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Q9H4X1 (RGCC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of cell cycle RGCC
Alternative name(s):
Response gene to complement 32 protein
Short name=RGC-32
Gene names
Name:RGCC
Synonyms:C13orf15, RGC32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.8

Subunit structure

Interacts with SMAD3 By similarity. Interacts with CDK1 and PLK1. Ref.5

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase. Ref.1 Ref.5

Tissue specificity

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. Ref.1 Ref.4

Induction

By Epstein-Barr virus (EBV). Up-regulated in aorta endothelial cells in response to complement activation. Ref.1 Ref.8

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hypoxia

Inferred from mutant phenotype PubMed 19652095. Source: BHF-UCL

complement activation

Inferred from mutant phenotype PubMed 19162005. Source: BHF-UCL

fibroblast activation

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle arrest

Inferred from direct assay Ref.5. Source: BHF-UCL

negative regulation of angiogenesis

Inferred from direct assay PubMed 19652095. Source: BHF-UCL

negative regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 19652095. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.5. Source: BHF-UCL

negative regulation of cell-cell adhesion mediated by cadherin

Inferred from direct assay Ref.6PubMed 21307346. Source: BHF-UCL

negative regulation of cytokine secretion

Inferred from mutant phenotype PubMed 19162005. Source: BHF-UCL

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 19652095. Source: BHF-UCL

negative regulation of exit from mitosis

Inferred from direct assay Ref.5. Source: BHF-UCL

negative regulation of fibroblast growth factor production

Inferred from direct assay PubMed 19652095. Source: BHF-UCL

negative regulation of mitotic cell cycle phase transition

Inferred from direct assay Ref.5. Source: BHF-UCL

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell cycle arrest

Inferred from direct assay Ref.5. Source: BHF-UCL

positive regulation of collagen biosynthetic process

Inferred from direct assay Ref.6. Source: BHF-UCL

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from direct assay Ref.1PubMed 19162005. Source: BHF-UCL

positive regulation of cytokine secretion

Inferred from mutant phenotype PubMed 19162005. Source: BHF-UCL

positive regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 19652095. Source: BHF-UCL

positive regulation of epithelial to mesenchymal transition

Inferred from direct assay PubMed 21307346. Source: BHF-UCL

positive regulation of extracellular matrix constituent secretion

Inferred from direct assay Ref.6. Source: BHF-UCL

positive regulation of gene expression involved in extracellular matrix organization

Inferred from direct assay PubMed 21307346. Source: BHF-UCL

positive regulation of mitosis

Inferred from mutant phenotype PubMed 19162005. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

positive regulation of stress fiber assembly

Inferred from direct assay Ref.6. Source: BHF-UCL

   Cellular_componentcentrosome

Inferred from direct assay Ref.5. Source: BHF-UCL

cytoplasm

Inferred from direct assay Ref.1Ref.5. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.1. Source: BHF-UCL

   Molecular_functionR-SMAD binding

Inferred from physical interaction PubMed 21307346. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 19162005. Source: BHF-UCL

protein kinase activator activity

Inferred from direct assay Ref.1. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction Ref.1Ref.5. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H4X1-1)

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.
Isoform 2 (identifier: Q9H4X1-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 137137Regulator of cell cycle RGCC
PRO_0000274701

Regions

Compositional bias11 – 2616Ala-rich
Compositional bias64 – 10946Ser/Thr-rich

Amino acid modifications

Modified residue691Phosphoserine Ref.7
Modified residue711Phosphoserine Ref.7
Modified residue751Phosphoserine Ref.7
Modified residue971Phosphoserine Ref.7
Modified residue1111Phosphothreonine; by CDK1 Ref.1 Ref.7

Natural variations

Alternative sequence6 – 2520Missing in isoform 2.
VSP_022873

Experimental info

Mutagenesis1111T → A: Loss of phosphorylation. Reduced stimulation of CDK1 activity. Ref.1
Sequence conflict31P → Q in AAH66334. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 76265677DBCD9525

FASTA13714,559
        10         20         30         40         50         60 
MKPPAAQGSP AAAAAAAPAL DSAAAEDLSD ALCEFDAVLA DFASPFHERH FHYEEHLERM 

        70         80         90        100        110        120 
KRRSSASVSD SSGFSDSESA DSLYRNSFSF SDEKLNSPTD STPALLSATV TPQKAKLGDT 

       130 
KELEAFIADL DKTLASM 

« Hide

Isoform 2 [UniParc].

Checksum: 3F01B45873DE5909
Show »

FASTA11712,924

References

« Hide 'large scale' references
[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(2002) [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. expand/collapse author list , 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(2004) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Overexpression of RGC-32 in colon cancer and other tumors."
Fosbrink M., Cudrici C., Niculescu F., Badea T.C., David S., Shamsuddin A., Shin M.L., Rus H.
Exp. Mol. Pathol. 78:116-122(2005) [PubMed] [Europe PMC] [Abstract]
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(2007) [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(2009) [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(2009) [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(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF036549 mRNA. Translation: AAF04336.1.
AL354833 Genomic DNA. Translation: CAC13101.1.
BC066334 mRNA. Translation: AAH66334.1.
CCDSCCDS41880.1. [Q9H4X1-1]
RefSeqNP_054778.2. NM_014059.2. [Q9H4X1-1]
UniGeneHs.507866.

3D structure databases

ProteinModelPortalQ9H4X1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118805. 4 interactions.
STRING9606.ENSP00000368664.

PTM databases

PhosphoSiteQ9H4X1.

Polymorphism databases

DMDM74752653.

Proteomic databases

MaxQBQ9H4X1.
PaxDbQ9H4X1.
PRIDEQ9H4X1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379359; ENSP00000368664; ENSG00000102760. [Q9H4X1-1]
GeneID28984.
KEGGhsa:28984.
UCSCuc001uyi.2. human. [Q9H4X1-1]

Organism-specific databases

CTD28984.
GeneCardsGC13P042032.
H-InvDBHIX0011268.
HGNCHGNC:20369. RGCC.
HPAHPA035638.
MIM610077. gene.
neXtProtNX_Q9H4X1.
PharmGKBPA134895181.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39648.
HOGENOMHOG000294092.
HOVERGENHBG060999.
InParanoidQ9H4X1.
OMAFRYDEHL.
OrthoDBEOG7ZGX5S.
PhylomeDBQ9H4X1.
TreeFamTF336312.

Gene expression databases

BgeeQ9H4X1.
CleanExHS_C13orf15.
GenevestigatorQ9H4X1.

Family and domain databases

InterProIPR029252. RGCC.
[Graphical view]
PfamPF15151. RGCC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiC13orf15.
GenomeRNAi28984.
NextBio51881.
PROQ9H4X1.
SOURCESearch...

Entry information

Entry nameRGCC_HUMAN
AccessionPrimary (citable) accession number: Q9H4X1
Secondary accession number(s): Q6NZ48, Q9UL69
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM