UBP44_HUMAN
ID UBP44_HUMAN Reviewed; 712 AA.
AC Q9H0E7; B2RDW3;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 44;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 44;
DE AltName: Full=Ubiquitin thioesterase 44;
DE AltName: Full=Ubiquitin-specific-processing protease 44;
GN Name=USP44;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-91.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-91.
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-91.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY, AND ENZYME ACTIVITY.
RX PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
RA Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
RA Lopez-Otin C.;
RT "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
RT proteases.";
RL Biochem. Biophys. Res. Commun. 314:54-62(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF CYS-282.
RX PubMed=17443180; DOI=10.1038/nature05694;
RA Stegmeier F., Rape M., Draviam V.M., Nalepa G., Sowa M.E., Ang X.L.,
RA McDonald E.R. III, Li M.Z., Hannon G.J., Sorger P.K., Kirschner M.W.,
RA Harper J.W., Elledge S.J.;
RT "Anaphase initiation is regulated by antagonistic ubiquitination and
RT deubiquitination activities.";
RL Nature 446:876-881(2007).
RN [7]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, AND MUTAGENESIS
RP OF CYS-282.
RX PubMed=20402667; DOI=10.1042/cbi20090144;
RA Suresh B., Ramakrishna S., Lee H.J., Choi J.H., Kim J.Y., Ahn W.S.,
RA Baek K.H.;
RT "K48- and K63-linked polyubiquitination of deubiquitinating enzyme USP44.";
RL Cell Biol. Int. 34:799-808(2010).
RN [8]
RP INDUCTION.
RX PubMed=20505756; DOI=10.1371/journal.pone.0010709;
RA Jung M., Peterson H., Chavez L., Kahlem P., Lehrach H., Vilo J., Adjaye J.;
RT "A data integration approach to mapping OCT4 gene regulatory networks
RT operative in embryonic stem cells and embryonal carcinoma cells.";
RL PLoS ONE 5:E10709-E10709(2010).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=21853124; DOI=10.1371/journal.pone.0023389;
RA Zhang Y., van Deursen J., Galardy P.J.;
RT "Overexpression of ubiquitin specific protease 44 (USP44) induces
RT chromosomal instability and is frequently observed in human T-cell
RT leukemia.";
RL PLoS ONE 6:E23389-E23389(2011).
RN [10]
RP FUNCTION.
RX PubMed=22681888; DOI=10.1016/j.molcel.2012.05.023;
RA Fuchs G., Shema E., Vesterman R., Kotler E., Wolchinsky Z., Wilder S.,
RA Golomb L., Pribluda A., Zhang F., Haj-Yahya M., Feldmesser E., Brik A.,
RA Yu X., Hanna J., Aberdam D., Domany E., Oren M.;
RT "RNF20 and USP44 regulate stem cell differentiation by modulating H2B
RT monoubiquitylation.";
RL Mol. Cell 46:662-673(2012).
RN [11]
RP PHOSPHORYLATION AT SER-169; SER-239; THR-269 AND SER-401, AND
RP DEPHOSPHORYLATION.
RX PubMed=22692537; DOI=10.1038/ncomms1886;
RA Visconti R., Palazzo L., Della Monica R., Grieco D.;
RT "Fcp1-dependent dephosphorylation is required for M-phase-promoting factor
RT inactivation at mitosis exit.";
RL Nat. Commun. 3:894-894(2012).
CC -!- FUNCTION: Deubiquitinase that plays a key regulatory role in the
CC spindle assembly checkpoint or mitotic checkpoint by preventing
CC premature anaphase onset. Acts by specifically mediating
CC deubiquitination of CDC20, a negative regulator of the anaphase
CC promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to
CC stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic
CC checkpoint complex), thereby preventing premature activation of the
CC APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the
CC spindle assembly checkpoint. Acts as a negative regulator of histone
CC H2B (H2BK120ub1) ubiquitination. {ECO:0000269|PubMed:17443180,
CC ECO:0000269|PubMed:22681888}.
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:14715245,
CC ECO:0000269|PubMed:17443180, ECO:0000269|PubMed:20402667};
CC -!- INTERACTION:
CC Q9H0E7; P41208: CETN2; NbExp=2; IntAct=EBI-2512823, EBI-1789926;
CC Q9H0E7; Q9BZS1: FOXP3; NbExp=3; IntAct=EBI-2512823, EBI-983719;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20402667}. Note=Peaks
CC in interphase, with relatively low levels maintained throughout
CC mitosis. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. Expressed at high levels in T-
CC cell acute lymphoblastic leukemia. {ECO:0000269|PubMed:14715245,
CC ECO:0000269|PubMed:21853124}.
CC -!- DEVELOPMENTAL STAGE: Elevated in mitosis; levels increase in mitotic
CC cells and rapidly decrease once cells have completed chromosome
CC attachment and exit from mitosis. {ECO:0000269|PubMed:17443180}.
CC -!- INDUCTION: Transcriptionally regulated by POU5F1/OCT4 in embryonic stem
CC cells and embryonal carcinoma cells. {ECO:0000269|PubMed:20505756}.
CC -!- PTM: Dephosphorylated by CTDP1.
CC -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
CC polyubiquitination and is degraded by the proteasome.
CC {ECO:0000269|PubMed:20402667}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP44 subfamily.
CC {ECO:0000305}.
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DR EMBL; AL136825; CAB66759.1; -; mRNA.
DR EMBL; AK315697; BAG38060.1; -; mRNA.
DR EMBL; AC018475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030704; AAH30704.1; -; mRNA.
DR CCDS; CCDS9053.1; -.
DR RefSeq; NP_001035862.1; NM_001042403.2.
DR RefSeq; NP_001265322.1; NM_001278393.1.
DR RefSeq; NP_001334865.1; NM_001347936.1.
DR RefSeq; NP_001334866.1; NM_001347937.1.
DR RefSeq; NP_115523.2; NM_032147.4.
DR RefSeq; XP_016875499.1; XM_017020010.1.
DR AlphaFoldDB; Q9H0E7; -.
DR BioGRID; 123890; 42.
DR IntAct; Q9H0E7; 12.
DR MINT; Q9H0E7; -.
DR STRING; 9606.ENSP00000258499; -.
DR MEROPS; C19.057; -.
DR iPTMnet; Q9H0E7; -.
DR PhosphoSitePlus; Q9H0E7; -.
DR BioMuta; USP44; -.
DR DMDM; 300669621; -.
DR EPD; Q9H0E7; -.
DR jPOST; Q9H0E7; -.
DR MassIVE; Q9H0E7; -.
DR PaxDb; Q9H0E7; -.
DR PeptideAtlas; Q9H0E7; -.
DR PRIDE; Q9H0E7; -.
DR ProteomicsDB; 80264; -.
DR Antibodypedia; 17590; 299 antibodies from 24 providers.
DR DNASU; 84101; -.
DR Ensembl; ENST00000258499.8; ENSP00000258499.3; ENSG00000136014.12.
DR Ensembl; ENST00000393091.6; ENSP00000376806.2; ENSG00000136014.12.
DR Ensembl; ENST00000537435.2; ENSP00000442629.2; ENSG00000136014.12.
DR GeneID; 84101; -.
DR KEGG; hsa:84101; -.
DR MANE-Select; ENST00000258499.8; ENSP00000258499.3; NM_032147.5; NP_115523.2.
DR UCSC; uc001teg.5; human.
DR CTD; 84101; -.
DR DisGeNET; 84101; -.
DR GeneCards; USP44; -.
DR HGNC; HGNC:20064; USP44.
DR HPA; ENSG00000136014; Tissue enhanced (testis).
DR MIM; 610993; gene.
DR neXtProt; NX_Q9H0E7; -.
DR OpenTargets; ENSG00000136014; -.
DR PharmGKB; PA134931457; -.
DR VEuPathDB; HostDB:ENSG00000136014; -.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000160526; -.
DR HOGENOM; CLU_008279_13_1_1; -.
DR InParanoid; Q9H0E7; -.
DR OMA; HLLIFRE; -.
DR OrthoDB; 1230415at2759; -.
DR PhylomeDB; Q9H0E7; -.
DR TreeFam; TF315281; -.
DR PathwayCommons; Q9H0E7; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q9H0E7; -.
DR BioGRID-ORCS; 84101; 13 hits in 1121 CRISPR screens.
DR ChiTaRS; USP44; human.
DR GeneWiki; USP44; -.
DR GenomeRNAi; 84101; -.
DR Pharos; Q9H0E7; Tbio.
DR PRO; PR:Q9H0E7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H0E7; protein.
DR Bgee; ENSG00000136014; Expressed in secondary oocyte and 105 other tissues.
DR ExpressionAtlas; Q9H0E7; baseline and differential.
DR Genevisible; Q9H0E7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Hydrolase; Metal-binding; Mitosis; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..712
FT /note="Ubiquitin carboxyl-terminal hydrolase 44"
FT /id="PRO_0000080673"
FT DOMAIN 273..678
FT /note="USP"
FT ZN_FING 5..102
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 690..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 282
FT /note="Nucleophile"
FT ACT_SITE 636
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:22692537"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:22692537"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:22692537"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:22692537"
FT VARIANT 91
FT /note="T -> A (in dbSNP:rs3812813)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_017125"
FT VARIANT 316
FT /note="E -> Q (in dbSNP:rs7305024)"
FT /id="VAR_057043"
FT VARIANT 348
FT /note="R -> G (in dbSNP:rs7135642)"
FT /id="VAR_057044"
FT MUTAGEN 282
FT /note="C->S,A: Abolishes deubiquitinase activity."
FT /evidence="ECO:0000269|PubMed:17443180,
FT ECO:0000269|PubMed:20402667"
SQ SEQUENCE 712 AA; 81185 MW; A8211DFAD78EE731 CRC64;
MLAMDTCKHV GQLQLAQDHS SLNPQKWHCV DCNTTESIWA CLSCSHVACG RYIEEHALKH
FQESSHPVAL EVNEMYVFCY LCDDYVLNDN TTGDLKLLRR TLSAIKSQNY HCTTRSGRFL
RSMGTGDDSY FLHDGAQSLL QSEDQLYTAL WHRRRILMGK IFRTWFEQSP IGRKKQEEPF
QEKIVVKREV KKRRQELEYQ VKAELESMPP RKSLRLQGLA QSTIIEIVSV QVPAQTPASP
AKDKVLSTSE NEISQKVSDS SVKRRPIVTP GVTGLRNLGN TCYMNSVLQV LSHLLIFRQC
FLKLDLNQWL AMTASEKTRS CKHPPVTDTV VYQMNECQEK DTGFVCSRQS SLSSGLSGGA
SKGRKMELIQ PKEPTSQYIS LCHELHTLFQ VMWSGKWALV SPFAMLHSVW RLIPAFRGYA
QQDAQEFLCE LLDKIQRELE TTGTSLPALI PTSQRKLIKQ VLNVVNNIFH GQLLSQVTCL
ACDNKSNTIE PFWDLSLEFP ERYQCSGKDI ASQPCLVTEM LAKFTETEAL EGKIYVCDQC
NSKRRRFSSK PVVLTEAQKQ LMICHLPQVL RLHLKRFRWS GRNNREKIGV HVGFEEILNM
EPYCCRETLK SLRPECFIYD LSAVVMHHGK GFGSGHYTAY CYNSEGGFWV HCNDSKLSMC
TMDEVCKAQA YILFYTQRVT ENGHSKLLPP ELLLGSQHPN EDADTSSNEI LS
