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P62070 (RRAS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein R-Ras2
Alternative name(s):
Ras-like protein TC21
Teratocarcinoma oncogene
Gene names
Name:RRAS2
Synonyms:TC21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS).

Tissue specificity

Ubiquitously present in all tissues examined, with the highest levels in heart, placenta, and skeletal muscle. Moderate levels in lung and liver; low levels in brain, kidney, and pancreas. Ref.2

Post-translational modification

May be post-translationally modified by both palmitoylation and polyisoprenylation.

Involvement in disease

Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Sequence caution

The sequence AAA36545.1 differs from that shown. Reason: Frameshift at positions 4, 8 and 12.

The sequence AAM12638.1 differs from that shown. Reason: Frameshift at positions 4, 8 and 12.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARAFP103983EBI-491037,EBI-365961

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62070-1)

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: P62070-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P62070-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQ → M
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 201200Ras-related protein R-Ras2
PRO_0000082652
Propeptide202 – 2043Removed in mature form By similarity
PRO_0000281302

Regions

Nucleotide binding21 – 299GTP
Nucleotide binding68 – 725GTP By similarity
Nucleotide binding127 – 1304GTP
Nucleotide binding157 – 1593GTP
Motif43 – 519Effector region

Amino acid modifications

Modified residue21N-acetylalanine Ref.12
Modified residue1861Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
Modified residue2011Cysteine methyl ester Probable
Lipidation1991S-palmitoyl cysteine Potential
Lipidation2011S-farnesyl cysteine Ref.8

Natural variations

Alternative sequence1 – 7777Missing in isoform 2.
VSP_043066
Alternative sequence1 – 3636MAAAG…IQFIQ → M in isoform 3.
VSP_044485
Natural variant721Q → L in an ovarian cancer sample; somatic mutation. Ref.2
VAR_006848

Secondary structure

........................... 204
Helix Strand Turn

Details...

Sequences

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

Last modified June 21, 2004. Version 1.
Checksum: BA7D4759DC49446F

FASTA20423,400
        10         20         30         40         50         60 
MAAAGWRDGS GQEKYRLVVV GGGGVGKSAL TIQFIQSYFV TDYDPTIEDS YTKQCVIDDR 

        70         80         90        100        110        120 
AARLDILDTA GQEEFGAMRE QYMRTGEGFL LVFSVTDRGS FEEIYKFQRQ ILRVKDRDEF 

       130        140        150        160        170        180 
PMILIGNKAD LDHQRQVTQE EGQQLARQLK VTYMEASAKI RMNVDQAFHE LVRVIRKFQE 

       190        200 
QECPPSPEPT RKEKDKKGCH CVIF 

« Hide

Isoform 2 [UniParc].

Checksum: 58F3090C7A5F9B60
Show »

FASTA12715,094
Isoform 3 [UniParc].

Checksum: A9C28F683B9E5A63
Show »

FASTA16919,841

References

« Hide 'large scale' references
[1]"Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line."
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.
Mol. Cell. Biol. 10:1793-1798(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A human oncogene of the RAS superfamily unmasked by expression cDNA cloning."
Chan A.M.-L., Miki T., Meyers K.A., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 91:7558-7562(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 5-11, TISSUE SPECIFICITY, VARIANT OVARIAN CANCER LEU-72.
[3]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Heart.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Pericardium and Uterus.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Bone.
[8]"A tagging-via-substrate technology for detection and proteomics of farnesylated proteins."
Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.
Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-201.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"The crystal structure of the Ras related protein RRAS2 in the GDP bound state."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 10-181 IN COMPLEX WITH GDP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31468 mRNA. Translation: AAA36545.1. Frameshift.
AF493924 mRNA. Translation: AAM12638.1. Frameshift.
AK300103 mRNA. Translation: BAH13210.1.
AK302033 mRNA. Translation: BAH13612.1.
AK313976 mRNA. Translation: BAG36690.1.
AC011084 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68487.1.
BC013106 mRNA. Translation: AAH13106.1.
PIRTVHUC2. B34788.
RefSeqNP_001096139.1. NM_001102669.2.
NP_001170785.1. NM_001177314.1.
NP_001170786.1. NM_001177315.1.
NP_036382.2. NM_012250.5.
UniGeneHs.502004.
Hs.712835.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ERYX-ray1.70A/B12-181[»]
ProteinModelPortalP62070.
SMRP62070. Positions 13-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116480. 15 interactions.
IntActP62070. 14 interactions.
MINTMINT-5001153.
STRING9606.ENSP00000256196.

PTM databases

PhosphoSiteP62070.

Polymorphism databases

DMDM49065833.

Proteomic databases

PaxDbP62070.
PeptideAtlasP62070.
PRIDEP62070.

Protocols and materials databases

DNASU22800.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256196; ENSP00000256196; ENSG00000133818. [P62070-1]
ENST00000414023; ENSP00000403282; ENSG00000133818. [P62070-2]
ENST00000526063; ENSP00000434104; ENSG00000133818. [P62070-2]
ENST00000529237; ENSP00000433230; ENSG00000133818. [P62070-2]
ENST00000532814; ENSP00000431954; ENSG00000133818. [P62070-2]
ENST00000534746; ENSP00000437083; ENSG00000133818. [P62070-2]
ENST00000537760; ENSP00000437547; ENSG00000133818. [P62070-3]
ENST00000571727; ENSP00000460749; ENSG00000262489. [P62070-2]
ENST00000572201; ENSP00000460504; ENSG00000262489. [P62070-2]
ENST00000572397; ENSP00000459423; ENSG00000262489. [P62070-2]
ENST00000572894; ENSP00000458232; ENSG00000262489. [P62070-1]
ENST00000573870; ENSP00000458679; ENSG00000262489. [P62070-2]
ENST00000574530; ENSP00000460998; ENSG00000262489. [P62070-2]
GeneID22800.
KEGGhsa:22800.
UCSCuc001mlf.4. human. [P62070-1]
uc021qed.1. human. [P62070-3]

Organism-specific databases

CTD22800.
GeneCardsGC11M014299.
HGNCHGNC:17271. RRAS2.
HPACAB010420.
MIM167000. phenotype.
600098. gene.
neXtProtNX_P62070.
PharmGKBPA34862.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233973.
HOVERGENHBG009351.
InParanoidP62070.
KOK07830.
OMAXKFQEQE.
PhylomeDBP62070.
TreeFamTF312796.

Enzyme and pathway databases

SignaLinkP62070.

Gene expression databases

ArrayExpressP62070.
BgeeP62070.
CleanExHS_RRAS2.
GenevestigatorP62070.

Family and domain databases

InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62070.
GeneWikiRRAS2.
GenomeRNAi22800.
NextBio43146.
PROP62070.
SOURCESearch...

Entry information

Entry nameRRAS2_HUMAN
AccessionPrimary (citable) accession number: P62070
Secondary accession number(s): B2R9Z3 expand/collapse secondary AC list , B7Z6C4, B7Z7H6, P17082
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: March 19, 2014
This is version 117 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM