ID ASB9_MOUSE Reviewed; 290 AA.
AC Q91ZT8; Q6GT43; Q9DAF7;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Ankyrin repeat and SOCS box protein 9;
DE Short=ASB-9;
GN Name=Asb9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11509662; DOI=10.1128/mcb.21.18.6189-6197.2001;
RA Kile B.T., Metcalf D., Mifsud S., DiRago L., Nicola N.A., Hilton D.J.,
RA Alexander W.S.;
RT "Functional analysis of Asb-1 using genetic modification in mice.";
RL Mol. Cell. Biol. 21:6189-6197(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Substrate-recognition component of a SCF-like ECS (Elongin-
CC Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation of
CC target proteins. Recognizes at least two forms of creatine kinase, CKB
CC and CKMT1A (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin-protein ligase
CC complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC {ECO:0000305}.
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DR EMBL; AF398970; AAK97492.1; -; mRNA.
DR EMBL; AK005878; BAB24293.1; -; mRNA.
DR EMBL; AL772243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466571; EDL40751.1; -; Genomic_DNA.
DR EMBL; BC061038; AAH61038.1; -; mRNA.
DR CCDS; CCDS30524.1; -.
DR RefSeq; NP_081303.1; NM_027027.2.
DR AlphaFoldDB; Q91ZT8; -.
DR SMR; Q91ZT8; -.
DR BioGRID; 213344; 1.
DR STRING; 10090.ENSMUSP00000033756; -.
DR iPTMnet; Q91ZT8; -.
DR PhosphoSitePlus; Q91ZT8; -.
DR SwissPalm; Q91ZT8; -.
DR MaxQB; Q91ZT8; -.
DR PaxDb; 10090-ENSMUSP00000033756; -.
DR ProteomicsDB; 277044; -.
DR Antibodypedia; 502; 196 antibodies from 28 providers.
DR DNASU; 69299; -.
DR Ensembl; ENSMUST00000033756.3; ENSMUSP00000033756.3; ENSMUSG00000031384.3.
DR GeneID; 69299; -.
DR KEGG; mmu:69299; -.
DR UCSC; uc009uvs.1; mouse.
DR AGR; MGI:1916549; -.
DR CTD; 140462; -.
DR MGI; MGI:1916549; Asb9.
DR VEuPathDB; HostDB:ENSMUSG00000031384; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000157160; -.
DR HOGENOM; CLU_000134_4_0_1; -.
DR InParanoid; Q91ZT8; -.
DR OMA; QHHKITG; -.
DR OrthoDB; 50291at2759; -.
DR PhylomeDB; Q91ZT8; -.
DR TreeFam; TF331945; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 69299; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Asb9; mouse.
DR PRO; PR:Q91ZT8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q91ZT8; Protein.
DR Bgee; ENSMUSG00000031384; Expressed in spermatid and 31 other cell types or tissues.
DR Genevisible; Q91ZT8; MM.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.750.20; SOCS box; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR24136:SF17; ANKYRIN REPEAT AND SOCS BOX PROTEIN 9; 1.
DR PANTHER; PTHR24136; SOWAH (DROSOPHILA) HOMOLOG; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF158235; SOCS box-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Acetylation; ANK repeat; Mitochondrion; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..290
FT /note="Ankyrin repeat and SOCS box protein 9"
FT /id="PRO_0000066941"
FT REPEAT 31..60
FT /note="ANK 1"
FT REPEAT 64..93
FT /note="ANK 2"
FT REPEAT 97..126
FT /note="ANK 3"
FT REPEAT 129..158
FT /note="ANK 4"
FT REPEAT 162..191
FT /note="ANK 5"
FT REPEAT 194..223
FT /note="ANK 6"
FT DOMAIN 236..290
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 103
FT /note="Essential for binding to CKB"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96DX5"
FT CONFLICT 275
FT /note="S -> C (in Ref. 1; AAK97492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31656 MW; 52FB9A086951BB42 CRC64;
MDGEQRGRSD RPGGSPHLPF LSNPLMGDVV SDWSPLHDAA IHGCLLTLRN LISQGWPVNI
ITADHVSPLH EACLRGHLSC ASVLLSHGAQ VNGMTIDWRT PLFNACVSGS QDCVNLLLQH
GATPHPETEL ASPIHEAAKR GYVKCIESLA AHGANIDYNI SHLGTPLYVA CKNQQVACAK
KLLESGVSVN QGKGLDSPLH VVARMSSVEL VHLLMDFGAN AQAKNADGKR PVDLVPLESP
LIQIFLQNEG PQSLRQLCRL RIRKCFGIRQ HHKISELLLP EDLKRFLLHL
//
