Reviewed, UniProtKB/Swiss-Prot P20936 (RASA1_HUMAN)

Names and origin

Protein names

Recommended name:
    Ras GTPase-activating protein 1
      Short name=RasGAP
      Short name=GTPase-activating protein
      Short name=GAP
Alternative name(s):
    Ras p21 protein activator
    p120GAP

Gene names

Name:	RASA1
Synonyms:	RASA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1047 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subunit structure	Interacts with SQTSM1. Interacts with SPSB1; the interaction does not promote degradation. Interacts with CAV2 (tyrosine phosphorylated form). Ref.6 Ref.7 Ref.8 Ref.18
Subcellular location	Cytoplasm.
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).
Post-translational modification	The N-terminus is blocked.
Involvement in disease	Mutations in the SH2 domain of RASA seem to be oncogenic and cause basal cell carcinomas. Defects in RASA1 are the cause of capillary malformation-arteriovenous malformation (CMAVM) [MIM:608354]. CMAVM is 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. Ref.17 Defects in RASA1 are a cause of Parkes Weber syndrome (PKWS) [MIM:608355]. PKWS is a disorder characterized by a cutaneous flush with underlying multiple micro-arteriovenous fistulas, in association with soft tissue and skeletal hypertrophy of the affected limb.
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 component	Cytoplasm
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Proto-oncogene
Domain	Repeat SH2 domain SH3 domain
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB embryonic development Inferred from sequence or structural similarity. Source: UniProtKB intracellular signaling cascade Non-traceable author statement. Source: UniProtKB negative regulation of cell-matrix adhesion Inferred from direct assay. Source: UniProtKB negative regulation of neuron apoptosis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of anti-apoptosis Inferred from direct assay. Source: UniProtKB regulation of RNA metabolic process Non-traceable author statement. Source: UniProtKB regulation of actin filament polymerization Inferred from direct assay. Source: UniProtKB regulation of cell shape Non-traceable author statement. Source: UniProtKB regulation of small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro vasculogenesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Non-traceable author statement. Source: UniProtKB
Molecular function	GTPase binding Inferred from physical interaction. Source: UniProtKB Ras GTPase activator activity Traceable author statement. Source: ProtInc glycoprotein binding Ref.6 Inferred from physical interaction. Source: UniProtKB potassium channel inhibitor activity Non-traceable author statement. Source: UniProtKB receptor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HRAS	P01112	1	EBI-1026476,EBI-350145

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1047

1047

Ras GTPase-activating protein 1

PRO_0000056636

Regions

Domain

181 – 272

92

SH2 1

Domain

279 – 341

63

SH3

Domain

351 – 441

91

SH2 2

Domain

474 – 577

104

PH

Domain

581 – 676

96

C2

Domain

748 – 942

195

Ras-GAP

Compositional bias

17 – 22

6

Poly-Gly

Compositional bias

135 – 141

7

Poly-Pro

Compositional bias

163 – 168

6

Poly-Glu

Amino acid modifications

Modified residue

615

1

Phosphotyrosine Ref.9 Ref.10

Natural variations

Alternative sequence

1 – 177

177

Missing in isoform 2.

VSP_001625

Alternative sequence

178 – 180

3

TNQ → MKG in isoform 2.

VSP_001626

Natural variant

398

1

R → L in basal cell carcinomas. Ref.16

VAR_002650

Natural variant

400

1

K → E in basal cell carcinomas. Ref.16

VAR_002651

Natural variant

401

1

I → V in basal cell carcinomas. Ref.16

VAR_002652

Natural variant

540

1

C → Y in CMAVM. Ref.17

VAR_017744

Experimental info

Sequence conflict

789

1

R → A AA sequence Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1047

Helix Strand Turn

Details...

Beta strand

283 – 288

6

Beta strand

296 – 298

3

Beta strand

306 – 312

7

Beta strand

316 – 322

7

Turn

323 – 325

3

Beta strand

328 – 332

5

Helix

333 – 335

3

Beta strand

336 – 338

3

Helix

720 – 723

4

Helix

724 – 730

7

Helix

736 – 744

9

Helix

749 – 762

14

Helix

766 – 780

15

Helix

784 – 786

3

Helix

793 – 805

13

Helix

807 – 823

17

Helix

832 – 834

3

Helix

841 – 860

20

Helix

861 – 865

5

Helix

868 – 884

17

Helix

891 – 900

10

Turn

901 – 904

4

Helix

905 – 910

6

Turn

912 – 916

5

Helix

924 – 941

18

Helix

951 – 956

6

Helix

957 – 974

18

Helix

992 – 1004

13

Helix

1006 – 1013

8

Helix

1020 – 1038

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified February 1, 1991. Version 1. Checksum: C35B6567F5BC5370	FASTA	1,047	116,403
	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
	Isoform 2 (Short). Checksum: B328E701911065F9	FASTA	870	100,398
	10 20 30 40 50 60 MKGWYHGKLD RTIAEERLRQ AGKSGSYLIR ESDRRPGSFV LSFLSQMNVV NHFRIIAMCG 70 80 90 100 110 120 DYYIGGRRFS SLSDLIGYYS HVSCLLKGEK LLYPVAPPEP VEDRRRVRAI LPYTKVPDTD 130 140 150 160 170 180 EISFLKGDMF IVHNELEDGW MWVTNLRTDE QGLIVEDLVE EVGREEDPHE GKIWFHGKIS 190 200 210 220 230 240 KQEAYNLLMT VGQVCSFLVR PSDNTPGDYS LYFRTNENIQ RFKICPTPNN QFMMGGRYYN 250 260 270 280 290 300 SIGDIIDHYR KEQIVEGYYL KEPVPMQDQE QVLNDTVDGK EIYNTIRRKT KDAFYKNIVK 310 320 330 340 350 360 KGYLLKKGKG KRWKNLYFIL EGSDAQLIYF ESEKRATKPK GLIDLSVCSV YVVHDSLFGR 370 380 390 400 410 420 PNCFQIVVQH FSEEHYIFYF AGETPEQAED WMKGLQAFCN LRKSSPGTSN KRLRQVSSLV 430 440 450 460 470 480 LHIEEAHKLP VKHFTNPYCN IYLNSVQVAK THAREGQNPV WSEEFVFDDL PPDINRFEIT 490 500 510 520 530 540 LSNKTKKSKD PDILFMRCQL SRLQKGHATD EWFLLSSHIP LKGIEPGSLR VRARYSMEKI 550 560 570 580 590 600 MPEEEYSEFK ELILQKELHV VYALSHVCGQ DRTLLASILL RIFLHEKLES LLLCTLNDRE 610 620 630 640 650 660 ISMEDEATTL FRATTLASTL MEQYMKATAT QFVHHALKDS ILKIMESKQS CELSPSKLEK 670 680 690 700 710 720 NEDVNTNLTH LLNILSELVE KIFMASEILP PTLRYIYGCL QKSVQHKWPT NTTMRTRVVS 730 740 750 760 770 780 GFVFLRLICP AILNPRMFNI ISDSPSPIAA RTLILVAKSV QNLANLVEFG AKEPYMEGVN 790 800 810 820 830 840 PFIKSNKHRM IMFLDELGNV PELPDTTEHS RTDLSRDLAA LHEICVAHSD ELRTLSNERG 850 860 870 AQQHVLKKLL AITELLQQKQ NQYTKTNDVR

References

	« Hide 'large scale' referencesShow '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: 3201259] [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: 14702039] [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: 15489334] [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: 8360177] [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: 2123878] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7 (ISOFORM 2).
[6]	"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: 8618896] [Abstract] Cited for: INTERACTION WITH SQSTM1.
[7]	"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: 12091389] [Abstract] Cited for: INTERACTION WITH CAV2.
[8]	"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: 15504032] [Abstract] Cited for: INTERACTION WITH CAV2.
[9]	"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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, MASS SPECTROMETRY.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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: 8137811] [Abstract] Cited for: STRUCTURE BY NMR OF 275-350.
[13]	"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: 8955277] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 714-1047.
[14]	"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: 9219684] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 714-1047 IN COMPLEX WITH RAS.
[15]	"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.
[16]	"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: 8275088] [Abstract] Cited for: VARIANTS LEU-398; GLU-400 AND VAL-401.
[17]	"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: 14639529] [Abstract] Cited for: VARIANT CMAVM TYR-540.
[18]	"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: 15713673] [Abstract] Cited for: INTERACTION WITH SPSB1.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00026262.
IPI00220356.

PIR

A40121.
B40121.

RefSeq

NP_002881.1.
NP_072179.1.

UniGene

Hs.664080

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

SMR

P20936. Positions 177-279, 180-442, 475-573, 592-700, 677-1011.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-144N.

IntAct

P20936. 2 interactions.

STRING

P20936.

PTM databases

PhosphoSite

P20936.

Proteomic databases

PRIDE

P20936.

Genome annotation databases

Ensembl

ENST00000274376; ENSP00000274376; ENSG00000145715; Homo sapiens. [Genome view]

GeneID

5921.

KEGG

hsa:5921.

UCSC

uc003kiw.1. human.
uc003kix.1. human.

Organism-specific databases

CTD

5921.

GeneCards

GC05P086599.

H-InvDB

HIX0005015.

HGNC

HGNC:9871. RASA1.

HPA

CAB007789.

MIM

139150. gene.
608354. phenotype.
608355. phenotype.

Orphanet

2346. Angio-osteohypertrophic syndrome.
137667. Capillary malformation-arteriovenous malformation.

PharmGKB

PA34232.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG315246.

HOVERGEN

P20936.

InParanoid

P20936.

OMA

VLNDTVD.

OrthoDB

EOG9P2SNF.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
aurora_a_pathway. Aurora A signaling.
aurora_b_pathway. Aurora B signaling.
bcr_5pathway. BCR signaling pathway.
ephbfwdpathway. EPHB forward signaling.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
il2_1pathway. IL2-mediated signaling events.
insulin_pathway. Insulin Pathway.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
pdgfrbpathway. PDGFR-beta signaling pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_16888. Signaling by PDGF.

Gene expression databases

ArrayExpress

P20936.

Bgee

P20936.

CleanEx

HS_RASA1.

Genevestigator

P20936.

GermOnline

ENSG00000145715. Homo sapiens.

Family and domain databases

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR001936. RasGAP.
IPR008936. Rho_GTPase_activation_prot.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:3.30.505.10. SH2. 2 hits.

Pfam

PF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00616. RasGAP. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.

SMART

SM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other Resources

NextBio

23056.

PMAP-CutDB

P20936.

SOURCE

Search...

Entry information

Entry name

RASA1_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.