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Protein

Ras GTPase-activating protein 1

Gene

Rasa1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21 (By similarity).By similarity

GO - Molecular functioni

  • GTPase activator activity Source: RGD
  • ion channel binding Source: RGD
  • kinase binding Source: RGD
  • platelet-derived growth factor receptor binding Source: RGD
  • protein complex binding Source: RGD
  • protein kinase B binding Source: RGD
  • protein tyrosine kinase binding Source: RGD
  • receptor tyrosine kinase binding Source: RGD
  • transcription factor binding Source: RGD

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • activation of GTPase activity Source: RGD
  • cell adhesion Source: UniProtKB
  • cellular response to epidermal growth factor stimulus Source: RGD
  • cellular response to fibroblast growth factor stimulus Source: RGD
  • cellular response to platelet-derived growth factor stimulus Source: RGD
  • embryo development Source: UniProtKB
  • male genitalia development Source: RGD
  • mitotic cytokinesis Source: UniProtKB
  • negative regulation of cell adhesion Source: UniProtKB
  • negative regulation of cell-matrix adhesion Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • negative regulation of Ras protein signal transduction Source: GO_Central
  • positive regulation of fibroblast proliferation Source: RGD
  • positive regulation of glucose import Source: RGD
  • positive regulation of GTPase activity Source: RGD
  • positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • regulation of actin filament polymerization Source: UniProtKB
  • response to drug Source: RGD
  • response to insulin Source: RGD
  • signal transduction Source: UniProtKB
  • vasculogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

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:Rasa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3537. Rasa1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • intrinsic component of the cytoplasmic side of the plasma membrane Source: GO_Central
  • membrane Source: RGD
  • nuclear membrane Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10381038Ras GTPase-activating protein 1PRO_0000056637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei606 – 6061PhosphotyrosineBy similarity
Modified residuei822 – 8221PhosphoserineBy similarity

Post-translational modificationi

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP50904.
PRIDEiP50904.

PTM databases

iPTMnetiP50904.
PhosphoSiteiP50904.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • ion channel binding Source: RGD
  • kinase binding Source: RGD
  • platelet-derived growth factor receptor binding Source: RGD
  • protein complex binding Source: RGD
  • protein kinase B binding Source: RGD
  • protein tyrosine kinase binding Source: RGD
  • receptor tyrosine kinase binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi247705. 2 interactions.
IntActiP50904. 3 interactions.
MINTiMINT-1519584.
STRINGi10116.ENSRNOP00000047300.

Structurei

3D structure databases

ProteinModelPortaliP50904.
SMRiP50904. Positions 272-437, 709-1032.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini172 – 26392SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini270 – 33263SH3PROSITE-ProRule annotationAdd
BLAST
Domaini342 – 43291SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini465 – 568104PHPROSITE-ProRule annotationAdd
BLAST
Domaini572 – 66796C2PROSITE-ProRule annotationAdd
BLAST
Domaini739 – 933195Ras-GAPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 996Poly-Ala
Compositional biasi126 – 1327Poly-Pro
Compositional biasi154 – 1596Poly-Glu

Sequence similaritiesi

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

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG3508. Eukaryota.
ENOG410XPU1. LUCA.
HOGENOMiHOG000007794.
HOVERGENiHBG057470.
InParanoidiP50904.
KOiK04352.
PhylomeDBiP50904.

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.
IPR028554. p120-RasGAP.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10194:SF19. PTHR10194:SF19. 1 hit.
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.
SSF50729. SSF50729. 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]

Sequencei

Sequence statusi: Complete.

P50904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAAEAGSEE GGPATAGTGG AAATGSSAYP AACRVKLPAA PPMAVAPCPG
60 70 80 90 100
LADTDLAAAL GGGAASGSGF LGTGPVSGVL GGAALTGGAA AGVAGAAAAG
110 120 130 140 150
PAGDIALTKG TLSLPAETLG PGGGFPPLPP PPLLPPLGSG LGTVDEGDSL
160 170 180 190 200
DGPEYEEEEV AIPLTAPPTN QWYHGKLDRT IAEERLRQAG KSGSYLIRES
210 220 230 240 250
DRRPGSFVLS FLSQTNVVNH FRIIAMCGDY YIGGRRFSSL SDLIGYYSHV
260 270 280 290 300
SCLLKGEKLL YPVAPPEPVE DRRRVRAILP YTKVPDTDEI SFLKGDMFIV
310 320 330 340 350
HNELEDGWMW VTNLRTDEQG LIVEDLVEEV GREEDPHEGK IWFHGKISKQ
360 370 380 390 400
EAYNLLMTVG QVCSFLVRPS DNTPGDYSLY FRTNENIQRF KICPTPNNQF
410 420 430 440 450
MMGGRYYNSI GDIIDHYRKE QIVEGYYLKE PVPMQDQGQV LNDTVDGKEI
460 470 480 490 500
YNTIRRKTKD AFYKNIVKKG YLLKKGKGKR WKNLYFILEG SDAQLIYFES
510 520 530 540 550
EKRATKPKGL IDLSVCSVYV VHDSLFGRPN CFQIVVQHFS EEHYIFYFAG
560 570 580 590 600
ETPEQAEDWM KGLQAFCSLR KSSPGTSNKR LRQVSSLVLH IEEAHKLPVK
610 620 630 640 650
HFTNPYCNIY LNSVQVAKTH AREGQNPVWS EEFVFDDLPP DINRFEITLS
660 670 680 690 700
NKTKKSKDPD ILFMRCQLSR LQKGHATDEW FLLSSHIPLK GIEPGSLRVR
710 720 730 740 750
ARYSMEKIMP EEEYSEFKEL ILQKELHVVY ALSHVCGQDR TLLASILLKI
760 770 780 790 800
FLHEKLESLL LCTLNDREIS MEDEATTLFR ATTLASTLME QYMKATATQF
810 820 830 840 850
VHHALKDSIL KIMESKQSCE LSPSKLEKNE DVNTNLAHLL SILSELVEKI
860 870 880 890 900
FMASEILPPT LRYIYGCLQK SVQHKWPTNN TMRTRVVSGF VFLRLICPAI
910 920 930 940 950
LNPRMFNIIS DSPSPIAART LTLVAKSVQN LANLVEFGAK EPYMEGVNPF
960 970 980 990 1000
IKSNKHRMIM FLDELGNVPE LPDTTEHSRT DLSRDLAALH EICVAHSDEL
1010 1020 1030
RTLSNERGVQ QHVLKKLLAI TELLQQKQNQ YTKTNDVR
Length:1,038
Mass (Da):115,440
Last modified:October 1, 1996 - v1
Checksum:i242EE47131C1811E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13151 Unassigned DNA. Translation: AAA16319.1.
PIRiJT0663.
RefSeqiNP_037267.1. NM_013135.1.
UniGeneiRn.228988.

Genome annotation databases

GeneIDi25676.
KEGGirno:25676.
UCSCiRGD:3537. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13151 Unassigned DNA. Translation: AAA16319.1.
PIRiJT0663.
RefSeqiNP_037267.1. NM_013135.1.
UniGeneiRn.228988.

3D structure databases

ProteinModelPortaliP50904.
SMRiP50904. Positions 272-437, 709-1032.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247705. 2 interactions.
IntActiP50904. 3 interactions.
MINTiMINT-1519584.
STRINGi10116.ENSRNOP00000047300.

PTM databases

iPTMnetiP50904.
PhosphoSiteiP50904.

Proteomic databases

PaxDbiP50904.
PRIDEiP50904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25676.
KEGGirno:25676.
UCSCiRGD:3537. rat.

Organism-specific databases

CTDi5921.
RGDi3537. Rasa1.

Phylogenomic databases

eggNOGiKOG3508. Eukaryota.
ENOG410XPU1. LUCA.
HOGENOMiHOG000007794.
HOVERGENiHBG057470.
InParanoidiP50904.
KOiK04352.
PhylomeDBiP50904.

Miscellaneous databases

PROiP50904.

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.
IPR028554. p120-RasGAP.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10194:SF19. PTHR10194:SF19. 1 hit.
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.
SSF50729. SSF50729. 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]
ProtoNetiSearch...

Publicationsi

  1. "Sequence of the cDNA encoding Ras GTPase-activating protein from rat."
    Davis M.M., Catino J.J., Satoh T., Kaziro Y., Perkins L.M.
    Gene 134:305-306(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiRASA1_RAT
AccessioniPrimary (citable) accession number: P50904
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.