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T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5)

 TGTP1_MOUSE             Reviewed;         415 AA.
Q62293; Q60711; Q8BN19;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
08-MAY-2019, entry version 152.
RecName: Full=T-cell-specific guanine nucleotide triphosphate-binding protein 1;
EC=3.6.5.- {ECO:0000269|PubMed:9725230};
AltName: Full=Interferon-gamma-inducible GTPase Ifggb5 {ECO:0000303|PubMed:22892676};
Name=Tgtp1;
Synonyms=Ifggb5 {ECO:0000303|PubMed:22892676},
Irgb6 {ECO:0000303|PubMed:22892676},
Mg21 {ECO:0000303|PubMed:7884320};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY IFNG, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Peritoneal macrophage;
PubMed=7884320;
Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
"Cloning and characterization of a novel cDNA that is IFN-gamma-
induced in mouse peritoneal macrophages and encodes a putative GTP-
binding protein.";
J. Leukoc. Biol. 57:477-483(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic stem cell, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=7836757;
Carlow D.A., Marth J., Clark-Lewis I., Teh H.S.;
"Isolation of a gene encoding a developmentally regulated T cell-
specific protein with a guanine nucleotide triphosphate-binding
motif.";
J. Immunol. 154:1724-1734(1995).
[7]
FUNCTION, INDUCTION BY IFNG, AND CATALYTIC ACTIVITY.
PubMed=9725230;
Carlow D.A., Teh S.J., Teh H.S.;
"Specific antiviral activity demonstrated by TGTP, a member of a new
family of interferon-induced GTPases.";
J. Immunol. 161:2348-2355(1998).
[8]
GENOMIC ORGANIZATION OF P47 GTPASE CLUSTER.
PubMed=16277747; DOI=10.1186/gb-2005-6-11-r92;
Bekpen C., Hunn J.P., Rohde C., Parvanova I., Guethlein L., Dunn D.M.,
Glowalla E., Leptin M., Howard J.C.;
"The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of
the cell autonomous resistance mechanism in the human lineage.";
Genome Biol. 6:R92.1-R92.18(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION
BY TNF, AND TISSUE SPECIFICITY.
PubMed=19285957; DOI=10.1016/j.bbrc.2009.03.043;
Yamada K., Akimoto H., Ogawa Y., Kinumi T., Kamagata Y., Ohmiya Y.;
"Upregulation of immunity-related GTPase (IRG) proteins by TNF-alpha
in murine astrocytes.";
Biochem. Biophys. Res. Commun. 382:434-439(2009).
[10]
FUNCTION.
PubMed=19265156; DOI=10.4049/jimmunol.0804190;
Zhao Y., Ferguson D.J., Wilson D.C., Howard J.C., Sibley L.D.,
Yap G.S.;
"Virulent Toxoplasma gondii evade immunity-related GTPase-mediated
parasite vacuole disruption within primed macrophages.";
J. Immunol. 182:3775-3781(2009).
[11]
IDENTIFICATION, AND GENOMIC ANALYSIS.
PubMed=22892676; DOI=10.1007/s10142-012-0291-2;
Premzl M.;
"Comparative genomic analysis of eutherian interferon-gamma-inducible
GTPases.";
Funct. Integr. Genomics 12:599-607(2012).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION, AND INDUCTION BY IFNG.
PubMed=24563254; DOI=10.4049/jimmunol.1302822;
Ohshima J., Lee Y., Sasai M., Saitoh T., Su Ma J., Kamiyama N.,
Matsuura Y., Pann-Ghill S., Hayashi M., Ebisu S., Takeda K., Akira S.,
Yamamoto M.;
"Role of mouse and human autophagy proteins in IFN-gamma-induced cell-
autonomous responses against Toxoplasma gondii.";
J. Immunol. 192:3328-3335(2014).
-!- FUNCTION: Involved in innate cell-autonomous resistance to
intracellular pathogens, such as Toxoplasma gondii. During
avirulent type II T. gondii infection, recruited to the
parasitophorous vacuole (PV) membrane, leading to PV vesiculation
and rupture, and subsequent digestion of the parasite within the
cytosol (PubMed:19265156, PubMed:24563254). Not recruited to
virulent type I T. gondii PV membrane (PubMed:19265156). May
confer an antiviral state for vesicular stomatitis virus
(PubMed:9725230). {ECO:0000269|PubMed:19265156,
ECO:0000269|PubMed:24563254, ECO:0000269|PubMed:9725230}.
-!- CATALYTIC ACTIVITY:
Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
Evidence={ECO:0000269|PubMed:9725230};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19285957}.
Endoplasmic reticulum {ECO:0000269|PubMed:19285957}. Golgi
apparatus {ECO:0000269|PubMed:19285957}. Note=In astrocytes
stimulated with IFNG or TNF, diffuse cytoplasmic localization
decreases and the protein partially relocalizes to the endoplasmic
reticulum and Golgi apparatus (PubMed:19285957). Due to sequence
similarity with Tgtp2, it is impossible to assign unambiguously
experimental data published in the literature to Tgtp1 or Tgtp2
gene (Probable). {ECO:0000269|PubMed:19285957,
ECO:0000305|PubMed:22892676}.
-!- TISSUE SPECIFICITY: Expressed in thymus and lymph nodes,
predominantly T-cells. Not expressed by immature CD4(+) CD8(+)
thymocytes (at protein level) (PubMed:7836757). Expressed in IFNG-
stimulated macrophages (PubMed:7884320). Expressed at low levels
in unstimulated astrocytes (PubMed:19285957). Due to sequence
similarity with Tgtp2, it is impossible to assign unambiguously
experimental data published in the literature to Tgtp1 or Tgtp2
gene. {ECO:0000269|PubMed:19285957, ECO:0000269|PubMed:7836757,
ECO:0000269|PubMed:7884320}.
-!- INDUCTION: In macrophages, up-regulated by IFNG, but not by IL2,
IL4, IL10, nor TNF (PubMed:7884320). Up-regulated by IFNG in lymph
node cells and thymocytes and other cell types (PubMed:7836757,
PubMed:9725230, PubMed:24563254). In astrocytes, up-regulated by
TNF and IFNG; when both cytokines are combined, the effect is
synergistic (PubMed:19285957). Due to sequence similarity with
Tgtp2, it is impossible to assign unambiguously experimental data
published in the literature to Tgtp1 or Tgtp2 gene (Probable).
{ECO:0000269|PubMed:19285957, ECO:0000269|PubMed:24563254,
ECO:0000269|PubMed:7836757, ECO:0000269|PubMed:7884320,
ECO:0000269|PubMed:9725230, ECO:0000305|PubMed:22892676}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. IRG family. {ECO:0000305}.
-!- CAUTION: The gene Tgtp1 belongs to a large family of eutherian
IFNG-inducible GTPases, called immunity-related p47 GTPases, which
comprises a variable amount of paralogs depending upon the species
studied. In C57BL/6J mice, there is over 20 genes, whereas humans
have only one ortholog. Tgtp1 closest paralog is Tgtp2. Both genes
encode identical proteins. At the nucleotide sequence level, their
CDSs differ at only 4 positions. Consequently it is almost
impossible to assign unambiguously to one gene or the other
experimental data published in the literature.
{ECO:0000305|PubMed:16277747, ECO:0000305|PubMed:22892676}.
-----------------------------------------------------------------------
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EMBL; U15636; AAA66220.1; -; mRNA.
EMBL; AK089836; BAC40974.1; -; mRNA.
EMBL; AK163978; BAE37565.1; -; mRNA.
EMBL; AK172473; BAE43026.1; -; mRNA.
EMBL; AL627237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466575; EDL33781.1; -; Genomic_DNA.
EMBL; BC085259; AAH85259.1; -; mRNA.
EMBL; FR734025; CBY65988.1; -; Genomic_DNA.
CCDS; CCDS24593.1; -.
PIR; I56251; I56251.
RefSeq; NP_001138636.1; NM_001145164.1.
RefSeq; NP_035709.3; NM_011579.3.
SMR; Q62293; -.
IntAct; Q62293; 2.
MINT; Q62293; -.
STRING; 10090.ENSMUSP00000069914; -.
iPTMnet; Q62293; -.
PhosphoSitePlus; Q62293; -.
EPD; Q62293; -.
MaxQB; Q62293; -.
PaxDb; Q62293; -.
PRIDE; Q62293; -.
DNASU; 21822; -.
Ensembl; ENSMUST00000046745; ENSMUSP00000045025; ENSMUSG00000078921.
Ensembl; ENSMUST00000068063; ENSMUSP00000069914; ENSMUSG00000078922.
Ensembl; ENSMUST00000229241; ENSMUSP00000155831; ENSMUSG00000115886.
Ensembl; ENSMUST00000229815; ENSMUSP00000155662; ENSMUSG00000115886.
GeneID; 100039796; -.
GeneID; 21822; -.
KEGG; mmu:100039796; -.
KEGG; mmu:21822; -.
UCSC; uc007ipm.3; mouse.
CTD; 100039796; -.
CTD; 21822; -.
MGI; MGI:98734; Tgtp1.
eggNOG; ENOG410IJSM; Eukaryota.
eggNOG; ENOG41125KF; LUCA.
GeneTree; ENSGT00950000183007; -.
InParanoid; Q62293; -.
OMA; QCKILEL; -.
OrthoDB; 688334at2759; -.
PhylomeDB; Q62293; -.
TreeFam; TF331897; -.
PRO; PR:Q62293; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000078921; Expressed in 26 organ(s), highest expression level in spleen.
ExpressionAtlas; Q62293; baseline and differential.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
GO; GO:0006952; P:defense response; IBA:GO_Central.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEP:MGI.
GO; GO:0035455; P:response to interferon-alpha; IDA:MGI.
GO; GO:0034341; P:response to interferon-gamma; IDA:MGI.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
InterPro; IPR030385; G_IRG_dom.
InterPro; IPR007743; Immunity-related_GTPase-like.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF05049; IIGP; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51716; G_IRG; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
GTP-binding; Hydrolase; Immunity; Innate immunity; Nucleotide-binding;
Reference proteome.
CHAIN 1 415 T-cell-specific guanine nucleotide
triphosphate-binding protein 1.
/FTId=PRO_0000437942.
DOMAIN 55 237 IRG-type G.
NP_BIND 64 71 GTP. {ECO:0000250}.
NP_BIND 89 93 GTP. {ECO:0000250}.
NP_BIND 218 220 GTP. {ECO:0000250}.
CONFLICT 91 91 A -> G (in Ref. 1; AAA66220).
{ECO:0000305}.
CONFLICT 272 272 E -> G (in Ref. 2; BAC40974).
{ECO:0000305}.
SEQUENCE 415 AA; 47121 MW; 3AFB5F940242952A CRC64;
MAWASSFDAF FKNFKRESKI ISEYDITLIM TYIEENKLQK AVSVIEKVLR DIESAPLHIA
VTGETGAGKS TFINTLRGVG HEEKGAAPTG AIETTMKRTP YPHPKLPNVT IWDLPGIGTT
NFTPQNYLTE MKFGEYDFFI IISATRFKEN DAQLAKAIAQ MGMNFYFVRT KIDSDLDNEQ
KFKPKSFNKE EVLKNIKDYC SNHLQESLDS EPPVFLVSNV DISKYDFPKL ETKLLQDLPA
HKRHVFSLSL QSLTEATINY KRDSLKQKVF LEAMKAGALA TIPLGGMISD ILENLDETFN
LYRSYFGLDD ASLENIAQDL NMSVDDFKVH LRFPHLFAEH NDESLEDKLF KYIKHISSVT
GGPVAAVTYY RMAYYLQNLF LDTAANDAIA LLNSKALFEK KVGPYISEPP EYWEA


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Related Genes :
[Tgtp1 Ifggb5 Irgb6 Mg21] T-cell-specific guanine nucleotide triphosphate-binding protein 1 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb5)
[Tgtp2 Ifggb6 Irgb6 Mg21 Tgtp] T-cell-specific guanine nucleotide triphosphate-binding protein 2 (EC 3.6.5.-) (Interferon-gamma-inducible GTPase Ifggb6 protein) (T-cell-specific guanine nucleotide triphosphate-binding protein)
[Irgm1 Ifi1 Iigp3 Irgm] Immunity-related GTPase family M protein 1 (EC 3.6.5.-) (Interferon-inducible GTPase 3) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47) (LRG-47)
[Samhd1 Mg21] Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1) (mSAMHD1)
[IRGM IFI1 IRGM1 LRG47] Immunity-related GTPase family M protein (EC 3.6.5.-) (Immunity-related GTPase family M protein 1) (Interferon-inducible protein 1) (LPS-stimulated RAW 264.7 macrophage protein 47 homolog) (LRG-47)
[CXCL11 ITAC SCYB11 SCYB9B] C-X-C motif chemokine 11 (Beta-R1) (H174) (Interferon gamma-inducible protein 9) (IP-9) (Interferon-inducible T-cell alpha chemoattractant) (I-TAC) (Small-inducible cytokine B11)
[ADAR ADAR1 DSRAD G1P1 IFI4] Double-stranded RNA-specific adenosine deaminase (DRADA) (EC 3.5.4.37) (136 kDa double-stranded RNA-binding protein) (p136) (Interferon-inducible protein 4) (IFI-4) (K88DSRBP)
[Ifi30 Gilt Ip30] Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Lysosomal thiol reductase IP30)
[Gngt1 Gng1] Guanine nucleotide-binding protein G(T) subunit gamma-T1 (Transducin gamma chain)
[Ifih1] Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Helicase with 2 CARD domains) (Helicard) (Interferon induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (RIG-I-like receptor 2) (RLR-2)
[Cxcl10 Crg2 Ifi10 Inp10 Scyb10] C-X-C motif chemokine 10 (10 kDa interferon gamma-induced protein) (Gamma-IP10) (IP-10) (C7) (Interferon-gamma induced protein CRG-2) (Small-inducible cytokine B10)
[Ifitm3] Interferon-induced transmembrane protein 3 (Dispanin subfamily A member 2b) (DSPA2b) (Fragilis protein) (Interferon-inducible protein 15) (Mouse ifitm-like protein 1) (Mil-1)
[ITK EMT LYK] Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (Interleukin-2-inducible T-cell kinase) (IL-2-inducible T-cell kinase) (Kinase EMT) (T-cell-specific kinase) (Tyrosine-protein kinase Lyk)
[IFI30 GILT IP30] Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (Legumaturain)
[IFI16 IFNGIP1] Gamma-interferon-inducible protein 16 (Ifi-16) (Interferon-inducible myeloid differentiation transcriptional activator)
[Cdc42] Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein)
[XLG3 At1g31930 F5M6.7 T12O21.16] Extra-large guanine nucleotide-binding protein 3 (Extra-large GTP-binding protein 3) (Extra-large G-protein 3)
[Gnai3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[CCL4 LAG1 MIP1B SCYA4] C-C motif chemokine 4 (G-26 T-lymphocyte-secreted protein) (HC21) (Lymphocyte activation gene 1 protein) (LAG-1) (MIP-1-beta(1-69)) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (PAT 744) (Protein H400) (SIS-gamma) (Small-inducible cytokine A4) (T-cell activation protein 2) (ACT-2) [Cleaved into: MIP-1-beta(3-69)]
[Gnat3] Guanine nucleotide-binding protein G(t) subunit alpha-3 (Gustducin alpha-3 chain)
[Itk Emt Tlk Tsk] Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (IL-2-inducible T-cell kinase) (Kinase EMT) (Kinase TLK) (T-cell-specific kinase)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[ATL1 GBP3 SPG3A] Atlastin-1 (EC 3.6.5.-) (Brain-specific GTP-binding protein) (GTP-binding protein 3) (GBP-3) (hGBP3) (Guanine nucleotide-binding protein 3) (Spastic paraplegia 3 protein A)
[DRG1 NEDD3] Developmentally-regulated GTP-binding protein 1 (DRG-1) (Neural precursor cell expressed developmentally down-regulated protein 3) (NEDD-3) (Translation factor GTPase DRG1) (TRAFAC GTPase DRG1) (EC 3.6.5.-)
[Gapvd1 Gapex5 Kiaa1521] GTPase-activating protein and VPS9 domain-containing protein 1 (GAPex-5) (Rab5-activating protein 6)
[Gnb1] Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1)
[Ccl1 Scya1 Tca3] C-C motif chemokine 1 (P500) (SIS-epsilon) (Small-inducible cytokine A1) (T-cell activation protein 3) (TCA-3) (TCA3)
[Rasgrp1 Rasgrp] RAS guanyl-releasing protein 1 (Calcium and DAG-regulated guanine nucleotide exchange factor II) (CalDAG-GEFII) (Ras guanyl-releasing protein)
[GPA1 At2g26300 T1D16.6] Guanine nucleotide-binding protein alpha-1 subunit (GP-alpha-1)

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