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P20936

- RASA1_HUMAN

UniProt

P20936 - RASA1_HUMAN

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Protein
Ras GTPase-activating protein 1
Gene
RASA1, GAP, RASA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1.2 Publications

GO - Molecular functioni

  1. GTPase binding Source: UniProtKB
  2. Ras GTPase activator activity Source: RefGenome
  3. glycoprotein binding Source: UniProtKB
  4. potassium channel inhibitor activity Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. receptor binding Source: UniProtKB

GO - Biological processi

  1. embryo development Source: UniProtKB
  2. intracellular signal transduction Source: UniProtKB
  3. mitotic cytokinesis Source: UniProtKB
  4. negative regulation of Ras protein signal transduction Source: RefGenome
  5. negative regulation of cell adhesion Source: UniProtKB
  6. negative regulation of cell-matrix adhesion Source: UniProtKB
  7. negative regulation of neuron apoptotic process Source: UniProtKB
  8. positive regulation of Ras GTPase activity Source: RefGenome
  9. regulation of RNA metabolic process Source: UniProtKB
  10. regulation of actin filament polymerization Source: UniProtKB
  11. regulation of cell shape Source: UniProtKB
  12. signal transduction Source: UniProtKB
  13. vasculogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiREACT_17025. Downstream signal transduction.
SignaLinkiP20936.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras GTPase-activating protein 1
Short name:
GAP
Short name:
GTPase-activating protein
Short name:
RasGAP
Alternative name(s):
Ras p21 protein activator
p120GAP
Gene namesi
Name:RASA1
Synonyms:GAP, RASA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:9871. RASA1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. intrinsic component of the cytoplasmic side of the plasma membrane Source: RefGenome
  4. ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Mutations in the SH2 domain of RASA seem to be oncogenic and cause basal cell carcinomas.
Capillary malformation-arteriovenous malformation (CMAVM) [MIM:608354]: A disorder characterized by atypical capillary malformations that are multiple, small, round to oval in shape and pinkish red in color. These capillary malformations are associated with either arteriovenous malformation, arteriovenous fistula, or Parkes Weber syndrome.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti540 – 5401C → Y in CMAVM. 1 Publication
VAR_017744
Parkes Weber syndrome (PKWS) [MIM:608355]: Disorder characterized by a cutaneous flush with underlying multiple micro-arteriovenous fistulas, in association with soft tissue and skeletal hypertrophy of the affected limb.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MIMi608354. phenotype.
608355. phenotype.
Orphaneti137667. Capillary malformation - arteriovenous malformation.
90307. Parkes Weber syndrome.
PharmGKBiPA34232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10471047Ras GTPase-activating protein 1
PRO_0000056636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei615 – 6151Phosphotyrosine1 Publication

Post-translational modificationi

The N-terminus is blocked.
Phosphorylated by SRC and LCK. The phosphorylation SRC inhibits its ability to stimulate the Ras-GTPase activity, whereas phosphorylation by LCK does not display any effect on stimulation activity.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP20936.
PaxDbiP20936.
PRIDEiP20936.

PTM databases

PhosphoSiteiP20936.

Miscellaneous databases

PMAP-CutDBP20936.

Expressioni

Tissue specificityi

In placental villi, detected only in the trophoblast layer (cytotrophoblast and syncytiotrophoblast). Not detected in stromal, endothelial or Hofbauer cells (at protein level).1 Publication

Gene expression databases

ArrayExpressiP20936.
BgeeiP20936.
CleanExiHS_RASA1.
GenevestigatoriP20936.

Organism-specific databases

HPAiCAB007789.

Interactioni

Subunit structurei

Interacts with SQSTM1. Interacts with SPSB1; the interaction does not promote degradation. Interacts with CAV2 (tyrosine phosphorylated form). Directly interacts with NCK1. Interacts with PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP02EBI-1026476,EBI-375446
ARP1027516EBI-1026476,EBI-608057
CAPNS1P046323EBI-1026476,EBI-711828
DLC1Q96QB16EBI-1026476,EBI-2608428
EGFRP005337EBI-1026476,EBI-297353
ERBB2P046267EBI-1026476,EBI-641062
ERBB3P218606EBI-1026476,EBI-720706
GAB1Q1348025EBI-1026476,EBI-517684
KITP1072116EBI-1026476,EBI-1379503
METP0858115EBI-1026476,EBI-1039152
NCK1P163336EBI-1026476,EBI-389883
PDGFRBP096193EBI-1026476,EBI-641237

Protein-protein interaction databases

BioGridi111856. 54 interactions.
DIPiDIP-144N.
IntActiP20936. 36 interactions.
MINTiMINT-195165.
STRINGi9606.ENSP00000274376.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi283 – 2886
Beta strandi296 – 2983
Beta strandi306 – 3127
Beta strandi316 – 3227
Turni323 – 3253
Beta strandi328 – 3325
Helixi333 – 3353
Beta strandi336 – 3383
Helixi720 – 7234
Helixi724 – 7307
Helixi736 – 7449
Beta strandi746 – 7483
Helixi749 – 76214
Helixi766 – 78015
Helixi784 – 7863
Turni787 – 7893
Helixi793 – 80513
Helixi807 – 82317
Helixi832 – 8343
Helixi841 – 86020
Helixi861 – 8655
Helixi868 – 88417
Helixi891 – 90010
Turni901 – 9044
Helixi905 – 9106
Turni912 – 9165
Helixi924 – 94118
Beta strandi946 – 9494
Helixi951 – 9566
Helixi957 – 97418
Helixi992 – 100413
Helixi1006 – 10138
Helixi1020 – 103819

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WERX-ray1.60A714-1047[»]
1WQ1X-ray2.50G714-1047[»]
2GQINMR-A282-339[»]
2GSBNMR-A341-446[»]
2J05X-ray1.50A/B281-341[»]
2J06X-ray1.80A/B281-341[»]
2M51NMR-A281-341[»]
4FSSX-ray2.25A/B/C281-341[»]
ProteinModelPortaliP20936.
SMRiP20936. Positions 168-446, 475-573, 593-713, 718-1041.

Miscellaneous databases

EvolutionaryTraceiP20936.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 27292SH2 1
Add
BLAST
Domaini279 – 34163SH3
Add
BLAST
Domaini351 – 44191SH2 2
Add
BLAST
Domaini474 – 577104PH
Add
BLAST
Domaini581 – 67696C2
Add
BLAST
Domaini748 – 942195Ras-GAP
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 226Poly-Gly
Compositional biasi135 – 1417Poly-Pro
Compositional biasi163 – 1686Poly-Glu

Sequence similaritiesi

Contains 1 C2 domain.
Contains 1 PH domain.
Contains 1 Ras-GAP domain.
Contains 2 SH2 domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG282054.
HOGENOMiHOG000007794.
HOVERGENiHBG057470.
InParanoidiP20936.
KOiK04352.
OMAiQAQDWMK.
OrthoDBiEOG7HTHG8.
PhylomeDBiP20936.
TreeFamiTF105301.

Family and domain databases

Gene3Di1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00616. RasGAP. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P20936-1) [UniParc]FASTAAdd to Basket

Also known as: Long

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

MMAAEAGSEE GGPVTAGAGG GGAAAGSSAY PAVCRVKIPA ALPVAAAPYP     50
GLVETGVAGT LGGGAALGSE FLGAGSVAGA LGGAGLTGGG TAAGVAGAAA 100
GVAGAAVAGP SGDMALTKLP TSLLAETLGP GGGFPPLPPP PYLPPLGAGL 150
GTVDEGDSLD GPEYEEEEVA IPLTAPPTNQ WYHGKLDRTI AEERLRQAGK 200
SGSYLIRESD RRPGSFVLSF LSQMNVVNHF RIIAMCGDYY IGGRRFSSLS 250
DLIGYYSHVS CLLKGEKLLY PVAPPEPVED RRRVRAILPY TKVPDTDEIS 300
FLKGDMFIVH NELEDGWMWV TNLRTDEQGL IVEDLVEEVG REEDPHEGKI 350
WFHGKISKQE AYNLLMTVGQ VCSFLVRPSD NTPGDYSLYF RTNENIQRFK 400
ICPTPNNQFM MGGRYYNSIG DIIDHYRKEQ IVEGYYLKEP VPMQDQEQVL 450
NDTVDGKEIY NTIRRKTKDA FYKNIVKKGY LLKKGKGKRW KNLYFILEGS 500
DAQLIYFESE KRATKPKGLI DLSVCSVYVV HDSLFGRPNC FQIVVQHFSE 550
EHYIFYFAGE TPEQAEDWMK GLQAFCNLRK SSPGTSNKRL RQVSSLVLHI 600
EEAHKLPVKH FTNPYCNIYL NSVQVAKTHA REGQNPVWSE EFVFDDLPPD 650
INRFEITLSN KTKKSKDPDI LFMRCQLSRL QKGHATDEWF LLSSHIPLKG 700
IEPGSLRVRA RYSMEKIMPE EEYSEFKELI LQKELHVVYA LSHVCGQDRT 750
LLASILLRIF LHEKLESLLL CTLNDREISM EDEATTLFRA TTLASTLMEQ 800
YMKATATQFV HHALKDSILK IMESKQSCEL SPSKLEKNED VNTNLTHLLN 850
ILSELVEKIF MASEILPPTL RYIYGCLQKS VQHKWPTNTT MRTRVVSGFV 900
FLRLICPAIL NPRMFNIISD SPSPIAARTL ILVAKSVQNL ANLVEFGAKE 950
PYMEGVNPFI KSNKHRMIMF LDELGNVPEL PDTTEHSRTD LSRDLAALHE 1000
ICVAHSDELR TLSNERGAQQ HVLKKLLAIT ELLQQKQNQY TKTNDVR 1047
Length:1,047
Mass (Da):116,403
Last modified:February 1, 1991 - v1
Checksum:iC35B6567F5BC5370
GO
Isoform 2 (identifier: P20936-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-177: Missing.
     178-180: TNQ → MKG

Show »
Length:870
Mass (Da):100,398
Checksum:iB328E701911065F9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti398 – 3981R → L in basal cell carcinomas. 1 Publication
VAR_002650
Natural varianti400 – 4001K → E in basal cell carcinomas. 1 Publication
VAR_002651
Natural varianti401 – 4011I → V in basal cell carcinomas. 1 Publication
VAR_002652
Natural varianti540 – 5401C → Y in CMAVM. 1 Publication
VAR_017744

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 177177Missing in isoform 2.
VSP_001625Add
BLAST
Alternative sequencei178 – 1803TNQ → MKG in isoform 2.
VSP_001626

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti789 – 7891R → A AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23379 mRNA. Translation: AAA52517.1.
M23612 mRNA. Translation: AAA35865.1.
AK312739 mRNA. Translation: BAG35610.1.
BC033015 mRNA. Translation: AAH33015.1.
CCDSiCCDS34200.1. [P20936-1]
CCDS47243.1. [P20936-2]
PIRiA40121.
B40121.
RefSeqiNP_002881.1. NM_002890.2. [P20936-1]
NP_072179.1. NM_022650.2. [P20936-2]
UniGeneiHs.664080.

Genome annotation databases

EnsembliENST00000274376; ENSP00000274376; ENSG00000145715. [P20936-1]
ENST00000456692; ENSP00000411221; ENSG00000145715. [P20936-2]
GeneIDi5921.
KEGGihsa:5921.
UCSCiuc003kiw.3. human. [P20936-1]
uc003kix.3. human. [P20936-2]

Polymorphism databases

DMDMi121743.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23379 mRNA. Translation: AAA52517.1 .
M23612 mRNA. Translation: AAA35865.1 .
AK312739 mRNA. Translation: BAG35610.1 .
BC033015 mRNA. Translation: AAH33015.1 .
CCDSi CCDS34200.1. [P20936-1 ]
CCDS47243.1. [P20936-2 ]
PIRi A40121.
B40121.
RefSeqi NP_002881.1. NM_002890.2. [P20936-1 ]
NP_072179.1. NM_022650.2. [P20936-2 ]
UniGenei Hs.664080.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WER X-ray 1.60 A 714-1047 [» ]
1WQ1 X-ray 2.50 G 714-1047 [» ]
2GQI NMR - A 282-339 [» ]
2GSB NMR - A 341-446 [» ]
2J05 X-ray 1.50 A/B 281-341 [» ]
2J06 X-ray 1.80 A/B 281-341 [» ]
2M51 NMR - A 281-341 [» ]
4FSS X-ray 2.25 A/B/C 281-341 [» ]
ProteinModelPortali P20936.
SMRi P20936. Positions 168-446, 475-573, 593-713, 718-1041.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111856. 54 interactions.
DIPi DIP-144N.
IntActi P20936. 36 interactions.
MINTi MINT-195165.
STRINGi 9606.ENSP00000274376.

PTM databases

PhosphoSitei P20936.

Polymorphism databases

DMDMi 121743.

Proteomic databases

MaxQBi P20936.
PaxDbi P20936.
PRIDEi P20936.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274376 ; ENSP00000274376 ; ENSG00000145715 . [P20936-1 ]
ENST00000456692 ; ENSP00000411221 ; ENSG00000145715 . [P20936-2 ]
GeneIDi 5921.
KEGGi hsa:5921.
UCSCi uc003kiw.3. human. [P20936-1 ]
uc003kix.3. human. [P20936-2 ]

Organism-specific databases

CTDi 5921.
GeneCardsi GC05P086565.
GeneReviewsi RASA1.
HGNCi HGNC:9871. RASA1.
HPAi CAB007789.
MIMi 139150. gene.
608354. phenotype.
608355. phenotype.
neXtProti NX_P20936.
Orphaneti 137667. Capillary malformation - arteriovenous malformation.
90307. Parkes Weber syndrome.
PharmGKBi PA34232.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282054.
HOGENOMi HOG000007794.
HOVERGENi HBG057470.
InParanoidi P20936.
KOi K04352.
OMAi QAQDWMK.
OrthoDBi EOG7HTHG8.
PhylomeDBi P20936.
TreeFami TF105301.

Enzyme and pathway databases

Reactomei REACT_17025. Downstream signal transduction.
SignaLinki P20936.

Miscellaneous databases

ChiTaRSi RASA1. human.
EvolutionaryTracei P20936.
GeneWikii RAS_p21_protein_activator_1.
GenomeRNAii 5921.
NextBioi 23056.
PMAP-CutDB P20936.
PROi P20936.
SOURCEi Search...

Gene expression databases

ArrayExpressi P20936.
Bgeei P20936.
CleanExi HS_RASA1.
Genevestigatori P20936.

Family and domain databases

Gene3Di 1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.30.505.10. 2 hits.
InterProi IPR000008. C2_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00616. RasGAP. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
SMARTi SM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50004. C2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of two types of GAP complementary DNA from human placenta."
    Trahey M., Wong G., Halenbeck R., Rubinfeld B., Martin G.A., Ladner M., Long C.M., Crosier W.J., Watt K., Koths K., McCormick F.
    Science 242:1697-1700(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta.
  2. "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] (ISOFORM 2).
    Tissue: Placenta.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "Purification, characterization, and cellular localization of the 100-kDa human placental GTPase-activating protein."
    Zhang Y., Zhang G., Mollat P., Carles C., Riva M., Frobert Y., Malassine A., Rostene W., Thang D.C., Beltchev B., Tavitian A., Thane M.N.
    J. Biol. Chem. 268:18875-18881(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 294-303; 326-334; 392-398; 439-457; 458-466; 479-483; 777-790 AND 821-825, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  5. "Purification, characterization, and western blot analysis of human GTPase-activating protein from native and recombinant sources."
    Halenbeck R., Crosier W.J., Clark R., McCormick F., Koths K.
    J. Biol. Chem. 265:21922-21928(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-7 (ISOFORM 2).
  6. "Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm."
    Giglione C., Gonfloni S., Parmeggiani A.
    Eur. J. Biochem. 268:3275-3283(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, FUNCTION.
  7. "GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit."
    Kazlauskas A., Kashishian A., Cooper J.A., Valius M.
    Mol. Cell. Biol. 12:2534-2544(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRB.
  8. "Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region."
    Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.
    Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1.
  9. "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
    Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
    J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  10. "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)."
    Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W., Campos-Gonzalez R., Lisanti M.P.
    Biochemistry 43:13694-13706(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV2.
  11. "The SPRY domain-containing SOCS box protein 1 (SSB-1) interacts with MET and enhances the hepatocyte growth factor-induced Erk-Elk-1-serum response element pathway."
    Wang D., Li Z., Messing E.M., Wu G.
    J. Biol. Chem. 280:16393-16401(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPSB1.
  12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding."
    Yang K.J., Shin S., Piao L., Shin E., Li Y., Park K.A., Byun H.S., Won M., Hong J., Kweon G.R., Hur G.M., Seok J.H., Chun T., Brazil D.P., Hemmings B.A., Park J.
    J. Biol. Chem. 283:1480-1491(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDPK1.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity."
    Ger M., Zitkus Z., Valius M.
    Cell. Signal. 23:1651-1658(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NCK1.
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence."
    Yang Y.S., Garbay C., Duschesne M., Cornille F., Jullian N., Fromage N., Tocque B., Roques B.P.
    EMBO J. 13:1270-1279(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 275-350.
  19. "Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras."
    Scheffzek K., Lautwein A., Kabsch W., Reza Ahmadian M., Wittinghofer A.
    Nature 384:591-596(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 714-1047.
  20. "The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants."
    Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A., Schmitz F., Wittinghofer A.
    Science 277:333-338(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 714-1047 IN COMPLEX WITH RAS.
  21. "Solution structure of the SH3 domain and of the second SH2 domain of human RAS GTPase-activating protein 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (MAY-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 282-446.
  22. "Nonsense mutations in the C-terminal SH2 region of the GTPase activating protein (GAP) gene in human tumours."
    Friedman E., Gejman P.V., Martin G.A., McCormick F.
    Nat. Genet. 5:242-247(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LEU-398; GLU-400 AND VAL-401.
  23. "Capillary malformation-arteriovenous malformation, a new clinical and genetic disorder caused by RASA1 mutations."
    Eerola I., Boon L.M., Mulliken J.B., Burrows P.E., Dompmartin A., Watanabe S., Vanwijck R., Vikkula M.
    Am. J. Hum. Genet. 73:1240-1249(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMAVM TYR-540.

Entry informationi

Entry nameiRASA1_HUMAN
AccessioniPrimary (citable) accession number: P20936
Secondary accession number(s): B2R6W3, Q9UDI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: September 3, 2014
This is version 178 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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

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