ID D3TTY8_HUMAN Unreviewed; 532 AA.
AC D3TTY8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=TNFAIP3 {ECO:0000313|EMBL:ACN87234.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ACN87234.1};
RN [1] {ECO:0000313|EMBL:ACN87234.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mt8 {ECO:0000313|EMBL:ACN87234.1};
RC TISSUE=Primary lymphoma {ECO:0000313|EMBL:ACN87234.1};
RA Kato M., Kobayashi Y., Ogawa S.;
RT "Inactivation of a negative regulator of inflammation in malignant
RT lymphomas of B cell lineage.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ434408; ACN87234.1; -; mRNA.
DR AlphaFoldDB; D3TTY8; -.
DR MEROPS; C64.003; -.
DR PeptideAtlas; D3TTY8; -.
DR ChiTaRS; TNFAIP3; human.
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; cd22766; OTU_TNFAIP3; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR Gene3D; 4.10.240.30; -; 2.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF3; TUMOR NECROSIS FACTOR ALPHA-INDUCED PROTEIN 3; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 2.
DR SMART; SM00259; ZnF_A20; 2.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 2.
PE 2: Evidence at transcript level;
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00451}.
FT DOMAIN 92..263
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 381..416
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT DOMAIN 472..507
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 61248 MW; 7844AE6644852376 CRC64;
MAEQVLPQAL YLSNMRKAVK IRERTPEDIF KPTNGIIHHF KTMHRYTLEM FRTCQFCPQF
REIIHKALID RNIQATLESQ KKLNWCREVR KLVALKTNGD GNCLMHATSQ YMWGVQDTDL
VLRKALFSTL KETDTRNFKF RWQLESLKSQ EFVETGLCYD TRNWNDEWDN LIKMASTDTP
MARSGLQYNS LEEIHIFVLC NILRRPIIVI SDKMLRSLES GSNFAPLKVG GIYLPLHWPA
QECYRYPIVL GYDSHHFVPL VTLKDSGPEI RAVPLVNRDR GRFEDLKVHF LTDPENEMKE
KLLKEYLMVI EIPVQGWDHG TTHLINAAKL DEANLPKEIN LVDDYFELVQ HEYKKWQENS
EQGRREGHAQ NPMEPSVPQL SLMDVKCETP NCPFFMSVNT QPLCHECSER RQKNQNKLPK
LNSKPGPEGL PGMALGASRG EAYEPLAWNP EESTGGPHSA PPTAPSPFLF SETTAMKCRS
PGCPFTLNVQ HNGFCERCHN ARQLQRQPRP RPHKALGSRE VPSLPPGCYQ DI
//
