(data stored in ACNUC5371 zone)

HOGENOM: HS3_PE1770

ID   HS3_PE1770                           STANDARD;      PRT;   493 AA.
AC   HS3_PE1770; O95376; Q9HBZ6; Q9UEM9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=E3 ubiquitin-protein ligase ARIH2; Short=ARI-2;
DE   Short=Protein ariadne-2 homolog; EC=6.3.2 -;AltName: Full=Triad1 protein;
DE   (HS3.PE1770).
GN   Name=ARIH2; Synonyms=ARI2, TRIAD1; ORFNames=HT005;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS3.PE1770.
CC       Homo sapiens chromosome 3 GRCh37  sequence 1..197962430 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ARI2_HUMAN
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       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   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
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   -!- GENE_FAMILY: HOG000216611 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000177479;ENST00000356401;ENSP00000348769.
DR   EMBL; AC134028; - ;
DR   EMBL; AC137630; - ;
DR   EMBL; AF099149; - ;
DR   EMBL; AF183427; - ;
DR   EMBL; AJ130978; - ;
DR   EMBL; AK223550; - ;
DR   EMBL; AK313434; - ;
DR   EMBL; BC000422; - ;
DR   EMBL; CH471055; - ;
DR   EMBL; CR456785; - ;
DR   UniProtKB/Swiss-Prot; O95376; Q9HBZ6; Q9UEM9; -.
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   IPI; IPI00007304; -.
DR   RefSeq; NP_006312.1; NM_006321.2.
DR   UniGene; Hs.633601; -.
DR   ProteinModelPortal; O95376; -.
DR   SMR; O95376; 133-197, 203-271, 289-345.
DR   IntAct; O95376; 36.
DR   MINT; MINT-1376284; -.
DR   STRING; O95376; -.
DR   PhosphoSite; O95376; -.
DR   PRIDE; O95376; -.
DR   Ensembl; ENST00000356401; ENSP00000348769; ENSG00000177479.
DR   Ensembl; ENST00000449376; ENSP00000403222; ENSG00000177479.
DR   GeneID; 10425; -.
DR   KEGG; hsa:10425; -.
DR   UCSC; uc003cvb.1; human.
DR   CTD; 10425; -.
DR   GeneCards; GC03P048931; -.
DR   H-InvDB; HIX0021402; -.
DR   HGNC; HGNC:690; ARIH2.
DR   MIM; 605615; gene.
DR   neXtProt; NX_O95376; -.
DR   PharmGKB; PA24983; -.
DR   eggNOG; prNOG15549; -.
DR   InParanoid; O95376; -.
DR   OMA; KLILVHF; -.
DR   OrthoDB; EOG4ZCT49; -.
DR   PhylomeDB; O95376; -.
DR   Reactome; REACT_6900; Immune System.
DR   NextBio; 39512; -.
DR   ArrayExpress; O95376; -.
DR   Bgee; O95376; -.
DR   CleanEx; HS_ARIH2; -.
DR   Genevestigator; O95376; -.
DR   GermOnline; ENSG00000177479; Homo sapiens.
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:0005515; F:protein binding; IPI:UniProtKB.
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:hemopoietic 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   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   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
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.
DR   HOGENOMDNA; HS3.PE1770; -.
KW   ENSG000001774791755old_1320000031; ENSP000003487697901old_1320000031;
KW   C9JAU2_HUMAN; C9JBC5_HUMAN; C9JCL4_HUMAN; C9JZ71_HUMAN; Q53ET9_HUMAN;
KW   AC134028; AC137630; AF099149; AF183427; AJ130978; AK223550; AK313434;
KW   CH471055; CR456785;
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.
SQ   SEQUENCE   493 AA;  UNKNOWN MW;  UNKNOWN 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
//

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