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Ras-like protein 1 (Dras1) (Dmras85D)

 RAS1_DROME              Reviewed;         189 AA.
P08646; Q9V448;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
10-OCT-2018, entry version 190.
RecName: Full=Ras-like protein 1;
Short=Dras1;
AltName: Full=Dmras85D;
Flags: Precursor;
Name=Ras85D; Synonyms=Ras1; ORFNames=CG9375;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3110012; DOI=10.1016/0378-1119(87)90301-5;
Brock H.W.;
"Sequence and genomic structure of ras homologues Dmras85D and
Dmras64B of Drosophila melanogaster.";
Gene 51:129-137(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6430564; DOI=10.1016/0092-8674(84)90437-9;
Neuman-Silberberg F.S., Schejter E., Hoffmann F.M., Shilo B.-Z.;
"The Drosophila ras oncogenes: structure and nucleotide sequence.";
Cell 37:1027-1033(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=W13;
PubMed=10552039; DOI=10.1007/PL00006579;
Gasperini R., Gibson G.;
"Absence of protein polymorphism in the Ras genes of Drosophila
melanogaster.";
J. Mol. Evol. 49:583-590(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46, AND TISSUE SPECIFICITY.
STRAIN=Canton-S;
PubMed=7873789; DOI=10.1002/aja.1002010208;
Ezer S.T., Sahar D., Salzberg A., Lev Z.;
"Differential expression during embryogenesis of three genes clustered
in the Ras1 region of Drosophila melanogaster.";
Dev. Dyn. 201:179-190(1994).
[8]
FUNCTION, AND MUTAGENESIS OF GLY-12; ASP-38 AND TYR-40.
PubMed=11290305;
Halfar K., Rommel C., Stocker H., Hafen E.;
"Ras controls growth, survival and differentiation in the Drosophila
eye by different thresholds of MAP kinase activity.";
Development 128:1687-1696(2001).
[9]
SUBCELLULAR LOCATION, AND ISOPRENYLATION AT CYS-186.
PubMed=18503409; DOI=10.1042/BJ20080560;
Day J.P., Cleghon V., Houslay M.D., Davies S.-A.;
"Regulation of a Drosophila melanogaster cGMP-specific
phosphodiesterase by prenylation and interaction with a prenyl-binding
protein.";
Biochem. J. 414:363-374(2008).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19965758; DOI=10.1126/science.1176450;
Rewitz K.F., Yamanaka N., Gilbert L.I., O'Connor M.B.;
"The insect neuropeptide PTTH activates receptor tyrosine kinase torso
to initiate metamorphosis.";
Science 326:1403-1405(2009).
-!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
activity (By similarity). Plays a role in eye development by
regulating cell growth, survival of postmitotic ommatidial cells
and differentiation of photoreceptor cells (PubMed:11290305).
During larval development, mediates Ptth/tor signaling leading to
the production of ecdysone, a hormone required for the initiation
of metamorphosis (PubMed:19965758). {ECO:0000250|UniProtKB:P01112,
ECO:0000269|PubMed:11290305, ECO:0000269|PubMed:19965758}.
-!- ACTIVITY REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP).
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18503409};
Lipid-anchor {ECO:0000269|PubMed:18503409}; Cytoplasmic side
{ECO:0000269|PubMed:18503409}. Note=Loss of prenylation causes
protein location to the cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in the posterior termini of the
embryo, restricted mainly to the embryonic central nervous system,
and in the eye imaginal disk. {ECO:0000269|PubMed:7873789}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the prothoracic
gland (PG) delays the onset of pupariation by prolonging the L3
larval stage. {ECO:0000269|PubMed:19965758}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
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EMBL; M16429; AAA28847.1; -; Genomic_DNA.
EMBL; M16123; AAA28847.1; JOINED; Genomic_DNA.
EMBL; M16428; AAA28847.1; JOINED; Genomic_DNA.
EMBL; K01960; AAA28846.1; -; mRNA.
EMBL; AF186648; AAF15514.1; -; Genomic_DNA.
EMBL; AE014297; AAF54388.1; -; Genomic_DNA.
EMBL; AY089541; AAL90279.1; -; mRNA.
EMBL; AY094888; AAM11241.1; -; mRNA.
EMBL; X73219; CAA51689.1; -; Genomic_DNA.
PIR; A29048; TVFF85.
PIR; S35097; S35097.
RefSeq; NP_476699.1; NM_057351.5.
UniGene; Dm.4812; -.
ProteinModelPortal; P08646; -.
SMR; P08646; -.
BioGrid; 66301; 232.
DIP; DIP-23541N; -.
STRING; 7227.FBpp0081600; -.
PaxDb; P08646; -.
PRIDE; P08646; -.
EnsemblMetazoa; FBtr0082122; FBpp0081600; FBgn0003205.
GeneID; 41140; -.
KEGG; dme:Dmel_CG9375; -.
CTD; 41140; -.
FlyBase; FBgn0003205; Ras85D.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133672; -.
InParanoid; P08646; -.
KO; K07827; -.
OMA; QSWAVNM; -.
OrthoDB; EOG091G0UAU; -.
PhylomeDB; P08646; -.
Reactome; R-DME-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-DME-1433557; Signaling by SCF-KIT.
Reactome; R-DME-171007; p38MAPK events.
Reactome; R-DME-179812; GRB2 events in EGFR signaling.
Reactome; R-DME-180336; SHC1 events in EGFR signaling.
Reactome; R-DME-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-DME-210993; Tie2 Signaling.
Reactome; R-DME-2179392; EGFR Transactivation by Gastrin.
Reactome; R-DME-2424491; DAP12 signaling.
Reactome; R-DME-2871796; FCERI mediated MAPK activation.
Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
Reactome; R-DME-3928662; EPHB-mediated forward signaling.
Reactome; R-DME-432553; Phosphorylation of PER and TIM.
Reactome; R-DME-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-DME-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-DME-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-DME-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-DME-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-DME-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-DME-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-DME-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-DME-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-DME-5658442; Regulation of RAS by GAPs.
Reactome; R-DME-5673000; RAF activation.
Reactome; R-DME-5673001; RAF/MAP kinase cascade.
Reactome; R-DME-5674135; MAP2K and MAPK activation.
Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-DME-8851805; MET activates RAS signaling.
Reactome; R-DME-8951936; RUNX3 regulates p14-ARF.
SignaLink; P08646; -.
ChiTaRS; Ras85D; fly.
GenomeRNAi; 41140; -.
PRO; PR:P08646; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0003205; Expressed in 32 organ(s), highest expression level in embryonic/larval hemocyte (Drosophila).
Genevisible; P08646; DM.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0001709; P:cell fate determination; IMP:FlyBase.
GO; GO:0008283; P:cell proliferation; IMP:FlyBase.
GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
GO; GO:0030381; P:chorion-containing eggshell pattern formation; IMP:FlyBase.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:FlyBase.
GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase.
GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
GO; GO:0007369; P:gastrulation; IMP:FlyBase.
GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
GO; GO:0002168; P:instar larval development; IMP:FlyBase.
GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
GO; GO:0007479; P:leg disc proximal/distal pattern formation; IEP:FlyBase.
GO; GO:0072002; P:Malpighian tubule development; IMP:FlyBase.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:FlyBase.
GO; GO:0010507; P:negative regulation of autophagy; IMP:FlyBase.
GO; GO:0046673; P:negative regulation of compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:FlyBase.
GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
GO; GO:0007309; P:oocyte axis specification; IMP:FlyBase.
GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
GO; GO:0042461; P:photoreceptor cell development; IGI:UniProtKB.
GO; GO:0046530; P:photoreceptor cell differentiation; IMP:FlyBase.
GO; GO:0043703; P:photoreceptor cell fate determination; IGI:FlyBase.
GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:FlyBase.
GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:FlyBase.
GO; GO:0035208; P:positive regulation of hemocyte proliferation; IMP:FlyBase.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:FlyBase.
GO; GO:0046534; P:positive regulation of photoreceptor cell differentiation; IMP:FlyBase.
GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
GO; GO:0007265; P:Ras protein signal transduction; IMP:FlyBase.
GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
GO; GO:0008361; P:regulation of cell size; IMP:FlyBase.
GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
GO; GO:0045610; P:regulation of hemocyte differentiation; IMP:FlyBase.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
GO; GO:0045500; P:sevenless signaling pathway; IMP:FlyBase.
GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
GO; GO:0048865; P:stem cell fate commitment; IMP:FlyBase.
GO; GO:0072089; P:stem cell proliferation; IMP:FlyBase.
GO; GO:0007362; P:terminal region determination; IGI:FlyBase.
GO; GO:0038202; P:TORC1 signaling; IMP:FlyBase.
GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
GO; GO:0060438; P:trachea development; IMP:FlyBase.
GO; GO:0007426; P:tracheal outgrowth, open tracheal system; IMP:FlyBase.
GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Prenylation; Reference proteome.
CHAIN 1 186 Ras-like protein 1.
/FTId=PRO_0000082665.
PROPEP 187 189 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000281313.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 116 119 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region.
MOD_RES 186 186 Cysteine methyl ester. {ECO:0000305}.
LIPID 186 186 S-geranylgeranyl cysteine.
{ECO:0000305|PubMed:18503409}.
MUTAGEN 12 12 G->V: Rough eyes characterized by the
presence of additional R7 photoreceptor
cells. Normal survival of postmitotic
ommatidial cells but differentiation into
photoreceptor cells is limited to R8
cells. Less severe Rough eye phenotype;
when associated with E-38. Normal eyes;
when associated with C-40.
{ECO:0000269|PubMed:11290305}.
MUTAGEN 38 38 D->E: Mild rough eye phenotype; when
associated with V-12.
{ECO:0000269|PubMed:11290305}.
MUTAGEN 40 40 Y->C: Impaired cell growth, survival of
postmitotic ommatidial cells and
differentiation into R8 photoreceptors.
Normal eye morphology; when associated
with V-12. {ECO:0000269|PubMed:11290305}.
CONFLICT 11 11 A -> P (in Ref. 2; AAA28846).
{ECO:0000305}.
CONFLICT 44 45 VV -> RF (in Ref. 2; AAA28846).
{ECO:0000305}.
CONFLICT 84 84 V -> I (in Ref. 2; AAA28846).
{ECO:0000305}.
CONFLICT 102 102 R -> H (in Ref. 2; AAA28846).
{ECO:0000305}.
CONFLICT 114 114 V -> A (in Ref. 2; AAA28846).
{ECO:0000305}.
CONFLICT 182 182 R -> C (in Ref. 2; AAA28846).
{ECO:0000305}.
SEQUENCE 189 AA; 21594 MW; 14236DCD65EACCD2 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLL VFAVNSAKSF EDIGTYREQI KRVKDAEEVP MVLVGNKCDL
ASWNVNNEQA REVAKQYGIP YIETSAKTRM GVDDAFYTLV REIRKDKDNK GRRGRKMNKP
NRRFKCKML


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10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.1 mg
EIAAB43485 C20orf188,Homo sapiens,Human,Protein TAP1,Protein TRUSS,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp4-associated protein,TR
EIAAB33912 E3 ubiquitin-protein ligase RBBP6,Mouse,Mus musculus,P2pr,p53-associated cellular protein of testis,Pact,Proliferation potential-related protein,Protein P2P-R,Rbbp6,Retinoblastoma-binding protein 6
EIAAB38162 Homo sapiens,Human,MAP,Merlin-associated protein,RabGAPLP,RABGAPLP,Rab-GTPase-activating protein-like protein,RUN and TBC1 domain-containing protein 3,RUTBC3,SGSM3,Small G protein signaling modulator
EIAAB29908 Cap1,Contraception-associated protein 1,Fertility protein SP22,Park7,Parkinson disease protein 7 homolog,Protein CAP1,Protein DJ-1,Rat,Rattus norvegicus
EIAAB31031 DDXBP1,DEAD_H box-binding protein 1,E3 SUMO-protein ligase PIAS1,GBP,Gu-binding protein,Homo sapiens,Human,PIAS1,Protein inhibitor of activated STAT protein 1,RNA helicase II-binding protein


 

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