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Protein

GTP-binding protein Di-Ras2

Gene

DIRAS2

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 – 218GTP
Nucleotide bindingi33 – 397GTP
Nucleotide bindingi61 – 655GTP
Nucleotide bindingi121 – 1244GTP

GO - Molecular functioni

  • 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-Ras2
Alternative name(s):
Distinct subgroup of the Ras family member 2
Gene namesi
Name:DIRAS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:19323. DIRAS2.

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

PharmGKBiPA134958969.

Polymorphism and mutation databases

BioMutaiDIRAS2.
DMDMi62286631.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196GTP-binding protein Di-Ras2PRO_0000191650Add
BLAST
Propeptidei197 – 1993Removed in mature formSequence analysisPRO_0000370777

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei126 – 1261PhosphoserineBy similarity
Modified residuei196 – 1961Cysteine methyl esterSequence analysis
Lipidationi196 – 1961S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiQ96HU8.
PaxDbiQ96HU8.
PRIDEiQ96HU8.

PTM databases

iPTMnetiQ96HU8.
PhosphoSiteiQ96HU8.

Expressioni

Tissue specificityi

Highly expressed in brain.1 Publication

Gene expression databases

BgeeiQ96HU8.
CleanExiHS_DIRAS2.
GenevisibleiQ96HU8. HS.

Organism-specific databases

HPAiHPA043758.

Interactioni

Protein-protein interaction databases

BioGridi120143. 6 interactions.
IntActiQ96HU8. 5 interactions.
STRINGi9606.ENSP00000364919.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137Combined sources
Helixi20 – 289Combined sources
Beta strandi42 – 509Combined sources
Beta strandi53 – 619Combined sources
Helixi69 – 7810Combined sources
Beta strandi80 – 878Combined sources
Helixi91 – 955Combined sources
Helixi98 – 10811Combined sources
Beta strandi116 – 1216Combined sources
Helixi123 – 1286Combined sources
Helixi133 – 14311Combined sources
Beta strandi146 – 1494Combined sources
Turni152 – 1554Combined sources
Helixi158 – 16710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ERXX-ray1.65A/B5-176[»]
ProteinModelPortaliQ96HU8.
SMRiQ96HU8. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96HU8.

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.
InParanoidiQ96HU8.
KOiK07841.
OMAiWGVSFME.
OrthoDBiEOG7SBNQ3.
PhylomeDBiQ96HU8.
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.

Q96HU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEQSNDYRV AVFGAGGVGK SSLVLRFVKG TFRESYIPTV EDTYRQVISC
60 70 80 90 100
DKSICTLQIT DTTGSHQFPA MQRLSISKGH AFILVYSITS RQSLEELKPI
110 120 130 140 150
YEQICEIKGD VESIPIMLVG NKCDESPSRE VQSSEAEALA RTWKCAFMET
160 170 180 190
SAKLNHNVKE LFQELLNLEK RRTVSLQIDG KKSKQQKRKE KLKGKCVIM
Length:199
Mass (Da):22,485
Last modified:December 1, 2001 - v1
Checksum:i429D17026CC3EADC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076889 mRNA. Translation: BAC01116.1.
AK122986 mRNA. Translation: BAG53834.1.
AL353619 Genomic DNA. Translation: CAI15748.1.
CH471089 Genomic DNA. Translation: EAW62780.1.
BC008065 mRNA. Translation: AAH08065.1.
CCDSiCCDS6687.1.
RefSeqiNP_060064.2. NM_017594.4.
UniGeneiHs.165636.

Genome annotation databases

EnsembliENST00000375765; ENSP00000364919; ENSG00000165023.
GeneIDi54769.
KEGGihsa:54769.
UCSCiuc004aqx.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB076889 mRNA. Translation: BAC01116.1.
AK122986 mRNA. Translation: BAG53834.1.
AL353619 Genomic DNA. Translation: CAI15748.1.
CH471089 Genomic DNA. Translation: EAW62780.1.
BC008065 mRNA. Translation: AAH08065.1.
CCDSiCCDS6687.1.
RefSeqiNP_060064.2. NM_017594.4.
UniGeneiHs.165636.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ERXX-ray1.65A/B5-176[»]
ProteinModelPortaliQ96HU8.
SMRiQ96HU8. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120143. 6 interactions.
IntActiQ96HU8. 5 interactions.
STRINGi9606.ENSP00000364919.

PTM databases

iPTMnetiQ96HU8.
PhosphoSiteiQ96HU8.

Polymorphism and mutation databases

BioMutaiDIRAS2.
DMDMi62286631.

Proteomic databases

EPDiQ96HU8.
PaxDbiQ96HU8.
PRIDEiQ96HU8.

Protocols and materials databases

DNASUi54769.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375765; ENSP00000364919; ENSG00000165023.
GeneIDi54769.
KEGGihsa:54769.
UCSCiuc004aqx.2. human.

Organism-specific databases

CTDi54769.
GeneCardsiDIRAS2.
HGNCiHGNC:19323. DIRAS2.
HPAiHPA043758.
MIMi607863. gene.
neXtProtiNX_Q96HU8.
PharmGKBiPA134958969.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121857.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiQ96HU8.
KOiK07841.
OMAiWGVSFME.
OrthoDBiEOG7SBNQ3.
PhylomeDBiQ96HU8.
TreeFamiTF313014.

Miscellaneous databases

ChiTaRSiDIRAS2. human.
EvolutionaryTraceiQ96HU8.
GenomeRNAii54769.
PROiQ96HU8.
SOURCEiSearch...

Gene expression databases

BgeeiQ96HU8.
CleanExiHS_DIRAS2.
GenevisibleiQ96HU8. 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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Ovary.
  6. "Crystal structure of DIRAS2."
    Papagrigoriou E., Yang X., Elkins J., Niesen F.E., Burgess N., Salah E., Fedorov O., Ball L.J., Von Delft F., Sundstrom M., Edwards A., Arrowsmith C., Weigelt J., Doyle D.
    Submitted (DEC-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 5-176 IN COMPLEX WITH GTP ANALOG.

Entry informationi

Entry nameiDIRA2_HUMAN
AccessioniPrimary (citable) accession number: Q96HU8
Secondary accession number(s): B3KVM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 132 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 9
    Human chromosome 9: 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.