CYBP_HUMAN
ID CYBP_HUMAN Reviewed; 228 AA.
AC Q9HB71; B2ZWH2; B3KSF1; O60666; Q5R370; Q5R371;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Calcyclin-binding protein;
DE Short=CacyBP;
DE Short=hCacyBP;
DE AltName: Full=S100A6-binding protein;
DE AltName: Full=Siah-interacting protein;
GN Name=CACYBP; Synonyms=S100A6BP, SIP; ORFNames=PNAS-107;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=12006993;
RA Liu W.X., Wu J., Zhao Z., Zhou Y., Peng X.Z., Yuan J.G., Qiang B.Q.;
RT "Cloning and expression of human calcyclin binding protein (hCacyBP)
RT gene.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:181-186(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Petersen S., Schluens K., Dietel M., Petersen I.;
RT "Amplification and overexpression of the gene encoding the human calcyclin
RT binding protein on chromosome 1q24-q25 in advanced lung carcinomas.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Rhodes S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human growth inhibition gene 5 (GIG5).";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Skeletal muscle, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Skin;
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 [10]
RP PROTEIN SEQUENCE OF 2-14; 34-41; 112-118 AND 124-143, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 2-19 AND 112-118, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (MAR-2008) to UniProtKB.
RN [12]
RP ALTERNATIVE SPLICING (ISOFORM 2), SUBUNIT OF A COMPLEX WITH UBE2D1; SIAH1;
RP SKP1; APC AND TBL1X, AND INTERACTION WITH SIAH1; SIAH2 AND SKP1.
RX PubMed=11389839; DOI=10.1016/s1097-2765(01)00242-8;
RA Matsuzawa S., Reed J.C.;
RT "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
RT degradation linked to p53 responses.";
RL Mol. Cell 7:915-926(2001).
RN [13]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12895292; DOI=10.5483/bmbrep.2003.36.4.354;
RA Wu J., Tan X., Peng X.Z., Yuan J.G., Qiang B.Q.;
RT "Translocation and phosphorylation of calcyclin binding protein during
RT retinoic acid-induced neuronal differentiation of neuroblastoma SH-SY5Y
RT cells.";
RL J. Biochem. Mol. Biol. 36:354-358(2003).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-19; LYS-85 AND LYS-118,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-34, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 1-70, SUBUNIT, MUTAGENESIS OF
RP 23-LYS--ARG-26; VAL-64 AND PRO-66, FUNCTION, AND INTERACTION WITH SIAH1.
RX PubMed=16085652; DOI=10.1074/jbc.m506707200;
RA Santelli E., Leone M., Li C., Fukushima T., Preece N.E., Olson A.J.,
RA Ely K.R., Reed J.C., Pellecchia M., Liddington R.C., Matsuzawa S.;
RT "Structural analysis of Siah1-Siah-interacting protein interactions and
RT insights into the assembly of an E3 ligase multiprotein complex.";
RL J. Biol. Chem. 280:34278-34287(2005).
RN [23]
RP STRUCTURE BY NMR OF 63-176.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the core domain of calcyclin binding protein; SIAH-
RT interacting protein (SIP).";
RL Submitted (NOV-2005) to the PDB data bank.
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).
CC {ECO:0000269|PubMed:16085652}.
CC -!- SUBUNIT: Homodimer. Interacts with proteins of the S100 family S100A1,
CC S100A6, S100B, S100P and S100A12 in a calcium-dependent manner (By
CC similarity). 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. {ECO:0000250, ECO:0000269|PubMed:11389839,
CC ECO:0000269|PubMed:16085652}.
CC -!- INTERACTION:
CC Q9HB71; P04626: ERBB2; NbExp=2; IntAct=EBI-1047302, EBI-641062;
CC Q9HB71; P26447: S100A4; NbExp=2; IntAct=EBI-1047302, EBI-717058;
CC Q9HB71; P33763: S100A5; NbExp=3; IntAct=EBI-1047302, EBI-7211732;
CC Q9HB71; P06703: S100A6; NbExp=2; IntAct=EBI-1047302, EBI-352877;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12895292}. Cytoplasm
CC {ECO:0000269|PubMed:12895292}. Note=Cytoplasmic at low calcium
CC concentrations. In neuroblastoma cells, after a retinoic acid (RA)
CC induction and calcium increase, it localizes in both the nucleus and
CC cytoplasm. The nuclear fraction may be phosphorylated.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HB71-1; Sequence=Displayed;
CC Name=2; Synonyms=SIP-S, S;
CC IsoId=Q9HB71-2; Sequence=VSP_010171, VSP_010172;
CC Name=3;
CC IsoId=Q9HB71-3; Sequence=VSP_046862;
CC -!- PTM: Phosphorylated on serine residues. Phosphorylated upon induction
CC by RA or at high calcium concentrations. {ECO:0000269|PubMed:12895292}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23817.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG52713.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF057356; AAC21458.1; -; mRNA.
DR EMBL; AF314752; AAG34170.1; -; mRNA.
DR EMBL; AL035305; CAA22910.1; -; mRNA.
DR EMBL; AF275803; AAG23817.1; ALT_FRAME; mRNA.
DR EMBL; AY423723; AAS00486.1; -; mRNA.
DR EMBL; AK093425; BAG52713.1; ALT_FRAME; mRNA.
DR EMBL; AK313278; BAG36086.1; -; mRNA.
DR EMBL; Z99127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90982.1; -; Genomic_DNA.
DR EMBL; BC005975; AAH05975.1; -; mRNA.
DR EMBL; BC022352; AAH22352.1; -; mRNA.
DR EMBL; BC078151; AAH78151.1; -; mRNA.
DR CCDS; CCDS1315.1; -. [Q9HB71-1]
DR CCDS; CCDS30942.1; -. [Q9HB71-3]
DR RefSeq; NP_001007215.1; NM_001007214.1. [Q9HB71-3]
DR RefSeq; NP_055227.1; NM_014412.2. [Q9HB71-1]
DR RefSeq; XP_016856535.1; XM_017001046.1. [Q9HB71-3]
DR PDB; 1X5M; NMR; -; A=63-176.
DR PDB; 2A25; X-ray; 2.20 A; B=58-70.
DR PDB; 2A26; X-ray; 1.20 A; A/B/C=1-47.
DR PDBsum; 1X5M; -.
DR PDBsum; 2A25; -.
DR PDBsum; 2A26; -.
DR AlphaFoldDB; Q9HB71; -.
DR SMR; Q9HB71; -.
DR BioGRID; 118001; 162.
DR CORUM; Q9HB71; -.
DR ELM; Q9HB71; -.
DR IntAct; Q9HB71; 135.
DR MINT; Q9HB71; -.
DR STRING; 9606.ENSP00000356652; -.
DR ChEMBL; CHEMBL4295948; -.
DR GlyGen; Q9HB71; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HB71; -.
DR MetOSite; Q9HB71; -.
DR PhosphoSitePlus; Q9HB71; -.
DR SwissPalm; Q9HB71; -.
DR BioMuta; CACYBP; -.
DR DMDM; 46576651; -.
DR UCD-2DPAGE; Q9HB71; -.
DR CPTAC; CPTAC-321; -.
DR CPTAC; CPTAC-322; -.
DR EPD; Q9HB71; -.
DR jPOST; Q9HB71; -.
DR MassIVE; Q9HB71; -.
DR MaxQB; Q9HB71; -.
DR PaxDb; Q9HB71; -.
DR PeptideAtlas; Q9HB71; -.
DR PRIDE; Q9HB71; -.
DR ProteomicsDB; 3636; -.
DR ProteomicsDB; 63708; -.
DR ProteomicsDB; 81499; -. [Q9HB71-1]
DR ProteomicsDB; 81500; -. [Q9HB71-2]
DR TopDownProteomics; Q9HB71-1; -. [Q9HB71-1]
DR Antibodypedia; 20569; 378 antibodies from 35 providers.
DR DNASU; 27101; -.
DR Ensembl; ENST00000367679.7; ENSP00000356652.2; ENSG00000116161.18. [Q9HB71-1]
DR Ensembl; ENST00000405362.1; ENSP00000385771.1; ENSG00000116161.18. [Q9HB71-3]
DR Ensembl; ENST00000406752.1; ENSP00000384139.1; ENSG00000116161.18. [Q9HB71-2]
DR Ensembl; ENST00000613570.4; ENSP00000479414.1; ENSG00000116161.18. [Q9HB71-3]
DR GeneID; 27101; -.
DR KEGG; hsa:27101; -.
DR MANE-Select; ENST00000367679.7; ENSP00000356652.2; NM_014412.3; NP_055227.1.
DR UCSC; uc001gki.2; human. [Q9HB71-1]
DR CTD; 27101; -.
DR DisGeNET; 27101; -.
DR GeneCards; CACYBP; -.
DR HGNC; HGNC:30423; CACYBP.
DR HPA; ENSG00000116161; Tissue enhanced (brain).
DR MIM; 606186; gene.
DR neXtProt; NX_Q9HB71; -.
DR OpenTargets; ENSG00000116161; -.
DR PharmGKB; PA134894213; -.
DR VEuPathDB; HostDB:ENSG00000116161; -.
DR eggNOG; KOG3260; Eukaryota.
DR GeneTree; ENSGT00390000016470; -.
DR HOGENOM; CLU_081441_2_0_1; -.
DR InParanoid; Q9HB71; -.
DR OMA; WDVLTSI; -.
DR PhylomeDB; Q9HB71; -.
DR TreeFam; TF323891; -.
DR PathwayCommons; Q9HB71; -.
DR SignaLink; Q9HB71; -.
DR BioGRID-ORCS; 27101; 37 hits in 1042 CRISPR screens.
DR ChiTaRS; CACYBP; human.
DR EvolutionaryTrace; Q9HB71; -.
DR GeneWiki; CACYBP; -.
DR GenomeRNAi; 27101; -.
DR Pharos; Q9HB71; Tbio.
DR PRO; PR:Q9HB71; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HB71; protein.
DR Bgee; ENSG00000116161; Expressed in endothelial cell and 217 other tissues.
DR ExpressionAtlas; Q9HB71; baseline and differential.
DR Genevisible; Q9HB71; HS.
DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IPI:UniProtKB.
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 DisProt; DP00907; -. [Q9HB71-2]
DR Gene3D; 2.60.40.790; -; 1.
DR IDEAL; IID00125; -.
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; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10, ECO:0000269|Ref.11,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..228
FT /note="Calcyclin-binding protein"
FT /id="PRO_0000185389"
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 REGION 73..228
FT /note="Interaction with SKP1"
FT /evidence="ECO:0000269|PubMed:11389839"
FT REGION 154..228
FT /note="Interaction with S100A6"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.10, ECO:0000269|Ref.11,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046862"
FT VAR_SEQ 73..80
FT /note="VKISNYGW -> DGISQISL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010171"
FT VAR_SEQ 81..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010172"
FT MUTAGEN 23..26
FT /note="KRVR->AAVA: Abolishes interaction with SIAH1."
FT /evidence="ECO:0000269|PubMed:16085652"
FT MUTAGEN 64
FT /note="V->N: Abolishes interaction with SIAH1; when
FT associated with N-66."
FT /evidence="ECO:0000269|PubMed:16085652"
FT MUTAGEN 66
FT /note="P->N: Abolishes interaction with SIAH1; when
FT associated with N-64."
FT /evidence="ECO:0000269|PubMed:16085652"
FT CONFLICT 44
FT /note="M -> V (in Ref. 4; AAG23817)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="E -> K (in Ref. 4; AAG23817)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="T -> P (in Ref. 4; AAG23817)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="T -> P (in Ref. 4; AAG23817)"
FT /evidence="ECO:0000305"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:2A26"
FT HELIX 23..46
FT /evidence="ECO:0007829|PDB:2A26"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2A25"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1X5M"
FT TURN 94..98
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1X5M"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:1X5M"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1X5M"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:1X5M"
SQ SEQUENCE 228 AA; 26210 MW; 88C822FB14A7EF89 CRC64;
MASEELQKDL EEVKVLLEKA TRKRVRDALT AEKSKIETEI KNKMQQKSQK KAELLDNEKP
AAVVAPITTG YTVKISNYGW DQSDKFVKIY ITLTGVHQVP TENVQVHFTE RSFDLLVKNL
NGKSYSMIVN NLLKPISVEG SSKKVKTDTV LILCRKKVEN TRWDYLTQVE KECKEKEKPS
YDTETDPSEG LMNVLKKIYE DGDDDMKRTI NKAWVESREK QAKGDTEF
