Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P62070

- RRAS2_HUMAN

UniProt

P62070 - RRAS2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ras-related protein R-Ras2

Gene

RRAS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 299GTP
Nucleotide bindingi68 – 725GTPBy similarity
Nucleotide bindingi127 – 1304GTP
Nucleotide bindingi157 – 1593GTP

GO - Molecular functioni

  1. GTPase activity Source: ProtInc
  2. GTP binding Source: UniProtKB-KW

GO - Biological processi

  1. osteoblast differentiation Source: UniProt
  2. positive regulation of cell migration Source: Ensembl
  3. Ras protein signal transduction Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiP62070.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein R-Ras2
Alternative name(s):
Ras-like protein TC21
Teratocarcinoma oncogene
Gene namesi
Name:RRAS2
Synonyms:TC21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:17271. RRAS2.

Subcellular locationi

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

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. extracellular vesicular exosome Source: UniProt
  3. focal adhesion Source: UniProtKB
  4. membrane Source: UniProt
  5. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MIMi167000. phenotype.
PharmGKBiPA34862.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 201200Ras-related protein R-Ras2PRO_0000082652Add
BLAST
Propeptidei202 – 2043Removed in mature formBy similarityPRO_0000281302

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei186 – 1861Phosphoserine5 Publications
Lipidationi199 – 1991S-palmitoyl cysteineSequence Analysis
Modified residuei201 – 2011Cysteine methyl esterCurated
Lipidationi201 – 2011S-farnesyl cysteine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP62070.
PaxDbiP62070.
PeptideAtlasiP62070.
PRIDEiP62070.

PTM databases

PhosphoSiteiP62070.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiP62070.
CleanExiHS_RRAS2.
ExpressionAtlasiP62070. baseline and differential.
GenevestigatoriP62070.

Organism-specific databases

HPAiCAB010420.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAFP103983EBI-491037,EBI-365961

Protein-protein interaction databases

BioGridi116480. 17 interactions.
IntActiP62070. 14 interactions.
MINTiMINT-5001153.
STRINGi9606.ENSP00000256196.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 218Combined sources
Helixi27 – 3610Combined sources
Beta strandi49 – 579Combined sources
Beta strandi60 – 689Combined sources
Helixi77 – 859Combined sources
Beta strandi87 – 948Combined sources
Helixi98 – 1025Combined sources
Helixi104 – 11512Combined sources
Beta strandi121 – 1277Combined sources
Helixi139 – 14810Combined sources
Beta strandi152 – 1554Combined sources
Turni158 – 1614Combined sources
Helixi164 – 17815Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ERYX-ray1.70A/B12-181[»]
ProteinModelPortaliP62070.
SMRiP62070. Positions 13-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62070.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 519Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118909.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiP62070.
KOiK07830.
OMAiXKFQEQE.
PhylomeDBiP62070.
TreeFamiTF312796.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00173. RAS. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P62070-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAAGWRDGS GQEKYRLVVV GGGGVGKSAL TIQFIQSYFV TDYDPTIEDS
60 70 80 90 100
YTKQCVIDDR AARLDILDTA GQEEFGAMRE QYMRTGEGFL LVFSVTDRGS
110 120 130 140 150
FEEIYKFQRQ ILRVKDRDEF PMILIGNKAD LDHQRQVTQE EGQQLARQLK
160 170 180 190 200
VTYMEASAKI RMNVDQAFHE LVRVIRKFQE QECPPSPEPT RKEKDKKGCH

CVIF
Length:204
Mass (Da):23,400
Last modified:June 21, 2004 - v1
Checksum:iBA7D4759DC49446F
GO
Isoform 2 (identifier: P62070-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.

Note: No experimental confirmation available.

Show »
Length:127
Mass (Da):15,094
Checksum:i58F3090C7A5F9B60
GO
Isoform 3 (identifier: P62070-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQ → M

Note: No experimental confirmation available.

Show »
Length:169
Mass (Da):19,841
Checksum:iA9C28F683B9E5A63
GO
Isoform 4 (identifier: P62070-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-36: Q → QFFLFLQ

Note: No experimental confirmation available.

Show »
Length:210
Mass (Da):24,196
Checksum:i881713C4D54A663E
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721Q → L in an ovarian cancer sample; somatic mutation. 1 Publication
VAR_006848

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7777Missing in isoform 2. 1 PublicationVSP_043066Add
BLAST
Alternative sequencei1 – 3636MAAAG…IQFIQ → M in isoform 3. 1 PublicationVSP_044485Add
BLAST
Alternative sequencei36 – 361Q → QFFLFLQ in isoform 4. 1 PublicationVSP_055842

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31468 mRNA. Translation: AAA36545.1. Frameshift.
AF493924 mRNA. Translation: AAM12638.1. Frameshift.
AK299606 mRNA. Translation: BAH13078.1.
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.
CCDSiCCDS44544.1. [P62070-2]
CCDS53603.1. [P62070-3]
CCDS7814.1. [P62070-1]
PIRiB34788. TVHUC2.
RefSeqiNP_001096139.1. NM_001102669.2. [P62070-2]
NP_001170785.1. NM_001177314.1. [P62070-3]
NP_001170786.1. NM_001177315.1. [P62070-2]
NP_036382.2. NM_012250.5. [P62070-1]
UniGeneiHs.502004.
Hs.712835.

Genome annotation databases

EnsembliENST00000256196; 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]
ENST00000545643; ENSP00000441722; ENSG00000133818.
GeneIDi22800.
KEGGihsa:22800.
UCSCiuc001mlf.4. human. [P62070-1]
uc021qed.1. human. [P62070-3]

Polymorphism databases

DMDMi49065833.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31468 mRNA. Translation: AAA36545.1 . Frameshift.
AF493924 mRNA. Translation: AAM12638.1 . Frameshift.
AK299606 mRNA. Translation: BAH13078.1 .
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 .
CCDSi CCDS44544.1. [P62070-2 ]
CCDS53603.1. [P62070-3 ]
CCDS7814.1. [P62070-1 ]
PIRi B34788. TVHUC2.
RefSeqi NP_001096139.1. NM_001102669.2. [P62070-2 ]
NP_001170785.1. NM_001177314.1. [P62070-3 ]
NP_001170786.1. NM_001177315.1. [P62070-2 ]
NP_036382.2. NM_012250.5. [P62070-1 ]
UniGenei Hs.502004.
Hs.712835.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ERY X-ray 1.70 A/B 12-181 [» ]
ProteinModelPortali P62070.
SMRi P62070. Positions 13-181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116480. 17 interactions.
IntActi P62070. 14 interactions.
MINTi MINT-5001153.
STRINGi 9606.ENSP00000256196.

PTM databases

PhosphoSitei P62070.

Polymorphism databases

DMDMi 49065833.

Proteomic databases

MaxQBi P62070.
PaxDbi P62070.
PeptideAtlasi P62070.
PRIDEi P62070.

Protocols and materials databases

DNASUi 22800.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256196 ; 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 ]
ENST00000545643 ; ENSP00000441722 ; ENSG00000133818 .
GeneIDi 22800.
KEGGi hsa:22800.
UCSCi uc001mlf.4. human. [P62070-1 ]
uc021qed.1. human. [P62070-3 ]

Organism-specific databases

CTDi 22800.
GeneCardsi GC11M014299.
HGNCi HGNC:17271. RRAS2.
HPAi CAB010420.
MIMi 167000. phenotype.
600098. gene.
neXtProti NX_P62070.
PharmGKBi PA34862.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00760000118909.
HOGENOMi HOG000233973.
HOVERGENi HBG009351.
InParanoidi P62070.
KOi K07830.
OMAi XKFQEQE.
PhylomeDBi P62070.
TreeFami TF312796.

Enzyme and pathway databases

SignaLinki P62070.

Miscellaneous databases

EvolutionaryTracei P62070.
GeneWikii RRAS2.
GenomeRNAii 22800.
NextBioi 35479838.
PROi P62070.
SOURCEi Search...

Gene expression databases

Bgeei P62070.
CleanExi HS_RRAS2.
ExpressionAtlasi P62070. baseline and differential.
Genevestigatori P62070.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view ]
PANTHERi PTHR24070. PTHR24070. 1 hit.
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00173. RAS. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51421. RAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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; 3 AND 4).
    Tissue: Brain, Pericardium and Uterus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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. 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. 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. 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.

Entry informationi

Entry nameiRRAS2_HUMAN
AccessioniPrimary (citable) accession number: P62070
Secondary accession number(s): B2R9Z3
, B7Z5Z2, B7Z6C4, B7Z7H6, P17082
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: October 29, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3