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Q9DBX1 (RGCC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:Rgc32
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.5

Subunit structure

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

Subcellular location

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

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from sequence orthology Ref.1. Source: MGI

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

complement activation

Inferred from electronic annotation. Source: Ensembl

fibroblast activation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

mitotic cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

negative regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-cell adhesion mediated by cadherin

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of exit from mitosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of fibroblast growth factor production

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitotic cell cycle phase transition

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

positive regulation of collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

positive regulation of extracellular matrix constituent secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression involved in extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence orthology Ref.1. Source: MGI

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence orthology Ref.1. Source: MGI

   Molecular_functionprotein kinase activator activity

Inferred from sequence orthology Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 137137Regulator of cell cycle RGCC
PRO_0000274702

Regions

Compositional bias11 – 2616Ala-rich
Compositional bias64 – 10845Ser/Thr-rich

Amino acid modifications

Modified residue691Phosphoserine By similarity
Modified residue711Phosphoserine By similarity
Modified residue751Phosphoserine By similarity
Modified residue971Phosphoserine By similarity
Modified residue1111Phosphothreonine; by CDK1 By similarity

Experimental info

Sequence conflict681V → I in BAB23310. Ref.2
Sequence conflict701D → N in BAB23310. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9DBX1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 01646F247F8B284A

FASTA13714,717
        10         20         30         40         50         60 
MKPPSAQSSP AAVAAAAPAM DSAAAADLTD VLCEFDAVLA DFASPFHERH FHYEEHLERM 

        70         80         90        100        110        120 
KRRSSASVSD SSGFSDSESA DSVYRDSFTF SDEKLNSPTN SSPALLPSAV TPRKAKLGDT 

       130 
KELEDFIADL DRTLASM 

« Hide

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].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Lung.
[3]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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].
Strain: C57BL/6.
Tissue: Brain and Testis.
[5]"Response gene to complement 32 is essential for fibroblast activation in renal fibrosis."
Li Z., Xie W.B., Escano C.S., Asico L.D., Xie Q., Jose P.A., Chen S.Y.
J. Biol. Chem. 286:41323-41330(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SMAD3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF276981 mRNA. Translation: AAK69442.1.
AK004451 mRNA. Translation: BAB23310.1.
AK004705 mRNA. Translation: BAB23490.1.
CT010403 mRNA. Translation: CAJ18609.1.
BC049580 mRNA. Translation: AAH49580.1.
BC050935 mRNA. Translation: AAH50935.1.
RefSeqNP_079703.2. NM_025427.2.
UniGeneMm.29811.

3D structure databases

ProteinModelPortalQ9DBX1.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9DBX1.

Proteomic databases

PaxDbQ9DBX1.
PRIDEQ9DBX1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022595; ENSMUSP00000022595; ENSMUSG00000022018.
GeneID66214.
KEGGmmu:66214.
UCSCuc007ust.1. mouse.

Organism-specific databases

CTD28984.
MGIMGI:1913464. Rgcc.

Phylogenomic databases

eggNOGNOG39648.
GeneTreeENSGT00390000011709.
HOGENOMHOG000294092.
HOVERGENHBG060999.
InParanoidQ9DBX1.
OMAFRYDEHL.
OrthoDBEOG7ZGX5S.
PhylomeDBQ9DBX1.
TreeFamTF336312.

Gene expression databases

BgeeQ9DBX1.
CleanExMM_1190002H23RIK.
GenevestigatorQ9DBX1.

Family and domain databases

ProtoNetSearch...

Other

NextBio320993.
PROQ9DBX1.
SOURCESearch...

Entry information

Entry nameRGCC_MOUSE
AccessionPrimary (citable) accession number: Q9DBX1
Secondary accession number(s): Q9D0U0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot