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P29992 (GNA11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Interacts with RGS22. Ref.9

Subcellular location

Cell membrane; Lipid-anchor Probable. Cytoplasm. Note: In testicular cells, expressed exclusively in the cytoplasm. Ref.9

Tissue specificity

Expressed in testis. Ref.9

Involvement in disease

Hypocalciuric hypercalcemia, familial 2 (HHC2) [MIM:145981]: A form of hypocalciuric hypercalcemia, a disorder of mineral homeostasis that is transmitted as an autosomal dominant trait with a high degree of penetrance. It is characterized biochemically by lifelong elevation of serum calcium concentrations and is associated with inappropriately low urinary calcium excretion and a normal or mildly elevated circulating parathyroid hormone level. Hypermagnesemia is typically present. Affected individuals are usually asymptomatic and the disorder is considered benign. However, chondrocalcinosis and pancreatitis occur in some adults.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Hypocalcemia, autosomal dominant 2 (HYPOC2) [MIM:615361]: A form of hypocalcemia, a disorder of mineral homeostasis characterized by blood calcium levels below normal, and low or normal serum parathyroid hormone concentrations. Disease manifestations include hypocalcemia, paresthesias, carpopedal spasm, seizures, hypercalciuria with nephrocalcinosis or kidney stones, and ectopic and basal ganglia calcifications.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13

Sequence similarities

Belongs to the G-alpha family. G(q) subfamily.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DiseaseDisease mutation
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMADP-ribosylation
Lipoprotein
Palmitate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaction potential

Inferred from Biological aspect of Ancestor. Source: RefGenome

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

blood coagulation

Traceable author statement. Source: Reactome

developmental pigmentation

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating dopamine receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

platelet activation

Traceable author statement. Source: Reactome

regulation of melanocyte differentiation

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 8530500. Source: ProtInc

skeletal system development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Traceable author statement PubMed 9175863. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionG-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Guanine nucleotide-binding protein subunit alpha-11
PRO_0000203746

Regions

Nucleotide binding46 – 538GTP By similarity
Nucleotide binding180 – 1867GTP By similarity
Nucleotide binding205 – 2095GTP By similarity
Nucleotide binding274 – 2774GTP By similarity

Sites

Metal binding531Magnesium By similarity
Metal binding1861Magnesium By similarity
Binding site3311GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue1831ADP-ribosylarginine; by cholera toxin By similarity
Lipidation91S-palmitoyl cysteine Ref.11
Lipidation101S-palmitoyl cysteine Ref.11

Natural variations

Natural variant601R → C in HYPOC2. Ref.12
VAR_070165
Natural variant1351L → Q in HHC2; induces a decrease in sensitivity to changes in extracellular calcium concentrations. Ref.13
VAR_070166
Natural variant1811R → Q in HYPOC2; induces an increase in sensitivity to changes in extracellular calcium concentrations. Ref.13
VAR_070167
Natural variant2001Missing in HHC2; induces a decrease in sensitivity to changes in extracellular calcium concentrations. Ref.13
VAR_070168
Natural variant2111S → W in HYPOC2. Ref.12
VAR_070169
Natural variant3411F → L in HYPOC2; induces an increase in sensitivity to changes in extracellular calcium concentrations. Ref.13
VAR_070170

Experimental info

Sequence conflict61M → I in AAB64303. Ref.2
Sequence conflict2661N → H in AAA99949. Ref.8
Sequence conflict2851Y → H in AAA99949. Ref.8
Sequence conflict301 – 3022DA → EP in AAA58624. Ref.1
Sequence conflict3101L → P in AAB64303. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29992 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: DD37176589E66046

FASTA35942,123
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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]"RGS22, a novel testis-specific regulator of G-protein signaling involved in human and mouse spermiogenesis along with GNA12/13 subunits."
Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z., Sha J.
Biol. Reprod. 79:1021-1029(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RGS22, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Testis.
[10]"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].
[11]"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.
[12]"A rude awakening--the perioperative sleep apnea epidemic."
Memtsoudis S.G., Besculides M.C., Mazumdar M.
N. Engl. J. Med. 368:2352-2353(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HYPOC2 CYS-60 AND TRP-211.
[13]"Mutations affecting G-protein subunit alpha11 in hypercalcemia and hypocalcemia."
Nesbit M.A., Hannan F.M., Howles S.A., Babinsky V.N., Head R.A., Cranston T., Rust N., Hobbs M.R., Heath H. III, Thakker R.V.
N. Engl. J. Med. 368:2476-2486(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HHC2 GLN-135 AND ILE-200 DEL, VARIANTS HYPOC2 GLN-181 AND LEU-341, CHARACTERIZATION OF VARIANTS HHC2 GLN-135 AND ILE-200 DEL, CHARACTERIZATION OF VARIANTS HYPOC2 GLN-181 AND LEU-341.
+Additional computationally mapped references.

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.
PIRRGHUGY. A39394.
RefSeqNP_002058.2. NM_002067.4.
UniGeneHs.650575.
Hs.654784.

3D structure databases

ProteinModelPortalP29992.
SMRP29992. Positions 37-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109029. 15 interactions.
IntActP29992. 2 interactions.
MINTMINT-4999662.
STRING9606.ENSP00000078429.

PTM databases

PhosphoSiteP29992.

Polymorphism databases

DMDM3041682.

Proteomic databases

PaxDbP29992.
PRIDEP29992.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000078429; ENSP00000078429; ENSG00000088256.
GeneID2767.
KEGGhsa:2767.
UCSCuc002lxd.3. human.

Organism-specific databases

CTD2767.
GeneCardsGC19P003094.
HGNCHGNC:4379. GNA11.
HPAHPA048886.
MIM139313. gene.
145981. phenotype.
615361. phenotype.
neXtProtNX_P29992.
Orphanet428. Autosomal dominant hypocalcemia.
101049. Familial hypocalciuric hypercalcemia type 2.
PharmGKBPA28764.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322962.
HOGENOMHOG000038729.
HOVERGENHBG063184.
InParanoidP29992.
KOK04635.
OMAEHRYVNA.
OrthoDBEOG7ZWD1W.
PhylomeDBP29992.
TreeFamTF300673.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP29992.
BgeeP29992.
CleanExHS_GNA11.
GenevestigatorP29992.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR000654. Gprotein_alpha_Q.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00442. GPROTEINAQ.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSGNA11. human.
GeneWikiGNA11.
GenomeRNAi2767.
NextBio10884.
PROP29992.
SOURCESearch...

Entry information

Entry nameGNA11_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM