ASB2_RAT
ID ASB2_RAT Reviewed; 634 AA.
AC Q5U2S6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ankyrin repeat and SOCS box protein 2;
DE Short=ASB-2;
GN Name=Asb2 {ECO:0000312|EMBL:AAH85882.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Heart;
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: 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 E2A and JAK2 (By similarity).
CC Required during embryonic heart development for complete heart looping
CC (By similarity). Required for cardiomyocyte differentiation (By
CC similarity). Involved in myogenic differentiation and targets filamin
CC FLNB for proteasomal degradation but not filamin FLNA (By similarity).
CC Also targets DES for proteasomal degradation (By similarity). Acts as a
CC negative regulator of skeletal muscle mass (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0L0, ECO:0000250|UniProtKB:Q96Q27}.
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 (By similarity). Interacts with DES (By
CC similarity). {ECO:0000250|UniProtKB:Q8K0L0,
CC ECO:0000250|UniProtKB:Q96Q27}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q96Q27}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q8K0L0}. Note=Localizes to the Z line in
CC cardiomyocytes. {ECO:0000250|UniProtKB:Q8K0L0}.
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: The UIM domain is required for monoubiquitination.
CC {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:Q96Q27}.
CC -!- SIMILARITY: Belongs to the ankyrin SOCS box (ASB) family.
CC {ECO:0000305}.
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DR EMBL; BC085882; AAH85882.1; -; mRNA.
DR RefSeq; NP_001011984.1; NM_001011984.1.
DR AlphaFoldDB; Q5U2S6; -.
DR SMR; Q5U2S6; -.
DR CORUM; Q5U2S6; -.
DR STRING; 10116.ENSRNOP00000012045; -.
DR PaxDb; Q5U2S6; -.
DR PRIDE; Q5U2S6; -.
DR Ensembl; ENSRNOT00000085517; ENSRNOP00000071182; ENSRNOG00000051619.
DR GeneID; 299266; -.
DR KEGG; rno:299266; -.
DR UCSC; RGD:1306414; rat.
DR CTD; 51676; -.
DR RGD; 1306414; Asb2.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000155490; -.
DR HOGENOM; CLU_023739_2_0_1; -.
DR InParanoid; Q5U2S6; -.
DR OMA; WTCIKEK; -.
DR OrthoDB; 581716at2759; -.
DR PhylomeDB; Q5U2S6; -.
DR TreeFam; TF315127; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5U2S6; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000051619; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q5U2S6; RN.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0097602; F:cullin family protein binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0055013; P:cardiac muscle cell development; ISS:UniProtKB.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0036336; P:dendritic cell migration; ISO:RGD.
DR GO; GO:0001947; P:heart looping; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0071800; P:podosome assembly; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:0014732; P:skeletal muscle atrophy; ISS:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR CDD; cd03721; SOCS_ASB2; 1.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037330; ASB2_SOCS.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
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; 1.
DR PROSITE; PS50088; ANK_REPEAT; 8.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..634
FT /note="Ankyrin repeat and SOCS box protein 2"
FT /id="PRO_0000233304"
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 35..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..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"
SQ SEQUENCE 634 AA; 70205 MW; CB4E89389609C199 CRC64;
MSTEISTRGR QRAIGHEEYS LYSSLSEEEL VQMAIEQSLA DKTRGPTPAE TSVSSQTNHQ
PGHIHPWTRS SSPPESPPAR APLGLFQGVM QKYSSNLFKT SQMAAMDPVL KAIKEGDEEA
LKAMIQDGKN LAEPNKEGWL PLHEAAYYGK LGCLKVLQRA YPGTIDQRTL QEETALYLAT
CREHLDCLLS LLQAGAEPDI SNKSRETPLY KACERKNAEA VRILVQYNAD ANHRCNRGWT
ALHESVSRND LEVMEILVSG GAKVEAKNVY SITPLFVAAQ SGQLEALRFL AKHGADINTQ
ASDSASALYE ACKNEHEDVV EFLLSQGADA NKANKDGLLP LHVASKKGNY RIVQMLLPVT
SRTRVRRSGI SPLHLAAERN HDAVLEALLA ARFDVNTPLA PERARLYEDR RTSALYFAVV
NNNVYATELL LLAGADPNRD VISPLLVAIR HGCLRTMQLL LDHGANIDAY IATHPTAFPA
TIMFAMKCLS LLKFLMDLGC DGEPCFSCLY GNGPHPPAPR SGRFNDAPVD DKAPSVVQFC
EFLSAPEVSR WAGPIIDVLL DYVGNVQLCS RLKEHIDSFE DWAVIKEKAE PPRPLAHLCR
LRVRKAIGKY RIKLLDTLPL PGRLIRYLKY ENTQ
