ASB10_MOUSE
ID ASB10_MOUSE Reviewed; 467 AA.
AC Q91ZT7; B2RUP6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ankyrin repeat and SOCS box protein 10;
DE Short=ASB-10;
GN Name=Asb10;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Skin;
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 MRNA].
RC TISSUE=Brain;
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF398971; AAK97493.1; -; mRNA.
DR EMBL; AK028538; BAC25997.1; -; mRNA.
DR EMBL; AK052929; BAC35206.1; -; mRNA.
DR EMBL; BC141311; AAI41312.1; -; mRNA.
DR EMBL; BC141313; AAI41314.1; -; mRNA.
DR CCDS; CCDS19124.1; -.
DR RefSeq; NP_001297405.1; NM_001310476.1.
DR RefSeq; NP_536692.1; NM_080444.5.
DR AlphaFoldDB; Q91ZT7; -.
DR SMR; Q91ZT7; -.
DR STRING; 10090.ENSMUSP00000041539; -.
DR PhosphoSitePlus; Q91ZT7; -.
DR PaxDb; Q91ZT7; -.
DR PRIDE; Q91ZT7; -.
DR ProteomicsDB; 281914; -.
DR Antibodypedia; 32988; 141 antibodies from 19 providers.
DR DNASU; 117590; -.
DR Ensembl; ENSMUST00000048302; ENSMUSP00000041539; ENSMUSG00000038204.
DR GeneID; 117590; -.
DR KEGG; mmu:117590; -.
DR UCSC; uc008wry.1; mouse.
DR CTD; 136371; -.
DR MGI; MGI:2152836; Asb10.
DR VEuPathDB; HostDB:ENSMUSG00000038204; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000158974; -.
DR HOGENOM; CLU_035721_0_0_1; -.
DR InParanoid; Q91ZT7; -.
DR OMA; LHLCQGA; -.
DR OrthoDB; 540084at2759; -.
DR PhylomeDB; Q91ZT7; -.
DR TreeFam; TF323921; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 117590; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q91ZT7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91ZT7; protein.
DR Bgee; ENSMUSG00000038204; Expressed in hindlimb stylopod muscle and 52 other tissues.
DR ExpressionAtlas; Q91ZT7; baseline and differential.
DR Genevisible; Q91ZT7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.20; -; 3.
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 Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00253; SOCS; 1.
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; 5.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..467
FT /note="Ankyrin repeat and SOCS box protein 10"
FT /id="PRO_0000066943"
FT REPEAT 115..144
FT /note="ANK 1"
FT REPEAT 147..176
FT /note="ANK 2"
FT REPEAT 180..209
FT /note="ANK 3"
FT REPEAT 214..243
FT /note="ANK 4"
FT REPEAT 247..289
FT /note="ANK 5"
FT REPEAT 293..322
FT /note="ANK 6"
FT REPEAT 326..361
FT /note="ANK 7"
FT DOMAIN 412..467
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
SQ SEQUENCE 467 AA; 51583 MW; 7DF5BCFDD2EAA4AF CRC64;
MLMSWSPEEC RDQGEPQGDR YSLCAKLVEK PDRGSEEHLE PGLGPIIIRS ASGPTLAFWQ
AVLVGDVGSV SRILSDSSTG LAPDSIFDTS DPERWRDYRF NIRALRLWSL TYEEELTTPL
HVAASRGHTE VLELLLRRRA KPDSAPGGRT ALHEACSAGH AACVRVLLVA GADPNTLDQD
GKRPLHLCRG PGILECVELL LKFGAQVDGR TEDEEETPLH IAARLGHVEL ADLLLRWGAC
PDVRNSEGWT PLLAACDIRC QSPKDAEATT NRCFQLCRLL LSVGADADAA NQDKQRPLHL
ACRHGHSAVV QLLLSCGVNA NAMDYGGHTP LHCALLGPTT AVAHSPEHTV RDLLNHGAVR
VWPGALPKVL DRWCMSPRTI EVLMNTYRVV QLPEEAKGLV PPEILQKYHG FYSSLFALVR
QPRSLQHLCR CALRSHLEGC LPHALPRLPL PPRMLRFLQL DFEDLLY
