ID CYBP_RAT Reviewed; 229 AA.
AC Q6AYK6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 24-JAN-2024, entry version 131.
DE RecName: Full=Calcyclin-binding protein;
DE Short=CacyBP;
GN Name=Cacybp;
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 TISSUE=Testis;
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).
RN [2]
RP PROTEIN SEQUENCE OF 38-43 AND 53-75, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH S100A1; S100A6; S100B; S100P AND S100A12.
RX PubMed=12042313; DOI=10.1074/jbc.m203602200;
RA Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.;
RT "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand
RT proteins of the S100 family.";
RL J. Biol. Chem. 277:28848-28852(2002).
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. {ECO:0000250, ECO:0000269|PubMed:12042313}.
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; BC079007; AAH79007.1; -; mRNA.
DR RefSeq; NP_001004208.1; NM_001004208.1.
DR AlphaFoldDB; Q6AYK6; -.
DR BMRB; Q6AYK6; -.
DR SMR; Q6AYK6; -.
DR STRING; 10116.ENSRNOP00000003586; -.
DR iPTMnet; Q6AYK6; -.
DR PhosphoSitePlus; Q6AYK6; -.
DR SwissPalm; Q6AYK6; -.
DR jPOST; Q6AYK6; -.
DR PaxDb; 10116-ENSRNOP00000003586; -.
DR Ensembl; ENSRNOT00000003586.6; ENSRNOP00000003586.3; ENSRNOG00000002572.6.
DR Ensembl; ENSRNOT00055030456; ENSRNOP00055024510; ENSRNOG00055017979.
DR Ensembl; ENSRNOT00060013523; ENSRNOP00060010301; ENSRNOG00060008165.
DR Ensembl; ENSRNOT00065032409; ENSRNOP00065025881; ENSRNOG00065019263.
DR GeneID; 289144; -.
DR KEGG; rno:289144; -.
DR UCSC; RGD:1303146; rat.
DR AGR; RGD:1303146; -.
DR CTD; 27101; -.
DR RGD; 1303146; Cacybp.
DR eggNOG; KOG3260; Eukaryota.
DR GeneTree; ENSGT00390000016470; -.
DR HOGENOM; CLU_081441_2_0_1; -.
DR InParanoid; Q6AYK6; -.
DR OrthoDB; 616630at2759; -.
DR PhylomeDB; Q6AYK6; -.
DR TreeFam; TF323891; -.
DR PRO; PR:Q6AYK6; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002572; Expressed in cerebellum and 19 other cell types or tissues.
DR ExpressionAtlas; Q6AYK6; baseline and differential.
DR Genevisible; Q6AYK6; RN.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISO:RGD.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005641; C:nuclear envelope lumen; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IDA:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; IEP:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:RGD.
DR GO; GO:0060416; P:response to growth hormone; IMP:RGD.
DR CDD; cd06468; p23_CacyBP; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 4.10.860.10; UVR domain; 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 PANTHER; PTHR13164:SF3; CALCYCLIN-BINDING PROTEIN; 1.
DR PANTHER; PTHR13164; CALICYLIN BINDING PROTEIN; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 1.
DR Pfam; PF09032; Siah-Interact_N; 1.
DR SUPFAM; SSF140106; Calcyclin-binding protein-like; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT CHAIN 2..229
FT /note="Calcyclin-binding protein"
FT /id="PRO_0000271391"
FT DOMAIN 74..168
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 169..229
FT /note="SGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00386"
FT REGION 2..81
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 74..229
FT /note="Interaction with SKP1"
FT /evidence="ECO:0000250"
FT REGION 155..229
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 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 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB71"
SQ SEQUENCE 229 AA; 26541 MW; E5158FA10314CC1B CRC64;
MASALEELQK DLEEVKVLLE KSTRKRLRDT LTNEKSKIET ELRNKMQQKS QKKPEFDNEK
PAAVVAPLTT GYTVKISNYG WDQSDKFVKI YITLTGVHQV PAENVQVHFT ERSFDLLVKN
LNGKNYSMIV NNLLKPISVE SSSKKVKTDT VIILCRKKAE NTRWDYLTQV EKECKEKEKP
SYDTEADPSE GLMNVLKKIY EDGDDDMKRT INKAWVESRE KQAREDTEF
//
