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Q14344 (GNA13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein subunit alpha-13

Short name=G alpha-13
Short name=G-protein subunit alpha-13
Gene names
Name:GNA13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length377 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.

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 with HAX1. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane. Interacts with RGS22. Ref.8 Ref.9 Ref.11

Subcellular location

Membrane; Lipid-anchor. Melanosome. Cytoplasm. Nucleus. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Detected in the cytoplasm of Leydig cells and in the seminiferous epithelium, including differentiating cells from the spermatogonia to mature spermatozoa stages. In round spermatids, also present in the nuclei. Ref.10 Ref.11

Tissue specificity

Expressed in testis, including in Leydig cells and in the seminiferous epithelium, in differentiating cells from the spermatogonia to mature spermatozoa stages and round spermatids (at protein level). Expressed in 99.2% of spermatozoa from healthy individuals, but only in 28.6% of macrocephalic spermatozoa from infertile patients (at protein level). Ref.11

Post-translational modification

Palmitoylation is critical for proper membrane localization and signaling. Ref.6

Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRho protein signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

activation of phospholipase D activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

adenylate cyclase-activating 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

cellular component movement

Traceable author statement PubMed 8999798. Source: ProtInc

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentbrush border membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. 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

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

protein binding

Inferred from physical interaction PubMed 10026210. Source: UniProtKB

signal transducer activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

type 1 angiotensin receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARHGEF1Q928883EBI-465387,EBI-465400
CXCR5P323029EBI-465387,EBI-2835269

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14344-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14344-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-95: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Guanine nucleotide-binding protein subunit alpha-13
PRO_0000203773

Regions

Nucleotide binding55 – 628GTP By similarity
Nucleotide binding197 – 2037GTP By similarity
Nucleotide binding222 – 2265GTP By similarity
Nucleotide binding291 – 2944GTP By similarity

Sites

Metal binding621Magnesium By similarity
Metal binding2031Magnesium By similarity
Binding site3491GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue2031Phosphothreonine; by PKA Ref.7
Lipidation141S-palmitoyl cysteine Ref.6
Lipidation181S-palmitoyl cysteine Ref.6

Natural variations

Alternative sequence1 – 9595Missing in isoform 2.
VSP_055140
Natural variant2211V → L. Ref.1
Corresponds to variant rs1062597 [ dbSNP | Ensembl ].
VAR_017160

Experimental info

Mutagenesis141C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. Ref.6
Mutagenesis181C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. Ref.6
Mutagenesis2031T → A: Abolishes phosphorylation by PKA; disrupts heterotrimer stability. Ref.7
Sequence conflict2111F → L in BAH13696. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2003. Version 2.
Checksum: 929B7B6473C54F2E

FASTA37744,050
        10         20         30         40         50         60 
MADFLPSRSV LSVCFPGCLL TSGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG 

        70         80         90        100        110        120 
KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNSNQQHGD 

       130        140        150        160        170        180 
KMMSFDTRAP MAAQGMVETR VFLQYLPAIR ALWADSGIQN AYDRRREFQL GESVKYFLDN 

       190        200        210        220        230        240 
LDKLGEPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV 

       250        260        270        280        290        300 
TSILFLVSSS EFDQVLMEDR LTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV 

       310        320        330        340        350        360 
QIVSIKDYFL EFEGDPHCLR DVQKFLVECF RNKRRDQQQK PLYHHFTTAI NTENIRLVFR 

       370 
DVKDTILHDN LKQLMLQ 

« Hide

Isoform 2 [UniParc].

Checksum: E32B6298504794BB
Show »

FASTA28233,287

References

« Hide 'large scale' references
[1]"Expression of GTP-binding protein alpha subunits in human thymocytes."
Kabouridis P.S., Waters S.T., Escobar S., Stanners J., Tsoukas C.D.
Mol. Cell. Biochem. 144:45-51(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-221.
Tissue: Thymus.
[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] (ISOFORM 1).
Tissue: Brain.
[3]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Hippocampus and Testis.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Melanoma.
[6]"Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding."
Bhattacharyya R., Wedegaertner P.B.
J. Biol. Chem. 275:14992-14999(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-14 AND CYS-18, MUTAGENESIS OF CYS-14 AND CYS-18.
[7]"PKA-mediated phosphorylation of Galpha 13 switch I region alters the Galpha beta gamma 13-GPCR complex and inhibits Rho activation."
Manganello J.M., Huang J.-S., Kozasa T., Voyno-Yasenetskaya T.A., Le Breton G.C.
J. Biol. Chem. 278:124-130(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-203, MUTAGENESIS OF THR-203.
[8]"Galpha13 stimulates cell migration through cortactin-interacting protein Hax-1."
Radhika V., Onesime D., Ha J.H., Dhanasekaran N.
J. Biol. Chem. 279:49406-49413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAX1.
[9]"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.
[10]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[11]"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.
[12]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L22075 mRNA. Translation: AAA74235.1.
AF493902 mRNA. Translation: AAM12616.1.
AK302400 mRNA. Translation: BAH13696.1.
AK313672 mRNA. Translation: BAG36424.1.
AC037487 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW88993.1.
BC036756 mRNA. Translation: AAH36756.1.
CCDSCCDS11661.1.
PIRI57490.
RefSeqNP_006563.2. NM_006572.5.
UniGeneHs.515018.

3D structure databases

ProteinModelPortalQ14344.
SMRQ14344. Positions 47-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115914. 29 interactions.
IntActQ14344. 5 interactions.
MINTMINT-85993.
STRING9606.ENSP00000400717.

PTM databases

PhosphoSiteQ14344.

Polymorphism databases

DMDM38258936.

Proteomic databases

MaxQBQ14344.
PaxDbQ14344.
PeptideAtlasQ14344.
PRIDEQ14344.

Protocols and materials databases

DNASU10672.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000439174; ENSP00000400717; ENSG00000120063.
ENST00000541118; ENSP00000439647; ENSG00000120063.
GeneID10672.
KEGGhsa:10672.
UCSCuc002jfc.3. human.

Organism-specific databases

CTD10672.
GeneCardsGC17M063005.
HGNCHGNC:4381. GNA13.
HPAHPA010087.
MIM604406. gene.
neXtProtNX_Q14344.
PharmGKBPA28766.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279688.
HOGENOMHOG000038729.
HOVERGENHBG063184.
InParanoidQ14344.
KOK04639.
OMACFPGCVL.
OrthoDBEOG7HF1JF.
PhylomeDBQ14344.
TreeFamTF300673.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
SignaLinkQ14344.

Gene expression databases

ArrayExpressQ14344.
BgeeQ14344.
CleanExHS_GNA13.
GenevestigatorQ14344.

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

ChiTaRSGNA13. human.
GeneWikiGNA13.
GenomeRNAi10672.
NextBio40583.
PROQ14344.
SOURCESearch...

Entry information

Entry nameGNA13_HUMAN
AccessionPrimary (citable) accession number: Q14344
Secondary accession number(s): B2R977 expand/collapse secondary AC list , B7Z7R0, F5H1G8, Q8TD70
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 31, 2003
Last modified: July 9, 2014
This is version 136 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 17

Human chromosome 17: entries, gene names and cross-references to MIM