HUMAN:RASH

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HRAS (synonyms: HRAS1)
Protein Name(s)	GTPase HRas H-Ras-1 Ha-Ras Transforming protein p21 c-H-ras p21ras GTPase HRas, N-terminally processed
External Links
UniProt	P01112
EMBL	J00277 AJ437024 AF493916 CR536579 CR542271 BT019421 EF015887 AB451336 AB451485 CH471158 CH471158 BC006499 BC095471 M17232
CCDS	CCDS7698.1 CCDS7699.1
PIR	A93299
RefSeq	NP_001123914.1 NP_005334.1 NP_789765.1 XP_006718280.1 XP_006725199.1
UniGene	Hs.37003
PDB	121P 1AA9 1AGP 1BKD 1CLU 1CRP 1CRQ 1CRR 1CTQ 1GNP 1GNQ 1GNR 1HE8 1IAQ 1IOZ 1JAH 1JAI 1K8R 1LF0 1LF5 1LFD 1NVU 1NVV 1NVW 1NVX 1P2S 1P2T 1P2U 1P2V 1PLJ 1PLK 1PLL 1Q21 1QRA 1RVD 1WQ1 1XCM 1XD2 1XJ0 1ZVQ 1ZW6 221P 2C5L 2CE2 2CL0 2CL6 2CL7 2CLC 2CLD 2EVW 2GDP 2LCF 2LWI 2Q21 2QUZ 2RGA 2RGB 2RGC 2RGD 2RGE 2RGG 2UZI 2VH5 2X1V 3DDC 3I3S 3K8Y 3K9L 3K9N 3KKM 3KKN 3KUD 3L8Y 3L8Z 3LBH 3LBI 3LBN 3LO5 3OIU 3OIV 3OIW 3RRY 3RRZ 3RS0 3RS2 3RS3 3RS4 3RS5 3RS7 3RSL 3RSO 3TGP 421P 4DLR 4DLS 4DLT 4DLU 4DLV 4DLW 4DLX 4DLY 4DLZ 4DST 4DSU 4EFL 4EFM 4EFN 4G0N 4G3X 4K81 4L9S 4L9W 4NYI 4NYJ 4NYM 4Q21 521P 5P21 621P 6Q21 721P 821P
PDBsum	121P 1AA9 1AGP 1BKD 1CLU 1CRP 1CRQ 1CRR 1CTQ 1GNP 1GNQ 1GNR 1HE8 1IAQ 1IOZ 1JAH 1JAI 1K8R 1LF0 1LF5 1LFD 1NVU 1NVV 1NVW 1NVX 1P2S 1P2T 1P2U 1P2V 1PLJ 1PLK 1PLL 1Q21 1QRA 1RVD 1WQ1 1XCM 1XD2 1XJ0 1ZVQ 1ZW6 221P 2C5L 2CE2 2CL0 2CL6 2CL7 2CLC 2CLD 2EVW 2GDP 2LCF 2LWI 2Q21 2QUZ 2RGA 2RGB 2RGC 2RGD 2RGE 2RGG 2UZI 2VH5 2X1V 3DDC 3I3S 3K8Y 3K9L 3K9N 3KKM 3KKN 3KUD 3L8Y 3L8Z 3LBH 3LBI 3LBN 3LO5 3OIU 3OIV 3OIW 3RRY 3RRZ 3RS0 3RS2 3RS3 3RS4 3RS5 3RS7 3RSL 3RSO 3TGP 421P 4DLR 4DLS 4DLT 4DLU 4DLV 4DLW 4DLX 4DLY 4DLZ 4DST 4DSU 4EFL 4EFM 4EFN 4G0N 4G3X 4K81 4L9S 4L9W 4NYI 4NYJ 4NYM 4Q21 521P 5P21 621P 6Q21 721P 821P
DisProt	DP00153
ProteinModelPortal	P01112
SMR	P01112
BioGrid	109501
DIP	DIP-1050N
IntAct	P01112
MINT	MINT-5002362
STRING	9606.ENSP00000309845
BindingDB	P01112
ChEMBL	CHEMBL2167
PhosphoSite	P01112
DMDM	131869
MaxQB	P01112
PaxDb	P01112
PRIDE	P01112
DNASU	3265
Ensembl	ENST00000311189 ENST00000397594 ENST00000397596 ENST00000417302 ENST00000451590 ENST00000493230 ENST00000610977 ENST00000615062 ENST00000616241
GeneID	3265
KEGG	hsa:3265
UCSC	uc001lpv.3 uc010qvw.2
CTD	3265
GeneCards	GC11M000522
GeneReviews	HRAS
HGNC	HGNC:5173
HPA	CAB002015
MIM	109800 163200 190020 218040 607464
neXtProt	NX_P01112
Orphanet	3071 2612 2874
PharmGKB	PA29444
eggNOG	COG1100
GeneTree	ENSGT00770000120468
HOGENOM	HOG000233973
HOVERGEN	HBG009351
InParanoid	P01112
KO	K02833
OMA	DSGPGCM
OrthoDB	EOG7QVM41
PhylomeDB	P01112
TreeFam	TF312796
Reactome	REACT_111040 REACT_115852 REACT_115854 REACT_115993 REACT_116005 REACT_118778 REACT_12033 REACT_12065 REACT_121096 REACT_121398 REACT_12579 REACT_12606 REACT_12621 REACT_147814 REACT_163701 REACT_17025 REACT_18334 REACT_20546 REACT_2077 REACT_21247 REACT_21374 REACT_228024 REACT_228085 REACT_23891 REACT_524 REACT_614 REACT_661 REACT_962
SignaLink	P01112
EvolutionaryTrace	P01112
GeneWiki	HRAS
GenomeRNAi	3265
NextBio	12961
PRO	PR:P01112
Proteomes	UP000005640 UP000005640
Bgee	P01112
CleanEx	HS_HRAS
ExpressionAtlas	P01112
Genevestigator	P01112
GO	GO:0005737 GO:0005829 GO:0005794 GO:0000139 GO:0005634 GO:0048471 GO:0005886 GO:0005525 GO:0008022 GO:0030036 GO:0000186 GO:0007411 GO:0007596 GO:0007050 GO:0008283 GO:0007166 GO:0090398 GO:0006935 GO:0006897 GO:0007173 GO:0060441 GO:0038095 GO:0008543 GO:0006184 GO:0045087 GO:0008286 GO:0097193 GO:0050900 GO:0000165 GO:0007093 GO:0045596 GO:0008285 GO:0010629 GO:0043524 GO:0034259 GO:0048011 GO:0009887 GO:2000251 GO:0030335 GO:0008284 GO:0045740 GO:0050679 GO:0070374 GO:0046330 GO:0043406 GO:0043410 GO:2000630 GO:0001934 GO:0032855 GO:0035022 GO:1900029 GO:0045944 GO:0090303 GO:0051291 GO:0007265 GO:0048169 GO:0032228 GO:0007165 GO:0007264 GO:0035176 GO:0051146 GO:0007268 GO:0008542
Gene3D	3.40.50.300
InterPro	IPR027417 IPR005225 IPR001806 IPR020849
PANTHER	PTHR24070
Pfam	PF00071
PRINTS	PR00449
SMART	SM00173
SUPFAM	SSF52540
TIGRFAMs	TIGR00231
PROSITE	PS51421

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0019003	GDP binding	PMID:8142349^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:9230043^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0019003	GDP binding	PMID:9230043^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:9230043^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:9178006^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:21968647^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21968647^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071480	cellular response to gamma radiation	PMID:16213212^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010863	positive regulation of phospholipase C activity	PMID:11022048^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090314	positive regulation of protein targeting to membrane	PMID:11022048^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	PMID:8607982^[7]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
	GO:0005886	plasma membrane	PMID:21968647^[4]	ECO:0000314			C		When HRas was overexpressed in Hela cells, it was largely localized on the PM with a little Golgi localization (Figure 2A),	complete CACAO 2190
involved_in	GO:2000630	positive regulation of miRNA metabolic process	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
	GO:0005794	Golgi apparatus	PMID:21968647^[4]	ECO:0000314			C		When HRas was overexpressed in Hela cells, it was largely localized on the PM with a little Golgi localization (Figure 2A), (summarized in Figure 2E).	complete CACAO 2191
involved_in	GO:2000251	positive regulation of actin cytoskeleton reorganization	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900029	positive regulation of ruffle assembly	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090398	cellular senescence	PMID:9054499^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090303	positive regulation of wound healing	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070374	positive regulation of ERK1 and ERK2 cascade	PMID:22065586^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050679	positive regulation of epithelial cell proliferation	PMID:20154697^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046330	positive regulation of JNK cascade	PMID:22065586^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:22065586^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043410	positive regulation of MAPK cascade	PMID:9765203^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043406	positive regulation of MAP kinase activity	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034260	negative regulation of GTPase activity	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043547	positive regulation of GTPase activity	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030335	positive regulation of cell migration	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	PMID:9054499^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:9765203^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007265	Ras protein signal transduction	PMID:23027131^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007093	mitotic cell cycle checkpoint	PMID:9054499^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007050	cell cycle arrest	PMID:9765203^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007050	cell cycle arrest	PMID:9054499^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:17260967^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:22065586^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:9219684^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P20936	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:14500341^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:14500341^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:14500341^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:12202034^[16]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:12202034^[16]	ECO:0006013	patch-clamp recording evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
involved_in	GO:0098696	regulation of neurotransmitter receptor localization to postsynaptic specialization membrane	PMID:12202034^[16]	ECO:0006063	over expression analysis evidence used in manual assertion		P	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
involved_in	GO:0098696	regulation of neurotransmitter receptor localization to postsynaptic specialization membrane	PMID:12202034^[16]	ECO:0006013	patch-clamp recording evidence used in manual assertion		P	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:17724343^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090398	cellular senescence	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
involved_in	GO:0070374	positive regulation of ERK1 and ERK2 cascade	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
involved_in	GO:0046579	positive regulation of Ras protein signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
involved_in	GO:0045740	positive regulation of DNA replication	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	C		Seeded From UniProt	complete
involved_in	GO:0035900	response to isolation stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
involved_in	GO:0007265	Ras protein signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P20171 ensembl:ENSRNOP00000022363	C		Seeded From UniProt	complete
involved_in	GO:0097193	intrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0050852	T cell receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0048169	regulation of long-term neuronal synaptic plasticity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0042832	defense response to protozoan	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0042088	T-helper 1 type immune response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0032729	positive regulation of interferon-gamma production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0008283	cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0007569	cell aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0007265	Ras protein signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0007264	small GTPase mediated signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	P		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q61411 ensembl:ENSMUSP00000026572	F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001806	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001806 InterPro:IPR005225 InterPro:IPR020849	F		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020849	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020849	C		Seeded From UniProt	complete
involved_in	GO:0009887	animal organ morphogenesis	PMID:10848592^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007166	cell surface receptor signaling pathway	PMID:9020890^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006935	chemotaxis	PMID:10848592^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:9880516^[20] PMID:9020890^[19] Reactome:R-NUL-9617449 Reactome:R-HSA-8981355 Reactome:R-HSA-8981353 Reactome:R-HSA-8941628 Reactome:R-HSA-8941623 Reactome:R-HSA-8941618 Reactome:R-HSA-8941613 Reactome:R-HSA-8936731 Reactome:R-HSA-8936676 Reactome:R-HSA-8853307 Reactome:R-HSA-8851899 Reactome:R-HSA-8851877 Reactome:R-HSA-8851827 Reactome:R-HSA-6803240 Reactome:R-HSA-6803234 Reactome:R-HSA-6803233 Reactome:R-HSA-6803230 Reactome:R-HSA-6802943 Reactome:R-HSA-6802942 Reactome:R-HSA-6802941 Reactome:R-HSA-6802937 Reactome:R-HSA-6802926 Reactome:R-HSA-6802925 Reactome:R-HSA-6802924 Reactome:R-HSA-6802922 Reactome:R-HSA-6802921 Reactome:R-HSA-6802919 Reactome:R-HSA-6802918 Reactome:R-HSA-6802916 Reactome:R-HSA-6802915 Reactome:R-HSA-6802914 Reactome:R-HSA-6802908 Reactome:R-HSA-6802837 Reactome:R-HSA-6802834 Reactome:R-HSA-5675433 Reactome:R-HSA-5675431 Reactome:R-HSA-5675417 Reactome:R-HSA-5674022 Reactome:R-HSA-5674018 Reactome:R-HSA-5672980 Reactome:R-HSA-5672978 Reactome:R-HSA-5672973 Reactome:R-HSA-5672972 Reactome:R-HSA-5672969 Reactome:R-HSA-5672966 Reactome:R-HSA-5672965 Reactome:R-HSA-5672950 Reactome:R-HSA-5658435 Reactome:R-HSA-5658231 Reactome:R-HSA-5655347 Reactome:R-HSA-5655326 Reactome:R-HSA-5655277 Reactome:R-HSA-5655241 Reactome:R-HSA-5654663 Reactome:R-HSA-5654647 Reactome:R-HSA-5654618 Reactome:R-HSA-5654600 Reactome:R-HSA-5654426 Reactome:R-HSA-5654413 Reactome:R-HSA-5654402 Reactome:R-HSA-5654392 Reactome:R-HSA-5637808 Reactome:R-HSA-5637806 Reactome:R-HSA-5624494 Reactome:R-HSA-5624492 Reactome:R-HSA-5624486 Reactome:R-HSA-5621573 Reactome:R-HSA-5218845 Reactome:R-HSA-4093339 Reactome:R-HSA-4093331 Reactome:R-HSA-392054 Reactome:R-HSA-2424477 Reactome:R-HSA-2179407 Reactome:R-HSA-210977 Reactome:R-HSA-186834 Reactome:R-HSA-177945 Reactome:R-HSA-177938 Reactome:R-HSA-170986 Reactome:R-HSA-1433471 Reactome:R-HSA-1306972 Reactome:R-HSA-1250383 Reactome:R-HSA-1225957 Reactome:R-HSA-1225951 Reactome:R-HSA-1168636	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10842192^[21]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0048013	ephrin receptor signaling pathway	Reactome:R-HSA-2682334	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007265	Ras protein signal transduction	Reactome:R-HSA-167044	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0002223	stimulatory C-type lectin receptor signaling pathway	Reactome:R-HSA-5621481	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000165	MAPK cascade	Reactome:R-HSA-5673001	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333 UniProtKB-SubCell:SL-0132	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0134	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Kraulis, PJ et al. (1994) Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry 33 3515-31 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Ito, Y et al. (1997) Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein. Biochemistry 36 9109-19 PubMed GONUTS page
↑ Eisenmann, DM & Kim, SK (1997) Mechanism of activation of the Caenorhabditis elegans ras homologue let-60 by a novel, temperature-sensitive, gain-of-function mutation. Genetics 146 553-65 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Jin, T et al. (2012) PAQR10 and PAQR11 mediate Ras signaling in the Golgi apparatus. Cell Res. 22 661-76 PubMed GONUTS page
↑ Takagi, M et al. (2005) Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin. Cell 123 49-63 PubMed GONUTS page
↑ ^6.0 ^6.1 Song, C et al. (2001) Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J. Biol. Chem. 276 2752-7 PubMed GONUTS page
↑ McCormick, F (1995) Ras-related proteins in signal transduction and growth control. Mol. Reprod. Dev. 42 500-6 PubMed GONUTS page
↑ ^8.00 ^8.01 ^8.02 ^8.03 ^8.04 ^8.05 ^8.06 ^8.07 ^8.08 ^8.09 ^8.10 De Menna, M et al. (2013) Wnt4 inhibits cell motility induced by oncogenic Ras. Oncogene 32 4110-9 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Serrano, M et al. (1997) Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88 593-602 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Oh, YT et al. (2012) Oncogenic Ras and B-Raf proteins positively regulate death receptor 5 expression through co-activation of ERK and JNK signaling. J. Biol. Chem. 287 257-67 PubMed GONUTS page
↑ Min, J et al. (2010) An oncogene-tumor suppressor cascade drives metastatic prostate cancer by coordinately activating Ras and nuclear factor-kappaB. Nat. Med. 16 286-94 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Lin, AW et al. (1998) Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling. Genes Dev. 12 3008-19 PubMed GONUTS page
↑ Ito, G et al. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemistry 46 1380-8 PubMed GONUTS page
↑ Scheffzek, K et al. (1997) The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277 333-8 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Guil, S et al. (2003) Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus. Cancer Res. 63 5178-87 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Zhu, JJ et al. (2002) Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell 110 443-55 PubMed GONUTS page
↑ Feng, L et al. (2007) Spatial regulation of Raf kinase signaling by RKTG. Proc. Natl. Acad. Sci. U.S.A. 104 14348-53 PubMed GONUTS page
↑ ^18.0 ^18.1 Suzuki, J et al. (2000) Involvement of Ras and Ral in chemotactic migration of skeletal myoblasts. Mol. Cell. Biol. 20 4658-65 PubMed GONUTS page
↑ ^19.0 ^19.1 Shock, DD et al. (1997) Ras activation in platelets after stimulation of the thrombin receptor, thromboxane A2 receptor or protein kinase C. Biochem. J. 321 ( Pt 2) 525-30 PubMed GONUTS page
↑ Booden, MA et al. (1999) A non-farnesylated Ha-Ras protein can be palmitoylated and trigger potent differentiation and transformation. J. Biol. Chem. 274 1423-31 PubMed GONUTS page
↑ Romanenko, A et al. (2000) Increased oxidative stress with gene alteration in urinary bladder urothelium after the Chernobyl accident. Int. J. Cancer 86 790-8 PubMed GONUTS page

[PMID:8142349-1] Kraulis, PJ et al. (1994) Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry 33 3515-31 PubMed GONUTS page

[PMID:9230043-2] 2.0 ^2.1 ^2.2 Ito, Y et al. (1997) Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein. Biochemistry 36 9109-19 PubMed GONUTS page

[PMID:9178006-3] Eisenmann, DM & Kim, SK (1997) Mechanism of activation of the Caenorhabditis elegans ras homologue let-60 by a novel, temperature-sensitive, gain-of-function mutation. Genetics 146 553-65 PubMed GONUTS page

[PMID:21968647-4] 4.0 ^4.1 ^4.2 ^4.3 Jin, T et al. (2012) PAQR10 and PAQR11 mediate Ras signaling in the Golgi apparatus. Cell Res. 22 661-76 PubMed GONUTS page

[PMID:16213212-5] Takagi, M et al. (2005) Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin. Cell 123 49-63 PubMed GONUTS page

[PMID:11022048-6] 6.0 ^6.1 Song, C et al. (2001) Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J. Biol. Chem. 276 2752-7 PubMed GONUTS page

[PMID:8607982-7] McCormick, F (1995) Ras-related proteins in signal transduction and growth control. Mol. Reprod. Dev. 42 500-6 PubMed GONUTS page

[PMID:23027131-8] 8.00 ^8.01 ^8.02 ^8.03 ^8.04 ^8.05 ^8.06 ^8.07 ^8.08 ^8.09 ^8.10 De Menna, M et al. (2013) Wnt4 inhibits cell motility induced by oncogenic Ras. Oncogene 32 4110-9 PubMed GONUTS page

[PMID:9054499-9] 9.0 ^9.1 ^9.2 ^9.3 Serrano, M et al. (1997) Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88 593-602 PubMed GONUTS page

[PMID:22065586-10] 10.0 ^10.1 ^10.2 ^10.3 Oh, YT et al. (2012) Oncogenic Ras and B-Raf proteins positively regulate death receptor 5 expression through co-activation of ERK and JNK signaling. J. Biol. Chem. 287 257-67 PubMed GONUTS page

[PMID:20154697-11] Min, J et al. (2010) An oncogene-tumor suppressor cascade drives metastatic prostate cancer by coordinately activating Ras and nuclear factor-kappaB. Nat. Med. 16 286-94 PubMed GONUTS page

[PMID:9765203-12] 12.0 ^12.1 ^12.2 Lin, AW et al. (1998) Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogenic signaling. Genes Dev. 12 3008-19 PubMed GONUTS page

[PMID:17260967-13] Ito, G et al. (2007) GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. Biochemistry 46 1380-8 PubMed GONUTS page

[PMID:9219684-14] Scheffzek, K et al. (1997) The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277 333-8 PubMed GONUTS page

[PMID:14500341-15] 15.0 ^15.1 ^15.2 Guil, S et al. (2003) Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus. Cancer Res. 63 5178-87 PubMed GONUTS page

[PMID:12202034-16] 16.0 ^16.1 ^16.2 ^16.3 Zhu, JJ et al. (2002) Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell 110 443-55 PubMed GONUTS page

[PMID:17724343-17] Feng, L et al. (2007) Spatial regulation of Raf kinase signaling by RKTG. Proc. Natl. Acad. Sci. U.S.A. 104 14348-53 PubMed GONUTS page

[PMID:10848592-18] 18.0 ^18.1 Suzuki, J et al. (2000) Involvement of Ras and Ral in chemotactic migration of skeletal myoblasts. Mol. Cell. Biol. 20 4658-65 PubMed GONUTS page

[PMID:9020890-19] 19.0 ^19.1 Shock, DD et al. (1997) Ras activation in platelets after stimulation of the thrombin receptor, thromboxane A2 receptor or protein kinase C. Biochem. J. 321 ( Pt 2) 525-30 PubMed GONUTS page

[PMID:9880516-20] Booden, MA et al. (1999) A non-farnesylated Ha-Ras protein can be palmitoylated and trigger potent differentiation and transformation. J. Biol. Chem. 274 1423-31 PubMed GONUTS page

[PMID:10842192-21] Romanenko, A et al. (2000) Increased oxidative stress with gene alteration in urinary bladder urothelium after the Chernobyl accident. Int. J. Cancer 86 790-8 PubMed GONUTS page

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