RERG_HUMAN
ID RERG_HUMAN Reviewed; 199 AA.
AC Q96A58; B2R9R0; B4DI02;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ras-related and estrogen-regulated growth inhibitor;
DE EC=3.6.5.2 {ECO:0000269|PubMed:11533059};
GN Name=RERG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11533059; DOI=10.1074/jbc.m105888200;
RA Finlin B.S., Gau C.-L., Murphy G.A., Shao H., Kimel T., Seitz R.S.,
RA Chiu Y.-F., Botstein D., Brown P.O., Der C.J., Tamanoi F., Andres D.A.,
RA Perou C.M.;
RT "RERG is a novel ras-related, estrogen-regulated and growth-inhibitory gene
RT in breast cancer.";
RL J. Biol. Chem. 276:42259-42267(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Caudate nucleus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-174 IN COMPLEX WITH GDP.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human RERG in the GDP bound state.";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: Binds GDP/GTP and possesses intrinsic GTPase activity. Has
CC higher affinity for GDP than for GTP. In cell lines overexpression
CC leads to a reduction in the rate of proliferation, colony formation and
CC in tumorigenic potential. {ECO:0000269|PubMed:11533059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:11533059};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11533059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96A58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96A58-2; Sequence=VSP_043393;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver,
CC skin, kidney and pancreas. Detected in estrogen receptor-positive
CC breast-derived cell lines, but not in estrogen receptor-negative cell
CC lines. Expression is decreased or lost in a significant proportion of
CC primary breast tumors with poor clinical prognosis.
CC {ECO:0000269|PubMed:11533059}.
CC -!- INDUCTION: Up-regulated by estradiol. Down-regulated by tamoxifen.
CC {ECO:0000269|PubMed:11533059}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AF339750; AAK98530.1; -; mRNA.
DR EMBL; AK295343; BAG58314.1; -; mRNA.
DR EMBL; AK313881; BAG36607.1; -; mRNA.
DR EMBL; AC007543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96345.1; -; Genomic_DNA.
DR EMBL; BC007997; AAH07997.1; -; mRNA.
DR CCDS; CCDS53753.1; -. [Q96A58-2]
DR CCDS; CCDS8673.1; -. [Q96A58-1]
DR RefSeq; NP_001177655.1; NM_001190726.1. [Q96A58-2]
DR RefSeq; NP_116307.1; NM_032918.2. [Q96A58-1]
DR PDB; 2ATV; X-ray; 1.90 A; A=1-174.
DR PDBsum; 2ATV; -.
DR AlphaFoldDB; Q96A58; -.
DR SMR; Q96A58; -.
DR BioGRID; 124423; 4.
DR IntAct; Q96A58; 2.
DR STRING; 9606.ENSP00000256953; -.
DR iPTMnet; Q96A58; -.
DR PhosphoSitePlus; Q96A58; -.
DR BioMuta; RERG; -.
DR DMDM; 74731090; -.
DR EPD; Q96A58; -.
DR jPOST; Q96A58; -.
DR MassIVE; Q96A58; -.
DR PaxDb; Q96A58; -.
DR PeptideAtlas; Q96A58; -.
DR PRIDE; Q96A58; -.
DR ProteomicsDB; 75918; -. [Q96A58-1]
DR ProteomicsDB; 75919; -. [Q96A58-2]
DR Antibodypedia; 23714; 146 antibodies from 27 providers.
DR DNASU; 85004; -.
DR Ensembl; ENST00000256953.6; ENSP00000256953.2; ENSG00000134533.6. [Q96A58-1]
DR Ensembl; ENST00000536465.5; ENSP00000438280.1; ENSG00000134533.6. [Q96A58-1]
DR Ensembl; ENST00000538313.5; ENSP00000441505.1; ENSG00000134533.6. [Q96A58-1]
DR Ensembl; ENST00000546331.5; ENSP00000444485.1; ENSG00000134533.6. [Q96A58-2]
DR GeneID; 85004; -.
DR KEGG; hsa:85004; -.
DR MANE-Select; ENST00000256953.6; ENSP00000256953.2; NM_032918.3; NP_116307.1.
DR UCSC; uc001rcs.4; human. [Q96A58-1]
DR CTD; 85004; -.
DR DisGeNET; 85004; -.
DR GeneCards; RERG; -.
DR HGNC; HGNC:15980; RERG.
DR HPA; ENSG00000134533; Tissue enhanced (endometrium).
DR MIM; 612664; gene.
DR neXtProt; NX_Q96A58; -.
DR OpenTargets; ENSG00000134533; -.
DR PharmGKB; PA34333; -.
DR VEuPathDB; HostDB:ENSG00000134533; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000159750; -.
DR HOGENOM; CLU_041217_9_7_1; -.
DR InParanoid; Q96A58; -.
DR OMA; TETVQWA; -.
DR PhylomeDB; Q96A58; -.
DR TreeFam; TF318030; -.
DR PathwayCommons; Q96A58; -.
DR SignaLink; Q96A58; -.
DR BioGRID-ORCS; 85004; 8 hits in 1073 CRISPR screens.
DR ChiTaRS; RERG; human.
DR EvolutionaryTrace; Q96A58; -.
DR GenomeRNAi; 85004; -.
DR Pharos; Q96A58; Tbio.
DR PRO; PR:Q96A58; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96A58; protein.
DR Bgee; ENSG00000134533; Expressed in germinal epithelium of ovary and 173 other tissues.
DR ExpressionAtlas; Q96A58; baseline and differential.
DR Genevisible; Q96A58; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; NAS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; NAS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; GTP-binding; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..199
FT /note="Ras-related and estrogen-regulated growth inhibitor"
FT /id="PRO_0000082723"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT VAR_SEQ 21..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043393"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2ATV"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:2ATV"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:2ATV"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:2ATV"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:2ATV"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:2ATV"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2ATV"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:2ATV"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2ATV"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:2ATV"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:2ATV"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2ATV"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2ATV"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:2ATV"
SQ SEQUENCE 199 AA; 22608 MW; 18A0F8BDD40CEAF0 CRC64;
MAKSAEVKLA IFGRAGVGKS ALVVRFLTKR FIWEYDPTLE STYRHQATID DEVVSMEILD
TAGQEDTIQR EGHMRWGEGF VLVYDITDRG SFEEVLPLKN ILDEIKKPKN VTLILVGNKA
DLDHSRQVST EEGEKLATEL ACAFYECSAC TGEGNITEIF YELCREVRRR RMVQGKTRRR
SSTTHVKQAI NKMLTKISS
