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Protein

Regulator of cell cycle RGCC

Gene

RGCC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation.4 Publications

GO - Molecular functioni

  1. protein kinase activator activity Source: BHF-UCL
  2. protein kinase binding Source: BHF-UCL
  3. R-SMAD binding Source: BHF-UCL

GO - Biological processi

  1. cellular response to hypoxia Source: BHF-UCL
  2. complement activation Source: BHF-UCL
  3. fibroblast activation Source: UniProtKB
  4. mitotic cell cycle arrest Source: BHF-UCL
  5. negative regulation of angiogenesis Source: BHF-UCL
  6. negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  7. negative regulation of cell-cell adhesion mediated by cadherin Source: BHF-UCL
  8. negative regulation of cell proliferation Source: BHF-UCL
  9. negative regulation of cytokine secretion Source: BHF-UCL
  10. negative regulation of endothelial cell proliferation Source: BHF-UCL
  11. negative regulation of exit from mitosis Source: BHF-UCL
  12. negative regulation of fibroblast growth factor production Source: BHF-UCL
  13. negative regulation of mitotic cell cycle phase transition Source: BHF-UCL
  14. positive regulation of cell cycle arrest Source: BHF-UCL
  15. positive regulation of collagen biosynthetic process Source: BHF-UCL
  16. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
  17. positive regulation of cytokine secretion Source: BHF-UCL
  18. positive regulation of DNA biosynthetic process Source: BHF-UCL
  19. positive regulation of endothelial cell apoptotic process Source: BHF-UCL
  20. positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  21. positive regulation of extracellular matrix assembly Source: BHF-UCL
  22. positive regulation of extracellular matrix constituent secretion Source: BHF-UCL
  23. positive regulation of gene expression Source: BHF-UCL
  24. positive regulation of mitotic nuclear division Source: BHF-UCL
  25. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  26. positive regulation of stress fiber assembly Source: BHF-UCL
  27. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of cell cycle RGCC
Alternative name(s):
Response gene to complement 32 protein
Short name:
RGC-32
Gene namesi
Name:RGCC
Synonyms:C13orf15, RGC32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20369. RGCC.

Subcellular locationi

Cytoplasm. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase.

GO - Cellular componenti

  1. centrosome Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111T → A: Loss of phosphorylation. Reduced stimulation of CDK1 activity. 1 Publication

Organism-specific databases

PharmGKBiPA134895181.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Regulator of cell cycle RGCCPRO_0000274701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691Phosphoserine1 Publication
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei75 – 751Phosphoserine1 Publication
Modified residuei97 – 971Phosphoserine1 Publication
Modified residuei111 – 1111Phosphothreonine; by CDK12 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H4X1.
PaxDbiQ9H4X1.
PRIDEiQ9H4X1.

PTM databases

PhosphoSiteiQ9H4X1.

Expressioni

Tissue specificityi

Detected in brain, heart and liver (at protein level). Highly expressed in liver, skeletal muscle, kidney and pancreas. Detected at lower levels in heart, brain and placenta. Detected in aorta endothelial cells. Overexpressed in colon, breast, prostate, bladder, lung, and ovarian cancer tissues.2 Publications

Inductioni

By Epstein-Barr virus (EBV). Up-regulated in aorta endothelial cells in response to complement activation.2 Publications

Gene expression databases

BgeeiQ9H4X1.
CleanExiHS_C13orf15.
GenevestigatoriQ9H4X1.

Organism-specific databases

HPAiHPA035638.

Interactioni

Subunit structurei

Interacts with SMAD3 (By similarity). Interacts with CDK1 and PLK1.By similarity1 Publication

Protein-protein interaction databases

BioGridi118805. 8 interactions.
IntActiQ9H4X1. 2 interactions.
STRINGi9606.ENSP00000368664.

Structurei

3D structure databases

ProteinModelPortaliQ9H4X1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 2616Ala-richAdd
BLAST
Compositional biasi64 – 10946Ser/Thr-richAdd
BLAST

Phylogenomic databases

eggNOGiNOG39648.
GeneTreeiENSGT00390000011709.
HOGENOMiHOG000294092.
HOVERGENiHBG060999.
InParanoidiQ9H4X1.
OMAiFRYDEHL.
OrthoDBiEOG7ZGX5S.
PhylomeDBiQ9H4X1.
TreeFamiTF336312.

Family and domain databases

InterProiIPR029252. RGCC.
[Graphical view]
PfamiPF15151. RGCC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H4X1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKPPAAQGSP AAAAAAAPAL DSAAAEDLSD ALCEFDAVLA DFASPFHERH
60 70 80 90 100
FHYEEHLERM KRRSSASVSD SSGFSDSESA DSLYRNSFSF SDEKLNSPTD
110 120 130
STPALLSATV TPQKAKLGDT KELEAFIADL DKTLASM
Length:137
Mass (Da):14,559
Last modified:March 1, 2001 - v1
Checksum:i76265677DBCD9525
GO
Isoform 2 (identifier: Q9H4X1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     6-25: Missing.

Show »
Length:117
Mass (Da):12,924
Checksum:i3F01B45873DE5909
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31P → Q in AAH66334 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei6 – 2520Missing in isoform 2. 1 PublicationVSP_022873Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036549 mRNA. Translation: AAF04336.1.
AL354833 Genomic DNA. Translation: CAC13101.1.
BC066334 mRNA. Translation: AAH66334.1.
CCDSiCCDS41880.1. [Q9H4X1-1]
RefSeqiNP_054778.2. NM_014059.2. [Q9H4X1-1]
UniGeneiHs.507866.

Genome annotation databases

EnsembliENST00000379359; ENSP00000368664; ENSG00000102760. [Q9H4X1-1]
GeneIDi28984.
KEGGihsa:28984.
UCSCiuc001uyi.2. human. [Q9H4X1-1]

Polymorphism databases

DMDMi74752653.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036549 mRNA. Translation: AAF04336.1.
AL354833 Genomic DNA. Translation: CAC13101.1.
BC066334 mRNA. Translation: AAH66334.1.
CCDSiCCDS41880.1. [Q9H4X1-1]
RefSeqiNP_054778.2. NM_014059.2. [Q9H4X1-1]
UniGeneiHs.507866.

3D structure databases

ProteinModelPortaliQ9H4X1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118805. 8 interactions.
IntActiQ9H4X1. 2 interactions.
STRINGi9606.ENSP00000368664.

PTM databases

PhosphoSiteiQ9H4X1.

Polymorphism databases

DMDMi74752653.

Proteomic databases

MaxQBiQ9H4X1.
PaxDbiQ9H4X1.
PRIDEiQ9H4X1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379359; ENSP00000368664; ENSG00000102760. [Q9H4X1-1]
GeneIDi28984.
KEGGihsa:28984.
UCSCiuc001uyi.2. human. [Q9H4X1-1]

Organism-specific databases

CTDi28984.
GeneCardsiGC13P042032.
H-InvDBHIX0011268.
HGNCiHGNC:20369. RGCC.
HPAiHPA035638.
MIMi610077. gene.
neXtProtiNX_Q9H4X1.
PharmGKBiPA134895181.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39648.
GeneTreeiENSGT00390000011709.
HOGENOMiHOG000294092.
HOVERGENiHBG060999.
InParanoidiQ9H4X1.
OMAiFRYDEHL.
OrthoDBiEOG7ZGX5S.
PhylomeDBiQ9H4X1.
TreeFamiTF336312.

Miscellaneous databases

GeneWikiiC13orf15.
GenomeRNAii28984.
NextBioi51881.
PROiQ9H4X1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4X1.
CleanExiHS_C13orf15.
GenevestigatoriQ9H4X1.

Family and domain databases

InterProiIPR029252. RGCC.
[Graphical view]
PfamiPF15151. RGCC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth muscle cells into S-phase."
    Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V., Shin M.L., Rus H.
    J. Biol. Chem. 277:502-508(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-111, PHOSPHORYLATION AT THR-111, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. Cited for: TISSUE SPECIFICITY.
  5. "RGC32, a novel p53-inducible gene, is located on centrosomes during mitosis and results in G2/M arrest."
    Saigusa K., Imoto I., Tanikawa C., Aoyagi M., Ohno K., Nakamura Y., Inazawa J.
    Oncogene 26:1110-1121(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLK1, FUNCTION, SUBCELLULAR LOCATION.
  6. "RGC-32 mediates transforming growth factor-beta-induced epithelial-mesenchymal transition in human renal proximal tubular cells."
    Huang W.Y., Li Z.G., Rus H., Wang X., Jose P.A., Chen S.Y.
    J. Biol. Chem. 284:9426-9432(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-75; SER-97 AND THR-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Upregulation of the cell-cycle regulator RGC-32 in Epstein-Barr virus-immortalized cells."
    Schlick S.N., Wood C.D., Gunnell A., Webb H.M., Khasnis S., Schepers A., West M.J.
    PLoS ONE 6:E28638-E28638(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.

Entry informationi

Entry nameiRGCC_HUMAN
AccessioniPrimary (citable) accession number: Q9H4X1
Secondary accession number(s): Q6NZ48, Q9UL69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: March 1, 2001
Last modified: April 1, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.