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Protein

GTP-binding protein Di-Ras1

Gene

DIRAS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Displays low GTPase activity and exist predominantly in the GTP-bound form.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 218GTPBy similarity
Nucleotide bindingi61 – 655GTPBy similarity
Nucleotide bindingi121 – 1244GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein Di-Ras1
Alternative name(s):
Distinct subgroup of the Ras family member 1
Ras-related inhibitor of cell growth
Short name:
Rig
Small GTP-binding tumor suppressor 1
Gene namesi
Name:DIRAS1
Synonyms:GBTS1, RIG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:19127. DIRAS1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: InterPro
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134951835.

Polymorphism and mutation databases

BioMutaiDIRAS1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195GTP-binding protein Di-Ras1PRO_0000191648Add
BLAST
Propeptidei196 – 1983Removed in mature formSequence analysisPRO_0000370775

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei195 – 1951Cysteine methyl esterSequence analysis
Lipidationi195 – 1951S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiO95057.
PaxDbiO95057.
PRIDEiO95057.

PTM databases

iPTMnetiO95057.
PhosphoSiteiO95057.

Expressioni

Tissue specificityi

Highly expressed in heart and brain.2 Publications

Gene expression databases

BgeeiO95057.
CleanExiHS_DIRAS1.
ExpressionAtlasiO95057. baseline and differential.
GenevisibleiO95057. HS.

Organism-specific databases

HPAiHPA050164.

Interactioni

Protein-protein interaction databases

BioGridi127135. 9 interactions.
STRINGi9606.ENSP00000325836.

Structurei

Secondary structure

1
198
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 147Combined sources
Helixi20 – 2910Combined sources
Beta strandi42 – 509Combined sources
Beta strandi53 – 619Combined sources
Helixi64 – 663Combined sources
Helixi69 – 7810Combined sources
Beta strandi80 – 878Combined sources
Helixi91 – 955Combined sources
Helixi98 – 10811Combined sources
Helixi111 – 1133Combined sources
Beta strandi116 – 1216Combined sources
Helixi132 – 14211Combined sources
Beta strandi145 – 1484Combined sources
Turni151 – 1544Combined sources
Helixi157 – 16711Combined sources
Beta strandi169 – 1713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GF0X-ray1.90A/B/C/D1-198[»]
ProteinModelPortaliO95057.
SMRiO95057. Positions 3-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95057.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi36 – 449Effector regionSequence analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Di-Ras family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiO95057.
KOiK07840.
OMAiLGPIYQL.
OrthoDBiEOG7SBNQ3.
PhylomeDBiO95057.
TreeFamiTF313014.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O95057-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC
60 70 80 90 100
DKSVCTLQIT DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI
110 120 130 140 150
YKLIVQIKGS VEDIPVMLVG NKCDETQREV DTREAQAVAQ EWKCAFMETS
160 170 180 190
AKMNYNVKEL FQELLTLETR RNMSLNIDGK RSGKQKRTDR VKGKCTLM
Length:198
Mass (Da):22,329
Last modified:May 1, 1999 - v1
Checksum:i32E979AF80BB9A7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076888 mRNA. Translation: BAC01115.1.
AY056037 mRNA. Translation: AAL23715.1.
AY059641 mRNA. Translation: AAL17968.1.
AY180973 mRNA. Translation: AAO22153.1.
AC006538 Genomic DNA. Translation: AAD13119.1.
BC030660 mRNA. Translation: AAH30660.1.
CCDSiCCDS12092.1.
RefSeqiNP_660156.1. NM_145173.3.
UniGeneiHs.172753.

Genome annotation databases

EnsembliENST00000323469; ENSP00000325836; ENSG00000176490.
ENST00000585334; ENSP00000468417; ENSG00000176490.
GeneIDi148252.
KEGGihsa:148252.
UCSCiuc002lwf.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076888 mRNA. Translation: BAC01115.1.
AY056037 mRNA. Translation: AAL23715.1.
AY059641 mRNA. Translation: AAL17968.1.
AY180973 mRNA. Translation: AAO22153.1.
AC006538 Genomic DNA. Translation: AAD13119.1.
BC030660 mRNA. Translation: AAH30660.1.
CCDSiCCDS12092.1.
RefSeqiNP_660156.1. NM_145173.3.
UniGeneiHs.172753.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GF0X-ray1.90A/B/C/D1-198[»]
ProteinModelPortaliO95057.
SMRiO95057. Positions 3-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127135. 9 interactions.
STRINGi9606.ENSP00000325836.

PTM databases

iPTMnetiO95057.
PhosphoSiteiO95057.

Polymorphism and mutation databases

BioMutaiDIRAS1.

Proteomic databases

MaxQBiO95057.
PaxDbiO95057.
PRIDEiO95057.

Protocols and materials databases

DNASUi148252.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323469; ENSP00000325836; ENSG00000176490.
ENST00000585334; ENSP00000468417; ENSG00000176490.
GeneIDi148252.
KEGGihsa:148252.
UCSCiuc002lwf.4. human.

Organism-specific databases

CTDi148252.
GeneCardsiDIRAS1.
HGNCiHGNC:19127. DIRAS1.
HPAiHPA050164.
MIMi607862. gene.
neXtProtiNX_O95057.
PharmGKBiPA134951835.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiO95057.
KOiK07840.
OMAiLGPIYQL.
OrthoDBiEOG7SBNQ3.
PhylomeDBiO95057.
TreeFamiTF313014.

Miscellaneous databases

EvolutionaryTraceiO95057.
GenomeRNAii148252.
PROiO95057.
SOURCEiSearch...

Gene expression databases

BgeeiO95057.
CleanExiHS_DIRAS1.
ExpressionAtlasiO95057. baseline and differential.
GenevisibleiO95057. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Di-Ras, a distinct subgroup of ras family GTPases with unique biochemical properties."
    Kontani K., Tada M., Ogawa T., Okai T., Saito K., Araki Y., Katada T.
    J. Biol. Chem. 277:41070-41078(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GTPASE ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Rig is a novel Ras-related protein and potential neural tumor suppressor."
    Ellis C.A., Vos M.D., Howell H., Vallecorsa T., Fults D.W., Clark G.J.
    Proc. Natl. Acad. Sci. U.S.A. 99:9876-9881(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Molecular cloning of GBTS1, a novel gene encoding a small GTP-binding tumor suppressor."
    Gong L., Wu K.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Cismowski M.J., Kopatz S.A., Aronstam R.S., Sharma S.V.
    Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Brain.

Entry informationi

Entry nameiDIRA1_HUMAN
AccessioniPrimary (citable) accession number: O95057
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 135 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.