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Protein

Guanine nucleotide-binding protein subunit alpha-13

Gene

GNA13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621MagnesiumBy similarity
Metal bindingi203 – 2031MagnesiumBy similarity
Binding sitei349 – 3491GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi55 – 628GTPBy similarity
Nucleotide bindingi197 – 2037GTPBy similarity
Nucleotide bindingi222 – 2265GTPBy similarity
Nucleotide bindingi291 – 2944GTPBy similarity

GO - Molecular functioni

  1. D5 dopamine receptor binding Source: GO_Central
  2. G-protein beta/gamma-subunit complex binding Source: GO_Central
  3. GTPase activity Source: GO_Central
  4. GTP binding Source: UniProtKB-KW
  5. metal ion binding Source: UniProtKB-KW
  6. signal transducer activity Source: GO_Central
  7. type 1 angiotensin receptor binding Source: GO_Central

GO - Biological processi

  1. activation of phospholipase D activity Source: GO_Central
  2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: GO_Central
  3. blood coagulation Source: Reactome
  4. cell differentiation Source: Ensembl
  5. GTP catabolic process Source: InterPro
  6. in utero embryonic development Source: Ensembl
  7. movement of cell or subcellular component Source: ProtInc
  8. patterning of blood vessels Source: Ensembl
  9. platelet activation Source: Reactome
  10. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  11. regulation of cell migration Source: Ensembl
  12. regulation of cell shape Source: Ensembl
  13. Rho protein signal transduction Source: GO_Central
  14. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_18407. G alpha (12/13) signalling events.
REACT_20647. Thromboxane signalling through TP receptor.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinkiQ14344.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit alpha-13
Short name:
G alpha-13
Short name:
G-protein subunit alpha-13
Gene namesi
Name:GNA13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:4381. GNA13.

Subcellular locationi

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.

GO - Cellular componenti

  1. brush border membrane Source: GO_Central
  2. extracellular vesicular exosome Source: UniProtKB
  3. focal adhesion Source: UniProtKB
  4. heterotrimeric G-protein complex Source: GO_Central
  5. melanosome Source: UniProtKB-SubCell
  6. membrane Source: UniProtKB
  7. nucleus Source: UniProtKB-SubCell
  8. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. 1 Publication
Mutagenesisi18 – 181C → S: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation. 1 Publication
Mutagenesisi203 – 2031T → A: Abolishes phosphorylation by PKA; disrupts heterotrimer stability. 1 Publication

Organism-specific databases

PharmGKBiPA28766.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Guanine nucleotide-binding protein subunit alpha-13PRO_0000203773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi14 – 141S-palmitoyl cysteine1 Publication
Lipidationi18 – 181S-palmitoyl cysteine1 Publication
Modified residuei203 – 2031Phosphothreonine; by PKA1 Publication

Post-translational modificationi

Palmitoylation is critical for proper membrane localization and signaling.1 Publication
Phosphorylation on Thr-203 by PKA destabilizes the heterotrimer of alpha, beta and gamma, and inhibits Rho activation.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ14344.
PaxDbiQ14344.
PeptideAtlasiQ14344.
PRIDEiQ14344.

PTM databases

PhosphoSiteiQ14344.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

BgeeiQ14344.
CleanExiHS_GNA13.
ExpressionAtlasiQ14344. baseline and differential.
GenevestigatoriQ14344.

Organism-specific databases

HPAiHPA010087.

Interactioni

Subunit structurei

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 RGS22.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGEF1Q928883EBI-465387,EBI-465400
CXCR5P323029EBI-465387,EBI-2835269

Protein-protein interaction databases

BioGridi115914. 45 interactions.
IntActiQ14344. 8 interactions.
MINTiMINT-85993.
STRINGi9606.ENSP00000400717.

Structurei

3D structure databases

ProteinModelPortaliQ14344.
SMRiQ14344. Positions 47-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG279688.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiQ14344.
KOiK04639.
OMAiCFPGCVL.
OrthoDBiEOG7HF1JF.
PhylomeDBiQ14344.
TreeFamiTF300673.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12.
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.
PR00440. GPROTEINA12.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14344-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADFLPSRSV LSVCFPGCLL TSGEAEQQRK SKEIDKCLSR EKTYVKRLVK
60 70 80 90 100
ILLLGAGESG KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV
110 120 130 140 150
DAREKLHIPW GDNSNQQHGD KMMSFDTRAP MAAQGMVETR VFLQYLPAIR
160 170 180 190 200
ALWADSGIQN AYDRRREFQL GESVKYFLDN LDKLGEPDYI PSQQDILLAR
210 220 230 240 250
RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV TSILFLVSSS
260 270 280 290 300
EFDQVLMEDR LTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV
310 320 330 340 350
QIVSIKDYFL EFEGDPHCLR DVQKFLVECF RNKRRDQQQK PLYHHFTTAI
360 370
NTENIRLVFR DVKDTILHDN LKQLMLQ
Length:377
Mass (Da):44,050
Last modified:October 31, 2003 - v2
Checksum:i929B7B6473C54F2E
GO
Isoform 2 (identifier: Q14344-2) [UniParc]FASTAAdd to basket

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

Show »
Length:282
Mass (Da):33,287
Checksum:iE32B6298504794BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111F → L in BAH13696 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211V → L.1 Publication
Corresponds to variant rs1062597 [ dbSNP | Ensembl ].
VAR_017160

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9595Missing in isoform 2. 1 PublicationVSP_055140Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11661.1. [Q14344-1]
CCDS62302.1. [Q14344-2]
PIRiI57490.
RefSeqiNP_001269354.1. NM_001282425.1. [Q14344-2]
NP_006563.2. NM_006572.5. [Q14344-1]
UniGeneiHs.515018.

Genome annotation databases

EnsembliENST00000439174; ENSP00000400717; ENSG00000120063. [Q14344-1]
ENST00000541118; ENSP00000439647; ENSG00000120063. [Q14344-2]
GeneIDi10672.
KEGGihsa:10672.
UCSCiuc002jfc.3. human. [Q14344-1]

Polymorphism databases

DMDMi38258936.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11661.1. [Q14344-1]
CCDS62302.1. [Q14344-2]
PIRiI57490.
RefSeqiNP_001269354.1. NM_001282425.1. [Q14344-2]
NP_006563.2. NM_006572.5. [Q14344-1]
UniGeneiHs.515018.

3D structure databases

ProteinModelPortaliQ14344.
SMRiQ14344. Positions 47-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115914. 45 interactions.
IntActiQ14344. 8 interactions.
MINTiMINT-85993.
STRINGi9606.ENSP00000400717.

PTM databases

PhosphoSiteiQ14344.

Polymorphism databases

DMDMi38258936.

Proteomic databases

MaxQBiQ14344.
PaxDbiQ14344.
PeptideAtlasiQ14344.
PRIDEiQ14344.

Protocols and materials databases

DNASUi10672.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000439174; ENSP00000400717; ENSG00000120063. [Q14344-1]
ENST00000541118; ENSP00000439647; ENSG00000120063. [Q14344-2]
GeneIDi10672.
KEGGihsa:10672.
UCSCiuc002jfc.3. human. [Q14344-1]

Organism-specific databases

CTDi10672.
GeneCardsiGC17M063005.
HGNCiHGNC:4381. GNA13.
HPAiHPA010087.
MIMi604406. gene.
neXtProtiNX_Q14344.
PharmGKBiPA28766.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG279688.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiQ14344.
KOiK04639.
OMAiCFPGCVL.
OrthoDBiEOG7HF1JF.
PhylomeDBiQ14344.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiREACT_18407. G alpha (12/13) signalling events.
REACT_20647. Thromboxane signalling through TP receptor.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinkiQ14344.

Miscellaneous databases

ChiTaRSiGNA13. human.
GeneWikiiGNA13.
GenomeRNAii10672.
NextBioi35480296.
PROiQ14344.
SOURCEiSearch...

Gene expression databases

BgeeiQ14344.
CleanExiHS_GNA13.
ExpressionAtlasiQ14344. baseline and differential.
GenevestigatoriQ14344.

Family and domain databases

Gene3Di1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR000469. Gprotein_alpha_12.
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.
PR00440. GPROTEINA12.
SMARTiSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMiSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGNA13_HUMAN
AccessioniPrimary (citable) accession number: Q14344
Secondary accession number(s): B2R977
, B7Z7R0, F5H1G8, Q8TD70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 31, 2003
Last modified: March 4, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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.