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P20936 (RASA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 174. Feed History...

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

Names and origin

Protein namesRecommended 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 names
Name:RASA1
Synonyms:GAP, RASA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1047 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15

Subcellular location

Cytoplasm Ref.4.

Tissue specificity

In placental villi, detected only in the trophoblast layer (cytotrophoblast and syncytiotrophoblast). Not detected in stromal, endothelial or Hofbauer cells (at protein level). Ref.4

Post-translational modification

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. Ref.6

Involvement in disease

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. Ref.23

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.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PH domain.

Contains 1 Ras-GAP domain.

Contains 2 SH2 domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Proto-oncogene
   DomainRepeat
SH2 domain
SH3 domain
   Molecular functionGTPase activation
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processembryo development

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Non-traceable author statement PubMed 1581965. Source: UniProtKB

mitotic cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of Ras protein signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of cell adhesion

Inferred from direct assay PubMed 8344248. Source: UniProtKB

negative regulation of cell-matrix adhesion

Inferred from direct assay PubMed 8344248. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Ras GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of RNA metabolic process

Non-traceable author statement PubMed 9113414. Source: UniProtKB

regulation of actin filament polymerization

Inferred from direct assay PubMed 8344248. Source: UniProtKB

regulation of cell shape

Non-traceable author statement PubMed 9113414. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 1756860. Source: UniProtKB

vasculogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Non-traceable author statement PubMed 2821624. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intrinsic component of the cytoplasmic side of the plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

ruffle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTPase binding

Inferred from physical interaction PubMed 2122974. Source: UniProtKB

Ras GTPase activator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glycoprotein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

potassium channel inhibitor activity

Non-traceable author statement PubMed 1553544. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 2157284PubMed 2176151. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20936-1)

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.
Isoform 2 (identifier: P20936-2)

Also known as: Short;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10471047Ras GTPase-activating protein 1
PRO_0000056636

Regions

Domain181 – 27292SH2 1
Domain279 – 34163SH3
Domain351 – 44191SH2 2
Domain474 – 577104PH
Domain581 – 67696C2
Domain748 – 942195Ras-GAP
Compositional bias17 – 226Poly-Gly
Compositional bias135 – 1417Poly-Pro
Compositional bias163 – 1686Poly-Glu

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16 Ref.17
Modified residue6151Phosphotyrosine Ref.12

Natural variations

Alternative sequence1 – 177177Missing in isoform 2.
VSP_001625
Alternative sequence178 – 1803TNQ → MKG in isoform 2.
VSP_001626
Natural variant3981R → L in basal cell carcinomas. Ref.22
VAR_002650
Natural variant4001K → E in basal cell carcinomas. Ref.22
VAR_002651
Natural variant4011I → V in basal cell carcinomas. Ref.22
VAR_002652
Natural variant5401C → Y in CMAVM. Ref.23
VAR_017744

Experimental info

Sequence conflict7891R → A AA sequence Ref.4

Secondary structure

......................................................... 1047
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1991. Version 1.
Checksum: C35B6567F5BC5370

FASTA1,047116,403
        10         20         30         40         50         60 
MMAAEAGSEE GGPVTAGAGG GGAAAGSSAY PAVCRVKIPA ALPVAAAPYP GLVETGVAGT 

        70         80         90        100        110        120 
LGGGAALGSE FLGAGSVAGA LGGAGLTGGG TAAGVAGAAA GVAGAAVAGP SGDMALTKLP 

       130        140        150        160        170        180 
TSLLAETLGP GGGFPPLPPP PYLPPLGAGL GTVDEGDSLD GPEYEEEEVA IPLTAPPTNQ 

       190        200        210        220        230        240 
WYHGKLDRTI AEERLRQAGK SGSYLIRESD RRPGSFVLSF LSQMNVVNHF RIIAMCGDYY 

       250        260        270        280        290        300 
IGGRRFSSLS DLIGYYSHVS CLLKGEKLLY PVAPPEPVED RRRVRAILPY TKVPDTDEIS 

       310        320        330        340        350        360 
FLKGDMFIVH NELEDGWMWV TNLRTDEQGL IVEDLVEEVG REEDPHEGKI WFHGKISKQE 

       370        380        390        400        410        420 
AYNLLMTVGQ VCSFLVRPSD NTPGDYSLYF RTNENIQRFK ICPTPNNQFM MGGRYYNSIG 

       430        440        450        460        470        480 
DIIDHYRKEQ IVEGYYLKEP VPMQDQEQVL NDTVDGKEIY NTIRRKTKDA FYKNIVKKGY 

       490        500        510        520        530        540 
LLKKGKGKRW KNLYFILEGS DAQLIYFESE KRATKPKGLI DLSVCSVYVV HDSLFGRPNC 

       550        560        570        580        590        600 
FQIVVQHFSE EHYIFYFAGE TPEQAEDWMK GLQAFCNLRK SSPGTSNKRL RQVSSLVLHI 

       610        620        630        640        650        660 
EEAHKLPVKH FTNPYCNIYL NSVQVAKTHA REGQNPVWSE EFVFDDLPPD INRFEITLSN 

       670        680        690        700        710        720 
KTKKSKDPDI LFMRCQLSRL QKGHATDEWF LLSSHIPLKG IEPGSLRVRA RYSMEKIMPE 

       730        740        750        760        770        780 
EEYSEFKELI LQKELHVVYA LSHVCGQDRT LLASILLRIF LHEKLESLLL CTLNDREISM 

       790        800        810        820        830        840 
EDEATTLFRA TTLASTLMEQ YMKATATQFV HHALKDSILK IMESKQSCEL SPSKLEKNED 

       850        860        870        880        890        900 
VNTNLTHLLN ILSELVEKIF MASEILPPTL RYIYGCLQKS VQHKWPTNTT MRTRVVSGFV 

       910        920        930        940        950        960 
FLRLICPAIL NPRMFNIISD SPSPIAARTL ILVAKSVQNL ANLVEFGAKE PYMEGVNPFI 

       970        980        990       1000       1010       1020 
KSNKHRMIMF LDELGNVPEL PDTTEHSRTD LSRDLAALHE ICVAHSDELR TLSNERGAQQ 

      1030       1040 
HVLKKLLAIT ELLQQKQNQY TKTNDVR 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: B328E701911065F9
Show »

FASTA870100,398

References

« Hide 'large scale' references
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23379 mRNA. Translation: AAA52517.1.
M23612 mRNA. Translation: AAA35865.1.
AK312739 mRNA. Translation: BAG35610.1.
BC033015 mRNA. Translation: AAH33015.1.
PIRA40121.
B40121.
RefSeqNP_002881.1. NM_002890.2.
NP_072179.1. NM_022650.2.
UniGeneHs.664080.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP20936.
SMRP20936. Positions 110-446, 475-573, 692-1041.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111856. 54 interactions.
DIPDIP-144N.
IntActP20936. 33 interactions.
MINTMINT-195165.
STRING9606.ENSP00000274376.

PTM databases

PhosphoSiteP20936.

Polymorphism databases

DMDM121743.

Proteomic databases

PaxDbP20936.
PRIDEP20936.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274376; ENSP00000274376; ENSG00000145715. [P20936-1]
ENST00000456692; ENSP00000411221; ENSG00000145715. [P20936-2]
GeneID5921.
KEGGhsa:5921.
UCSCuc003kiw.3. human. [P20936-1]
uc003kix.3. human. [P20936-2]

Organism-specific databases

CTD5921.
GeneCardsGC05P086565.
HGNCHGNC:9871. RASA1.
HPACAB007789.
MIM139150. gene.
608354. phenotype.
608355. phenotype.
neXtProtNX_P20936.
Orphanet137667. Capillary malformation - arteriovenous malformation.
90307. Parkes Weber syndrome.
PharmGKBPA34232.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282054.
HOGENOMHOG000007794.
HOVERGENHBG057470.
InParanoidP20936.
KOK04352.
OMACLQNLAN.
OrthoDBEOG7HTHG8.
PhylomeDBP20936.
TreeFamTF105301.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP20936.

Gene expression databases

ArrayExpressP20936.
BgeeP20936.
CleanExHS_RASA1.
GenevestigatorP20936.

Family and domain databases

Gene3D1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
3.30.505.10. 2 hits.
InterProIPR000008. C2_dom.
IPR028554. p120-RasGAP.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10194:SF19. PTHR10194:SF19. 1 hit.
PfamPF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00616. RasGAP. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
SMARTSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEPS50004. 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]
ProtoNetSearch...

Other

ChiTaRSRASA1. human.
EvolutionaryTraceP20936.
GeneWikiRAS_p21_protein_activator_1.
GenomeRNAi5921.
NextBio23056.
PMAP-CutDBP20936.
PROP20936.
SOURCESearch...

Entry information

Entry nameRASA1_HUMAN
AccessionPrimary (citable) accession number: P20936
Secondary accession number(s): B2R6W3, Q9UDI1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM