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 27-MAR-2024, entry version 197. 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}; 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; 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. 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; 253. DR CORUM; Q9HB71; -. DR ELM; Q9HB71; -. DR IntAct; Q9HB71; 146. 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 CPTAC; CPTAC-321; -. DR CPTAC; CPTAC-322; -. DR EPD; Q9HB71; -. DR jPOST; Q9HB71; -. DR MassIVE; Q9HB71; -. DR MaxQB; Q9HB71; -. DR PaxDb; 9606-ENSP00000356652; -. DR PeptideAtlas; Q9HB71; -. DR ProteomicsDB; 3636; -. DR ProteomicsDB; 63708; -. DR ProteomicsDB; 81499; -. [Q9HB71-1] DR ProteomicsDB; 81500; -. [Q9HB71-2] DR Pumba; Q9HB71; -. DR TopDownProteomics; Q9HB71-1; -. [Q9HB71-1] DR Antibodypedia; 20569; 411 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 AGR; HGNC:30423; -. DR CTD; 27101; -. DR DisGeNET; 27101; -. DR GeneCards; CACYBP; -. DR HGNC; HGNC:30423; CACYBP. DR HPA; ENSG00000116161; Low tissue specificity. 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 OrthoDB; 616630at2759; -. DR PhylomeDB; Q9HB71; -. DR TreeFam; TF323891; -. DR PathwayCommons; Q9HB71; -. DR SignaLink; Q9HB71; -. DR BioGRID-ORCS; 27101; 37 hits in 1121 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 218 other cell types or tissues. DR ExpressionAtlas; Q9HB71; baseline and differential. 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 Gene3D; 4.10.860.10; UVR domain; 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 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. DR UCD-2DPAGE; Q9HB71; -. DR Genevisible; Q9HB71; HS. 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 //