Q9H4X1 (RGC32_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Response gene to complement 32 protein
Short name=RGC-32

Gene names

Name:	RGC32
Synonyms:	C13orf15

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	137 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.5
Subunit structure	Interacts with CDK1 and PLK1. Ref.5
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › centrosome. 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. Ref.1
Induction	Up-regulated in aorta endothelial cells in response to complement activation. Ref.1

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW regulation of cyclin-dependent protein kinase activity Traceable author statement. Source: ProtInc
Cellular component	microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: HPA
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 137	137	Response gene to complement 32 protein		PRO_0000274701
Regions
	Compositional bias	11 – 26	16	Ala-rich
	Compositional bias	64 – 109	46	Ser/Thr-rich
Amino acid modifications
	Modified residue	9	1	Phosphoserine Ref.4
	Modified residue	29	1	Phosphoserine Ref.4
	Modified residue	44	1	Phosphoserine Ref.4
	Modified residue	69	1	Phosphoserine Ref.6
	Modified residue	71	1	Phosphoserine Ref.6
	Modified residue	75	1	Phosphoserine Ref.6
	Modified residue	97	1	Phosphoserine Ref.6
	Modified residue	111	1	Phosphothreonine; by CDK1 Ref.1 Ref.6
Natural variations
	Alternative sequence	6 – 25	20	Missing in isoform 2.		VSP_022873
Experimental info
	Mutagenesis	111	1	T → A: Loss of phosphorylation. Reduced stimulation of CDK1 activity. Ref.1
	Sequence conflict	3	1	P → Q in AAH66334. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 76265677DBCD9525	FASTA	137	14,559
	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
	Isoform 2 [UniParc]. Checksum: 3F01B45873DE5909	FASTA	117	12,924
	10 20 30 40 50 60 MKPPAEDLSD ALCEFDAVLA DFASPFHERH FHYEEHLERM KRRSSASVSD SSGFSDSESA 70 80 90 100 110 DSLYRNSFSF SDEKLNSPTD STPALLSATV TPQKAKLGDT KELEAFIADL DKTLASM

References

	« Hide 'large scale' referencesShow '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: 11687586] [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(2004) [PubMed: 15057823] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-29 AND SER-44, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 17146433] [Abstract] Cited for: INTERACTION WITH PLK1, FUNCTION, SUBCELLULAR LOCATION.
[6]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-75; SER-97 AND THR-111, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	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.
IPI	IPI00022350. IPI00827579.
RefSeq	NP_054778.2. NM_014059.2.
UniGene	Hs.507866.
3D structure databases
ProteinModelPortal	Q9H4X1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9H4X1.
PTM databases
PhosphoSite	Q9H4X1.
Polymorphism databases
DMDM	74752653.
Proteomic databases
PRIDE	Q9H4X1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379359; ENSP00000368664; ENSG00000102760.
GeneID	28984.
KEGG	hsa:28984.
UCSC	uc001uyi.2. human.
Organism-specific databases
CTD	28984.
GeneCards	GC13P042031.
HGNC	HGNC:20369. C13orf15.
HPA	HPA035638.
MIM	610077. gene.
neXtProt	NX_Q9H4X1.
PharmGKB	PA134895181.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG21326.
GeneTree	ENSGT00390000011709.
HOGENOM	HBG447054.
HOVERGEN	HBG060999.
InParanoid	Q9H4X1.
OMA	FRYDEHL.
OrthoDB	EOG4NKBX7.
PhylomeDB	Q9H4X1.
Gene expression databases
ArrayExpress	Q9H4X1.
Bgee	Q9H4X1.
CleanEx	HS_C13orf15.
Genevestigator	Q9H4X1.
Family and domain databases
ProtoNet	Search...
Other
NextBio	51881.
SOURCE	Search...

Entry information

Entry name

RGC32_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.