UBP44_MOUSE
ID UBP44_MOUSE Reviewed; 711 AA.
AC Q8C2S0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 3.
DT 03-AUG-2022, entry version 141.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND PROTEASOMAL
RP DEGRADATION.
RC TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
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).
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:21853124}.
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;
CC -!- INTERACTION:
CC Q8C2S0; Q99JB6: Foxp3; NbExp=3; IntAct=EBI-26303241, EBI-10956246;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21853124}. Note=Peaks
CC in interphase, with relatively low levels maintained throughout
CC mitosis.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung,
CC pancreas, skin, liver, stomach and intestine.
CC {ECO:0000269|PubMed:20402667}.
CC -!- PTM: Dephosphorylated by CTDP1. {ECO:0000250}.
CC -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
CC polyubiquitination and is degraded by the proteasome.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP44 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI11887.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC40148.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK088109; BAC40148.1; ALT_SEQ; mRNA.
DR EMBL; CJ236846; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC124686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111886; AAI11887.1; ALT_SEQ; mRNA.
DR CCDS; CCDS88075.1; -.
DR RefSeq; NP_001193780.1; NM_001206851.1.
DR RefSeq; XP_011241781.1; XM_011243479.2.
DR RefSeq; XP_011241782.1; XM_011243480.2.
DR RefSeq; XP_011241783.1; XM_011243481.2.
DR RefSeq; XP_011241784.1; XM_011243482.2.
DR RefSeq; XP_011241785.1; XM_011243483.2.
DR RefSeq; XP_011241786.1; XM_011243484.2.
DR RefSeq; XP_011241787.1; XM_011243485.2.
DR RefSeq; XP_011241788.1; XM_011243486.2.
DR RefSeq; XP_011241789.1; XM_011243487.2.
DR RefSeq; XP_011241790.1; XM_011243488.2.
DR RefSeq; XP_011241791.1; XM_011243489.2.
DR RefSeq; XP_011241792.1; XM_011243490.2.
DR AlphaFoldDB; Q8C2S0; -.
DR BioGRID; 236490; 3.
DR IntAct; Q8C2S0; 1.
DR MINT; Q8C2S0; -.
DR STRING; 10090.ENSMUSP00000092975; -.
DR MEROPS; C19.057; -.
DR iPTMnet; Q8C2S0; -.
DR PhosphoSitePlus; Q8C2S0; -.
DR PRIDE; Q8C2S0; -.
DR ProteomicsDB; 298363; -.
DR Antibodypedia; 17590; 299 antibodies from 24 providers.
DR DNASU; 327799; -.
DR Ensembl; ENSMUST00000216224; ENSMUSP00000149020; ENSMUSG00000020020.
DR GeneID; 327799; -.
DR KEGG; mmu:327799; -.
DR UCSC; uc029rep.1; mouse.
DR CTD; 84101; -.
DR MGI; MGI:3045318; Usp44.
DR VEuPathDB; HostDB:ENSMUSG00000020020; -.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000160526; -.
DR InParanoid; Q8C2S0; -.
DR OMA; HLLIFRE; -.
DR OrthoDB; 1230415at2759; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 327799; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Usp44; mouse.
DR PRO; PR:Q8C2S0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8C2S0; protein.
DR Bgee; ENSMUSG00000020020; Expressed in spermatid and 25 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:MGI.
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; IMP:CACAO.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IDA: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 Protease; Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..711
FT /note="Ubiquitin carboxyl-terminal hydrolase 44"
FT /id="PRO_0000395811"
FT DOMAIN 272..677
FT /note="USP"
FT ZN_FING 2..99
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 170..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 635
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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"
SQ SEQUENCE 711 AA; 80479 MW; F176DB2BA3C658BE CRC64;
MDRCKHVEQL QLAQGHSILD PQKWYCMVCN TTESIWACLS CSHVACGKYI QEHALKHFQE
SSHPVAFEVN DMYAFCYLCN DYVLNDNAAG DLKSLRSTLS TIKSKKYPCV VPSDSVLHPV
DAQDRVYSLL DGTQSLPGNE DPTCAALWHR RRVLMGKAFR TWFEQSAIGR KGQEPTQERM
VAKREAKRRQ QQELEQQMKA ELESTPPRKS LRLQGSSEEA ATIEIVPVRA PPPPPASPAK
DKAALPTSED RTFKKVSDSL IKRRPMVTPG VTGLRNLGNT CYMNSVLQVL SHLLIFRQCF
LKLDLNQWLA VAASDKARSY KHSAVTEAAA QQMNEGQEKE KGFVCSRHSG LSSGLSGGAS
KGRNMELIQP REPSSPYSSL CHELHILFQV MWSGEWALVS PFAMLHSVWR LIPAFRGYAQ
QDAQEFLCEL LDKIQRELET TGTKLPALIP TSQRRLIEQV LNVVNNIFHG QFLSQVTCLA
CDNKSDTIES FWDLSLEFPE RYQCSGKDAA SQPCLVTDML DKFTETEALE GKIYMCDHCN
SKRRKFSSKS VVFTEAQKQL MICHLPQVLR LHLKRFRWSG RNNREKIGVH VVFEETLNME
PYCCRETLNA LRPECFLYNL SAVVIHHGKG FGSGHYTAYC YNSEGGFWVH CNDSKLSMCT
MEEVRKAQAY ILFYTQRVTE NGHSKLLPPE LLSNSQHPSK ETDASSNEVL S
