UBP7_CHICK
ID UBP7_CHICK Reviewed; 1101 AA.
AC Q6U7I1; Q6U7I2; Q6U7I3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q93009};
DE AltName: Full=Deubiquitinating enzyme 7;
DE AltName: Full=Ubiquitin thioesterase 7;
DE AltName: Full=Ubiquitin-specific-processing protease 7;
GN Name=USP7;
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 [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Skeletal muscle;
RA Lee M.H., Chung C.H.;
RT "Ubiquitin-specific protease in chick.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase that deubiquitinates target proteins, such as
CC p53/TP53. Deubiquitinates p53/TP53, and thereby modulates p53/TP53
CC stability, p53/TP53-dependent transcription regulation, cell growth
CC repression and apoptosis. May be involved in cell proliferation during
CC early embryonic development (By similarity).
CC {ECO:0000250|UniProtKB:Q93009}.
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:Q93009};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93009}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q93009}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q93009}. Chromosome
CC {ECO:0000250|UniProtKB:Q93009}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6U7I1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6U7I1-2; Sequence=VSP_021957, VSP_021958;
CC Name=3;
CC IsoId=Q6U7I1-3; Sequence=VSP_021955, VSP_021956;
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Polyneddylated. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AY376869; AAQ74886.1; -; mRNA.
DR EMBL; AY376870; AAQ74887.1; -; mRNA.
DR EMBL; AY376871; AAQ74888.1; -; mRNA.
DR RefSeq; NP_001334941.1; NM_001348012.1. [Q6U7I1-2]
DR AlphaFoldDB; Q6U7I1; -.
DR BMRB; Q6U7I1; -.
DR SMR; Q6U7I1; -.
DR BioGRID; 675423; 1.
DR STRING; 9031.ENSGALP00000039011; -.
DR MEROPS; C19.016; -.
DR PaxDb; Q6U7I1; -.
DR GeneID; 395126; -.
DR KEGG; gga:395126; -.
DR CTD; 7874; -.
DR VEuPathDB; HostDB:geneid_395126; -.
DR eggNOG; KOG1863; Eukaryota.
DR InParanoid; Q6U7I1; -.
DR PhylomeDB; Q6U7I1; -.
DR PRO; PR:Q6U7I1; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
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:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 2.60.210.10; -; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50144; MATH; 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 Alternative splicing; Chromosome; Cytoplasm; Developmental protein;
KW Hydrolase; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..1101
FT /note="Ubiquitin carboxyl-terminal hydrolase 7"
FT /id="PRO_0000268008"
FT DOMAIN 68..195
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 214..521
FT /note="USP"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..208
FT /note="Interaction with p53/TP53"
FT /evidence="ECO:0000250|UniProtKB:Q93009"
FT REGION 70..205
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250|UniProtKB:Q93009"
FT ACT_SITE 223
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 464
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT VAR_SEQ 632..677
FT /note="TKRPAMLDNEADGNKTMIELSDNENPWTIFLETVDPEMAATGATLP -> KR
FT NSSSSSSITWSTGIVAKDKMLIILISTPVGTIYSQLVFLESGHS (in isoform
FT 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021955"
FT VAR_SEQ 678..1101
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021956"
FT VAR_SEQ 683..687
FT /note="HDVML -> RKLMC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021957"
FT VAR_SEQ 688..1101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_021958"
SQ SEQUENCE 1101 AA; 128297 MW; 71A8FA4B02A4D2E9 CRC64;
MNHHQQQQHQ KPGEQQLSEP EDMEMEAGDA DDPPRITQNP VINGNVAMAD GHNNTEEDME
DDTSWRSEAT FQFTVERFNR LSESVLSPPC FVRNLPWKIM VMPRLYPDRP HQKSVGFFLQ
CNAESDSTSW SCHAQAVLKI INYKDDEKSF SRRISHLFFH KENDWGFSNF MAWSEVTDPE
KGFIEEDKVT FEVYVQADAP HGVAWDSKKH TGYVGLKNQG ATCYMNSLLQ TLFFTNQLRK
AVYMMPTEGD DSSKSVPLAL QRVFYELQHS DKPVGTKKLT KSFGWETLDS FMQHDVQELC
RVLLDNVENK MKGTCVEGTI PKLFRGKMVS YIQCKHVDYR SERIEDYYDI QLSIKGKKNI
FESFIDYVAV EQLDGDNKYD AGEHGLQEAE KGVKFLTLPP VLHLQLMRFM YDPQTDQNIK
INDRFEFPEQ LPLDEFLQKT DPKDPANYIL HAVLVHSGDN HGGHYVVYLN PKGDGKWCKF
DDDVVSRCTK EEAIEHNYGG HDDDLSVRHC TNAYMLVYIR ESKLSEVLQP VTDHDIPQQL
VERLQEEKRI EAQKRKERQE AHLYMQVQIV AEDQFCGHQG NDMYDEEKVK YTVFKVLKNS
TLTEFVQNLS QTMGFPQDQI RLWPMQARSN GTKRPAMLDN EADGNKTMIE LSDNENPWTI
FLETVDPEMA ATGATLPKFD KDHDVMLFLK MYDPKTRSLN YCGHIYTPIS CKIRDLLPVM
CERAGFPQET NLILYEEVKP NLTERIQDYD VSLDKALDEL MDGDIIVFQK DDPENDSSEL
PTAKEYFRDL YSRVDVIFCD KTIPNDPGFV VTLSNRMNYF QVAKTVAQRL NTDPMLLQFF
KSQGYRDGPG NPLRHNYEGT LRDLLQFFKP RQPKKLYYQQ LKMKITDFEN RRSFKCTWLN
SQFREEEITV YPDKHGCVRD LLEECKKVVE LSEKGSGKLR LLEIVSYKII GVHQEDELLE
CLSPATSRTF RIEEIPLAQV DIDKENEMLI TVAHFHKEVF GTFGIPFLLR IHQGGHFREV
MKRIQTMLDI QEKEFEKFKF AIVMMGRHTY LNEDEYEVNL KDFEPQPGNM SHPRPWLGLD
HFNKAPKDRY TYLEKAYKIH N
