Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ras GTPase-activating protein 3

Gene

Rasa3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri679 – 71537Btk-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ras GTPase-activating protein 3
Alternative name(s):
GAP1(IP4BP)
Ins P4-binding protein
R-ras GAP
Gene namesi
Name:Rasa3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69365. Rasa3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 834834Ras GTPase-activating protein 3PRO_0000056644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661PhosphotyrosineBy similarity
Modified residuei77 – 771PhosphoserineBy similarity
Modified residuei110 – 1101PhosphothreonineBy similarity
Modified residuei809 – 8091PhosphoserineCombined sources
Modified residuei833 – 8331PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9QYJ2.
PRIDEiQ9QYJ2.

PTM databases

iPTMnetiQ9QYJ2.
PhosphoSiteiQ9QYJ2.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061587.

Structurei

3D structure databases

ProteinModelPortaliQ9QYJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9696C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 247116C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini330 – 524195Ras-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini576 – 677102PHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Btk-type zinc finger.PROSITE-ProRule annotation
Contains 2 C2 domains.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Ras-GAP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri679 – 71537Btk-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2059. Eukaryota.
ENOG410Y128. LUCA.
HOGENOMiHOG000007183.
HOVERGENiHBG055643.
InParanoidiQ9QYJ2.
KOiK12380.
PhylomeDBiQ9QYJ2.

Family and domain databases

Gene3Di1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR001562. Znf_Btk_motif.
[Graphical view]
PfamiPF00779. BTK. 1 hit.
PF00168. C2. 2 hits.
PF00169. PH. 1 hit.
PF00616. RasGAP. 2 hits.
[Graphical view]
SMARTiSM00107. BTK. 1 hit.
SM00239. C2. 2 hits.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50004. C2. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
PS51113. ZF_BTK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QYJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVEEEGLRV FQSVRIKIGE AKNLPSYPGP NKMRDCYCTV NLDQEEVFRT
60 70 80 90 100
KIVEKSLCPF YGEDFYCEIP RSFRHLSFYI FDRDVFRRDS IIGKVAIQKE
110 120 130 140 150
DLQRYHNRDT WFQLQHVDAD SEVQGKVHLE LRLSEVITDT GVVCHKLAAR
160 170 180 190 200
IFECQGLPIV NGQCDPYATV TLAGPFRSEA KKTKVKKKTN NPQFDEVFYF
210 220 230 240 250
EVTRPCSYSK KSHFDFEEED VDKLEIRVDL WNASNLKFGD EFLGELRIPL
260 270 280 290 300
HVLRYASSYE AWYFLQPRDN GSKSVKPDDL GSLRLNVVYT EDHVFSSEYY
310 320 330 340 350
SPLRDLLLKS ADVEPVSASA AHILGEVCRD KQEAAIPLVR LLLHYGRVVP
360 370 380 390 400
FISAIASAEV KRTQDPNTIF RGNSLTSKCI DETMKLAGMH YLHVTLKPTI
410 420 430 440 450
EEICQSHKSC EIDPVKLKDG ENLENNMESL RQYVDRIFSV ITKSGVSCPT
460 470 480 490 500
VMCDIFFSLR EAAAKRFQDD LDVRYTAVSS FIFLRFFAPA ILSPNLFQLT
510 520 530 540 550
PHHTDPQTSR TLTLISKTIQ TLGSLSKSKS ASFKESYMAT FYEFFNEQKY
560 570 580 590 600
ADAVKNFLDL ISSSGRRDPK SIEQPILLKE GFMIKRAQGR KRFGMKNFKK
610 620 630 640 650
RWFRLTNHEF TYQKSKGDQP LCNIPIENIL AVERLEEESF RMKNMFQVIQ
660 670 680 690 700
PERALYIQAN NCVEAKDWID ILTKVSQCNQ KRLTVFHPSA YLNGHWLCCR
710 720 730 740 750
ASSDTAIGCT PCTGGLPANI QLDIDGDRET ERIYSLFNLY MGKLEKMQEA
760 770 780 790 800
CGSKSVYDGP EQEEYSTFII DDPQETYRTL KQVIAGVGTL EQEHAQYRRN
810 820 830
KFKKTRYGSQ EHPIGDKSFQ NYIRQQSEIS THSI
Length:834
Mass (Da):96,020
Last modified:November 28, 2006 - v2
Checksum:i04F9B79A3C2F946F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti778 – 7781R → K in BAA89032 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86045 mRNA. Translation: BAF31891.1.
AB028626 mRNA. Translation: BAA89032.1.
RefSeqiNP_113762.1. NM_031574.1.
UniGeneiRn.224604.

Genome annotation databases

GeneIDi29372.
KEGGirno:29372.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86045 mRNA. Translation: BAF31891.1.
AB028626 mRNA. Translation: BAA89032.1.
RefSeqiNP_113762.1. NM_031574.1.
UniGeneiRn.224604.

3D structure databases

ProteinModelPortaliQ9QYJ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061587.

PTM databases

iPTMnetiQ9QYJ2.
PhosphoSiteiQ9QYJ2.

Proteomic databases

PaxDbiQ9QYJ2.
PRIDEiQ9QYJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29372.
KEGGirno:29372.

Organism-specific databases

CTDi22821.
RGDi69365. Rasa3.

Phylogenomic databases

eggNOGiKOG2059. Eukaryota.
ENOG410Y128. LUCA.
HOGENOMiHOG000007183.
HOVERGENiHBG055643.
InParanoidiQ9QYJ2.
KOiK12380.
PhylomeDBiQ9QYJ2.

Miscellaneous databases

PROiQ9QYJ2.

Family and domain databases

Gene3Di1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023152. RasGAP_CS.
IPR001936. RasGAP_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR001562. Znf_Btk_motif.
[Graphical view]
PfamiPF00779. BTK. 1 hit.
PF00168. C2. 2 hits.
PF00169. PH. 1 hit.
PF00616. RasGAP. 2 hits.
[Graphical view]
SMARTiSM00107. BTK. 1 hit.
SM00239. C2. 2 hits.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 2 hits.
SSF50729. SSF50729. 1 hit.
PROSITEiPS50004. C2. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
PS51113. ZF_BTK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Essential role of R-ras GAP in embryogenesis: embryonic lethality by underdeveloped adherent junctions between capillary endothelial cells."
    Iwashita S., Kubo Y., Sezaki M., Hinohara Y., Kobayashi M., Satoh S., Fukuda M., Nakamura K., Suzuki-Migishima R., Yokoyama M., Ohba M., Katoh C., Adachi E., Song S.Y.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
  2. "Expression of the R-ras GTPase activating protein gene during rat brain development."
    Sezaki M., Iwashita S.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 711-834.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809 AND SER-833, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRASA3_RAT
AccessioniPrimary (citable) accession number: Q9QYJ2
Secondary accession number(s): Q09YN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: November 28, 2006
Last modified: July 6, 2016
This is version 95 of the entry and version 2 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.