ASB2_MOUSE
ID ASB2_MOUSE Reviewed; 634 AA.
AC Q8K0L0; Q9CTH4; Q9WV73;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ankyrin repeat and SOCS box protein 2;
DE Short=ASB-2;
GN Name=Asb2 {ECO:0000312|EMBL:AAH31161.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAD38809.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAD38809.2};
RX PubMed=11111040; DOI=10.1016/s0378-1119(00)00402-9;
RA Kile B.T., Viney E.M., Willson T.A., Brodnicki T.C., Cancilla M.R.,
RA Herlihy A.S., Croker B.A., Baca M., Nicola N.A., Hilton D.J.,
RA Alexander W.S.;
RT "Cloning and characterization of the genes encoding the ankyrin repeat and
RT SOCS box-containing proteins Asb-1, Asb-2, Asb-3 and Asb-4.";
RL Gene 258:31-41(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH31161.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH31161.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH31161.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAB22862.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-634.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22862.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:16141072};
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 [4]
RP MUTAGENESIS OF LEU-595 (ISOFORM 1).
RX PubMed=19300455; DOI=10.1038/cdd.2009.27;
RA Bello N.F., Lamsoul I., Heuze M.L., Metais A., Moreaux G., Calderwood D.A.,
RA Duprez D., Moog-Lutz C., Lutz P.G.;
RT "The E3 ubiquitin ligase specificity subunit ASB2beta is a novel regulator
RT of muscle differentiation that targets filamin B to proteasomal
RT degradation.";
RL Cell Death Differ. 16:921-932(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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).
RN [6]
RP FUNCTION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2), DEVELOPMENTAL
RP STAGE (ISOFORM 2), AND DISRUPTION PHENOTYPE (ISOFORM 2).
RX PubMed=23632887; DOI=10.1182/blood-2012-11-466649;
RA Lamsoul I., Metais A., Gouot E., Heuze M.L., Lennon-Dumenil A.M.,
RA Moog-Lutz C., Lutz P.G.;
RT "ASB2alpha regulates migration of immature dendritic cells.";
RL Blood 122:533-541(2013).
RN [7]
RP FUNCTION (ISOFORM 1), INTERACTION WITH DES (ISOFORM 1), SUBCELLULAR
RP LOCATION (ISOFORM 1), AND MUTAGENESIS OF LEU-595 (ISOFORM 1).
RX PubMed=26343497; DOI=10.1016/j.yjmcc.2015.08.020;
RA Thottakara T., Friedrich F.W., Reischmann S., Braumann S., Schlossarek S.,
RA Kraemer E., Juhr D., Schlueter H., van der Velden J., Muench J., Patten M.,
RA Eschenhagen T., Moog-Lutz C., Carrier L.;
RT "The E3 ubiquitin ligase Asb2beta is downregulated in a mouse model of
RT hypertrophic cardiomyopathy and targets desmin for proteasomal
RT degradation.";
RL J. Mol. Cell. Cardiol. 87:214-224(2015).
RN [8]
RP FUNCTION (ISOFORM 1), AND INDUCTION.
RX PubMed=27182554; DOI=10.1172/jci.insight.85477;
RA Davey J.R., Watt K.I., Parker B.L., Chaudhuri R., Ryall J.G.,
RA Cunningham L., Qian H., Sartorelli V., Sandri M., Chamberlain J.,
RA James D.E., Gregorevic P.;
RT "Integrated expression analysis of muscle hypertrophy identifies Asb2 as a
RT negative regulator of muscle mass.";
RL JCI Insight 1:0-0(2016).
RN [9]
RP FUNCTION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2), DEVELOPMENTAL
RP STAGE (ISOFORMS 1 AND 2), AND DISRUPTION PHENOTYPE.
RX PubMed=29374072; DOI=10.1161/circresaha.117.312015;
RA Metais A., Lamsoul I., Melet A., Uttenweiler-Joseph S., Poincloux R.,
RA Stefanovic S., Valiere A., Gonzalez de Peredo A., Stella A.,
RA Burlet-Schiltz O., Zaffran S., Lutz P.G., Moog-Lutz C.;
RT "Asb2alpha-Filamin A Axis Is Essential for Actin Cytoskeleton Remodeling
RT During Heart Development.";
RL Circ. Res. 122:e34-e48(2018).
RN [10]
RP TISSUE SPECIFICITY (ISOFORM 2), AND DISRUPTION PHENOTYPE (ISOFORM 2).
RX PubMed=31175139; DOI=10.1158/2326-6066.cir-18-0562;
RA Spinner C.A., Lamsoul I., Metais A., Febrissy C., Moog-Lutz C., Lutz P.G.;
RT "The E3 Ubiquitin Ligase Asb2alpha in T Helper 2 Cells Negatively Regulates
RT Antitumor Immunity in Colorectal Cancer.";
RL Cancer Immunol. Res. 7:1332-1344(2019).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE (ISOFORM 1), AND
RP DISRUPTION PHENOTYPE.
RX PubMed=32179481; DOI=10.1016/j.isci.2020.100959;
RA Yamak A., Hu D., Mittal N., Buikema J.W., Ditta S., Lutz P.G.,
RA Moog-Lutz C., Ellinor P.T., Domian I.J.;
RT "Loss of Asb2 Impairs Cardiomyocyte Differentiation and Leads to Congenital
RT Double Outlet Right Ventricle.";
RL IScience 23:100959-100959(2020).
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 (By similarity). Mediates Notch-induced ubiquitination
CC and degradation of substrates including TCF3/E2A and JAK2 (By
CC similarity). Required during embryonic heart development for complete
CC heart looping (PubMed:32179481). Required for cardiomyocyte
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q96Q27,
CC ECO:0000269|PubMed:32179481}.
CC -!- FUNCTION: [Isoform 1]: Involved in myogenic differentiation and targets
CC filamin FLNB for proteasomal degradation but not filamin FLNA
CC (PubMed:26343497). Also targets DES for proteasomal degradation
CC (PubMed:26343497). Acts as a negative regulator of skeletal muscle mass
CC (PubMed:27182554). {ECO:0000269|PubMed:26343497,
CC ECO:0000269|PubMed:27182554}.
CC -!- FUNCTION: [Isoform 2]: Targets filamins FLNA and FLNB for proteasomal
CC degradation (PubMed:23632887). This leads to enhanced adhesion of
CC hematopoietic cells to fibronectin (By similarity). Required for FLNA
CC degradation in immature cardiomyocytes which is necessary for actin
CC cytoskeleton remodeling, leading to proper organization of myofibrils
CC and function of mature cardiomyocytes (PubMed:29374072). Required for
CC degradation of FLNA and FLNB in immature dendritic cells (DC) which
CC enhances immature DC migration by promoting DC podosome formation and
CC DC-mediated degradation of the extracellular matrix (PubMed:23632887).
CC Does not promote proteasomal degradation of tyrosine-protein kinases
CC JAK1 or JAK2 in hematopoietic cells (By similarity).
CC {ECO:0000250|UniProtKB:Q96Q27, ECO:0000269|PubMed:23632887,
CC ECO:0000269|PubMed:29374072}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of a probable ECS E3 ubiquitin-protein ligase
CC complex which contains CUL5, either RBX1 or RNF7/RBX2, Elongin BC
CC complex (ELOB and ELOC) and ASB2. Interacts with SKP2. Through its
CC interaction with SKP2, likely to bridge the formation of dimeric E3-
CC ubiquitin-protein ligase complexes composed of an ECS complex and an
CC SCF(SKP2) complex. Interacts with JAK2; the interaction targets JAK2
CC for Notch-mediated proteasomal degradation. Interacts with TCF3/E2A;
CC the interaction is mediated by SKP2 and targets TCF3 for Notch-mediated
CC proteasomal degradation. {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with DES.
CC {ECO:0000269|PubMed:26343497}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000269|PubMed:26343497}. Note=Localizes to the Z line in
CC cardiomyocytes. {ECO:0000269|PubMed:26343497}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334}; Synonyms=ASB2beta
CC {ECO:0000303|PubMed:23632887};
CC IsoId=Q8K0L0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11111040}; Synonyms=ASB2alpha
CC {ECO:0000303|PubMed:23632887};
CC IsoId=Q8K0L0-2; Sequence=VSP_052025, VSP_052026;
CC -!- TISSUE SPECIFICITY: Highest expression in muscle, heart and spleen
CC (PubMed:11111040). Highly expressed in cells of the first and second
CC heart fields in the developing embryonic heart (PubMed:32179481). At
CC 9.5 dpc, robust expression predominantly in the left and right
CC ventricles (RV) and to a lower extent in inflow and outflow tracts
CC (PubMed:32179481). At 10.5 and 11.5 dpc, expression is restricted to
CC the myocardium with no expression observed in the endocardium
CC (PubMed:32179481). {ECO:0000269|PubMed:11111040,
CC ECO:0000269|PubMed:32179481}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Not expressed in immature dendritic
CC cells (PubMed:23632887). Highly expressed in adult skeletal muscle with
CC very low levels in adult bone marrow (PubMed:29374072).
CC {ECO:0000269|PubMed:23632887, ECO:0000269|PubMed:29374072}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in immature dendritic cells
CC and in primary dendritic cells derived from the spleen
CC (PubMed:23632887). Highly expressed in adult bone marrow with
CC negligible levels in adult skeletal muscle (PubMed:29374072). Expressed
CC at higher levels in T helper type 2 (Th2) cells than in regulatory T
CC (Treg) cells, type 1 helper T (Th1) cells and T helper 17 (Th17) cells
CC (PubMed:31175139). {ECO:0000269|PubMed:23632887,
CC ECO:0000269|PubMed:29374072, ECO:0000269|PubMed:31175139}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 1]: Very low levels found in the
CC developing heart at 9.5 dpc when isoform 2 is the predominant isoform
CC (PubMed:29374072, PubMed:32179481). Expression increases from 11.5 dpc
CC and is the predominant isoform in adult heart (PubMed:29374072,
CC PubMed:32179481). {ECO:0000269|PubMed:29374072,
CC ECO:0000269|PubMed:32179481}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Barely detectable in bone marrow
CC cells but levels progressively increase as cells differentiate into
CC immature dendritic cells and are down-regulated after dendritic cell
CC maturation (PubMed:23632887). Highly expressed in the developing heart
CC at 9.5 dpc when isoform 1 levels are very low (PubMed:29374072). Levels
CC increase up to 11.5 dpc and fall in the adult heart (PubMed:29374072).
CC {ECO:0000269|PubMed:23632887, ECO:0000269|PubMed:29374072}.
CC -!- INDUCTION: Repressed by FST in 6-month-old mice but no effect is seen
CC in 24-month-old mice (PubMed:27182554). Expression is increased 4-fold
CC 3 days after denervation, becomes suppressed by approximately 75% 7
CC days after denervation, and eventually resolves to baseline by 28 days
CC after denervation (PubMed:27182554). {ECO:0000269|PubMed:27182554}.
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|UniProtKB:Q96Q27}.
CC -!- DOMAIN: [Isoform 2]: Both the N-terminus and ANK repeats 1 to 10 are
CC necessary for interaction with filamins.
CC {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- DOMAIN: [Isoform 1]: The UIM domain is required for monoubiquitination.
CC {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- PTM: [Isoform 1]: Monoubiquitinated. {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- PTM: [Isoform 2]: Not monoubiquitinated.
CC {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- PTM: [Isoform 2]: Phosphorylation at Ser-371 is required for
CC association with FLNA and subsequent FLNA degradation.
CC {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality with death occurring in utero
CC around 9.5 dpc (PubMed:29374072). Embryos display defects in vascular
CC development and hematopoiesis and increased protein levels of Flna in
CC the heart (PubMed:29374072). Conditional knockout in the whole heart
CC and in the first heart field results in pericardial edema and embryonic
CC lethality (PubMed:32179481). Conditional knockout in the embryonic
CC heart results in impaired heart looping, abnormal expression of Flna
CC expression which is expanded to include the myocardial layer and
CC increased expression of Smad2 (PubMed:32179481).
CC {ECO:0000269|PubMed:29374072, ECO:0000269|PubMed:32179481}.
CC -!- DISRUPTION PHENOTYPE: [Isoform 2]: Conditional knockout in
CC hematopoietic stem and progenitor cells results in increased protein
CC levels of Flna and Flnb in immature dendritic cells (PubMed:23632887).
CC Conditional knockout in hematopoietic cells reduces tumor development
CC in a mouse model of colitis-associated tumorigenesis with reduced
CC numbers of T helper type 2 (Th2) cells and regulatory T (Treg) cells
CC and increased numbers of type 1 helper T (Th1) cells and T helper 17
CC (Th17) cells in the colonic mucosa of tumor-bearing mice
CC (PubMed:31175139). {ECO:0000269|PubMed:23632887,
CC ECO:0000269|PubMed:31175139}.
CC -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38809.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF155353; AAD38809.2; ALT_INIT; mRNA.
DR EMBL; BC031161; AAH31161.1; -; mRNA.
DR EMBL; AK003566; BAB22862.1; -; mRNA.
DR CCDS; CCDS26128.1; -. [Q8K0L0-1]
DR CCDS; CCDS88394.1; -. [Q8K0L0-2]
DR RefSeq; NP_075536.1; NM_023049.1. [Q8K0L0-1]
DR AlphaFoldDB; Q8K0L0; -.
DR SMR; Q8K0L0; -.
DR BioGRID; 211145; 2.
DR IntAct; Q8K0L0; 1.
DR STRING; 10090.ENSMUSP00000021617; -.
DR iPTMnet; Q8K0L0; -.
DR PhosphoSitePlus; Q8K0L0; -.
DR EPD; Q8K0L0; -.
DR MaxQB; Q8K0L0; -.
DR PaxDb; Q8K0L0; -.
DR PRIDE; Q8K0L0; -.
DR ProteomicsDB; 281915; -. [Q8K0L0-1]
DR ProteomicsDB; 281916; -. [Q8K0L0-2]
DR Antibodypedia; 16; 192 antibodies from 25 providers.
DR DNASU; 65256; -.
DR Ensembl; ENSMUST00000021617; ENSMUSP00000021617; ENSMUSG00000021200. [Q8K0L0-1]
DR Ensembl; ENSMUST00000149431; ENSMUSP00000117595; ENSMUSG00000021200. [Q8K0L0-2]
DR GeneID; 65256; -.
DR UCSC; uc007ovc.1; mouse. [Q8K0L0-1]
DR UCSC; uc007ovd.1; mouse. [Q8K0L0-2]
DR CTD; 51676; -.
DR MGI; MGI:1929743; Asb2.
DR VEuPathDB; HostDB:ENSMUSG00000021200; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000155490; -.
DR HOGENOM; CLU_023739_2_0_1; -.
DR InParanoid; Q8K0L0; -.
DR OMA; WTCIKEK; -.
DR OrthoDB; 581716at2759; -.
DR PhylomeDB; Q8K0L0; -.
DR TreeFam; TF315127; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 65256; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q8K0L0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8K0L0; protein.
DR Bgee; ENSMUSG00000021200; Expressed in knee joint and 124 other tissues.
DR Genevisible; Q8K0L0; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0097602; F:cullin family protein binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:UniProtKB.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0036336; P:dendritic cell migration; IDA:UniProtKB.
DR GO; GO:0001947; P:heart looping; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0071800; P:podosome assembly; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0014732; P:skeletal muscle atrophy; IMP:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
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 InterPro; IPR003903; UIM_dom.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 11.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 7.
DR PROSITE; PS50088; ANK_REPEAT; 8.
DR PROSITE; PS50225; SOCS; 1.
DR PROSITE; PS50330; UIM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..634
FT /note="Ankyrin repeat and SOCS box protein 2"
FT /id="PRO_0000233303"
FT DOMAIN 26..45
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REPEAT 104..133
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 137..167
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 171..200
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 204..233
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 237..266
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 270..299
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 303..332
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 336..365
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 368..397
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 410..439
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT REPEAT 440..469
FT /note="ANK 11"
FT /evidence="ECO:0000255"
FT REPEAT 476..504
FT /note="ANK 12"
FT /evidence="ECO:0000255"
FT DOMAIN 580..634
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 36..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q27"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11111040"
FT /id="VSP_052025"
FT VAR_SEQ 49..68
FT /note="AEASASSQTNHQPGHFHPWT -> MTRFSYAEYFALFHSGSAPS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11111040"
FT /id="VSP_052026"
FT MUTAGEN 595
FT /note="L->A: Loss of E3 ubiquitin-protein ligase complex
FT association and loss of activity of the complex. Does not
FT affect localization of isoform 1 to the Z line or its
FT interaction with DES."
FT /evidence="ECO:0000269|PubMed:19300455,
FT ECO:0000269|PubMed:26343497"
FT CONFLICT 72..73
FT /note="SS -> LF (in Ref. 1; AAD38809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 70221 MW; E320CEBD39891D41 CRC64;
MATEISTRGR QRAIGHEEYS LYSSLSEEEL LQMAIEQSLA DKTRGPTPAE ASASSQTNHQ
PGHFHPWTRS PSSPENPPAR APLGLFQGVM QKYSSNLFKT SQMAAMDPVL KAIKEGDEEA
LKIMIQDGKN LAEPNKEGWL PLHEAAYYGQ LGCLKVLQQA YPGTIDQRTL QEETALYLAT
CREHLDCLLS LLQAGAEPDI SNKSRETPLY KACERKNAEA VRILVRYNAD ANHRCNRGWT
ALHESVSRND LEVMEILVSG GAKVEAKNVY SITPLFVAAQ SGQLEALRFL AKHGADINTQ
ASDSASALYE ASKNEHEDVV EFLLSQGADA NKANKDGLLP LHVASKKGNY RIVQMLLPVT
SRTRVRRSGI SPLHLAAERN HDAVLEALLA ARFDVNAPLA PERARLYEDR RSSALYFAVV
NNNVYATELL LLAGADPNRD VISPLLVAIR HGCLRTMQLL LDHGANIDAY IATHPTAFPA
TIMFAMKCLS LLKFLMDLGC DGEPCFSCLY GNGPHPPAPR PGRFHDAPVD DKAPSVVQFC
EFLSAPEVSR WAGPIIDVLL DYVGNVQLCS RLKEHIDSFE DWAVIKEKAE PPRPLAHLCR
LRVRKAIGKY RIKLLDTLPL PGRLIRYLKY ENTQ
