Full text data of ARIH2
ARIH2
(ARI2, TRIAD1)
[Confidence: low (only semi-automatic identification from reviews)]
E3 ubiquitin-protein ligase ARIH2; ARI-2; Protein ariadne-2 homolog; 6.3.2.- (Triad1 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase ARIH2; ARI-2; Protein ariadne-2 homolog; 6.3.2.- (Triad1 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95376
ID ARI2_HUMAN Reviewed; 493 AA.
AC O95376; Q9HBZ6; Q9UEM9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=E3 ubiquitin-protein ligase ARIH2;
DE Short=ARI-2;
DE Short=Protein ariadne-2 homolog;
DE EC=6.3.2.-;
DE AltName: Full=Triad1 protein;
GN Name=ARIH2; Synonyms=ARI2, TRIAD1; ORFNames=HT005;
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].
RX PubMed=10422847;
RA van der Reijden B.A., Erpelinck-Verschueren C.A.J., Loewenberg B.,
RA Jansen J.H.;
RT "TRIADs: a new class of proteins with a novel cysteine-rich
RT signature.";
RL Protein Sci. 8:1557-1561(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10880484;
RA Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.;
RT "Ariadne-1: a vital Drosophila gene is required in development and
RT defines a new conserved family of ring-finger proteins.";
RL Genetics 155:1231-1244(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [5]
RP FUNCTION, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION,
RP UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE
RP SPECIFICITY, AND INDUCTION BY ATRA.
RX PubMed=16118314; DOI=10.1182/blood-2005-04-1450;
RA Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G.,
RA Menke A., de Witte T., Loewenberg B., Jansen J.H.,
RA van der Reijden B.A.;
RT "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of
RT primary myeloid progenitor cells.";
RL Blood 106:4114-4123(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH GFI1 AND GFI1B.
RX PubMed=17646546; DOI=10.1182/blood-2006-11-058602;
RA Marteijn J.A., van der Meer L.T., van Emst L., van Reijmersdal S.,
RA Wissink W., de Witte T., Jansen J.H., Van der Reijden B.A.;
RT "Gfi1 ubiquitination and proteasomal degradation is inhibited by the
RT ubiquitin ligase Triad1.";
RL Blood 110:3128-3135(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP FUNCTION, INTERACTION WITH UBE2L3 AND UBE2N, AND SUBCELLULAR LOCATION.
RX PubMed=19340006; DOI=10.1038/leu.2009.57;
RA Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M.,
RA Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T.,
RA Sixma T.K., Jansen J.H., van der Reijden B.A.;
RT "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and
RT Ubc13 interacting domains.";
RL Leukemia 23:1480-1489(2009).
RN [9]
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: E3 ubiquitin-protein ligase mediating 'Lys-48'-and 'Lys-
CC 63'-linked polyubiquitination and subsequent proteasomal
CC degradation of modified proteins. May play a role in myelopoiesis.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via RING-type 1) with UBE2L3. Interacts (via
CC RING-type 2) with UBE2N. Interacts (via RING-type 2) with GFI1B.
CC Interacts with GFI1; prevents its ubiquitination and proteasomal
CC degradation.
CC -!- INTERACTION:
CC P04637:TP53; NbExp=5; IntAct=EBI-711158, EBI-366083;
CC P68036:UBE2L3; NbExp=3; IntAct=EBI-711158, EBI-711173;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in
CC granulocytes.
CC -!- INDUCTION: Up-regulated by all-trans retinoic acid (ATRA). Up-
CC regulated during differentiation of immature blood cells toward
CC monocytes and granulocytes.
CC -!- DOMAIN: RING-type 1 and RING-type 2 are required for the
CC inhibitory function in myelopoiesis.
CC -!- PTM: Ubiquitinated. Ubiquitination promotes proteasomal
CC degradation.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09696.1; Type=Frameshift; Positions=Several;
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; AF099149; AAC82469.1; -; mRNA.
DR EMBL; AJ130978; CAA10276.1; -; mRNA.
DR EMBL; AF183427; AAG09696.1; ALT_FRAME; mRNA.
DR EMBL; BC000422; AAH00422.1; -; mRNA.
DR RefSeq; NP_006312.1; NM_006321.2.
DR RefSeq; XP_005264855.1; XM_005264798.1.
DR UniGene; Hs.633601; -.
DR ProteinModelPortal; O95376; -.
DR SMR; O95376; 61-492.
DR IntAct; O95376; 41.
DR MINT; MINT-1376284; -.
DR STRING; 9606.ENSP00000348769; -.
DR PhosphoSite; O95376; -.
DR PaxDb; O95376; -.
DR PRIDE; O95376; -.
DR DNASU; 10425; -.
DR Ensembl; ENST00000356401; ENSP00000348769; ENSG00000177479.
DR Ensembl; ENST00000449376; ENSP00000403222; ENSG00000177479.
DR GeneID; 10425; -.
DR KEGG; hsa:10425; -.
DR UCSC; uc003cvb.3; human.
DR CTD; 10425; -.
DR GeneCards; GC03P048931; -.
DR HGNC; HGNC:690; ARIH2.
DR MIM; 605615; gene.
DR neXtProt; NX_O95376; -.
DR PharmGKB; PA24983; -.
DR eggNOG; NOG327249; -.
DR HOGENOM; HOG000216611; -.
DR HOVERGEN; HBG018737; -.
DR InParanoid; O95376; -.
DR KO; K11969; -.
DR OMA; THPPHHC; -.
DR OrthoDB; EOG7CZK58; -.
DR PhylomeDB; O95376; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR ChiTaRS; ARIH2; human.
DR GeneWiki; ARIH2; -.
DR GenomeRNAi; 10425; -.
DR NextBio; 39512; -.
DR PRO; PR:O95376; -.
DR ArrayExpress; O95376; -.
DR Bgee; O95376; -.
DR CleanEx; HS_ARIH2; -.
DR Genevestigator; O95376; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0048588; P:developmental cell growth; IDA:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR002867; Znf_C6HC.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SMART; SM00343; ZnF_C2HC; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 493 E3 ubiquitin-protein ligase ARIH2.
FT /FTId=PRO_0000055755.
FT ZN_FING 139 188 RING-type 1; atypical.
FT ZN_FING 208 270 IBR-type.
FT ZN_FING 297 326 RING-type 2.
FT COILED 369 400 Potential.
FT COILED 439 492 Potential.
FT COMPBIAS 4 75 Asp/Glu-rich (acidic).
FT COMPBIAS 22 29 Poly-Glu.
FT MOD_RES 353 353 Phosphoserine.
FT VARIANT 24 24 E -> K (in dbSNP:rs11507).
FT /FTId=VAR_054105.
FT VARIANT 29 29 E -> D (in dbSNP:rs34221642).
FT /FTId=VAR_054106.
FT MUTAGEN 158 158 H->A: Loss of effect in myelopoiesis.
FT MUTAGEN 161 161 C->A: Loss of effect in myelopoiesis.
FT CONFLICT 280 281 CA -> LQ (in Ref. 2; CAA10276).
SQ SEQUENCE 493 AA; 57819 MW; 30AFFDD327B51013 CRC64;
MSVDMNSQGS DSNEEDYDPN CEEEEEEEED DPGDIEDYYV GVASDVEQQG ADAFDPEEYQ
FTCLTYKESE GALNEHMTSL ASVLKVSHSV AKLILVNFHW QVSEILDRYK SNSAQLLVEA
RVQPNPSKHV PTSHPPHHCA VCMQFVRKEN LLSLACQHQF CRSCWEQHCS VLVKDGVGVG
VSCMAQDCPL RTPEDFVFPL LPNEELREKY RRYLFRDYVE SHYQLQLCPG ADCPMVIRVQ
EPRARRVQCN RCNEVFCFKC RQMYHAPTDC ATIRKWLTKC ADDSETANYI SAHTKDCPKC
NICIEKNGGC NHMQCSKCKH DFCWMCLGDW KTHGSEYYEC SRYKENPDIV NQSQQAQARE
ALKKYLFYFE RWENHNKSLQ LEAQTYQRIH EKIQERVMNN LGTWIDWQYL QNAAKLLAKC
RYTLQYTYPY AYYMESGPRK KLFEYQQAQL EAEIENLSWK VERADSYDRG DLENQMHIAE
QRRRTLLKDF HDT
//
ID ARI2_HUMAN Reviewed; 493 AA.
AC O95376; Q9HBZ6; Q9UEM9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=E3 ubiquitin-protein ligase ARIH2;
DE Short=ARI-2;
DE Short=Protein ariadne-2 homolog;
DE EC=6.3.2.-;
DE AltName: Full=Triad1 protein;
GN Name=ARIH2; Synonyms=ARI2, TRIAD1; ORFNames=HT005;
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].
RX PubMed=10422847;
RA van der Reijden B.A., Erpelinck-Verschueren C.A.J., Loewenberg B.,
RA Jansen J.H.;
RT "TRIADs: a new class of proteins with a novel cysteine-rich
RT signature.";
RL Protein Sci. 8:1557-1561(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10880484;
RA Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.;
RT "Ariadne-1: a vital Drosophila gene is required in development and
RT defines a new conserved family of ring-finger proteins.";
RL Genetics 155:1231-1244(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [5]
RP FUNCTION, INTERACTION WITH UBE2L3, SUBCELLULAR LOCATION,
RP UBIQUITINATION, MUTAGENESIS OF HIS-158 AND CYS-161, TISSUE
RP SPECIFICITY, AND INDUCTION BY ATRA.
RX PubMed=16118314; DOI=10.1182/blood-2005-04-1450;
RA Marteijn J.A., van Emst L., Erpelinck-Verschueren C.A., Nikoloski G.,
RA Menke A., de Witte T., Loewenberg B., Jansen J.H.,
RA van der Reijden B.A.;
RT "The E3 ubiquitin-protein ligase Triad1 inhibits clonogenic growth of
RT primary myeloid progenitor cells.";
RL Blood 106:4114-4123(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH GFI1 AND GFI1B.
RX PubMed=17646546; DOI=10.1182/blood-2006-11-058602;
RA Marteijn J.A., van der Meer L.T., van Emst L., van Reijmersdal S.,
RA Wissink W., de Witte T., Jansen J.H., Van der Reijden B.A.;
RT "Gfi1 ubiquitination and proteasomal degradation is inhibited by the
RT ubiquitin ligase Triad1.";
RL Blood 110:3128-3135(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP FUNCTION, INTERACTION WITH UBE2L3 AND UBE2N, AND SUBCELLULAR LOCATION.
RX PubMed=19340006; DOI=10.1038/leu.2009.57;
RA Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M.,
RA Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T.,
RA Sixma T.K., Jansen J.H., van der Reijden B.A.;
RT "The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and
RT Ubc13 interacting domains.";
RL Leukemia 23:1480-1489(2009).
RN [9]
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: E3 ubiquitin-protein ligase mediating 'Lys-48'-and 'Lys-
CC 63'-linked polyubiquitination and subsequent proteasomal
CC degradation of modified proteins. May play a role in myelopoiesis.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via RING-type 1) with UBE2L3. Interacts (via
CC RING-type 2) with UBE2N. Interacts (via RING-type 2) with GFI1B.
CC Interacts with GFI1; prevents its ubiquitination and proteasomal
CC degradation.
CC -!- INTERACTION:
CC P04637:TP53; NbExp=5; IntAct=EBI-711158, EBI-366083;
CC P68036:UBE2L3; NbExp=3; IntAct=EBI-711158, EBI-711173;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in
CC granulocytes.
CC -!- INDUCTION: Up-regulated by all-trans retinoic acid (ATRA). Up-
CC regulated during differentiation of immature blood cells toward
CC monocytes and granulocytes.
CC -!- DOMAIN: RING-type 1 and RING-type 2 are required for the
CC inhibitory function in myelopoiesis.
CC -!- PTM: Ubiquitinated. Ubiquitination promotes proteasomal
CC degradation.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09696.1; Type=Frameshift; Positions=Several;
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; AF099149; AAC82469.1; -; mRNA.
DR EMBL; AJ130978; CAA10276.1; -; mRNA.
DR EMBL; AF183427; AAG09696.1; ALT_FRAME; mRNA.
DR EMBL; BC000422; AAH00422.1; -; mRNA.
DR RefSeq; NP_006312.1; NM_006321.2.
DR RefSeq; XP_005264855.1; XM_005264798.1.
DR UniGene; Hs.633601; -.
DR ProteinModelPortal; O95376; -.
DR SMR; O95376; 61-492.
DR IntAct; O95376; 41.
DR MINT; MINT-1376284; -.
DR STRING; 9606.ENSP00000348769; -.
DR PhosphoSite; O95376; -.
DR PaxDb; O95376; -.
DR PRIDE; O95376; -.
DR DNASU; 10425; -.
DR Ensembl; ENST00000356401; ENSP00000348769; ENSG00000177479.
DR Ensembl; ENST00000449376; ENSP00000403222; ENSG00000177479.
DR GeneID; 10425; -.
DR KEGG; hsa:10425; -.
DR UCSC; uc003cvb.3; human.
DR CTD; 10425; -.
DR GeneCards; GC03P048931; -.
DR HGNC; HGNC:690; ARIH2.
DR MIM; 605615; gene.
DR neXtProt; NX_O95376; -.
DR PharmGKB; PA24983; -.
DR eggNOG; NOG327249; -.
DR HOGENOM; HOG000216611; -.
DR HOVERGEN; HBG018737; -.
DR InParanoid; O95376; -.
DR KO; K11969; -.
DR OMA; THPPHHC; -.
DR OrthoDB; EOG7CZK58; -.
DR PhylomeDB; O95376; -.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR ChiTaRS; ARIH2; human.
DR GeneWiki; ARIH2; -.
DR GenomeRNAi; 10425; -.
DR NextBio; 39512; -.
DR PRO; PR:O95376; -.
DR ArrayExpress; O95376; -.
DR Bgee; O95376; -.
DR CleanEx; HS_ARIH2; -.
DR Genevestigator; O95376; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0048588; P:developmental cell growth; IDA:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR002867; Znf_C6HC.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SMART; SM00343; ZnF_C2HC; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 493 E3 ubiquitin-protein ligase ARIH2.
FT /FTId=PRO_0000055755.
FT ZN_FING 139 188 RING-type 1; atypical.
FT ZN_FING 208 270 IBR-type.
FT ZN_FING 297 326 RING-type 2.
FT COILED 369 400 Potential.
FT COILED 439 492 Potential.
FT COMPBIAS 4 75 Asp/Glu-rich (acidic).
FT COMPBIAS 22 29 Poly-Glu.
FT MOD_RES 353 353 Phosphoserine.
FT VARIANT 24 24 E -> K (in dbSNP:rs11507).
FT /FTId=VAR_054105.
FT VARIANT 29 29 E -> D (in dbSNP:rs34221642).
FT /FTId=VAR_054106.
FT MUTAGEN 158 158 H->A: Loss of effect in myelopoiesis.
FT MUTAGEN 161 161 C->A: Loss of effect in myelopoiesis.
FT CONFLICT 280 281 CA -> LQ (in Ref. 2; CAA10276).
SQ SEQUENCE 493 AA; 57819 MW; 30AFFDD327B51013 CRC64;
MSVDMNSQGS DSNEEDYDPN CEEEEEEEED DPGDIEDYYV GVASDVEQQG ADAFDPEEYQ
FTCLTYKESE GALNEHMTSL ASVLKVSHSV AKLILVNFHW QVSEILDRYK SNSAQLLVEA
RVQPNPSKHV PTSHPPHHCA VCMQFVRKEN LLSLACQHQF CRSCWEQHCS VLVKDGVGVG
VSCMAQDCPL RTPEDFVFPL LPNEELREKY RRYLFRDYVE SHYQLQLCPG ADCPMVIRVQ
EPRARRVQCN RCNEVFCFKC RQMYHAPTDC ATIRKWLTKC ADDSETANYI SAHTKDCPKC
NICIEKNGGC NHMQCSKCKH DFCWMCLGDW KTHGSEYYEC SRYKENPDIV NQSQQAQARE
ALKKYLFYFE RWENHNKSLQ LEAQTYQRIH EKIQERVMNN LGTWIDWQYL QNAAKLLAKC
RYTLQYTYPY AYYMESGPRK KLFEYQQAQL EAEIENLSWK VERADSYDRG DLENQMHIAE
QRRRTLLKDF HDT
//
MIM
605615
*RECORD*
*FIELD* NO
605615
*FIELD* TI
*605615 ARIADNE, DROSOPHILA, HOMOLOG OF, 2; ARIH2
;;ARI2;;
TRIAD DOMAIN-CONTAINING PROTEIN 1; TRIAD1
read more*FIELD* TX
CLONING
Zinc-binding cysteine and histidine residues that form a 3-dimensional
structure, stabilized by zinc, are found in protein-interacting motifs
in LIM (e.g., LMO1; 186921), RING (e.g., RING1; 602045), or LAP (e.g.,
AF10; 602409) finger-containing proteins. Van der Reijden et al. (1999)
identified ARIH2, which they termed TRIAD1, a 493-amino acid nuclear
protein upregulated during retinoic acid-induced granulocytic
differentiation of acute promyelocytic leukemia cells. ARIH2 contains 2
RING fingers flanking a conserved cysteine-rich (C6HC) domain the
authors designated DRIL (double RING finger-linked domain); 2 C-terminal
coiled-coil domains; and an acidic N-terminal region. The DRIL domain
with its 2 flanking RING fingers, collectively referred to by the
authors as the TRIAD (2 RING fingers and DRIL) domain, spans
approximately 200 amino acids and was identified, with a preserved order
and distance, in more than 20 eukaryotic proteins.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ARIH2
gene to chromosome 3 (TMAP WI-11545).
*FIELD* RF
1. van der Reijden, B. A.; Erpelinck-Verschueren, C. A. J.; Lowenberg,
B.; Jansen, J. H.: TRIADs: a new class of proteins with a novel cysteine-rich
signature. Protein Sci. 8: 1557-1561, 1999.
*FIELD* CD
Paul J. Converse: 2/5/2001
*FIELD* ED
carol: 10/26/2009
mgross: 2/5/2001
*RECORD*
*FIELD* NO
605615
*FIELD* TI
*605615 ARIADNE, DROSOPHILA, HOMOLOG OF, 2; ARIH2
;;ARI2;;
TRIAD DOMAIN-CONTAINING PROTEIN 1; TRIAD1
read more*FIELD* TX
CLONING
Zinc-binding cysteine and histidine residues that form a 3-dimensional
structure, stabilized by zinc, are found in protein-interacting motifs
in LIM (e.g., LMO1; 186921), RING (e.g., RING1; 602045), or LAP (e.g.,
AF10; 602409) finger-containing proteins. Van der Reijden et al. (1999)
identified ARIH2, which they termed TRIAD1, a 493-amino acid nuclear
protein upregulated during retinoic acid-induced granulocytic
differentiation of acute promyelocytic leukemia cells. ARIH2 contains 2
RING fingers flanking a conserved cysteine-rich (C6HC) domain the
authors designated DRIL (double RING finger-linked domain); 2 C-terminal
coiled-coil domains; and an acidic N-terminal region. The DRIL domain
with its 2 flanking RING fingers, collectively referred to by the
authors as the TRIAD (2 RING fingers and DRIL) domain, spans
approximately 200 amino acids and was identified, with a preserved order
and distance, in more than 20 eukaryotic proteins.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ARIH2
gene to chromosome 3 (TMAP WI-11545).
*FIELD* RF
1. van der Reijden, B. A.; Erpelinck-Verschueren, C. A. J.; Lowenberg,
B.; Jansen, J. H.: TRIADs: a new class of proteins with a novel cysteine-rich
signature. Protein Sci. 8: 1557-1561, 1999.
*FIELD* CD
Paul J. Converse: 2/5/2001
*FIELD* ED
carol: 10/26/2009
mgross: 2/5/2001