Full text data of TRIM23
TRIM23
(ARD1, ARFD1, RNF46)
[Confidence: low (only semi-automatic identification from reviews)]
E3 ubiquitin-protein ligase TRIM23; 6.3.2.- (ADP-ribosylation factor domain-containing protein 1; GTP-binding protein ARD-1; RING finger protein 46; Tripartite motif-containing protein 23)
E3 ubiquitin-protein ligase TRIM23; 6.3.2.- (ADP-ribosylation factor domain-containing protein 1; GTP-binding protein ARD-1; RING finger protein 46; Tripartite motif-containing protein 23)
UniProt
P36406
ID TRI23_HUMAN Reviewed; 574 AA.
AC P36406; Q9BZY4; Q9BZY5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM23;
DE EC=6.3.2.-;
DE AltName: Full=ADP-ribosylation factor domain-containing protein 1;
DE AltName: Full=GTP-binding protein ARD-1;
DE AltName: Full=RING finger protein 46;
DE AltName: Full=Tripartite motif-containing protein 23;
GN Name=TRIM23; Synonyms=ARD1, ARFD1, RNF46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX PubMed=8473324;
RA Mishima K., Tsuchiya M., Nightingale M.S., Moss J., Vaughan M.;
RT "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-
RT terminal ADP-ribosylation factor domain.";
RL J. Biol. Chem. 268:8801-8807(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA Minucci S., Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9671726; DOI=10.1073/pnas.95.15.8613;
RA Vitale N., Horiba K., Ferrans V.J., Moss J., Vaughan M.;
RT "Localization of ADP-ribosylation factor domain protein 1 (ARD1) in
RT lysosomes and Golgi apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8613-8618(1998).
RN [5]
RP INTERACTION WITH PSCD1, AND MUTAGENESIS OF THR-418 AND LYS-458.
RX PubMed=10748148; DOI=10.1074/jbc.M909642199;
RA Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W.,
RA Moss J., Vaughan M.;
RT "Specific functional interaction of human cytohesin-1 and ADP-
RT ribosylation factor domain protein (ARD1).";
RL J. Biol. Chem. 275:21331-21339(2000).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-34 AND HIS-53.
RX PubMed=15684077; DOI=10.1073/pnas.0409800102;
RA Vichi A., Payne D.M., Pacheco-Rodriguez G., Moss J., Vaughan M.;
RT "E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-
RT ribosylation factor domain protein 1).";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1945-1950(2005).
RN [7]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL144.
RX PubMed=19176615; DOI=10.1128/JVI.02072-08;
RA Poole E., Groves I., MacDonald A., Pang Y., Alcami A., Sinclair J.;
RT "Identification of TRIM23 as a cofactor involved in the regulation of
RT NF-kappaB by human cytomegalovirus.";
RL J. Virol. 83:3581-3590(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. In the presence
CC of the human cytomegalovirus (HCMV) protein UL144, participates in
CC 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the
CC virally controlled activation of NF-kappa-B at early time of
CC infection. The C-terminus can act as an allosteric activator of
CC the cholera toxin catalytic subunit.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with PSCD1. Interacts with human
CC cytomegalovirus protein UL144; this interaction might causes auto-
CC ubiquitination of TRAF6, leading to NF-kappaB activation.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-740098, EBI-740098;
CC P55040:GEM; NbExp=3; IntAct=EBI-740098, EBI-744104;
CC P09022:Hoxa1 (xeno); NbExp=2; IntAct=EBI-740098, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Endomembrane system. Golgi apparatus
CC membrane. Lysosome membrane. Note=Membrane-associated with the
CC Golgi complex and lysosomal structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=P36406-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P36406-2; Sequence=VSP_000296;
CC Name=Gamma;
CC IsoId=P36406-3; Sequence=VSP_000297;
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity.
CC -!- SIMILARITY: In the C-terminal section; belongs to the small GTPase
CC superfamily. Arf family.
CC -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L04510; AAA35940.1; -; mRNA.
DR EMBL; AF230397; AAG50176.1; -; mRNA.
DR EMBL; AF230398; AAG50177.1; -; mRNA.
DR EMBL; AF230399; AAG50178.1; -; mRNA.
DR EMBL; BC022510; AAH22510.1; -; mRNA.
DR PIR; A46054; A46054.
DR RefSeq; NP_001647.1; NM_001656.3.
DR RefSeq; NP_150230.1; NM_033227.2.
DR RefSeq; NP_150231.1; NM_033228.2.
DR UniGene; Hs.792; -.
DR ProteinModelPortal; P36406; -.
DR SMR; P36406; 16-106, 127-219, 371-565.
DR IntAct; P36406; 43.
DR MINT; MINT-1442172; -.
DR STRING; 9606.ENSP00000231524; -.
DR PhosphoSite; P36406; -.
DR DMDM; 543839; -.
DR PaxDb; P36406; -.
DR PRIDE; P36406; -.
DR DNASU; 373; -.
DR Ensembl; ENST00000231524; ENSP00000231524; ENSG00000113595.
DR Ensembl; ENST00000274327; ENSP00000274327; ENSG00000113595.
DR Ensembl; ENST00000381018; ENSP00000370406; ENSG00000113595.
DR GeneID; 373; -.
DR KEGG; hsa:373; -.
DR UCSC; uc003jty.3; human.
DR CTD; 373; -.
DR GeneCards; GC05M064885; -.
DR HGNC; HGNC:660; TRIM23.
DR HPA; HPA039605; -.
DR MIM; 601747; gene.
DR neXtProt; NX_P36406; -.
DR PharmGKB; PA24943; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000008208; -.
DR HOVERGEN; HBG000551; -.
DR InParanoid; P36406; -.
DR KO; K07963; -.
DR OMA; RAVRCPF; -.
DR OrthoDB; EOG76DTS0; -.
DR PhylomeDB; P36406; -.
DR UniPathway; UPA00143; -.
DR GeneWiki; TRIM23; -.
DR GenomeRNAi; 373; -.
DR NextBio; 1557; -.
DR PRO; PR:P36406; -.
DR ArrayExpress; P36406; -.
DR Bgee; P36406; -.
DR CleanEx; HS_TRIM23; -.
DR Genevestigator; P36406; -.
DR GO; GO:0000139; C:Golgi membrane; IDA:HGNC.
DR GO; GO:0005765; C:lysosomal membrane; IDA:HGNC.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019003; F:GDP binding; IDA:HGNC.
DR GO; GO:0005525; F:GTP binding; IDA:HGNC.
DR GO; GO:0003924; F:GTPase activity; IDA:HGNC.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:HGNC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Golgi apparatus;
KW GTP-binding; Host-virus interaction; Ligase; Lysosome; Membrane;
KW Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 574 E3 ubiquitin-protein ligase TRIM23.
FT /FTId=PRO_0000207483.
FT ZN_FING 31 76 RING-type; degenerate.
FT ZN_FING 122 168 B box-type; degenerate.
FT NP_BIND 411 418 GTP (By similarity).
FT NP_BIND 454 458 GTP (By similarity).
FT NP_BIND 513 516 GTP (By similarity).
FT REGION 390 574 ARF-like.
FT COILED 352 379 Potential.
FT VAR_SEQ 541 574 WYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA -> CFS
FT DNM (in isoform Gamma).
FT /FTId=VSP_000297.
FT VAR_SEQ 551 574 GMGLYEGLDWLSRQLVAAGVLDVA -> VFQIICDQYTGKE
FT VVTEKG (in isoform Beta).
FT /FTId=VSP_000296.
FT VARIANT 480 480 D -> N (in dbSNP:rs34046496).
FT /FTId=VAR_048320.
FT MUTAGEN 34 34 C->A: Loss of E3 ubiquitin-protein ligase
FT activity.
FT MUTAGEN 53 53 H->A: Loss of E3 ubiquitin-protein ligase
FT activity.
FT MUTAGEN 418 418 T->N: Maintains GTPase activity.
FT Increases interaction with PSCD1.
FT MUTAGEN 458 458 K->I: Suppresses GTPase activity.
FT Decreases interaction with PSCD1.
SQ SEQUENCE 574 AA; 64067 MW; CB85923B29BF0320 CRC64;
MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL
TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS
GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ
HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF
TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI
TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI
LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD
SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS
WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA
//
ID TRI23_HUMAN Reviewed; 574 AA.
AC P36406; Q9BZY4; Q9BZY5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1994, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM23;
DE EC=6.3.2.-;
DE AltName: Full=ADP-ribosylation factor domain-containing protein 1;
DE AltName: Full=GTP-binding protein ARD-1;
DE AltName: Full=RING finger protein 46;
DE AltName: Full=Tripartite motif-containing protein 23;
GN Name=TRIM23; Synonyms=ARD1, ARFD1, RNF46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX PubMed=8473324;
RA Mishima K., Tsuchiya M., Nightingale M.S., Moss J., Vaughan M.;
RT "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-
RT terminal ADP-ribosylation factor domain.";
RL J. Biol. Chem. 268:8801-8807(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA Minucci S., Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9671726; DOI=10.1073/pnas.95.15.8613;
RA Vitale N., Horiba K., Ferrans V.J., Moss J., Vaughan M.;
RT "Localization of ADP-ribosylation factor domain protein 1 (ARD1) in
RT lysosomes and Golgi apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8613-8618(1998).
RN [5]
RP INTERACTION WITH PSCD1, AND MUTAGENESIS OF THR-418 AND LYS-458.
RX PubMed=10748148; DOI=10.1074/jbc.M909642199;
RA Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W.,
RA Moss J., Vaughan M.;
RT "Specific functional interaction of human cytohesin-1 and ADP-
RT ribosylation factor domain protein (ARD1).";
RL J. Biol. Chem. 275:21331-21339(2000).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-34 AND HIS-53.
RX PubMed=15684077; DOI=10.1073/pnas.0409800102;
RA Vichi A., Payne D.M., Pacheco-Rodriguez G., Moss J., Vaughan M.;
RT "E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-
RT ribosylation factor domain protein 1).";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1945-1950(2005).
RN [7]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL144.
RX PubMed=19176615; DOI=10.1128/JVI.02072-08;
RA Poole E., Groves I., MacDonald A., Pang Y., Alcami A., Sinclair J.;
RT "Identification of TRIM23 as a cofactor involved in the regulation of
RT NF-kappaB by human cytomegalovirus.";
RL J. Virol. 83:3581-3590(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. In the presence
CC of the human cytomegalovirus (HCMV) protein UL144, participates in
CC 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the
CC virally controlled activation of NF-kappa-B at early time of
CC infection. The C-terminus can act as an allosteric activator of
CC the cholera toxin catalytic subunit.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with PSCD1. Interacts with human
CC cytomegalovirus protein UL144; this interaction might causes auto-
CC ubiquitination of TRAF6, leading to NF-kappaB activation.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-740098, EBI-740098;
CC P55040:GEM; NbExp=3; IntAct=EBI-740098, EBI-744104;
CC P09022:Hoxa1 (xeno); NbExp=2; IntAct=EBI-740098, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Endomembrane system. Golgi apparatus
CC membrane. Lysosome membrane. Note=Membrane-associated with the
CC Golgi complex and lysosomal structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=P36406-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P36406-2; Sequence=VSP_000296;
CC Name=Gamma;
CC IsoId=P36406-3; Sequence=VSP_000297;
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity.
CC -!- SIMILARITY: In the C-terminal section; belongs to the small GTPase
CC superfamily. Arf family.
CC -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L04510; AAA35940.1; -; mRNA.
DR EMBL; AF230397; AAG50176.1; -; mRNA.
DR EMBL; AF230398; AAG50177.1; -; mRNA.
DR EMBL; AF230399; AAG50178.1; -; mRNA.
DR EMBL; BC022510; AAH22510.1; -; mRNA.
DR PIR; A46054; A46054.
DR RefSeq; NP_001647.1; NM_001656.3.
DR RefSeq; NP_150230.1; NM_033227.2.
DR RefSeq; NP_150231.1; NM_033228.2.
DR UniGene; Hs.792; -.
DR ProteinModelPortal; P36406; -.
DR SMR; P36406; 16-106, 127-219, 371-565.
DR IntAct; P36406; 43.
DR MINT; MINT-1442172; -.
DR STRING; 9606.ENSP00000231524; -.
DR PhosphoSite; P36406; -.
DR DMDM; 543839; -.
DR PaxDb; P36406; -.
DR PRIDE; P36406; -.
DR DNASU; 373; -.
DR Ensembl; ENST00000231524; ENSP00000231524; ENSG00000113595.
DR Ensembl; ENST00000274327; ENSP00000274327; ENSG00000113595.
DR Ensembl; ENST00000381018; ENSP00000370406; ENSG00000113595.
DR GeneID; 373; -.
DR KEGG; hsa:373; -.
DR UCSC; uc003jty.3; human.
DR CTD; 373; -.
DR GeneCards; GC05M064885; -.
DR HGNC; HGNC:660; TRIM23.
DR HPA; HPA039605; -.
DR MIM; 601747; gene.
DR neXtProt; NX_P36406; -.
DR PharmGKB; PA24943; -.
DR eggNOG; COG1100; -.
DR HOGENOM; HOG000008208; -.
DR HOVERGEN; HBG000551; -.
DR InParanoid; P36406; -.
DR KO; K07963; -.
DR OMA; RAVRCPF; -.
DR OrthoDB; EOG76DTS0; -.
DR PhylomeDB; P36406; -.
DR UniPathway; UPA00143; -.
DR GeneWiki; TRIM23; -.
DR GenomeRNAi; 373; -.
DR NextBio; 1557; -.
DR PRO; PR:P36406; -.
DR ArrayExpress; P36406; -.
DR Bgee; P36406; -.
DR CleanEx; HS_TRIM23; -.
DR Genevestigator; P36406; -.
DR GO; GO:0000139; C:Golgi membrane; IDA:HGNC.
DR GO; GO:0005765; C:lysosomal membrane; IDA:HGNC.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019003; F:GDP binding; IDA:HGNC.
DR GO; GO:0005525; F:GTP binding; IDA:HGNC.
DR GO; GO:0003924; F:GTPase activity; IDA:HGNC.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:HGNC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Golgi apparatus;
KW GTP-binding; Host-virus interaction; Ligase; Lysosome; Membrane;
KW Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 574 E3 ubiquitin-protein ligase TRIM23.
FT /FTId=PRO_0000207483.
FT ZN_FING 31 76 RING-type; degenerate.
FT ZN_FING 122 168 B box-type; degenerate.
FT NP_BIND 411 418 GTP (By similarity).
FT NP_BIND 454 458 GTP (By similarity).
FT NP_BIND 513 516 GTP (By similarity).
FT REGION 390 574 ARF-like.
FT COILED 352 379 Potential.
FT VAR_SEQ 541 574 WYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA -> CFS
FT DNM (in isoform Gamma).
FT /FTId=VSP_000297.
FT VAR_SEQ 551 574 GMGLYEGLDWLSRQLVAAGVLDVA -> VFQIICDQYTGKE
FT VVTEKG (in isoform Beta).
FT /FTId=VSP_000296.
FT VARIANT 480 480 D -> N (in dbSNP:rs34046496).
FT /FTId=VAR_048320.
FT MUTAGEN 34 34 C->A: Loss of E3 ubiquitin-protein ligase
FT activity.
FT MUTAGEN 53 53 H->A: Loss of E3 ubiquitin-protein ligase
FT activity.
FT MUTAGEN 418 418 T->N: Maintains GTPase activity.
FT Increases interaction with PSCD1.
FT MUTAGEN 458 458 K->I: Suppresses GTPase activity.
FT Decreases interaction with PSCD1.
SQ SEQUENCE 574 AA; 64067 MW; CB85923B29BF0320 CRC64;
MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL
TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS
GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ
HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF
TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI
TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI
LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD
SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS
WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA
//
MIM
601747
*RECORD*
*FIELD* NO
601747
*FIELD* TI
*601747 TRIPARTITE MOTIF-CONTAINING PROTEIN 23; TRIM23
;;ADP-RIBOSYLATION FACTOR DOMAIN PROTEIN 1; ARFD1; ARD1;;
read moreARF DOMAIN PROTEIN 1
*FIELD* TX
DESCRIPTION
TRIM23 belongs to the ADP-ribosylation factor (ARF) family of GTPases
and contains an N-terminal GTPase-activating protein (GAP) domain and a
C-terminal ARF domain (Vitale et al., 2000).
CLONING
Mishima et al. (1993) isolated a gene referred to as ARD1 from human and
rat cDNA libraries. ARD1 encodes a putative 64-kD protein that contains
an 18-kD ADP-ribosylation factor domain at the carboxyl terminus and is
much larger than the other monomeric guanine nucleotide-binding ARF
proteins previously identified.
GENE FUNCTION
Vitale et al. (2000) found that cytohesin-1 (PSCD1; 182115) interacted
with ARD1 in a yeast 2-hybrid screen of a human liver cDNA library.
ARD1-GDP interacted well with cytohesin-1 but poorly with cytohesin-2
(PSCD2; 602488), and cytohesin-1 accelerated binding of a
nonhydrolyzable GTP analog to ARD1. Mutation analysis showed that the
effector region of the ARF domain of ARD1 interacted with the Sec7
domain of cytohesin-1. Physical association between these domains was
highly dependent on experimental conditions, and a free Mg(2+)
concentration that favored nucleotide release from ARD1 and accumulation
of the nucleotide-free ARD1 form also favored interaction between ARD1
and cytohesin-1. In transfected COS-7 cells, ARD1 associated with
vesicular structures concentrated around the nucleus and scattered
throughout the cytoplasm, corresponding to Golgi and lysosomes,
respectively. A constitutively GDP-bound form of ARD1 showed a similar
distribution, whereas a constitutively GTP-bound form of ARD1 was
concentrated close to the nucleus in a Golgi-like distribution only.
Cytohesin-1 was distributed throughout the cell and was also present in
the nucleus. When ARD1 or its GDP- and GTP-bound forms were coexpressed
with cytohesin-1, only the GDP-bound form showed any change in
distribution or colocalization with cytohesin-1. In 90% of cells
coexpressing the proteins, the GDP-bound form of ARD1 was distributed
throughout the cell, except for the nucleus, and largely colocalized
with cytohesin-1. In less than 10% of cells coexpressing the proteins,
the GDP-bound form of ARD1 and cytohesin-1 colocalized in lysosomes.
*FIELD* RF
1. Mishima, K.; Tsuchiya, M.; Nightingale, M. S.; Moss, J.; Vaughan,
M.: ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal
ADP-ribosylation factor domain. J. Biol. Chem. 268: 8801-8807, 1993.
2. Vitale, N.; Pacheco-Rodriguez, G.; Ferrans, V. J.; Riemenschneider,
W.; Moss, J.; Vaughan, M.: Specific functional interaction of human
cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). J.
Biol. Chem. 275: 21331-21339, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 3/13/2007
*FIELD* CD
Lori M. Kelman: 4/10/1997
*FIELD* ED
mgross: 03/15/2007
mgross: 3/15/2007
terry: 3/13/2007
carol: 3/26/1999
joanna: 4/10/1997
*RECORD*
*FIELD* NO
601747
*FIELD* TI
*601747 TRIPARTITE MOTIF-CONTAINING PROTEIN 23; TRIM23
;;ADP-RIBOSYLATION FACTOR DOMAIN PROTEIN 1; ARFD1; ARD1;;
read moreARF DOMAIN PROTEIN 1
*FIELD* TX
DESCRIPTION
TRIM23 belongs to the ADP-ribosylation factor (ARF) family of GTPases
and contains an N-terminal GTPase-activating protein (GAP) domain and a
C-terminal ARF domain (Vitale et al., 2000).
CLONING
Mishima et al. (1993) isolated a gene referred to as ARD1 from human and
rat cDNA libraries. ARD1 encodes a putative 64-kD protein that contains
an 18-kD ADP-ribosylation factor domain at the carboxyl terminus and is
much larger than the other monomeric guanine nucleotide-binding ARF
proteins previously identified.
GENE FUNCTION
Vitale et al. (2000) found that cytohesin-1 (PSCD1; 182115) interacted
with ARD1 in a yeast 2-hybrid screen of a human liver cDNA library.
ARD1-GDP interacted well with cytohesin-1 but poorly with cytohesin-2
(PSCD2; 602488), and cytohesin-1 accelerated binding of a
nonhydrolyzable GTP analog to ARD1. Mutation analysis showed that the
effector region of the ARF domain of ARD1 interacted with the Sec7
domain of cytohesin-1. Physical association between these domains was
highly dependent on experimental conditions, and a free Mg(2+)
concentration that favored nucleotide release from ARD1 and accumulation
of the nucleotide-free ARD1 form also favored interaction between ARD1
and cytohesin-1. In transfected COS-7 cells, ARD1 associated with
vesicular structures concentrated around the nucleus and scattered
throughout the cytoplasm, corresponding to Golgi and lysosomes,
respectively. A constitutively GDP-bound form of ARD1 showed a similar
distribution, whereas a constitutively GTP-bound form of ARD1 was
concentrated close to the nucleus in a Golgi-like distribution only.
Cytohesin-1 was distributed throughout the cell and was also present in
the nucleus. When ARD1 or its GDP- and GTP-bound forms were coexpressed
with cytohesin-1, only the GDP-bound form showed any change in
distribution or colocalization with cytohesin-1. In 90% of cells
coexpressing the proteins, the GDP-bound form of ARD1 was distributed
throughout the cell, except for the nucleus, and largely colocalized
with cytohesin-1. In less than 10% of cells coexpressing the proteins,
the GDP-bound form of ARD1 and cytohesin-1 colocalized in lysosomes.
*FIELD* RF
1. Mishima, K.; Tsuchiya, M.; Nightingale, M. S.; Moss, J.; Vaughan,
M.: ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal
ADP-ribosylation factor domain. J. Biol. Chem. 268: 8801-8807, 1993.
2. Vitale, N.; Pacheco-Rodriguez, G.; Ferrans, V. J.; Riemenschneider,
W.; Moss, J.; Vaughan, M.: Specific functional interaction of human
cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). J.
Biol. Chem. 275: 21331-21339, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 3/13/2007
*FIELD* CD
Lori M. Kelman: 4/10/1997
*FIELD* ED
mgross: 03/15/2007
mgross: 3/15/2007
terry: 3/13/2007
carol: 3/26/1999
joanna: 4/10/1997