P29992 (GNA11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein subunit alpha-11
Short name=G alpha-11
Short name=G-protein subunit alpha-11

Alternative name(s):
Guanine nucleotide-binding protein G(y) subunit alpha

Gene names

Name:	GNA11
Synonyms:	GA11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C.
Subunit structure	G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site.
Subcellular location	Cell membrane; Lipid-anchor Probable.
Sequence similarities	Belongs to the G-alpha family. G(q) subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	ADP-ribosylation Lipoprotein Palmitate
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-modulating G-protein coupled receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome developmental pigmentation Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara phospholipase C-activating dopamine receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome platelet activation Traceable author statement. Source: Reactome regulation of action potential Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of melanocyte differentiation Inferred from electronic annotation. Source: Compara skeletal system development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Traceable author statement PubMed 9175863. Source: ProtInc heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein coupled receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement PubMed 8530500. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Guanine nucleotide-binding protein subunit alpha-11		PRO_0000203746
Regions
	Nucleotide binding	46 – 53	8	GTP By similarity
	Nucleotide binding	180 – 186	7	GTP By similarity
	Nucleotide binding	205 – 209	5	GTP By similarity
	Nucleotide binding	274 – 277	4	GTP By similarity
Sites
	Metal binding	53	1	Magnesium By similarity
	Metal binding	186	1	Magnesium By similarity
	Binding site	331	1	GTP; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	183	1	ADP-ribosylarginine; by cholera toxin By similarity
	Lipidation	9	1	S-palmitoyl cysteine Ref.10
	Lipidation	10	1	S-palmitoyl cysteine Ref.10
Experimental info
	Sequence conflict	6	1	M → I in AAB64303. Ref.2
	Sequence conflict	266	1	N → H in AAA99949. Ref.8
	Sequence conflict	285	1	Y → H in AAA99949. Ref.8
	Sequence conflict	301 – 302	2	DA → EP in AAA58624. Ref.1
	Sequence conflict	310	1	L → P in AAB64303. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29992 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: DD37176589E66046	FASTA	359	42,123
	10 20 30 40 50 60 MTLESMMACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR 70 80 90 100 110 120 IIHGAGYSEE DKRGFTKLVY QNIFTAMQAM IRAMETLKIL YKYEQNKANA LLIREVDVEK 130 140 150 160 170 180 VTTFEHQYVS AIKTLWEDPG IQECYDRRRE YQLSDSAKYY LTDVDRIATL GYLPTQQDVL 190 200 210 220 230 240 RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV 250 260 270 280 290 300 ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE DKILYSHLVD YFPEFDGPQR 310 320 330 340 350 DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells." Jiang M., Pandey S., Tran V.T., Fong H.K.W. Proc. Natl. Acad. Sci. U.S.A. 88:3907-3911(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[2]	Bai X.H., Acharya R., Bai Y.H., Murtagh J.J. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: Pancreas.
[7]	Bienvenut W.V., Calvo F., Kolch W. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 42-52 AND 159-166, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways." Thomas C.P., Dunn M.J., Mattera R. Biochem. J. 312:151-158(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 244-337. Tissue: Hematopoietic.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Site-specific analysis of protein S-acylation by resin-assisted capture." Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., Stamler J.S., Casey P.J. J. Lipid Res. 52:393-398(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-9 AND CYS-10.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	M69013 mRNA. Translation: AAA58624.1. AF011497 mRNA. Translation: AAB64303.1. AF493900 mRNA. Translation: AAM12614.1. CR457004 mRNA. Translation: CAG33285.1. AC005262 Genomic DNA. Translation: AAC25615.1. BC089041 mRNA. Translation: AAH89041.1. BC096225 mRNA. Translation: AAH96225.1. BC096226 mRNA. Translation: AAH96226.1. BC096227 mRNA. Translation: AAH96227.1. L40630 mRNA. Translation: AAA99949.1.
IPI	IPI00305551.
PIR	RGHUGY. A39394.
RefSeq	NP_002058.2. NM_002067.2.
UniGene	Hs.650575. Hs.654784.
3D structure databases
ProteinModelPortal	P29992.
ModBase	Search...
Protein-protein interaction databases
IntAct	P29992. 2 interactions.
MINT	MINT-4999662.
STRING	9606.ENSP00000078429.
PTM databases
PhosphoSite	P29992.
Polymorphism databases
DMDM	3041682.
Proteomic databases
PaxDb	P29992.
PRIDE	P29992.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000078429; ENSP00000078429; ENSG00000088256.
GeneID	2767.
KEGG	hsa:2767.
UCSC	uc002lxd.3. human.
Organism-specific databases
CTD	2767.
GeneCards	GC19P003045.
HGNC	HGNC:4379. GNA11.
HPA	HPA048886.
MIM	139313. gene.
neXtProt	NX_P29992.
PharmGKB	PA28764.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG322962.
HOGENOM	HOG000038729.
HOVERGEN	HBG063184.
InParanoid	P29992.
KO	K04635.
OMA	KTLWSDP.
OrthoDB	EOG4S4PGD.
PhylomeDB	P29992.
Enzyme and pathway databases
Pathway_Interaction_DB	arf6cyclingpathway. Arf6 signaling events. endothelinpathway. Endothelins. lysophospholipid_pathway. LPA receptor mediated events. er_nongenomic_pathway. Plasma membrane estrogen receptor signaling. s1p_s1p2_pathway. S1P2 pathway. s1p_s1p3_pathway. S1P3 pathway. s1p_meta_pathway. Sphingosine 1-phosphate (S1P) pathway. txa2pathway. Thromboxane A2 receptor signaling.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P29992.
Bgee	P29992.
CleanEx	HS_GNA11.
Genevestigator	P29992.
GermOnline	ENSG00000088256. Homo sapiens.
Family and domain databases
Gene3D	1.10.400.10. 1 hit.
InterPro	IPR000654. Gprotein_alpha_Q. IPR001019. Gprotein_alpha_su. IPR011025. GproteinA_insert. IPR027417. P-loop_NTPase. [Graphical view]
PANTHER	PTHR10218. PTHR10218. 1 hit.
Pfam	PF00503. G-alpha. 1 hit. [Graphical view]
PRINTS	PR00318. GPROTEINA. PR00442. GPROTEINAQ.
SMART	SM00275. G_alpha. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit. SSF47895. Transducn_insert. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	GNA11. human.
GenomeRNAi	2767.
NextBio	10884.
SOURCE	Search...

Entry information

Entry name

GNA11_HUMAN

Accession

Primary (citable) accession number: P29992
Secondary accession number(s): O15109, Q14350, Q6IB00

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	July 15, 1998
Last modified:	May 29, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.