(data stored in ACNUC5371 zone)

HOGENOM: MOUSE9_PE2111

ID   MOUSE9_PE2111                        STANDARD;      PRT;   492 AA.
AC   MOUSE9_PE2111; Q9Z1K6;
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
DE   protein;AltName: Full=UbcM4-interacting protein 48; (MOUSE9.PE2111).
GN   Name=Arih2; Synonyms=Ari2, Triad1, Uip48;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE9.PE2111.
CC       Mus musculus chromosome 9 NCBIM37  sequence 1..124076172 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ARI2_MOUSE
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       (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (via RING-type 2) with UBE2N. Interacts (via
CC       RING-type 2) with GFI1B. Interacts with GFI1; prevents its
CC       ubiquitination and proteasomal degradation (By similarity).
CC       Interacts (via RING-type 1) with UBE2L3.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (By similarity).
CC   -!- DOMAIN: RING-type 1 and RING-type 2 are required for the
CC       inhibitory function in myelopoiesis (By similarity).
CC   -!- PTM: Ubiquitinated. Ubiquitination promotes proteasomal
CC       degradation (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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   -!- GENE_FAMILY: HOG000216611 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000064145;ENSMUST00000013338;ENSMUSP00000013338.
DR   EMBL; AF124664; - ;
DR   EMBL; AJ130975; - ;
DR   EMBL; AK149936; - ;
DR   EMBL; AK167104; - ;
DR   EMBL; BC051998; - ;
DR   EMBL; BC052422; - ;
DR   EMBL; CH466560; - ;
DR   UniProtKB/Swiss-Prot; Q9Z1K6; -.
DR   EMBL; AF124664; AAD24573.1; -; mRNA.
DR   EMBL; AJ130975; CAA10273.1; -; mRNA.
DR   EMBL; BC051998; AAH51998.1; -; mRNA.
DR   EMBL; BC052422; AAH52422.1; -; mRNA.
DR   IPI; IPI00130237; -.
DR   RefSeq; NP_035920.1; NM_011790.4.
DR   UniGene; Mm.290447; -.
DR   ProteinModelPortal; Q9Z1K6; -.
DR   SMR; Q9Z1K6; 132-270, 288-344.
DR   STRING; Q9Z1K6; -.
DR   PhosphoSite; Q9Z1K6; -.
DR   PRIDE; Q9Z1K6; -.
DR   Ensembl; ENSMUST00000013338; ENSMUSP00000013338; ENSMUSG00000064145.
DR   GeneID; 23807; -.
DR   KEGG; mmu:23807; -.
DR   NMPDR; fig|10090.3.peg.20874; -.
DR   CTD; 10425; -.
DR   MGI; MGI:1344361; Arih2.
DR   GeneTree; ENSGT00600000084159; -.
DR   InParanoid; Q9Z1K6; -.
DR   OMA; KLILVHF; -.
DR   OrthoDB; EOG4ZCT49; -.
DR   PhylomeDB; Q9Z1K6; -.
DR   NextBio; 303437; -.
DR   ArrayExpress; Q9Z1K6; -.
DR   Bgee; Q9Z1K6; -.
DR   CleanEx; MM_ARIH2; -.
DR   Genevestigator; Q9Z1K6; -.
DR   GermOnline; ENSMUSG00000064145; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048588; P:developmental cell growth; ISS:UniProtKB.
DR   GO; GO:0071425; P:hemopoietic stem cell proliferation; ISS:UniProtKB.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS: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; MOUSE9.PE2111; -.
KW   ENSMUSG000000641455old_1320000031; ENSMUSP000000133381old_1320000031;
KW   Q3TK92_MOUSE; AF124664; AJ130975; AK149936; AK167104; BC051998; BC052422;
KW   CH466560;
KW   Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
SQ   SEQUENCE   492 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSVDMNSQGS DSNEEDYDPN CEEEEEEEED PGDIEDYYVG VASDVEQQGA DAFDPEEYQF
     TCLTYKESEG ALHEHMTSLA SVLKVSHSVA KLILVNFHWQ VSEILDRYRS NSAQLLVEAR
     VQPNPSKHVP TAHPPHHCAV CMQFVRKENL LSLACQHQFC RSCWEQHCSV LVKDGVGVGI
     SCMAQDCPLR TPEDFVFPLL PNEELRDKYR RYLFRDYVES HFQLQLCPGA DCPMVIRVQE
     PRARRVQCNR CSEVFCFKCR QMYHAPTDCA TIRKWLTKCA DDSETANYIS AHTKDCPKCN
     ICIEKNGGCN HMQCSKCKHD FCWMCLGDWK THGSEYYECS RYKENPDIVN QSQQAQAREA
     LKKYLFYFER WENHNKSLQL EAQTYERIHE KIQERVMNNL GTWIDWQYLQ NAAKLLAKCR
     YTLQYTYPYA YYMESGPRKK LFEYQQAQLE AEIENLSWKV ERADSYDRGD LENQMHIAEQ
     RRRTLLKDFH DT
//

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