UBP28_CHICK
ID UBP28_CHICK Reviewed; 1047 AA.
AC Q5ZID5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 28;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 28;
DE AltName: Full=Ubiquitin thioesterase 28;
DE AltName: Full=Ubiquitin-specific-processing protease 28;
GN Name=USP28; ORFNames=RCJMB04_27l24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Deubiquitinase involved in DNA damage response checkpoint and
CC MYC proto-oncogene stability. Involved in DNA damage induced apoptosis
CC by specifically deubiquitinating proteins of the DNA damage pathway
CC such as CLSPN. Also involved in G2 DNA damage checkpoint, by
CC deubiquitinating CLSPN, and preventing its degradation by the anaphase
CC promoting complex/cyclosome (APC/C). Specifically deubiquitinates MYC
CC in the nucleoplasm, leading to prevent MYC degradation by the
CC proteasome. Deubiquitinates ZNF304, hence may prevent ZNF304
CC degradation by the proteasome, leading to the activated KRAS-mediated
CC promoter hypermethylation and transcriptional silencing of tumor
CC suppressor genes (TSGs). {ECO:0000250|UniProtKB:Q96RU2}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP28 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ720849; CAG32508.1; -; mRNA.
DR RefSeq; NP_001026667.1; NM_001031496.1.
DR AlphaFoldDB; Q5ZID5; -.
DR SMR; Q5ZID5; -.
DR STRING; 9031.ENSGALP00000011273; -.
DR MEROPS; C19.054; -.
DR PaxDb; Q5ZID5; -.
DR GeneID; 428246; -.
DR KEGG; gga:428246; -.
DR CTD; 57646; -.
DR VEuPathDB; HostDB:geneid_428246; -.
DR eggNOG; KOG1863; Eukaryota.
DR InParanoid; Q5ZID5; -.
DR OrthoDB; 194025at2759; -.
DR PhylomeDB; Q5ZID5; -.
DR PRO; PR:Q5ZID5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Hydrolase; Nucleus; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1047
FT /note="Ubiquitin carboxyl-terminal hydrolase 28"
FT /id="PRO_0000080659"
FT DOMAIN 94..113
FT /note="UIM"
FT /evidence="ECO:0000305"
FT DOMAIN 156..651
FT /note="USP"
FT REGION 60..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 601
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1047 AA; 118747 MW; 93B40127861B2A00 CRC64;
MTAELQAASG GPGGLEADCQ VLNKMKEITG IQDADFLHAA LKAAKGNLME ALIVLTEERD
QEPVQNTAAA EPSSWEGSAV GKEPPQGGAA FDPEKKGDVH SAVAYGQLES PKAHAAERPQ
EVHSPEHKNR SKRKRCEVWG ENSKQSDWKR VGDWPVGMKN IGNTCWFSAV IQSLFQLPQF
RRLVLSYSFP PNVLESCRTR TGKRNIAFMQ ELQCLFALML GTRRKFVDPS AALELLRDAF
KSTEEQQQDV SEFTHKLLDW LEDAFQLAVN VRSPGDKSEN PMVQLFYGTF LTEGVHEGNT
FSKIETFGQY PLQVNGYRNL NECLEGAMVE GEMDEETATQ SVKYVQERWF TKLPPVLTFE
LSRFEFNQSL GQPEKIHTKL EFPQTIFMDR YLYCSKELIQ TKREEMKKLK EKMLVLQQKL
ERYMKYGSGP ARFPLPDMLQ YVLEFITTKP AGAVSSACVS STEDSQMMDR QSQGESLILG
TPSQPDSMLD GKDGKPEDEA VLLANSSPQQ QLNAPLQPSE PPAEMSDCPA PHVVSEEEMN
LVTTCLQRWR NEIEQDVRDL KESIARVSLS IDEMYSDPHL QQVPYHLHAV LVHEGQANAG
HYWAFIYDQP RKSWLKYNDI SVTESSWEEL ERDSFGGLRN ASAYCLMYIS DKVSHVVAGE
GDGSEVGQFQ KEVEALPPEL RRYIQEDNWR LEQEAEEWEE EQSCKIPSTA SESQELSPES
GLDPPAAHEQ SLRSLSSEHA MIAKEQTAKA IANAANVYEK NGVEAALCEA FHEEYSRLYL
LSKETPTPQN DARLQHVLVY FLQNDAPQQI VERTLLEQFA DKNLSYDERS ISIMKVARDK
LKEIGPDEVN MEEYKKWHED YSLFRKVSVY LLTGLELYQN RKYKESLTYL IYAYQSNTTL
LKKGANRGVN ESLITLYRRK CLLKLNEVAS SLFVSCEEAH VAEGISILNE LIIPCMHLIN
NFDISREDMD AIEVMRNRWC SYLGREDMDA SLQIRLGELL PRLLDGSTEV VVLKEPPKIR
PNSPYDLCSR FAAVMESIHD ASTVTVK
