CYBP_MOUSE
ID CYBP_MOUSE Reviewed; 229 AA.
AC Q9CXW3; O70140;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Calcyclin-binding protein;
DE Short=CacyBP;
DE AltName: Full=Siah-interacting protein;
GN Name=Cacybp; Synonyms=Sip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-22; 73-85 AND 222-229,
RP TISSUE SPECIFICITY, AND INTERACTION WITH S100A6.
RC TISSUE=Brain;
RX PubMed=9572262; DOI=10.1046/j.1471-4159.1998.70051793.x;
RA Filipek A., Kuznicki J.;
RT "Molecular cloning and expression of a mouse brain cDNA encoding a novel
RT protein target of calcyclin.";
RL J. Neurochem. 70:1793-1798(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP INTERACTION WITH S100A6.
RX PubMed=10884380; DOI=10.1074/jbc.m001622200;
RA Nowotny M., Bhattacharya S., Filipek A., Krezel A.M., Chazin W.,
RA Kuznicki J.;
RT "Characterization of the interaction of calcyclin (S100A6) and calcyclin-
RT binding protein.";
RL J. Biol. Chem. 275:31178-31182(2000).
RN [5]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=11927578; DOI=10.1074/jbc.m111010200;
RA Filipek A., Jastrzebska B., Nowotny M., Kwiatkowska K., Hetman M.,
RA Surmacz L., Wyroba E., Kuznicki J.;
RT "Ca2+-dependent translocation of the calcyclin-binding protein in neurons
RT and neuroblastoma NB-2a cells.";
RL J. Biol. Chem. 277:21103-21109(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP STRUCTURE BY NMR OF 1-77, INTERACTION WITH SKP1 AND S100A6, AND SUBUNIT.
RX PubMed=15996101; DOI=10.1021/bi0502689;
RA Bhattacharya S., Lee Y.-T., Michowski W., Jastrzebska B., Filipek A.,
RA Kuznicki J., Chazin W.J.;
RT "The modular structure of SIP facilitates its role in stabilizing
RT multiprotein assemblies.";
RL Biochemistry 44:9462-9471(2005).
RN [8]
RP STRUCTURE BY NMR OF 189-219 IN COMPLEX WITH S100A6, AND INTERACTION WITH
RP S100A6.
RX PubMed=18803400; DOI=10.1021/bi801233z;
RA Lee Y.-T., Dimitrova Y.N., Schneider G., Ridenour W.B., Bhattacharya S.,
RA Soss S.E., Caprioli R.M., Filipek A., Chazin W.J.;
RT "Structure of the S100A6 complex with a fragment from the C-terminal domain
RT of Siah-1 interacting protein: a novel mode for S100 protein target
RT recognition.";
RL Biochemistry 47:10921-10932(2008).
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 (By similarity).
CC Interacts with proteins of the S100 family S100A1, S100A6, S100B, S100P
CC and S100A12 in a calcium-dependent manner (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9CXW3; P14069: S100a6; NbExp=4; IntAct=EBI-767146, EBI-6478740;
CC Q9CXW3; P02639: S100A1; Xeno; NbExp=4; IntAct=EBI-767146, EBI-6477285;
CC Q9CXW3; P02638: S100B; Xeno; NbExp=4; IntAct=EBI-767146, EBI-458452;
CC Q9CXW3; P25815: S100P; Xeno; NbExp=2; IntAct=EBI-767146, EBI-743700;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11927578}. Cytoplasm
CC {ECO:0000269|PubMed:11927578}. Note=Cytoplasmic in unstimulated
CC cultured neurons. Upon increase of calcium, it localizes to a ring
CC around the nucleus. In neuroblastoma cells, after a Retinoic acid (RA)
CC induction and calcium increase, it localizes in both the nucleus and
CC cytoplasm. The nuclear and perinuclear fractions may be phosphorylated.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and EAT cells. Expressed
CC at low level in heart, muscle, and at very low level in the liver,
CC spleen, lung, kidney and stomach. {ECO:0000269|PubMed:9572262}.
CC -!- PTM: Phosphorylated on serine residues. Phosphorylated upon induction
CC by RA or at high calcium concentrations. {ECO:0000269|PubMed:11927578}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC16757.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U97327; AAC16757.1; ALT_INIT; mRNA.
DR EMBL; AK013924; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC025948; AAH25948.1; -; mRNA.
DR CCDS; CCDS15406.1; -.
DR RefSeq; NP_033916.1; NM_009786.2.
DR PDB; 1YSM; NMR; -; A=1-77.
DR PDB; 2JTT; NMR; -; C/D=189-219.
DR PDBsum; 1YSM; -.
DR PDBsum; 2JTT; -.
DR AlphaFoldDB; Q9CXW3; -.
DR BMRB; Q9CXW3; -.
DR SMR; Q9CXW3; -.
DR BioGRID; 198445; 27.
DR IntAct; Q9CXW3; 9.
DR MINT; Q9CXW3; -.
DR STRING; 10090.ENSMUSP00000014370; -.
DR iPTMnet; Q9CXW3; -.
DR PhosphoSitePlus; Q9CXW3; -.
DR SwissPalm; Q9CXW3; -.
DR REPRODUCTION-2DPAGE; Q9CXW3; -.
DR EPD; Q9CXW3; -.
DR jPOST; Q9CXW3; -.
DR MaxQB; Q9CXW3; -.
DR PaxDb; Q9CXW3; -.
DR PeptideAtlas; Q9CXW3; -.
DR PRIDE; Q9CXW3; -.
DR ProteomicsDB; 279307; -.
DR TopDownProteomics; Q9CXW3; -.
DR Antibodypedia; 20569; 378 antibodies from 35 providers.
DR DNASU; 12301; -.
DR Ensembl; ENSMUST00000014370; ENSMUSP00000014370; ENSMUSG00000014226.
DR GeneID; 12301; -.
DR KEGG; mmu:12301; -.
DR UCSC; uc007deg.2; mouse.
DR CTD; 27101; -.
DR MGI; MGI:1270839; Cacybp.
DR VEuPathDB; HostDB:ENSMUSG00000014226; -.
DR eggNOG; KOG3260; Eukaryota.
DR GeneTree; ENSGT00390000016470; -.
DR HOGENOM; CLU_081441_2_0_1; -.
DR InParanoid; Q9CXW3; -.
DR OMA; WDVLTSI; -.
DR OrthoDB; 1181437at2759; -.
DR PhylomeDB; Q9CXW3; -.
DR TreeFam; TF323891; -.
DR BioGRID-ORCS; 12301; 1 hit in 72 CRISPR screens.
DR EvolutionaryTrace; Q9CXW3; -.
DR PRO; PR:Q9CXW3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CXW3; protein.
DR Bgee; ENSMUSG00000014226; Expressed in 1st arch maxillary component and 273 other tissues.
DR ExpressionAtlas; Q9CXW3; baseline and differential.
DR Genevisible; Q9CXW3; MM.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IMP:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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; IPI:CAFA.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0060416; P:response to growth hormone; ISO:MGI.
DR CDD; cd06468; p23_CacyBP; 1.
DR DisProt; DP00226; -.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; 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_0000185390"
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..60
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 COMPBIAS 38..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT HELIX 2..21
FT /evidence="ECO:0007829|PDB:1YSM"
FT TURN 22..26
FT /evidence="ECO:0007829|PDB:1YSM"
FT HELIX 27..47
FT /evidence="ECO:0007829|PDB:1YSM"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:2JTT"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:2JTT"
SQ SEQUENCE 229 AA; 26510 MW; 2B04B54D0054ACE0 CRC64;
MASVLEELQK DLEEVKVLLE KSTRKRLRDT LTSEKSKIET ELKNKMQQKS QKKPELDNEK
PAAVVAPLTT GYTVKISNYG WDQSDKFVKI YITLTGVHQV PTENVQVHFT ERSFDLLVKN
LNGKNYSMIV NNLLKPISVE SSSKKVKTDT VIILCRKKAE NTRWDYLTQV EKECKEKEKP
SYDTEADPSE GLMNVLKKIY EDGDDDMKRT INKAWVESRE KQAREDTEF
