ID ASB11_MOUSE Reviewed; 323 AA.
AC Q9CQ31; A2AIH7; Q3UJ13; Q9D0V1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 154.
DE RecName: Full=Ankyrin repeat and SOCS box protein 11;
DE Short=ASB-11;
GN Name=Asb11;
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] (ISOFORM 1).
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Kidney, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex
CC which mediates the ubiquitination and subsequent proteasomal
CC degradation of target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CQ31-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQ31-2; Sequence=VSP_013946;
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; AF398972; AAK97494.1; -; mRNA.
DR EMBL; AK002412; BAB22080.1; -; mRNA.
DR EMBL; AK004396; BAB23286.1; -; mRNA.
DR EMBL; AK005404; BAB24004.1; -; mRNA.
DR EMBL; AK146664; BAE27342.1; -; mRNA.
DR EMBL; AL732475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064047; AAH64047.1; -; mRNA.
DR CCDS; CCDS30523.1; -. [Q9CQ31-2]
DR CCDS; CCDS85827.1; -. [Q9CQ31-1]
DR RefSeq; NP_001300666.1; NM_001313737.1. [Q9CQ31-1]
DR RefSeq; NP_081129.1; NM_026853.2. [Q9CQ31-2]
DR AlphaFoldDB; Q9CQ31; -.
DR SMR; Q9CQ31; -.
DR STRING; 10090.ENSMUSP00000044637; -.
DR iPTMnet; Q9CQ31; -.
DR PhosphoSitePlus; Q9CQ31; -.
DR PaxDb; 10090-ENSMUSP00000033755; -.
DR ProteomicsDB; 265113; -. [Q9CQ31-1]
DR ProteomicsDB; 265114; -. [Q9CQ31-2]
DR Antibodypedia; 353; 118 antibodies from 20 providers.
DR DNASU; 68854; -.
DR Ensembl; ENSMUST00000033755.6; ENSMUSP00000033755.6; ENSMUSG00000031382.15. [Q9CQ31-2]
DR Ensembl; ENSMUST00000036858.11; ENSMUSP00000044637.5; ENSMUSG00000031382.15. [Q9CQ31-1]
DR GeneID; 68854; -.
DR KEGG; mmu:68854; -.
DR UCSC; uc009uvq.1; mouse. [Q9CQ31-1]
DR UCSC; uc009uvr.1; mouse. [Q9CQ31-2]
DR AGR; MGI:1916104; -.
DR CTD; 140456; -.
DR MGI; MGI:1916104; Asb11.
DR VEuPathDB; HostDB:ENSMUSG00000031382; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000160592; -.
DR HOGENOM; CLU_000134_4_1_1; -.
DR InParanoid; Q9CQ31; -.
DR OMA; GRACHQV; -.
DR OrthoDB; 50291at2759; -.
DR PhylomeDB; Q9CQ31; -.
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; 68854; 0 hits in 62 CRISPR screens.
DR PRO; PR:Q9CQ31; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CQ31; Protein.
DR Bgee; ENSMUSG00000031382; Expressed in interventricular septum and 75 other cell types or tissues.
DR Genevisible; Q9CQ31; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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:SF14; ANKYRIN REPEAT AND SOCS BOX PROTEIN 11; 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 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..323
FT /note="Ankyrin repeat and SOCS box protein 11"
FT /id="PRO_0000066945"
FT REPEAT 64..93
FT /note="ANK 1"
FT REPEAT 97..126
FT /note="ANK 2"
FT REPEAT 130..159
FT /note="ANK 3"
FT REPEAT 162..191
FT /note="ANK 4"
FT REPEAT 195..224
FT /note="ANK 5"
FT REPEAT 227..256
FT /note="ANK 6"
FT REPEAT 260..289
FT /note="ANK 7"
FT DOMAIN 273..323
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT VAR_SEQ 1..60
FT /note="MEDAPAFYGFKNIFLTMFATFFFFKLLIKVFLALLTHFYIVKGNRKEAARIA
FT EEIYGGLS -> MLQLAGEEGVRRPGPWKEISFGDYICHTFQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013946"
SQ SEQUENCE 323 AA; 35331 MW; D1C0603CB7DBBB00 CRC64;
MEDAPAFYGF KNIFLTMFAT FFFFKLLIKV FLALLTHFYI VKGNRKEAAR IAEEIYGGLS
DCWADRSPLH EAAAQGRLLA LKTLIAQGIN VNLVTINRVS SLHEACLGGH VACAKALLEN
GAHVNAQTVH GATPLFNACC SGSAACVNVL LEFGAKAQLE IYLASPIHEA VKRGHRECME
ILLTKDVNIE QEVPQLGTPL YVACTYQRVD CVKKLLELGA SVDHGQWLDT PLHAAVRQSS
VEVINLLTVY GANLNLRNAQ GKSALDLAVP KSSVRQALLL HEGPPALSQL CRLCVRKCLG
RTCHHAIYAL GLPESLEKFL LYQ
//
