ASB2_BOVIN
ID ASB2_BOVIN Reviewed; 633 AA.
AC Q3SX45;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ankyrin repeat and SOCS box protein 2;
DE Short=ASB-2;
GN Name=ASB2 {ECO:0000250|UniProtKB:Q96Q27};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI04498.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI04498.1};
RC TISSUE=Uterus {ECO:0000312|EMBL:AAI04498.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BC104497; AAI04498.1; -; mRNA.
DR RefSeq; NP_001029841.1; NM_001034669.1.
DR AlphaFoldDB; Q3SX45; -.
DR SMR; Q3SX45; -.
DR STRING; 9913.ENSBTAP00000038371; -.
DR PaxDb; Q3SX45; -.
DR PRIDE; Q3SX45; -.
DR GeneID; 539244; -.
DR KEGG; bta:539244; -.
DR CTD; 51676; -.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q3SX45; -.
DR OrthoDB; 581716at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0014732; P:skeletal muscle atrophy; ISS:UniProtKB.
DR CDD; cd03721; SOCS_ASB2; 1.
DR Gene3D; 1.25.40.20; -; 2.
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; 3.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
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; 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..633
FT /note="Ankyrin repeat and SOCS box protein 2"
FT /id="PRO_0000233302"
FT DOMAIN 26..45
FT /note="UIM"
FT /evidence="ECO:0000305"
FT REPEAT 102..131
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 135..165
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 169..198
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 202..231
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 235..264
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 268..297
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 301..330
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 334..363
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 366..395
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 408..437
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT REPEAT 438..467
FT /note="ANK 11"
FT /evidence="ECO:0000255"
FT REPEAT 474..502
FT /note="ANK 12"
FT /evidence="ECO:0000255"
FT DOMAIN 579..633
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96Q27"
SQ SEQUENCE 633 AA; 70219 MW; C6CC2C400D9325C9 CRC64;
MATEISARGR PRAIGQEEYN LYSSLSEDEL VQMAIEQSLA DKTRGPTTTE TTVPTRVNRE
PAHFYPWTRS SVSPESALTS APKGLFQEVM QKYNRSKSSQ LAPVDPVLKA IKEDDEEALT
AMIKAGKNLS EPNKEGWLPL HEAAYYGQLN CLKALHRAYP AVIDQRTLQE ETALYLATCR
GHVDCLQFLL QAGAEPDISN KSRETPLYKA CERKNVEAVR ILVQYKADTN HRCNRGWTAL
HESVARNDLE VMEILVSGGA KVEAKNAYGI TPLFVAAQSG QLEALRFLAK YGADINTQAS
DSASALYEAC KNGHEEVVEF LLSQGADANK TNKDGMLPLH IASKKGNYRI VQMLLPVTSR
TRVRRSGISP LHLAAERNND EVLEALLGAR FDVNAPLAPE RARLYEDRRS SALYFAVVNN
NVYATELLLL AGADPNRDVI NPLLVAIRHG CLRTMQLLLD HGANIDAYIA THPTAFPATI
MFAMKCLSLL KFLMDLGCNG EPCFSCLYGN GPHPPAPPPS NRFNDAPASD KAPSAVQFCE
FLSAPEVSRW AGPIIDVLLD YVGNVQLCSR LKEHIDSFED WAVIKEKAEP PRPLAHLCRL
RVRKAIGKYR IKLLDTLPLP GRLIRYLKYE NTQ
