RGCC_HUMAN
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 03-AUG-2022, entry version 136.
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}.
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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; Q9H4X1; -.
DR PeptideAtlas; Q9H4X1; -.
DR PRIDE; Q9H4X1; -.
DR ProteomicsDB; 80878; -. [Q9H4X1-1]
DR ProteomicsDB; 80879; -. [Q9H4X1-2]
DR Antibodypedia; 23431; 98 antibodies from 16 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 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; RFFYGEH; -.
DR OrthoDB; 1604248at2759; -.
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; 9 hits in 1078 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 194 other tissues.
DR Genevisible; Q9H4X1; HS.
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; PTHR32193; 1.
DR Pfam; PF15151; RGCC; 1.
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
