GenomeNet

Database: UniProt
Entry: H2NMN8_PONAB
LinkDB: H2NMN8_PONAB
Original site: H2NMN8_PONAB 
ID   H2NMN8_PONAB            Unreviewed;       931 AA.
AC   H2NMN8; A0A2J8RGU6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=OTUD7A {ECO:0000313|Ensembl:ENSPPYP00000007132.2};
GN   ORFNames=CR201_G0050974 {ECO:0000313|EMBL:PNJ07753.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000007132.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000007132.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ07753.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ07753.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000007132.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000707};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase C64 family.
CC       {ECO:0000256|ARBA:ARBA00005865}.
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; NDHI03003694; PNJ07753.1; -; Genomic_DNA.
DR   STRING; 9601.ENSPPYP00000007132; -.
DR   Ensembl; ENSPPYT00000007428.2; ENSPPYP00000007132.2; ENSPPYG00000006293.2.
DR   eggNOG; KOG4345; Eukaryota.
DR   GeneTree; ENSGT00940000158999; -.
DR   HOGENOM; CLU_013263_0_0_1; -.
DR   OMA; RCAKQPE; -.
DR   OrthoDB; 2909231at2759; -.
DR   TreeFam; TF323312; -.
DR   Proteomes; UP000001595; Chromosome 15.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd22773; OTU_OTUD7A; 1.
DR   CDD; cd14347; UBA_Cezanne_like; 1.
DR   Gene3D; 1.20.5.4770; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR002653; Znf_A20.
DR   PANTHER; PTHR13367:SF9; OTU DOMAIN-CONTAINING PROTEIN 7A; 1.
DR   PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF01754; zf-A20; 1.
DR   SMART; SM00259; ZnF_A20; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS51036; ZF_A20; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00451}.
FT   DOMAIN          199..374
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   DOMAIN          889..924
FT                   /note="A20-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51036"
FT   REGION          75..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   931 AA;  100920 MW;  466A58C848E750ED CRC64;
     MVSSVLPNPT SAECWAALLH DPMTLDMDAV LSDFVRSTGA EPGLARDLLE GKNWDLTAAL
     SDYEQLRQVH TANLPHVFNE GRGPKQPERE PQPGHKVERP CLQRQDDIAQ EKRLSRGISH
     ASSAIVSLAR SHVASECNNE QFPLEMPIYT FQLPDLSVYS EDFRSFIERD LIEQATMVAL
     EQAGRLNWWS TVCTSCKRLL PLATTGDGNC LLHAASLGMW GFHDRDLVLR KALYTMMRTG
     AEREALKRRW RWQQTQQNKE EEWEREWTEL LKLASSEPRT HFSKNGGTGG GVDNSEDPVY
     ESLEEFHVFV LAHILRRPIV VVADTMLRDS GGEAFAPIPF GGIYLPLEVP PNRCHCSPLV
     LAYDQAHFSA LVSMEQRDQQ REQAVIPLTD SEHKLLPLHF AVDPGKDWEW GKDDNDNARL
     AHLILSLEAK LNLLHSYMNV TWIRIPSETR APLAQPESPT ASAGEDVQSL ADSLDSDRDS
     VCSNSNSNNG KNGKDKEKEK QRKEKDKTRA DSVANKLGSF SKTLGIKLKK NMGGLGGLVH
     GKMGRANSAN GKNGDSAERG KEKKAKSRKG SKEESGASAS TSPSEKTTPS PTDKAAGASP
     AEKGGGPRGD AWKYSTDVKL SLNILRAAMQ GERKFIFAGL LLTSHRHQFH EEMIGYYLTS
     AQERFSAEQE QRRRDAATAA AAAAAAAAAA AAASTAKRPP RRPETEGAPV PERASPGPPT
     QLVLKLKERP SPGPAAGRAA RAAAGGTASP GGGARRGGAS GPVPGRSPPA PARQSVIHVQ
     ASGARDEACA PAVGALRPCA TYPQQNRSLS SQSYSPARAA ALRTVNTVES LARAVPGALP
     GSAGAAGAAE HKSQTYTNGF GAARDGLEFA DADAPTARSN GECGRGGPGP VQRRCQRENC
     AFYGRAETEH YCSYCYREEL RRRREARGAR P
//
DBGET integrated database retrieval system