ASB5_MOUSE
ID ASB5_MOUSE Reviewed; 329 AA.
AC Q9D1A4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ankyrin repeat and SOCS box protein 5;
DE Short=ASB-5;
GN Name=Asb5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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).
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. May play a role in the initiation of
CC arteriogenesis (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
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; AK003770; BAB22987.1; -; mRNA.
DR EMBL; AF398966; AAK97488.1; -; mRNA.
DR CCDS; CCDS22307.1; -.
DR RefSeq; NP_083845.1; NM_029569.3.
DR AlphaFoldDB; Q9D1A4; -.
DR SMR; Q9D1A4; -.
DR BioGRID; 218064; 1.
DR STRING; 10090.ENSMUSP00000033918; -.
DR PaxDb; Q9D1A4; -.
DR PRIDE; Q9D1A4; -.
DR ProteomicsDB; 283184; -.
DR Antibodypedia; 28653; 97 antibodies from 22 providers.
DR DNASU; 76294; -.
DR Ensembl; ENSMUST00000033918; ENSMUSP00000033918; ENSMUSG00000031519.
DR GeneID; 76294; -.
DR KEGG; mmu:76294; -.
DR UCSC; uc009lse.1; mouse.
DR CTD; 140458; -.
DR MGI; MGI:1923544; Asb5.
DR VEuPathDB; HostDB:ENSMUSG00000031519; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000159851; -.
DR HOGENOM; CLU_000134_4_1_1; -.
DR InParanoid; Q9D1A4; -.
DR OrthoDB; 1546307at2759; -.
DR PhylomeDB; Q9D1A4; -.
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; 76294; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Asb5; mouse.
DR PRO; PR:Q9D1A4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D1A4; protein.
DR Bgee; ENSMUSG00000031519; Expressed in intercostal muscle and 109 other tissues.
DR ExpressionAtlas; Q9D1A4; baseline and differential.
DR Genevisible; Q9D1A4; MM.
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 CDD; cd03724; SOCS_ASB5; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037328; ASB5_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF48403; SSF48403; 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 ANK repeat; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..329
FT /note="Ankyrin repeat and SOCS box protein 5"
FT /id="PRO_0000066931"
FT REPEAT 69..98
FT /note="ANK 1"
FT REPEAT 102..131
FT /note="ANK 2"
FT REPEAT 135..164
FT /note="ANK 3"
FT REPEAT 167..196
FT /note="ANK 4"
FT REPEAT 200..229
FT /note="ANK 5"
FT REPEAT 232..261
FT /note="ANK 6"
FT DOMAIN 278..329
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
SQ SEQUENCE 329 AA; 36282 MW; 7556C8A984A12BF3 CRC64;
MSVLEESRPF AQQLSNVYFT ILSLFCFKLF VKISLAILSH FYIVKGNRKE AARIAAEFYG
VSQGQGSWAD RSPLHEAASQ GRLLALRTLL SQGYNVNAVT IDHVTPLHEA CLGDHVACAR
TLLEAGANAN AITIDGVTPL FNACSQGSAS CAELLLEYGA KAQLESCFPS PTHEAASKGH
HECLDILIAW GIDVDQDIPH LGTPLYVACM SQQFHCIWKL LYAGADVHKG KYWDTPLHAA
AQQPSTEIVN LLLEFGADIN AKNTDLLRPV DLATSNSAVE RILLQHEATP SSLCQLCRLC
IRNYIGRQRF HLIPQLQLPT LLQNFLQYR
