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Database: UniProt
Entry: G1RF33_NOMLE
LinkDB: G1RF33_NOMLE
Original site: G1RF33_NOMLE 
ID   G1RF33_NOMLE            Unreviewed;       903 AA.
AC   G1RF33;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   05-JUN-2019, entry version 58.
DE   RecName: Full=Ubiquitinyl hydrolase 1 {ECO:0000256|SAAS:SAAS01044305};
DE            EC=3.4.19.12 {ECO:0000256|SAAS:SAAS01044305};
GN   Name=USP33 {ECO:0000313|Ensembl:ENSNLEP00000011833};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates
OS   leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hylobatidae; Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000011833};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000011833}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000011833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC         Evidence={ECO:0000256|SAAS:SAAS01117307};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|SAAS:SAAS01045498}.
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DR   EMBL; ADFV01189159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01189160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01189161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 61853.ENSNLEP00000011833; -.
DR   Ensembl; ENSNLET00000012415; ENSNLEP00000011833; ENSNLEG00000009694.
DR   eggNOG; KOG1870; Eukaryota.
DR   eggNOG; COG5560; LUCA.
DR   GeneTree; ENSGT00940000157311; -.
DR   InParanoid; G1RF33; -.
DR   Proteomes; UP000001073; Chromosome 12.
DR   GO; GO:0044297; C:cell body; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR   GO; GO:0017160; F:Ral GTPase binding; IEA:Ensembl.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR   GO; GO:0051298; P:centrosome duplication; IEA:Ensembl.
DR   GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR   GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; IEA:Ensembl.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR035927; DUSP-like_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006615; Pept_C19_DUSP.
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; PF06337; DUSP; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00695; DUSP; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF143791; SSF143791; 2.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS51283; DUSP; 2.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001073};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01044238};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01044152};
KW   Protease {ECO:0000256|SAAS:SAAS01044292};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Thiol protease {ECO:0000256|SAAS:SAAS01044269};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01044331};
KW   Zinc {ECO:0000256|SAAS:SAAS01044373};
KW   Zinc-finger {ECO:0000256|SAAS:SAAS01044352}.
FT   DOMAIN       59    123       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   DOMAIN      185    676       USP. {ECO:0000259|PROSITE:PS50235}.
FT   DOMAIN      678    771       DUSP. {ECO:0000259|PROSITE:PS51283}.
FT   DOMAIN      779    882       DUSP. {ECO:0000259|PROSITE:PS51283}.
FT   ZN_FING      59    123       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
FT   REGION      380    430       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G1RF33}.
FT   COMPBIAS    380    401       Polar. {ECO:0000256|MobiDB-lite:G1RF33}.
SQ   SEQUENCE   903 AA;  102440 MW;  24C8E2778A3E60F2 CRC64;
     MTGSNSHITI LTLKVLPHFE SLGKQEKIPN KMSAFRNYCP HLDSVGEITK EDLMQKSQGT
     CQDCKVRGPN LWACLENRCS YVGCGESQVD HSTIHSQETK HYLTVNLTTL RVWCYACSKE
     VFLDRKLGTQ PSLPQVRQPH QIQENSVQDF KIPSNTTLKT PLVAVFDDLD IEVDEEDELR
     ARGLTGLKNI GNTCYMNAAL QALSNCPPLT QFFLDCGGLA RTDKKPAICK SYLKLMTELW
     HKSRPGSVVP TNLFQGIKTV NPTFRGYSQQ DGQEFLRCFM DDLHEDRKSK QWKKTRASRD
     VDFQSCESCS SSDKAENENG SRYWQKEKMC NKINKVNSEG ELDKDRESIS ETVDLNNQET
     VKVQIHSRAS EYITDVHSND LSTPQILPSN EGVNPRLSAS PPKSGNLWPG LAPPHKKAQS
     ASPKRKKQHK KYRSVISDIF DGTIISSVQC LTCDRVSVTL ETFQDLSLPI PGKEDLAKLH
     SSSHPTSIVK AGSCGEAYAP QGWIAFFMEY VKRFVVSCVP SWFWGPVVTL QDCLAAFFAR
     DELKGDNMYS CEKCKKLRNG VKFCKVQKFP EILCIHLKRF RHELMFSTKI STHVSFPLEG
     LDLQPFLAKD SPAQIVTYDL LSVICHHGTA SSGHYIAYCR NNLNNLWYEF DDQSVTEVSE
     STVQNAEAYV LFYRKSSEEA QKERRRISNL LNIMEPSLLQ FYISRQWLNK FKTFAEPGPI
     SNNDFLCIHG GVPPRKAGYI EDLVLMLPQN IWDNLYSRYG GGPAVNHLYI CHTCQIEAEK
     IEKRRKTELE IFIRLNRAFQ KEDSPATFYC ISMQWFREWE SFVKGKDGDP PGPIDNTKIA
     VTKCGNVMLR QGADSGQISE ETWNFLQSIY GGGPEVILRP PVVHVDPDIL QAEEKIEVET
     RSL
//
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