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RERGL_HUMAN
ID   RERGL_HUMAN             Reviewed;         205 AA.
AC   Q9H628;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Ras-related and estrogen-regulated growth inhibitor-like protein;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:Q96A58};
DE   AltName: Full=RERG/Ras-like protein;
GN   Name=RERGL;
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 [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Binds GDP/GTP and may possess intrinsic GTPase activity.
CC       {ECO:0000250}.
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:0000250|UniProtKB:Q96A58};
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; AK026308; BAB15439.1; -; mRNA.
DR   EMBL; CH471094; EAW96385.1; -; Genomic_DNA.
DR   EMBL; BC042888; AAH42888.1; -; mRNA.
DR   CCDS; CCDS8679.1; -.
DR   RefSeq; NP_001273130.1; NM_001286201.1.
DR   RefSeq; NP_079006.1; NM_024730.3.
DR   AlphaFoldDB; Q9H628; -.
DR   SMR; Q9H628; -.
DR   STRING; 9606.ENSP00000229002; -.
DR   iPTMnet; Q9H628; -.
DR   PhosphoSitePlus; Q9H628; -.
DR   BioMuta; RERGL; -.
DR   DMDM; 74752686; -.
DR   PaxDb; Q9H628; -.
DR   PeptideAtlas; Q9H628; -.
DR   PRIDE; Q9H628; -.
DR   Antibodypedia; 23848; 19 antibodies from 12 providers.
DR   DNASU; 79785; -.
DR   Ensembl; ENST00000229002.6; ENSP00000229002.2; ENSG00000111404.7.
DR   GeneID; 79785; -.
DR   KEGG; hsa:79785; -.
DR   UCSC; uc001rdq.4; human.
DR   CTD; 79785; -.
DR   DisGeNET; 79785; -.
DR   GeneCards; RERGL; -.
DR   HGNC; HGNC:26213; RERGL.
DR   HPA; ENSG00000111404; Low tissue specificity.
DR   neXtProt; NX_Q9H628; -.
DR   OpenTargets; ENSG00000111404; -.
DR   PharmGKB; PA162401119; -.
DR   VEuPathDB; HostDB:ENSG00000111404; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   GeneTree; ENSGT00940000161146; -.
DR   InParanoid; Q9H628; -.
DR   OrthoDB; 1384728at2759; -.
DR   PhylomeDB; Q9H628; -.
DR   TreeFam; TF318030; -.
DR   PathwayCommons; Q9H628; -.
DR   SignaLink; Q9H628; -.
DR   BioGRID-ORCS; 79785; 4 hits in 1065 CRISPR screens.
DR   ChiTaRS; RERGL; human.
DR   GenomeRNAi; 79785; -.
DR   Pharos; Q9H628; Tdark.
DR   PRO; PR:Q9H628; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9H628; protein.
DR   Bgee; ENSG00000111404; Expressed in tibial artery and 144 other tissues.
DR   ExpressionAtlas; Q9H628; baseline and differential.
DR   Genevisible; Q9H628; HS.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..205
FT                   /note="Ras-related and estrogen-regulated growth inhibitor-
FT                   like protein"
FT                   /id="PRO_0000320563"
FT   REGION          1..205
FT                   /note="Small GTPase-like"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         58..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         123..126
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   VARIANT         163
FT                   /note="M -> V (in dbSNP:rs941048)"
FT                   /id="VAR_039208"
SQ   SEQUENCE   205 AA;  23855 MW;  E8FDF8DEA09EC44A CRC64;
     MSNFLHLKYN EKSVSVTKAL TVRFLTKRFI GEYASNFESI YKKHLCLERK QLNLEIYDPC
     SQTQKAKFSL TSELHWADGF VIVYDISDRS SFAFAKALIY RIREPQTSHC KRAVESAVFL
     VGNKRDLCHV REVGWEEGQK LALENRCQFC ELSAAEQSLE VEMMFIRIIK DILINFKLKE
     KRRPSGSKSM AKLINNVFGK RRKSV
 
 
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