ID   CYBP_PONAB              Reviewed;         228 AA.
AC   Q5R6Z8;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Calcyclin-binding protein;
DE            Short=CacyBP;
GN   Name=CACYBP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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: Interacts with protein of the S100 family S100A1, S100A6,
CC       S100B, S100P and S100A12 in a calcium-dependent manner. Component of
CC       some large E3 complex at least composed of UBE2D1, SIAH1, CACYBP/SIP,
CC       SKP1, APC and TBL1X. Interacts directly with SIAH1, SIAH2 and SKP1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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; CR860325; CAH92462.1; -; mRNA.
DR   RefSeq; NP_001127554.1; NM_001134082.1.
DR   AlphaFoldDB; Q5R6Z8; -.
DR   BMRB; Q5R6Z8; -.
DR   SMR; Q5R6Z8; -.
DR   STRING; 9601.ENSPPYP00000000558; -.
DR   GeneID; 100174632; -.
DR   KEGG; pon:100174632; -.
DR   CTD; 27101; -.
DR   eggNOG; KOG3260; Eukaryota.
DR   InParanoid; Q5R6Z8; -.
DR   OrthoDB; 1181437at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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_0000185391"
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;  26233 MW;  737833EA14B6EF94 CRC64;
     MASEELQKDL EEVKVLLEKA TRKRVRDALT AEKSKIETEI KNKMQQKSQK KAELLDNEKP
     AAVVAPITTG YTVKISNYGW DQSDKFVKIY ITLTGVHQVP TENVQVHFTE RSFDLLVKNL
     NGKSYSMIVN NLLKPISVEG SSKKVKTDTV LILCRKKVEN TRWDYLTQVE KERKEKEKPS
     YDAETDPSEG LMNVLKKIYE DGDDDMKRTI NKAWVESREK QAKGDTEF