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Q03113 (GNA12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein subunit alpha-12

Short name=G alpha-12
Short name=G-protein subunit alpha-12
Gene names
Name:GNA12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length381 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. May play a role in the control of cell migration through the TOR signaling cascade. Ref.8

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with UBXD5. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane. Interacts with RGS22. Ref.6 Ref.7

Subcellular location

Membrane; Lipid-anchor.

Sequence similarities

Belongs to the G-alpha family. G(12) subfamily.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 8290554. Source: ProtInc

Rho protein signal transduction

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

cell differentiation

Inferred from electronic annotation. Source: Ensembl

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

regulation of TOR signaling

Inferred from mutant phenotype Ref.8. Source: UniProtKB

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

regulation of fibroblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.8. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbrush border membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

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

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionD5 dopamine receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

G-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 – 381381Guanine nucleotide-binding protein subunit alpha-12
PRO_0000203770

Regions

Nucleotide binding64 – 718GTP By similarity
Nucleotide binding202 – 2087GTP By similarity
Nucleotide binding227 – 2315GTP By similarity
Nucleotide binding296 – 2994GTP By similarity

Sites

Metal binding711Magnesium By similarity
Metal binding2081Magnesium By similarity
Binding site3531GTP; via amide nitrogen By similarity

Amino acid modifications

Lipidation111S-palmitoyl cysteine By similarity

Natural variations

Natural variant2421F → L.
Corresponds to variant rs45606633 [ dbSNP | Ensembl ].
VAR_049359
Natural variant3301Y → H.
Corresponds to variant rs45583847 [ dbSNP | Ensembl ].
VAR_049360

Experimental info

Sequence conflict1261K → E in AAM12615. Ref.2
Sequence conflict3231R → Q in AAA35867. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q03113 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 04C3F12B29255F89

FASTA38144,279
        10         20         30         40         50         60 
MSGVVRTLSR CLLPAEAGGA RERRAGSGAR DAEREARRRS RDIDALLARE RRAVRRLVKI 

        70         80         90        100        110        120 
LLLGAGESGK STFLKQMRII HGREFDQKAL LEFRDTIFDN ILKGSRVLVD ARDKLGIPWQ 

       130        140        150        160        170        180 
YSENEKHGMF LMAFENKAGL PVEPATFQLY VPALSALWRD SGIREAFSRR SEFQLGESVK 

       190        200        210        220        230        240 
YFLDNLDRIG QLNYFPSKQD ILLARKATKG IVEHDFVIKK IPFKMVDVGG QRSQRQKWFQ 

       250        260        270        280        290        300 
CFDGITSILF MVSSSEYDQV LMEDRRTNRL VESMNIFETI VNNKLFFNVS IILFLNKMDL 

       310        320        330        340        350        360 
LVEKVKTVSI KKHFPDFRGD PHRLEDVQRY LVQCFDRKRR NRSKPLFHHF TTAIDTENVR 

       370        380 
FVFHAVKDTI LQENLKDIML Q 

« Hide

References

« Hide 'large scale' references
[1]"Expression cDNA cloning of a transforming gene encoding the wild-type G alpha 12 gene product."
Chan A.M.-L., Fleming T.P., McGovern E.S., Chedid M., Miki T., Aaronson S.A.
Mol. Cell. Biol. 13:762-768(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Brain.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
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: Brain.
[6]"Socius, a novel binding partner of Galpha12/13, promotes the Galpha12-induced RhoA activation."
Tateiwa K., Katoh H., Negishi M.
Biochem. Biophys. Res. Commun. 337:615-620(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBXD5.
[7]"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.
Tissue: Testis.
[8]"PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and cell migration downstream of Galpha12."
Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D., Offermanns S., Simon M.I., Wu D.
Nat. Cell Biol. 14:686-696(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TOR SIGNALING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01694 mRNA. Translation: AAA35867.1.
AF493901 mRNA. Translation: AAM12615.1.
AC006028 Genomic DNA. Translation: AAP21870.1.
AC004933 Genomic DNA. Translation: AAD05026.1.
CH236953 Genomic DNA. Translation: EAL23961.1.
BC111464 mRNA. Translation: AAI11465.1.
PIRA48071.
RefSeqNP_031379.2. NM_007353.2.
UniGeneHs.487341.

3D structure databases

ProteinModelPortalQ03113.
SMRQ03113. Positions 56-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109030. 27 interactions.
IntActQ03113. 4 interactions.
MINTMINT-85969.
STRING9606.ENSP00000275364.

PTM databases

PhosphoSiteQ03113.

Polymorphism databases

DMDM38258934.

Proteomic databases

PaxDbQ03113.
PRIDEQ03113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275364; ENSP00000275364; ENSG00000146535.
GeneID2768.
KEGGhsa:2768.
UCSCuc003smu.3. human.

Organism-specific databases

CTD2768.
GeneCardsGC07M002767.
HGNCHGNC:4380. GNA12.
HPACAB010046.
MIM604394. gene.
neXtProtNX_Q03113.
PharmGKBPA28765.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279688.
HOGENOMHOG000038729.
HOVERGENHBG063184.
InParanoidQ03113.
KOK04346.
OMARDTIYEN.
OrthoDBEOG7HF1JF.
PhylomeDBQ03113.
TreeFamTF300673.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
SignaLinkQ03113.

Gene expression databases

ArrayExpressQ03113.
BgeeQ03113.
CleanExHS_GNA12.
GenevestigatorQ03113.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR000469. Gprotein_alpha_12.
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.
PR00440. GPROTEINA12.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSGNA12. human.
GeneWikiGNA12.
GenomeRNAi2768.
NextBio10888.
PROQ03113.
SOURCESearch...

Entry information

Entry nameGNA12_HUMAN
AccessionPrimary (citable) accession number: Q03113
Secondary accession number(s): A4D204 expand/collapse secondary AC list , Q2T9L1, Q86UM8, Q8TD71, Q9UDU9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 134 of the entry and version 4 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 7

Human chromosome 7: entries, gene names and cross-references to MIM