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, GN 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 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. DR Genevisible; Q9UGI0; HS. 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 FT 14-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 FT 'Lys-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 FT 'Lys-33'-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 FT 'Lys-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 FT 'Lys-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 FT 'Lys-33'-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 FT A-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 FT A-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 //