRNA.
DR EMBL; AK302810; BAG64010.1; ALT_INIT; mRNA.
DR EMBL; AL731577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49252.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49253.1; -; Genomic_DNA.
DR EMBL; AL832925; CAH10620.1; -; mRNA.
DR CCDS; CCDS7642.1; -.
DR RefSeq; NP_060050.2; NM_017580.2.
DR RefSeq; XP_005269983.1; XM_005269926.4.
DR RefSeq; XP_016871846.1; XM_017016357.1.
DR PDB; 3ZRH; X-ray; 2.23 A; A=245-697.
DR PDB; 5AF6; X-ray; 3.40 A; F/G/H/I/J=1-33.
DR PDBsum; 3ZRH; -.
DR PDBsum; 5AF6; -.
DR AlphaFoldDB; Q9UGI0; -.
DR SMR; Q9UGI0; -.
DR BioGRID; 120139; 4160.
DR DIP; DIP-33806N; -.
DR IntAct; Q9UGI0; 168.
DR MINT; Q9UGI0; -.
DR STRING; 9606.ENSP00000352676; -.
DR MEROPS; C64.004; -.
DR iPTMnet; Q9UGI0; -.
DR PhosphoSitePlus; Q9UGI0; -.
DR BioMuta; ZRANB1; -.
DR DMDM; 212276487; -.
DR EPD; Q9UGI0; -.
DR jPOST; Q9UGI0; -.
DR MassIVE; Q9UGI0; -.
DR MaxQB; Q9UGI0; -.
DR PaxDb; 9606-ENSP00000352676; -.
DR PeptideAtlas; Q9UGI0; -.
DR ProteomicsDB; 84215; -.
DR Antibodypedia; 35158; 185 antibodies from 27 providers.
DR DNASU; 54764; -.
DR Ensembl; ENST00000359653.4; ENSP00000352676.4; ENSG00000019995.6.
DR GeneID; 54764; -.
DR KEGG; hsa:54764; -.
DR MANE-Select; ENST00000359653.4; ENSP00000352676.4; NM_017580.3; NP_060050.2.
DR UCSC; uc001lic.4; human.
DR AGR; HGNC:18224; -.
DR CTD; 54764; -.
DR DisGeNET; 54764; -.
DR GeneCards; ZRANB1; -.
DR HGNC; HGNC:18224; ZRANB1.
DR HPA; ENSG00000019995; Low tissue specificity.
DR MIM; 611749; gene.
DR neXtProt; NX_Q9UGI0; -.
DR OpenTargets; ENSG00000019995; -.
DR PharmGKB; PA134933584; -.
DR VEuPathDB; HostDB:ENSG00000019995; -.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158045; -.
DR HOGENOM; CLU_013907_0_0_1; -.
DR InParanoid; Q9UGI0; -.
DR OMA; MCDTKDD; -.
DR OrthoDB; 2909231at2759; -.
DR PhylomeDB; Q9UGI0; -.
DR TreeFam; TF323312; -.
DR PathwayCommons; Q9UGI0; -.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR SignaLink; Q9UGI0; -.
DR SIGNOR; Q9UGI0; -.
DR BioGRID-ORCS; 54764; 38 hits in 1200 CRISPR screens.
DR ChiTaRS; ZRANB1; human.
DR GenomeRNAi; 54764; -.
DR Pharos; Q9UGI0; Tbio.
DR PRO; PR:Q9UGI0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9UGI0; Protein.
DR Bgee; ENSG00000019995; Expressed in tibialis anterior and 191 other cell types or tissues.
DR Genevisible; Q9UGI0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0101005; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0035523; P:protein K29-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990168; P:protein K33-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd22767; OTU_ZRANB1; 1.
DR Gene3D; 1.25.40.560; -; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3.
DR InterPro; IPR041294; AnkUBD.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR049768; ZRANB1_OTU.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR PANTHER; PTHR13367:SF28; UBIQUITIN THIOESTERASE ZRANB1; 1.
DR Pfam; PF18418; AnkUBD; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00547; ZnF_RBZ; 3.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..708
FT /note="Ubiquitin thioesterase ZRANB1"
FT /id="PRO_0000065595"
FT REPEAT 260..290
FT /note="ANK 1"
FT REPEAT 313..340
FT /note="ANK 2"
FT DOMAIN 432..592
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ZN_FING 3..33
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 84..113
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 149..178
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 38..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..641
FT /note="TRAF-binding"
FT /evidence="ECO:0000269|PubMed:11463333"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 443
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:22157957"
FT ACT_SITE 585
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6GQQ9"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322,
FT ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322,
FT ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322,
FT ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322,
FT ECO:0000269|PubMed:25752577, ECO:0007744|PDB:5AF6"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT MUTAGEN 10
FT /note="C->A: Abolishes the binding to ubiquitin chains but
FT not the deubiquitinating activity; when associated with 14-
FT LV-15; A-90; 94-LV-95; A-155 and 159-LV-160."
FT /evidence="ECO:0000269|PubMed:18281465"
FT MUTAGEN 12
FT /note="Y->A: Does not affect binding to 'Lys-29'- and 'Lys-
FT 33'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:25752573"
FT MUTAGEN 14..15
FT /note="TY->LV: Abolishes the binding to ubiquitin chains
FT but not the deubiquitinating activity; when associated with
FT A-10; A-90; 94-LV-95; A-155 and 159-LV-160."
FT /evidence="ECO:0000269|PubMed:18281465"
FT MUTAGEN 14
FT /note="T->A: Abolished binding to 'Lys-29'- and 'Lys-33'-
FT linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:25752573"
FT MUTAGEN 15
FT /note="Y->F: Strongly reduced binding to 'Lys-29'- and
FT 'Lys-33'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:25752573,
FT ECO:0000269|PubMed:25752577"
FT MUTAGEN 16
FT /note="E->A: Does not affect binding to 'Lys-29'- and 'Lys-
FT 33'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:25752573"
FT MUTAGEN 18
FT /note="W->A: Abolished binding to 'Lys-33'-linked
FT diubiquitin."
FT /evidence="ECO:0000269|PubMed:25752577"
FT MUTAGEN 20
FT /note="S->R: Strongly reduced binding to 'Lys-33'-linked
FT diubiquitin."
FT /evidence="ECO:0000269|PubMed:25752577"
FT MUTAGEN 25
FT /note="T->A: Does not affect binding to 'Lys-29'- and 'Lys-
FT 33'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:25752573"
FT MUTAGEN 25
FT /note="T->D: Abolished binding to 'Lys-33'-linked
FT diubiquitin."
FT /evidence="ECO:0000269|PubMed:25752577"
FT MUTAGEN 26
FT /note="M->A: Abolished binding to 'Lys-29'- and 'Lys-33'-
FT linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:25752573"
FT MUTAGEN 90
FT /note="C->A: Abolishes the binding to ubiquitin chains but
FT not the deubiquitinating activity; when associated with A-
FT 10; 14-LV-15; 94-LV-95; A-155 and 159-LV-160."
FT /evidence="ECO:0000269|PubMed:18281465"
FT MUTAGEN 94..95
FT /note="TY->LV: Abolishes the binding to ubiquitin chains
FT but not the deubiquitinating activity; when associated with
FT A-10; 14-LV-15; A-90; A-155 and 159-LV-160."
FT /evidence="ECO:0000269|PubMed:18281465"
FT MUTAGEN 155
FT /note="C->A: Abolishes the binding to ubiquitin chains but
FT not the deubiquitinating activity; when associated with A-
FT 10; 14-LV-15; A-90; 94-LV-95 and 159-LV-160."
FT /evidence="ECO:0000269|PubMed:18281465"
FT MUTAGEN 159..160
FT /note="TY->LV: Abolishes the binding to ubiquitin chains
FT but not the deubiquitinating activity; when associated with
FT A-10; 14-LV-15; A-90; 94-LV-95; and A-155."
FT /evidence="ECO:0000269|PubMed:18281465"
FT MUTAGEN 443
FT /note="C->S: Abolishes the deubiquitinating activity but
FT not the binding to ubiquitin chains."
FT /evidence="ECO:0000269|PubMed:18281465,
FT ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577"
FT CONFLICT 374
FT /note="F -> I (in Ref. 1; CAB64449)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="P -> A (in Ref. 1; CAB64449)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="A -> P (in Ref. 2; BAG64010)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5AF6"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5AF6"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:3ZRH"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:3ZRH"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 349..361
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:3ZRH"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 443..450
FT /evidence="ECO:0007829|PDB:3ZRH"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 461..472
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 500..513
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 523..532
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 577..582
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 612..620
FT /evidence="ECO:0007829|PDB:3ZRH"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 640..650
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:3ZRH"
FT STRAND 661..668
FT /evidence="ECO:0007829|PDB:3ZRH"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:3ZRH"
FT HELIX 674..688
FT /evidence="ECO:0007829|PDB:3ZRH"
SQ SEQUENCE 708 AA; 80967 MW; DBB831697F450248 CRC64;
MSERGIKWAC EYCTYENWPS AIKCTMCRAQ RPSGTIITED PFKSGSSDVG RDWDPSSTEG
GSSPLICPDS SARPRVKSSY SMENANKWSC HMCTYLNWPR AIRCTQCLSQ RRTRSPTESP
QSSGSGSRPV AFSVDPCEEY NDRNKLNTRT QHWTCSVCTY ENWAKAKRCV VCDHPRPNNI
EAIELAETEE ASSIINEQDR ARWRGSCSSG NSQRRSPPAT KRDSEVKMDF QRIELAGAVG
SKEELEVDFK KLKQIKNRMK KTDWLFLNAC VGVVEGDLAA IEAYKSSGGD IARQLTADEV
RLLNRPSAFD VGYTLVHLAI RFQRQDMLAI LLTEVSQQAA KCIPAMVCPE LTEQIRREIA
ASLHQRKGDF ACYFLTDLVT FTLPADIEDL PPTVQEKLFD EVLDRDVQKE LEEESPIINW
SLELATRLDS RLYALWNRTA GDCLLDSVLQ ATWGIYDKDS VLRKALHDSL HDCSHWFYTR
WKDWESWYSQ SFGLHFSLRE EQWQEDWAFI LSLASQPGAS LEQTHIFVLA HILRRPIIVY
GVKYYKSFRG ETLGYTRFQG VYLPLLWEQS FCWKSPIALG YTRGHFSALV AMENDGYGNR
GAGANLNTDD DVTITFLPLV DSERKLLHVH FLSAQELGNE EQQEKLLREW LDCCVTEGGV
LVAMQKSSRR RNHPLVTQMV EKWLDRYRQI RPCTSLSDGE EDEDDEDE
//
