ZUP1_MOUSE
ID ZUP1_MOUSE Reviewed; 577 AA.
AC Q3T9Z9; Q5FWB1; Q6NXI1; Q8BJZ1; Q8BK40; Q8BKH3; Q8BL75; Q9CSP5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Zinc finger-containing ubiquitin peptidase 1 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96AP4};
DE AltName: Full=Lys-63-specific deubiquitinase ZUFSP;
DE Short=DUB;
DE AltName: Full=Zinc finger with UFM1-specific peptidase domain protein;
GN Name=Zup1 {ECO:0000312|MGI:MGI:1919830}; Synonyms=Zufsp;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Eye, Pituitary, Spleen, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Eye, and Pituitary;
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).
CC -!- FUNCTION: Deubiquitinase with endodeubiquitinase activity that
CC specifically interacts with and cleaves 'Lys-63'-linked long
CC polyubiquitin chains. Shows only weak activity against 'Lys-11' and
CC 'Lys-48'-linked chains. Plays an important role in genome stability
CC pathways, functioning to prevent spontaneous DNA damage and also
CC promote cellular survival in response to exogenous DNA damage.
CC Modulates the ubiquitination status of replication protein A (RPA)
CC complex proteins in response to replication stress.
CC {ECO:0000250|UniProtKB:Q96AP4}.
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:0000250|UniProtKB:Q96AP4};
CC -!- SUBUNIT: Interacts with RPA1 and RPA2. {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AP4}. Nucleus
CC {ECO:0000250|UniProtKB:Q96AP4}. Note=Mostly present in the nuclear
CC fraction. Localizes to DNA lesions. {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3T9Z9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3T9Z9-2; Sequence=VSP_019537;
CC Name=3;
CC IsoId=Q3T9Z9-3; Sequence=VSP_019536;
CC Name=4;
CC IsoId=Q3T9Z9-4; Sequence=VSP_019534, VSP_019535;
CC -!- DOMAIN: The motif interacting with ubiquitin (MIU) and ZUFSP ubiquitin-
CC binding domain (zUBD, also called ZUFSP helical arm ZHA) are
CC responsible for binding the distal (outgoing) ubiquitin units S1 and S2
CC respectively. {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- DOMAIN: C2H2-type zinc finger 4 is a ubiquitin-binding zinc finger
CC (UBZ) and required for polyubiquitin binding, possibly binding the
CC proximal ubiqutin, and for catalytic activity. C2H2-type zinc fingers
CC 1-3 are required for localization to sites of DNA damage.
CC {ECO:0000250|UniProtKB:Q96AP4}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. ZUFSP subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36984.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK012263; BAB28126.1; -; mRNA.
DR EMBL; AK046191; BAC32628.1; -; mRNA.
DR EMBL; AK052071; BAC34846.1; -; mRNA.
DR EMBL; AK077304; BAC36739.1; -; mRNA.
DR EMBL; AK077730; BAC36984.1; ALT_FRAME; mRNA.
DR EMBL; AK172184; BAE42871.1; -; mRNA.
DR EMBL; BC067065; AAH67065.1; -; mRNA.
DR EMBL; BC089514; AAH89514.1; -; mRNA.
DR CCDS; CCDS23772.1; -. [Q3T9Z9-2]
DR CCDS; CCDS87987.1; -. [Q3T9Z9-1]
DR RefSeq; NP_082563.1; NM_028287.2. [Q3T9Z9-2]
DR RefSeq; XP_006512930.1; XM_006512867.3.
DR RefSeq; XP_006512931.1; XM_006512868.3. [Q3T9Z9-1]
DR RefSeq; XP_006512932.1; XM_006512869.3. [Q3T9Z9-1]
DR RefSeq; XP_006512933.1; XM_006512870.3. [Q3T9Z9-1]
DR AlphaFoldDB; Q3T9Z9; -.
DR SMR; Q3T9Z9; -.
DR BioGRID; 215450; 3.
DR STRING; 10090.ENSMUSP00000037121; -.
DR iPTMnet; Q3T9Z9; -.
DR PhosphoSitePlus; Q3T9Z9; -.
DR EPD; Q3T9Z9; -.
DR PaxDb; Q3T9Z9; -.
DR PeptideAtlas; Q3T9Z9; -.
DR PRIDE; Q3T9Z9; -.
DR ProteomicsDB; 275167; -. [Q3T9Z9-1]
DR ProteomicsDB; 275168; -. [Q3T9Z9-2]
DR ProteomicsDB; 275169; -. [Q3T9Z9-3]
DR ProteomicsDB; 275170; -. [Q3T9Z9-4]
DR Antibodypedia; 32518; 110 antibodies from 17 providers.
DR Ensembl; ENSMUST00000048222; ENSMUSP00000037121; ENSMUSG00000039531. [Q3T9Z9-2]
DR Ensembl; ENSMUST00000218055; ENSMUSP00000151811; ENSMUSG00000039531. [Q3T9Z9-1]
DR Ensembl; ENSMUST00000218275; ENSMUSP00000151484; ENSMUSG00000039531. [Q3T9Z9-4]
DR Ensembl; ENSMUST00000219457; ENSMUSP00000151455; ENSMUSG00000039531. [Q3T9Z9-4]
DR GeneID; 72580; -.
DR KEGG; mmu:72580; -.
DR UCSC; uc007euj.1; mouse. [Q3T9Z9-3]
DR UCSC; uc007euk.1; mouse. [Q3T9Z9-1]
DR UCSC; uc007eum.1; mouse. [Q3T9Z9-2]
DR CTD; 221302; -.
DR MGI; MGI:1919830; Zup1.
DR VEuPathDB; HostDB:ENSMUSG00000039531; -.
DR eggNOG; KOG4696; Eukaryota.
DR GeneTree; ENSGT00390000008232; -.
DR HOGENOM; CLU_017060_1_1_1; -.
DR InParanoid; Q3T9Z9; -.
DR OMA; EEPRIHT; -.
DR OrthoDB; 788957at2759; -.
DR PhylomeDB; Q3T9Z9; -.
DR TreeFam; TF323699; -.
DR BioGRID-ORCS; 72580; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Zufsp; mouse.
DR PRO; PR:Q3T9Z9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3T9Z9; protein.
DR Bgee; ENSMUSG00000039531; Expressed in spermatocyte and 255 other tissues.
DR ExpressionAtlas; Q3T9Z9; baseline and differential.
DR Genevisible; Q3T9Z9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF07910; Peptidase_C78; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..577
FT /note="Zinc finger-containing ubiquitin peptidase 1"
FT /id="PRO_0000244338"
FT ZN_FING 2..24
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 29..52
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ZN_FING 153..176
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ZN_FING 192..214
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..247
FT /note="MIU"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT REGION 238..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..273
FT /note="zUBD/ZHA"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 490
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT ACT_SITE 511
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT SITE 486
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT MOD_RES 261
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96AP4"
FT VAR_SEQ 264..279
FT /note="RQYGLDNSGGYKQQQL -> ELLKPSIGIIRTLPQM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019534"
FT VAR_SEQ 280..577
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019535"
FT VAR_SEQ 529..562
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019536"
FT VAR_SEQ 563..577
FT /note="ARKQASQVFTAEKIP -> VSIG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019537"
FT CONFLICT 5
FT /note="N -> D (in Ref. 1; BAE42871)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="T -> A (in Ref. 2; AAH89514)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> I (in Ref. 1; BAC36739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 65593 MW; 711B6DE1629DFD01 CRC64;
MLSCNICGET VNSEPDMKAH LIVHMENEII CPFCKLSGIN YNEICFHIET VHFEQNAPEK
NSEKLAAVQY GHSDRKNTNL QSTAEVTSGI HSACASSFPK ESSESLPKDR TVKHEAFYTE
NITESRKYQK SREKKPGLSE AQGSIYETTY SPPECPFCGK IEGCSQDMEI HVKTKHASLL
ESPLKDCHQP LYDCPMCGLV CTNYHILQEH VDLHLEESSF QQGMDRVQCS SDRELAHRLQ
QEEDRKRKSE ESRQEREEFQ KLQRQYGLDN SGGYKQQQLR HMELEVNRGR MHPSEFHSRK
ADMLESIAIG IDDGKTKTSG IIEALHRYYQ NTATDVRCVW LSTVVDHFHS SFGDKGWGCG
YRNFQMLLSS LLQSDVYGDC LKGMAVPCIP KIQSMIEDAW NEGFDPQGAS QLNNKLQGTK
AWIGACEIYT LLTSLRVKCR IIDFHKSTGP LGTHPRLFEW ILNYYSSETE GTPKIVCTSK
PPIYLQHQGH SRTVVGIEEK KNRTLCLLVF DPGCPSREMQ KLLKQDMEAS SLRQLRKSVG
NLKHKQYQIV AVEGVLSPEE KVARKQASQV FTAEKIP
