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Protein
Submitted name:

Guanine nucleotide binding protein (G protein), alpha transducing activity polypeptide 2

Gene

GNAT2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: InterPro
  2. detection of chemical stimulus involved in sensory perception of bitter taste Source: Ensembl
  3. detection of light stimulus involved in visual perception Source: Ensembl
  4. GTP catabolic process Source: InterPro
  5. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  6. response to light intensity Source: Ensembl
  7. retinal cone cell development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

TransducerSAAS annotation

Keywords - Ligandi

GTP-bindingSAAS annotation, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Guanine nucleotide binding protein (G protein), alpha transducing activity polypeptide 2Imported
Submitted name:
Guanine nucleotide binding protein (G protein), alpha transducing activity polypeptide 2, isoform CRA_aImported
Gene namesi
Name:GNAT2Imported
ORF Names:hCG_40256Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

GO - Cellular componenti

  1. photoreceptor inner segment Source: Ensembl
  2. photoreceptor outer segment Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28774.

Structurei

3D structure databases

ProteinModelPortaliQ5T697.
SMRiQ5T697. Positions 14-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00760000118851.
HOVERGENiHBG063184.
KOiK04631.
OMAiSICNHRF.
PhylomeDBiQ5T697.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q5T697-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSGASAEDK ELAKRSKELE KKLQEDADKE AKTVKLLLLG AGESGKSTIV
60 70 80 90 100
KQMKIIHQDG YSPEECLEFK AIIYGNVLQS ILAIIRAMTT LGIDYAEPSC
110 120 130 140 150
ADDGRQLNNL ADSIEEGTMP PELVEVIRRL WKDGGVQACF ERAAEYQLND
160 170 180 190 200
SASYYLNQLE RITDPEYLPS EQDVLRSRVK TTGIIETKFS VKDLNFRMFD
210 220 230 240 250
VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDDEV NRMHESLHLF
260 270 280 290 300
NSICNHKFFA ATSIVLFLNK KDLFEEKIKK VHLSICFPEY DGNNSYDDAG
310 320 330 340 350
NYIKSQFLDL NMRKDVKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD

CGLF
Length:354
Mass (Da):40,176
Last modified:May 10, 2005 - v1
Checksum:iBFF8D50C024F18DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT009844 mRNA. Translation: AAP88846.1.
CH471122 Genomic DNA. Translation: EAW56394.1.
CH471122 Genomic DNA. Translation: EAW56395.1.
RefSeqiNP_005263.1. NM_005272.3.
UniGeneiHs.36973.

Genome annotation databases

GeneIDi2780.
KEGGihsa:2780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT009844 mRNA. Translation: AAP88846.1.
CH471122 Genomic DNA. Translation: EAW56394.1.
CH471122 Genomic DNA. Translation: EAW56395.1.
RefSeqiNP_005263.1. NM_005272.3.
UniGeneiHs.36973.

3D structure databases

ProteinModelPortaliQ5T697.
SMRiQ5T697. Positions 14-354.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

DNASUi2780.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2780.
KEGGihsa:2780.

Organism-specific databases

CTDi2780.
PharmGKBiPA28774.

Phylogenomic databases

GeneTreeiENSGT00760000118851.
HOVERGENiHBG063184.
KOiK04631.
OMAiSICNHRF.
PhylomeDBiQ5T697.

Miscellaneous databases

ChiTaRSiGNAT2. human.
GenomeRNAii2780.
NextBioi10951.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001408. Gprotein_alpha_I.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10218. PTHR10218. 1 hit.
PfamiPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSiPR00318. GPROTEINA.
PR00441. GPROTEINAI.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ5T697_HUMAN
AccessioniPrimary (citable) accession number: Q5T697
Entry historyi
Integrated into UniProtKB/TrEMBL: May 10, 2005
Last sequence update: May 10, 2005
Last modified: March 4, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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 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.