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Protein

Guanine nucleotide-binding protein subunit alpha-12

Gene

GNA12

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. May play a role in the control of cell migration through the TOR signaling cascade.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711MagnesiumBy similarity
Metal bindingi208 – 2081MagnesiumBy similarity
Binding sitei353 – 3531GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 718GTPBy similarity
Nucleotide bindingi202 – 2087GTPBy similarity
Nucleotide bindingi227 – 2315GTPBy similarity
Nucleotide bindingi296 – 2994GTPBy 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

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: GO_Central
  2. blood coagulation Source: Reactome
  3. cell differentiation Source: Ensembl
  4. embryonic digit morphogenesis Source: Ensembl
  5. G-protein coupled receptor signaling pathway Source: ProtInc
  6. in utero embryonic development Source: Ensembl
  7. metabolic process Source: GOC
  8. platelet activation Source: Reactome
  9. regulation of cell shape Source: Ensembl
  10. regulation of fibroblast migration Source: UniProtKB
  11. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  12. regulation of TOR signaling Source: UniProtKB
  13. response to drug Source: Ensembl
  14. Rho protein signal transduction Source: GO_Central
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_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinkiQ03113.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit alpha-12
Short name:
G alpha-12
Short name:
G-protein subunit alpha-12
Gene namesi
Name:GNA12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:4380. GNA12.

Subcellular locationi

GO - Cellular componenti

  1. brush border membrane Source: GO_Central
  2. focal adhesion Source: UniProtKB
  3. heterotrimeric G-protein complex Source: GO_Central
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28765.

Polymorphism and mutation databases

BioMutaiGNA12.
DMDMi38258934.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Guanine nucleotide-binding protein subunit alpha-12PRO_0000203770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi11 – 111S-palmitoyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ03113.
PaxDbiQ03113.
PRIDEiQ03113.

PTM databases

PhosphoSiteiQ03113.

Expressioni

Gene expression databases

BgeeiQ03113.
CleanExiHS_GNA12.
ExpressionAtlasiQ03113. baseline and differential.
GenevestigatoriQ03113.

Organism-specific databases

HPAiCAB010046.

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 (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane. Interacts with RGS22.2 Publications

Protein-protein interaction databases

BioGridi109030. 29 interactions.
IntActiQ03113. 4 interactions.
MINTiMINT-85969.
STRINGi9606.ENSP00000275364.

Structurei

3D structure databases

ProteinModelPortaliQ03113.
SMRiQ03113. Positions 56-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG279688.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiQ03113.
KOiK04346.
OMAiRDILFCR.
OrthoDBiEOG7HF1JF.
PhylomeDBiQ03113.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q03113-1) [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
MSGVVRTLSR CLLPAEAGGA RERRAGSGAR DAEREARRRS RDIDALLARE
60 70 80 90 100
RRAVRRLVKI LLLGAGESGK STFLKQMRII HGREFDQKAL LEFRDTIFDN
110 120 130 140 150
ILKGSRVLVD ARDKLGIPWQ YSENEKHGMF LMAFENKAGL PVEPATFQLY
160 170 180 190 200
VPALSALWRD SGIREAFSRR SEFQLGESVK YFLDNLDRIG QLNYFPSKQD
210 220 230 240 250
ILLARKATKG IVEHDFVIKK IPFKMVDVGG QRSQRQKWFQ CFDGITSILF
260 270 280 290 300
MVSSSEYDQV LMEDRRTNRL VESMNIFETI VNNKLFFNVS IILFLNKMDL
310 320 330 340 350
LVEKVKTVSI KKHFPDFRGD PHRLEDVQRY LVQCFDRKRR NRSKPLFHHF
360 370 380
TTAIDTENVR FVFHAVKDTI LQENLKDIML Q
Length:381
Mass (Da):44,279
Last modified:January 23, 2007 - v4
Checksum:i04C3F12B29255F89
GO
Isoform 2 (identifier: Q03113-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: MSGVVRTLSR...RDTIFDNILK → MKRRMFPRPC...HLLIAHPGSR

Show »
Length:322
Mass (Da):37,601
Checksum:iAB035356C0AACD6F
GO
Isoform 3 (identifier: Q03113-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.
     174-190: Missing.

Note: No experimental confirmation available.

Show »
Length:288
Mass (Da):34,002
Checksum:i72CABE32D6FC5D6C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261K → E in AAM12615 (Ref. 2) Curated
Sequence conflicti323 – 3231R → Q in AAA35867 (PubMed:8423800).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681S → G.1 Publication
Corresponds to variant rs11552939 [ dbSNP | Ensembl ].
VAR_071044
Natural varianti242 – 2421F → L.
Corresponds to variant rs45606633 [ dbSNP | Ensembl ].
VAR_049359
Natural varianti330 – 3301Y → H.
Corresponds to variant rs45583847 [ dbSNP | Ensembl ].
VAR_049360

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 103103MSGVV…DNILK → MKRRMFPRPCLARMPGSRGS GSTPDGNRKCCRFEHLLIAH PGSR in isoform 2. 1 PublicationVSP_055171Add
BLAST
Alternative sequencei1 – 7676Missing in isoform 3. 1 PublicationVSP_055230Add
BLAST
Alternative sequencei174 – 19017Missing in isoform 3. 1 PublicationVSP_055231Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01694 mRNA. Translation: AAA35867.1.
AF493901 mRNA. Translation: AAM12615.1.
AK127842 mRNA. Translation: BAG54584.1.
AK295830 mRNA. Translation: BAH12193.1.
AC006028 Genomic DNA. Translation: AAP21870.1.
AC004933 Genomic DNA. Translation: AAD05026.1.
CH236953 Genomic DNA. Translation: EAL23961.1.
BC087537 mRNA. Translation: AAH87537.1.
BC111464 mRNA. Translation: AAI11465.1.
CCDSiCCDS5335.1. [Q03113-1]
CCDS64584.1. [Q03113-2]
PIRiA48071.
RefSeqiNP_001269370.1. NM_001282441.1. [Q03113-2]
NP_001280021.1. NM_001293092.1.
NP_031379.2. NM_007353.2. [Q03113-1]
UniGeneiHs.487341.

Genome annotation databases

EnsembliENST00000275364; ENSP00000275364; ENSG00000146535. [Q03113-1]
ENST00000407904; ENSP00000385935; ENSG00000146535. [Q03113-2]
GeneIDi2768.
KEGGihsa:2768.
UCSCiuc003smu.3. human. [Q03113-1]

Polymorphism and mutation databases

BioMutaiGNA12.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01694 mRNA. Translation: AAA35867.1.
AF493901 mRNA. Translation: AAM12615.1.
AK127842 mRNA. Translation: BAG54584.1.
AK295830 mRNA. Translation: BAH12193.1.
AC006028 Genomic DNA. Translation: AAP21870.1.
AC004933 Genomic DNA. Translation: AAD05026.1.
CH236953 Genomic DNA. Translation: EAL23961.1.
BC087537 mRNA. Translation: AAH87537.1.
BC111464 mRNA. Translation: AAI11465.1.
CCDSiCCDS5335.1. [Q03113-1]
CCDS64584.1. [Q03113-2]
PIRiA48071.
RefSeqiNP_001269370.1. NM_001282441.1. [Q03113-2]
NP_001280021.1. NM_001293092.1.
NP_031379.2. NM_007353.2. [Q03113-1]
UniGeneiHs.487341.

3D structure databases

ProteinModelPortaliQ03113.
SMRiQ03113. Positions 56-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109030. 29 interactions.
IntActiQ03113. 4 interactions.
MINTiMINT-85969.
STRINGi9606.ENSP00000275364.

PTM databases

PhosphoSiteiQ03113.

Polymorphism and mutation databases

BioMutaiGNA12.
DMDMi38258934.

Proteomic databases

MaxQBiQ03113.
PaxDbiQ03113.
PRIDEiQ03113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275364; ENSP00000275364; ENSG00000146535. [Q03113-1]
ENST00000407904; ENSP00000385935; ENSG00000146535. [Q03113-2]
GeneIDi2768.
KEGGihsa:2768.
UCSCiuc003smu.3. human. [Q03113-1]

Organism-specific databases

CTDi2768.
GeneCardsiGC07M002767.
HGNCiHGNC:4380. GNA12.
HPAiCAB010046.
MIMi604394. gene.
neXtProtiNX_Q03113.
PharmGKBiPA28765.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG279688.
GeneTreeiENSGT00770000120503.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiQ03113.
KOiK04346.
OMAiRDILFCR.
OrthoDBiEOG7HF1JF.
PhylomeDBiQ03113.
TreeFamiTF300673.

Enzyme and pathway databases

ReactomeiREACT_18407. G alpha (12/13) signalling events.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinkiQ03113.

Miscellaneous databases

ChiTaRSiGNA12. human.
GeneWikiiGNA12.
GenomeRNAii2768.
NextBioi10888.
PROiQ03113.
SOURCEiSearch...

Gene expression databases

BgeeiQ03113.
CleanExiHS_GNA12.
ExpressionAtlasiQ03113. baseline and differential.
GenevestigatoriQ03113.

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 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] (ISOFORM 1).
  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 2 AND 3).
    Tissue: Hippocampus and Placenta.
  4. "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.
    , 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].
  5. "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.
    , 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].
  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] (ISOFORM 1), VARIANT GLY-68.
    Tissue: Brain and Pancreas.
  7. "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.
  8. "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.
  9. "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.

Entry informationi

Entry nameiGNA12_HUMAN
AccessioniPrimary (citable) accession number: Q03113
Secondary accession number(s): A4D204
, B3KXS2, B7Z3F7, Q2T9L1, Q5PPR5, Q86UM8, Q8TD71, Q9UDU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 146 of the entry and version 4 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 7
    Human chromosome 7: 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.