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 27-MAR-2024, entry version 179. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 44; DE EC=3.4.19.12 {ECO:0000269|PubMed:23615962, ECO:0000269|PubMed:27880911, ECO:0000269|PubMed:31968013}; 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). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-282, AND CATALYTIC RP ACTIVITY. RX PubMed=23615962; DOI=10.1074/jbc.m113.459917; RA Mosbech A., Lukas C., Bekker-Jensen S., Mailand N.; RT "The deubiquitylating enzyme USP44 counteracts the DNA double-strand break RT response mediated by the RNF8 and RNF168 ubiquitin ligases."; RL J. Biol. Chem. 288:16579-16587(2013). RN [13] RP FUNCTION, INTERACTION WITH TBL1X AND TBLXR1, MUTAGENESIS OF CYS-282, AND RP CATALYTIC ACTIVITY. RX PubMed=27880911; DOI=10.1016/j.celrep.2016.10.076; RA Lan X., Atanassov B.S., Li W., Zhang Y., Florens L., Mohan R.D., RA Galardy P.J., Washburn M.P., Workman J.L., Dent S.Y.R.; RT "USP44 Is an Integral Component of N-CoR that Contributes to Gene RT Repression by Deubiquitinating Histone H2B."; RL Cell Rep. 17:2382-2393(2016). RN [14] RP FUNCTION, MUTAGENESIS OF CYS-282, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=31968013; DOI=10.1371/journal.ppat.1008178; RA Zhang H.Y., Liao B.W., Xu Z.S., Ran Y., Wang D.P., Yang Y., Luo W.W., RA Wang Y.Y.; RT "USP44 positively regulates innate immune response to DNA viruses through RT deubiquitinating MITA."; RL PLoS Pathog. 16:e1008178-e1008178(2020). RN [15] RP FUNCTION, INDUCTION BY TGF-BETA, AND SUBCELLULAR LOCATION. RX PubMed=32644293; DOI=10.15252/embr.202050308; RA Yang J., Wei P., Barbi J., Huang Q., Yang E., Bai Y., Nie J., Gao Y., RA Tao J., Lu Y., Xie C., Hou X., Ren J., Wu X., Meng J., Zhang Y., Fu J., RA Kou W., Gao Y., Chen Z., Liang R., Tsun A., Li D., Guo W., Zhang S., RA Zheng S.G., Niu J., Galardy P., Tong X., Shi G., Li H., Pan F., Li B.; RT "The deubiquitinase USP44 promotes Treg function during inflammation by RT preventing FOXP3 degradation."; RL EMBO Rep. 21:e50308-e50308(2020). 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) (PubMed:17443180). Deubiquitination CC of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex CC (also named mitotic checkpoint complex), thereby preventing premature CC activation of the APC/C (PubMed:17443180). Promotes association of CC MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint CC (PubMed:17443180). Promotes also the deubiquitination of histone H2A CC and H2B (PubMed:23615962, PubMed:27880911). Recruited to RNF8/RNF168- CC ubiquitinated chromatin surrounding double stranded breaks (DSBs), CC promotes hydrolysis of such ubiquitin conjugates, thus negatively CC regulating protein recruitment to damaged chromatin (PubMed:23615962). CC Participates in nucleotide excision repair (NER) pathway by CC deubiquitinating DDB2 to prevent its premature degradation so it can CC remain on damaged chromatin (By similarity). Promotes FOXP3 CC stabilization through 'Lys-48'-linked deubiquitination leading to CC increased stability and increased regulatory T-cell lineage stability CC (PubMed:32644293). Plays also a positive role in innate immune response CC to DNA viruses by deubiquitinating STING1, selectively removing its CC 'Lys-48'-linked polyubiquitin chains and stabilizing it CC (PubMed:31968013). {ECO:0000250|UniProtKB:Q8C2S0, CC ECO:0000269|PubMed:17443180, ECO:0000269|PubMed:22681888, CC ECO:0000269|PubMed:23615962, ECO:0000269|PubMed:27880911, CC ECO:0000269|PubMed:31968013, ECO:0000269|PubMed:32644293}. 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 ECO:0000269|PubMed:23615962, ECO:0000269|PubMed:27880911, CC ECO:0000269|PubMed:31968013}; CC -!- SUBUNIT: Interacts with the N-CoR components TBL1X and TBL1XR1. CC {ECO:0000269|PubMed:27880911}. 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, CC ECO:0000269|PubMed:23615962, ECO:0000269|PubMed:31968013, CC ECO:0000269|PubMed:32644293}. Cytoplasm {ECO:0000269|PubMed:31968013}. CC Note=Peaks in interphase, with relatively low levels maintained CC throughout 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. Induced by TGF-beta during CC regulatory T-cells differentiation (PubMed:32644293). CC {ECO:0000269|PubMed:20505756, ECO:0000269|PubMed:32644293}. 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}. 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; 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; 44. DR IntAct; Q9H0E7; 12. DR MINT; Q9H0E7; -. DR STRING; 9606.ENSP00000258499; -. DR MEROPS; C19.057; -. DR GlyGen; Q9H0E7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H0E7; -. DR PhosphoSitePlus; Q9H0E7; -. DR BioMuta; USP44; -. DR DMDM; 300669621; -. DR EPD; Q9H0E7; -. DR jPOST; Q9H0E7; -. DR MassIVE; Q9H0E7; -. DR PaxDb; 9606-ENSP00000258499; -. DR PeptideAtlas; Q9H0E7; -. DR ProteomicsDB; 80264; -. DR Antibodypedia; 17590; 341 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 AGR; HGNC:20064; -. DR CTD; 84101; -. DR DisGeNET; 84101; -. DR GeneCards; USP44; -. DR HGNC; HGNC:20064; USP44. DR HPA; ENSG00000136014; Tissue enriched (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; RYQCNGK; -. DR OrthoDB; 227085at2759; -. 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; 15 hits in 1200 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 107 other cell types or tissues. DR ExpressionAtlas; Q9H0E7; baseline and differential. DR GO; GO:0000785; C:chromatin; ISS:UniProt. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0072686; C:mitotic spindle; IC:UniProt. 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:0101005; F:deubiquitinase activity; IDA:UniProt. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProt. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl. DR GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IDA:UniProt. DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IMP:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProt. 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 GO; GO:0045066; P:regulatory T cell differentiation; IDA:UniProt. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR21646:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 44; 1. DR Pfam; PF00443; UCH; 1. DR Pfam; PF02148; zf-UBP; 1. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF57850; RING/U-box; 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. DR Genevisible; Q9H0E7; HS. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cytoplasm; Hydrolase; Immunity; Innate immunity; KW Metal-binding; Mitosis; Nucleus; Phosphoprotein; Protease; KW Reference proteome; Thiol protease; Ubl conjugation; KW 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, ECO:0000269|PubMed:23615962, FT ECO:0000269|PubMed:27880911, ECO:0000269|PubMed:31968013" 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 //