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Ras-related protein R-Ras2 (Ras-like protein TC21) (Teratocarcinoma oncogene)

 RRAS2_HUMAN             Reviewed;         204 AA.
P62070; B2R9Z3; B7Z5Z2; B7Z6C4; B7Z7H6; P17082;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 1.
20-JUN-2018, entry version 158.
RecName: Full=Ras-related protein R-Ras2;
AltName: Full=Ras-like protein TC21;
AltName: Full=Teratocarcinoma oncogene;
Flags: Precursor;
Name=RRAS2; Synonyms=TC21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2108320; DOI=10.1128/MCB.10.4.1793;
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.;
"Characterization of four novel ras-like genes expressed in a human
teratocarcinoma cell line.";
Mol. Cell. Biol. 10:1793-1798(1990).
[2]
SEQUENCE REVISION TO 5-11, TISSUE SPECIFICITY, AND VARIANT OVARIAN
CANCER LEU-72.
PubMed=8052619; DOI=10.1073/pnas.91.16.7558;
Chan A.M.-L., Miki T., Meyers K.A., Aaronson S.A.;
"A human oncogene of the RAS superfamily unmasked by expression cDNA
cloning.";
Proc. Natl. Acad. Sci. U.S.A. 91:7558-7562(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Heart;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Brain, Pericardium, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
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., 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.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
ISOPRENYLATION AT CYS-201.
PubMed=15308774; DOI=10.1073/pnas.0403413101;
Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,
Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
"A tagging-via-substrate technology for detection and proteomics of
farnesylated proteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 10-181 IN COMPLEX WITH GDP.
Structural genomics consortium (SGC);
"The crystal structure of the Ras related protein RRAS2 in the GDP
bound state.";
Submitted (FEB-2009) to the PDB data bank.
-!- 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.
-!- INTERACTION:
P10398:ARAF; NbExp=3; IntAct=EBI-491037, EBI-365961;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface
of plasma membrane possibly with attachment requiring acylation of
the C-terminal cysteine (By similarity with RAS).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P62070-1; Sequence=Displayed;
Name=2;
IsoId=P62070-2; Sequence=VSP_043066;
Note=No experimental confirmation available.;
Name=3;
IsoId=P62070-3; Sequence=VSP_044485;
Note=No experimental confirmation available.;
Name=4;
IsoId=P62070-4; Sequence=VSP_055842;
Note=No experimental confirmation available.;
-!- 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. {ECO:0000269|PubMed:8052619}.
-!- PTM: May be post-translationally modified by both palmitoylation
and polyisoprenylation.
-!- 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.
{ECO:0000269|PubMed:8052619}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA36545.1; Type=Frameshift; Positions=4, 8, 12; Evidence={ECO:0000305};
Sequence=AAM12638.1; Type=Frameshift; Positions=4, 8, 12; Evidence={ECO:0000305};
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EMBL; M31468; AAA36545.1; ALT_FRAME; mRNA.
EMBL; AF493924; AAM12638.1; ALT_FRAME; mRNA.
EMBL; AK299606; BAH13078.1; -; mRNA.
EMBL; AK300103; BAH13210.1; -; mRNA.
EMBL; AK302033; BAH13612.1; -; mRNA.
EMBL; AK313976; BAG36690.1; -; mRNA.
EMBL; AC011084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68487.1; -; Genomic_DNA.
EMBL; BC013106; AAH13106.1; -; mRNA.
CCDS; CCDS44544.1; -. [P62070-2]
CCDS; CCDS53603.1; -. [P62070-3]
CCDS; CCDS7814.1; -. [P62070-1]
PIR; B34788; TVHUC2.
RefSeq; NP_001096139.1; NM_001102669.2. [P62070-2]
RefSeq; NP_001170785.1; NM_001177314.1. [P62070-3]
RefSeq; NP_001170786.1; NM_001177315.1. [P62070-2]
RefSeq; NP_036382.2; NM_012250.5. [P62070-1]
UniGene; Hs.502004; -.
UniGene; Hs.712835; -.
PDB; 2ERY; X-ray; 1.70 A; A/B=12-181.
PDBsum; 2ERY; -.
ProteinModelPortal; P62070; -.
SMR; P62070; -.
BioGrid; 116480; 39.
IntAct; P62070; 38.
MINT; P62070; -.
STRING; 9606.ENSP00000256196; -.
iPTMnet; P62070; -.
PhosphoSitePlus; P62070; -.
SwissPalm; P62070; -.
BioMuta; RRAS2; -.
DMDM; 49065833; -.
EPD; P62070; -.
MaxQB; P62070; -.
PaxDb; P62070; -.
PeptideAtlas; P62070; -.
PRIDE; P62070; -.
ProteomicsDB; 57360; -.
ProteomicsDB; 57361; -. [P62070-2]
DNASU; 22800; -.
Ensembl; ENST00000256196; ENSP00000256196; ENSG00000133818. [P62070-1]
Ensembl; ENST00000414023; ENSP00000403282; ENSG00000133818. [P62070-2]
Ensembl; ENST00000526063; ENSP00000434104; ENSG00000133818. [P62070-2]
Ensembl; ENST00000529237; ENSP00000433230; ENSG00000133818. [P62070-2]
Ensembl; ENST00000532814; ENSP00000431954; ENSG00000133818. [P62070-2]
Ensembl; ENST00000534746; ENSP00000437083; ENSG00000133818. [P62070-2]
Ensembl; ENST00000537760; ENSP00000437547; ENSG00000133818. [P62070-3]
GeneID; 22800; -.
KEGG; hsa:22800; -.
UCSC; uc001mlf.5; human. [P62070-1]
CTD; 22800; -.
DisGeNET; 22800; -.
EuPathDB; HostDB:ENSG00000133818.12; -.
GeneCards; RRAS2; -.
HGNC; HGNC:17271; RRAS2.
HPA; CAB010420; -.
HPA; HPA050942; -.
MalaCards; RRAS2; -.
MIM; 167000; phenotype.
MIM; 600098; gene.
neXtProt; NX_P62070; -.
OpenTargets; ENSG00000133818; -.
PharmGKB; PA34862; -.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133672; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; P62070; -.
KO; K07830; -.
OMA; YAQTYKL; -.
OrthoDB; EOG091G0UAU; -.
PhylomeDB; P62070; -.
TreeFam; TF312796; -.
SignaLink; P62070; -.
SIGNOR; P62070; -.
ChiTaRS; RRAS2; human.
EvolutionaryTrace; P62070; -.
GeneWiki; RRAS2; -.
GenomeRNAi; 22800; -.
PRO; PR:P62070; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000133818; -.
CleanEx; HS_RRAS2; -.
ExpressionAtlas; P62070; baseline and differential.
Genevisible; P62070; HS.
GO; GO:0005783; C:endoplasmic reticulum; NAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
GO; GO:1901214; P:regulation of neuron death; IMP:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Complete proteome; Disease mutation; GTP-binding; Lipoprotein;
Membrane; Methylation; Nucleotide-binding; Palmitate; Phosphoprotein;
Prenylation; Proto-oncogene; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 201 Ras-related protein R-Ras2.
/FTId=PRO_0000082652.
PROPEP 202 204 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281302.
NP_BIND 21 29 GTP.
NP_BIND 68 72 GTP. {ECO:0000250}.
NP_BIND 127 130 GTP.
NP_BIND 157 159 GTP.
MOTIF 43 51 Effector region.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 201 201 Cysteine methyl ester. {ECO:0000305}.
LIPID 199 199 S-palmitoyl cysteine. {ECO:0000255}.
LIPID 201 201 S-farnesyl cysteine.
{ECO:0000269|PubMed:15308774}.
VAR_SEQ 1 77 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043066.
VAR_SEQ 1 36 MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQ -> M
(in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044485.
VAR_SEQ 36 36 Q -> QFFLFLQ (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055842.
VARIANT 72 72 Q -> L (in an ovarian cancer sample;
somatic mutation; dbSNP:rs113954997).
{ECO:0000269|PubMed:8052619}.
/FTId=VAR_006848.
STRAND 14 21 {ECO:0000244|PDB:2ERY}.
HELIX 27 36 {ECO:0000244|PDB:2ERY}.
STRAND 49 57 {ECO:0000244|PDB:2ERY}.
STRAND 60 68 {ECO:0000244|PDB:2ERY}.
HELIX 77 85 {ECO:0000244|PDB:2ERY}.
STRAND 87 94 {ECO:0000244|PDB:2ERY}.
HELIX 98 102 {ECO:0000244|PDB:2ERY}.
HELIX 104 115 {ECO:0000244|PDB:2ERY}.
STRAND 121 127 {ECO:0000244|PDB:2ERY}.
HELIX 139 148 {ECO:0000244|PDB:2ERY}.
STRAND 152 155 {ECO:0000244|PDB:2ERY}.
TURN 158 161 {ECO:0000244|PDB:2ERY}.
HELIX 164 178 {ECO:0000244|PDB:2ERY}.
SEQUENCE 204 AA; 23400 MW; BA7D4759DC49446F CRC64;
MAAAGWRDGS GQEKYRLVVV GGGGVGKSAL TIQFIQSYFV TDYDPTIEDS YTKQCVIDDR
AARLDILDTA GQEEFGAMRE QYMRTGEGFL LVFSVTDRGS FEEIYKFQRQ ILRVKDRDEF
PMILIGNKAD LDHQRQVTQE EGQQLARQLK VTYMEASAKI RMNVDQAFHE LVRVIRKFQE
QECPPSPEPT RKEKDKKGCH CVIF


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CSB-EL020514MO Mouse Ras-related protein R-Ras2(RRAS2) ELISA kit SpeciesMouse 96T
CSB-EL020514HU Human Ras-related protein R-Ras2(RRAS2) ELISA kit SpeciesHuman 96T
RRAS2_MOUSE ELISA Kit FOR Ras-related protein R-Ras2; organism: Mouse; gene name: Rras2 96T
EIAAB38565 Homo sapiens,Human,SKIL,Ski-like protein,Ski-related oncogene,Ski-related protein,SNO
EIAAB38566 Mouse,Mus musculus,Skil,Ski-like protein,Skir,Ski-related oncogene,Ski-related protein,Sno
EIAAB10615 DCN1-like protein 1,DCUN1 domain-containing protein 1,DCUN1D1,DCUN1L1,Defective in cullin neddylation protein 1-like protein 1,Homo sapiens,Human,RP42,SCCRO,Squamous cell carcinoma-related oncogene
18-003-43820 Ski-like protein - Ski-related protein; Ski-related oncogene Polyclonal 0.1 mg Protein A
E0978r ELISA Epidermal growth factor receptor-related protein,Erbb2,Neu,p185erbB2,p185neu,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-2 96T


 

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