CYBP_BOVIN
ID CYBP_BOVIN Reviewed; 230 AA.
AC Q3T168;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Calcyclin-binding protein;
DE Short=CacyBP;
GN Name=CACYBP;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in calcium-dependent ubiquitination and
CC subsequent proteasomal degradation of target proteins. Probably serves
CC as a molecular bridge in ubiquitin E3 complexes. Participates in the
CC ubiquitin-mediated degradation of beta-catenin (CTNNB1) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer or homodimer. Component of some large E3 complex at
CC least composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X.
CC Interacts directly with SIAH1, SIAH2 and SKP1. Interacts with proteins
CC of the S100 family S100A1, S100A6, S100B, S100P and S100A12 in a
CC calcium-dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine residues. Phosphorylated upon induction
CC by RA or at high calcium concentrations (By similarity). {ECO:0000250}.
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DR EMBL; BC102091; AAI02092.1; -; mRNA.
DR RefSeq; NP_001029981.1; NM_001034809.2.
DR AlphaFoldDB; Q3T168; -.
DR BMRB; Q3T168; -.
DR SMR; Q3T168; -.
DR STRING; 9913.ENSBTAP00000001464; -.
DR PaxDb; Q3T168; -.
DR PRIDE; Q3T168; -.
DR Ensembl; ENSBTAT00000001464; ENSBTAP00000001464; ENSBTAG00000001107.
DR GeneID; 618428; -.
DR KEGG; bta:618428; -.
DR CTD; 27101; -.
DR VEuPathDB; HostDB:ENSBTAG00000001107; -.
DR VGNC; VGNC:26693; CACYBP.
DR eggNOG; KOG3260; Eukaryota.
DR GeneTree; ENSGT00390000016470; -.
DR HOGENOM; CLU_081441_2_0_1; -.
DR InParanoid; Q3T168; -.
DR OMA; WDVLTSI; -.
DR OrthoDB; 1181437at2759; -.
DR TreeFam; TF323891; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000001107; Expressed in dorsal thalamus and 105 other tissues.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044548; F:S100 protein binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR CDD; cd06468; p23_CacyBP; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR037201; CacyBP_N.
DR InterPro; IPR037893; CS_CacyBP.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR015120; Siah-Interact_N.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR Pfam; PF09032; Siah-Interact_N; 1.
DR SUPFAM; SSF140106; SSF140106; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..230
FT /note="Calcyclin-binding protein"
FT /id="PRO_0000271389"
FT DOMAIN 75..169
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 170..230
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT REGION 1..82
FT /note="Interaction with SIAH1"
FT /evidence="ECO:0000250"
FT REGION 38..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..230
FT /note="Interaction with SKP1"
FT /evidence="ECO:0000250"
FT REGION 156..230
FT /note="Interaction with S100A6"
FT /evidence="ECO:0000250"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
SQ SEQUENCE 230 AA; 26332 MW; F0EF16DB553B1B5C CRC64;
MSSALEELQK DLEEVKVLLE KATRKRVRDA LTAEKSKIET EMKNKMQQKS QRKAELTENE
KPAAVVAPIT TGYTVKISNY GWDQSDKFVK IYITLPGVHQ VPAESVQVNF TERSFDLLVK
NLNGKSYSMI VNNLLKPISV EGSSKKVKTD TVLILCRKKA ENTRWDYLTQ VEKECKEKEK
PSYDTETDPS EGLMNVLKKI YEDGDDDMKR TINKAWVESR EKQAKGDTDF
