ID RGCC_HUMAN Reviewed; 137 AA. AC Q9H4X1; Q6NZ48; Q9UL69; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 143. DE RecName: Full=Regulator of cell cycle RGCC; DE AltName: Full=Response gene to complement 32 protein; DE Short=RGC-32; GN Name=RGCC; Synonyms=C13orf15, RGC32; 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 2), FUNCTION, INDUCTION, SUBCELLULAR RP LOCATION, MUTAGENESIS OF THR-111, PHOSPHORYLATION AT THR-111, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=11687586; DOI=10.1074/jbc.m109354200; RA Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V., RA Shin M.L., Rus H.; RT "RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth muscle RT cells into S-phase."; RL J. Biol. Chem. 277:502-508(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 TISSUE SPECIFICITY. RX PubMed=15713436; DOI=10.1016/j.yexmp.2004.11.001; RA Fosbrink M., Cudrici C., Niculescu F., Badea T.C., David S., Shamsuddin A., RA Shin M.L., Rus H.; RT "Overexpression of RGC-32 in colon cancer and other tumors."; RL Exp. Mol. Pathol. 78:116-122(2005). RN [5] RP INTERACTION WITH PLK1, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17146433; DOI=10.1038/sj.onc.1210148; RA Saigusa K., Imoto I., Tanikawa C., Aoyagi M., Ohno K., Nakamura Y., RA Inazawa J.; RT "RGC32, a novel p53-inducible gene, is located on centrosomes during RT mitosis and results in G2/M arrest."; RL Oncogene 26:1110-1121(2007). RN [6] RP FUNCTION. RX PubMed=19158077; DOI=10.1074/jbc.m900039200; RA Huang W.Y., Li Z.G., Rus H., Wang X., Jose P.A., Chen S.Y.; RT "RGC-32 mediates transforming growth factor-beta-induced epithelial- RT mesenchymal transition in human renal proximal tubular cells."; RL J. Biol. Chem. 284:9426-9432(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-75; SER-97 RP AND THR-111, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [8] RP FUNCTION, AND INDUCTION. RX PubMed=22163048; DOI=10.1371/journal.pone.0028638; RA Schlick S.N., Wood C.D., Gunnell A., Webb H.M., Khasnis S., Schepers A., RA West M.J.; RT "Upregulation of the cell-cycle regulator RGC-32 in Epstein-Barr virus- RT immortalized cells."; RL PLoS ONE 6:E28638-E28638(2011). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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). CC -!- FUNCTION: Modulates the activity of cell cycle-specific kinases. CC Enhances CDK1 activity. May contribute to the regulation of the cell CC cycle. May inhibit growth of glioma cells by promoting arrest of CC mitotic progression at the G2/M transition. Fibrogenic factor CC contributing to the pathogenesis of renal fibrosis through fibroblast CC activation. {ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:17146433, CC ECO:0000269|PubMed:19158077, ECO:0000269|PubMed:22163048}. CC -!- SUBUNIT: Interacts with SMAD3 (By similarity). Interacts with CDK1 and CC PLK1. {ECO:0000250, ECO:0000269|PubMed:17146433}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome. Note=Cytoplasmic in CC unstimulated cells. Nuclear after activation by complement. Associated CC with the centrosome during prometaphase and metaphase. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H4X1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H4X1-2; Sequence=VSP_022873; CC -!- TISSUE SPECIFICITY: Detected in brain, heart and liver (at protein CC level). Highly expressed in liver, skeletal muscle, kidney and CC pancreas. Detected at lower levels in heart, brain and placenta. CC Detected in aorta endothelial cells. Overexpressed in colon, breast, CC prostate, bladder, lung, and ovarian cancer tissues. CC {ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:15713436}. CC -!- INDUCTION: By Epstein-Barr virus (EBV). Up-regulated in aorta CC endothelial cells in response to complement activation. CC {ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:22163048}. 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; AF036549; AAF04336.1; -; mRNA. DR EMBL; AL354833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC066334; AAH66334.1; -; mRNA. DR CCDS; CCDS41880.1; -. [Q9H4X1-1] DR RefSeq; NP_054778.2; NM_014059.2. [Q9H4X1-1] DR AlphaFoldDB; Q9H4X1; -. DR BioGRID; 118805; 18. DR IntAct; Q9H4X1; 6. DR STRING; 9606.ENSP00000368664; -. DR iPTMnet; Q9H4X1; -. DR PhosphoSitePlus; Q9H4X1; -. DR BioMuta; RGCC; -. DR DMDM; 74752653; -. DR EPD; Q9H4X1; -. DR jPOST; Q9H4X1; -. DR MassIVE; Q9H4X1; -. DR MaxQB; Q9H4X1; -. DR PaxDb; 9606-ENSP00000368664; -. DR PeptideAtlas; Q9H4X1; -. DR ProteomicsDB; 80878; -. [Q9H4X1-1] DR ProteomicsDB; 80879; -. [Q9H4X1-2] DR Pumba; Q9H4X1; -. DR Antibodypedia; 23431; 141 antibodies from 17 providers. DR DNASU; 28984; -. DR Ensembl; ENST00000379359.4; ENSP00000368664.3; ENSG00000102760.13. [Q9H4X1-1] DR GeneID; 28984; -. DR KEGG; hsa:28984; -. DR MANE-Select; ENST00000379359.4; ENSP00000368664.3; NM_014059.3; NP_054778.2. DR UCSC; uc001uyi.3; human. [Q9H4X1-1] DR AGR; HGNC:20369; -. DR CTD; 28984; -. DR DisGeNET; 28984; -. DR GeneCards; RGCC; -. DR HGNC; HGNC:20369; RGCC. DR HPA; ENSG00000102760; Tissue enhanced (bone marrow, lung). DR MIM; 610077; gene. DR neXtProt; NX_Q9H4X1; -. DR OpenTargets; ENSG00000102760; -. DR PharmGKB; PA134895181; -. DR VEuPathDB; HostDB:ENSG00000102760; -. DR eggNOG; ENOG502S1UB; Eukaryota. DR GeneTree; ENSGT00390000011709; -. DR HOGENOM; CLU_154700_0_0_1; -. DR InParanoid; Q9H4X1; -. DR OMA; QRHFHYE; -. DR OrthoDB; 5359650at2759; -. DR PhylomeDB; Q9H4X1; -. DR TreeFam; TF336312; -. DR PathwayCommons; Q9H4X1; -. DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain. DR SignaLink; Q9H4X1; -. DR SIGNOR; Q9H4X1; -. DR BioGRID-ORCS; 28984; 10 hits in 1154 CRISPR screens. DR GeneWiki; C13orf15; -. DR GenomeRNAi; 28984; -. DR Pharos; Q9H4X1; Tbio. DR PRO; PR:Q9H4X1; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9H4X1; Protein. DR Bgee; ENSG00000102760; Expressed in decidua and 195 other cell types or tissues. DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0030295; F:protein kinase activator activity; IDA:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL. DR GO; GO:0006956; P:complement activation; IMP:BHF-UCL. DR GO; GO:0072537; P:fibroblast activation; ISS:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL. DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL. DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:BHF-UCL. DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:BHF-UCL. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL. DR GO; GO:0001100; P:negative regulation of exit from mitosis; IDA:BHF-UCL. DR GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IDA:BHF-UCL. DR GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; IDA:BHF-UCL. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL. DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL. DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:BHF-UCL. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:BHF-UCL. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:BHF-UCL. DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:BHF-UCL. DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL. DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IDA:BHF-UCL. DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IDA:BHF-UCL. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:BHF-UCL. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR InterPro; IPR029252; RGCC. DR PANTHER; PTHR32193; REGULATOR OF CELL CYCLE RGCC; 1. DR PANTHER; PTHR32193:SF3; REGULATOR OF CELL CYCLE RGCC; 1. DR Pfam; PF15151; RGCC; 1. DR Genevisible; Q9H4X1; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cytoplasm; Cytoskeleton; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..137 FT /note="Regulator of cell cycle RGCC" FT /id="PRO_0000274701" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 57..80 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 66..80 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9DBX1" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 75 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Z2P4" FT MOD_RES 97 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 111 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:11687586, FT ECO:0007744|PubMed:19690332" FT VAR_SEQ 6..25 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11687586" FT /id="VSP_022873" FT MUTAGEN 111 FT /note="T->A: Loss of phosphorylation. Reduced stimulation FT of CDK1 activity." FT /evidence="ECO:0000269|PubMed:11687586" FT CONFLICT 3 FT /note="P -> Q (in Ref. 3; AAH66334)" FT /evidence="ECO:0000305" SQ SEQUENCE 137 AA; 14559 MW; 76265677DBCD9525 CRC64; MKPPAAQGSP AAAAAAAPAL DSAAAEDLSD ALCEFDAVLA DFASPFHERH FHYEEHLERM KRRSSASVSD SSGFSDSESA DSLYRNSFSF SDEKLNSPTD STPALLSATV TPQKAKLGDT KELEAFIADL DKTLASM //