ID   CYBP_MACFA              Reviewed;         228 AA.
AC   Q4R4P3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Calcyclin-binding protein;
DE            Short=CacyBP;
GN   Name=CACYBP; ORFNames=QtrA-13480;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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: Component of some large E3 complex at least composed of
CC       UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts directly with
CC       SIAH1, SIAH2 and SKP1 (By similarity). Interacts with protein of the
CC       S100 family S100A1, S100A6, S100B, S100P and S100A12 in a calcium-
CC       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}.
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; AB169851; BAE01932.1; -; mRNA.
DR   RefSeq; XP_005540108.1; XM_005540051.2.
DR   AlphaFoldDB; Q4R4P3; -.
DR   BMRB; Q4R4P3; -.
DR   SMR; Q4R4P3; -.
DR   STRING; 9541.XP_005540108.1; -.
DR   Ensembl; ENSMFAT00000074168; ENSMFAP00000052292; ENSMFAG00000000624.
DR   GeneID; 101867292; -.
DR   KEGG; mcf:101867292; -.
DR   CTD; 27101; -.
DR   VEuPathDB; HostDB:ENSMFAG00000000624; -.
DR   eggNOG; KOG3260; Eukaryota.
DR   GeneTree; ENSGT00390000016470; -.
DR   OMA; WDVLTSI; -.
DR   OrthoDB; 1181437at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000000624; Expressed in temporal lobe and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:InterPro.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT   CHAIN           2..228
FT                   /note="Calcyclin-binding protein"
FT                   /id="PRO_0000271390"
FT   DOMAIN          73..167
FT                   /note="CS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT   DOMAIN          168..228
FT                   /note="SGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT   REGION          2..80
FT                   /note="Interaction with SIAH1"
FT                   /evidence="ECO:0000250"
FT   REGION          73..228
FT                   /note="Interaction with SKP1"
FT                   /evidence="ECO:0000250"
FT   REGION          154..228
FT                   /note="Interaction with S100A6"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT   MOD_RES         85
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT   MOD_RES         118
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HB71"
SQ   SEQUENCE   228 AA;  26196 MW;  8E1322FB127CED42 CRC64;
     MASEELQKDL EEVKVLLEKA TRKRVRDALT AEKSKIETEI KNKMQQKSQK KAELLDNEKP
     AAVVAPITTG YTVKISNYGW DQSDKFVKIY ITLSGVHQVP TENVQVHFTE RSFDLLVKNL
     NGKSYSMIVN NLLKPISVEG SSKKVKTDTV LILCRKKVEN TRWDYLTQVE KECKEKEKPS
     YDTETDPSEG LMNVLKKIYE DGDDDMKRTI NKAWVESREK QAKGDTEF