RGF1B_HUMAN
ID RGF1B_HUMAN Reviewed; 473 AA.
AC Q0VAM2; Q0VAM1; Q4W5L7; Q4W5M3; Q96MY8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ras-GEF domain-containing family member 1B;
DE AltName: Full=GPI gamma-4;
GN Name=RASGEF1B; Synonyms=GPIG4;
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] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [4]
RP INDUCTION.
RX PubMed=12488504;
RA Ferreira L.R.P., Abrantes E.F., Rodrigues C.V., Caetano B., Cerqueira G.C.,
RA Salim A.C., Reis L.F.L., Gazzinelli R.T.;
RT "Identification and characterization of a novel mouse gene encoding a Ras-
RT associated guanine nucleotide exchange factor: expression in macrophages
RT and myocarditis elicited by Trypanosoma cruzi parasites.";
RL J. Leukoc. Biol. 72:1215-1227(2002).
RN [5]
RP FUNCTION.
RX PubMed=19645719; DOI=10.1111/j.1742-4658.2009.07166.x;
RA Yaman E., Gasper R., Koerner C., Wittinghofer A., Tazebay U.H.;
RT "RasGEF1A and RasGEF1B are guanine nucleotide exchange factors that
RT discriminate between Rap GTP-binding proteins and mediate Rap2-specific
RT nucleotide exchange.";
RL FEBS J. 276:4607-4616(2009).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCDC124.
RX PubMed=23894443; DOI=10.1371/journal.pone.0069289;
RA Telkoparan P., Erkek S., Yaman E., Alotaibi H., Bayik D., Tazebay U.H.;
RT "Coiled-coil domain containing protein 124 is a novel centrosome and
RT midbody protein that interacts with the ras-guanine nucleotide exchange
RT factor 1B and is involved in cytokinesis.";
RL PLoS ONE 8:E69289-E69289(2013).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) with specificity for
CC RAP2A, it doesn't seems to activate other Ras family proteins (in
CC vitro). {ECO:0000269|PubMed:19645719, ECO:0000269|PubMed:23894443}.
CC -!- SUBUNIT: Interacts with Ras family proteins (By similarity). Interacts
CC with CCDC124 during cytokinesis. {ECO:0000250,
CC ECO:0000269|PubMed:23894443}.
CC -!- INTERACTION:
CC Q0VAM2-3; A0A0A0MR97: BAZ2B; NbExp=3; IntAct=EBI-12013954, EBI-11985607;
CC Q0VAM2-3; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-12013954, EBI-350517;
CC Q0VAM2-3; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12013954, EBI-742388;
CC Q0VAM2-3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-12013954, EBI-10241197;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Late endosome
CC {ECO:0000250}. Midbody {ECO:0000269|PubMed:23894443}. Note=May shuttle
CC between early and late endosomes (By similarity). Localizes to midbody
CC at telophase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0VAM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VAM2-2; Sequence=VSP_027313, VSP_027314;
CC Name=3;
CC IsoId=Q0VAM2-3; Sequence=VSP_027314;
CC -!- INDUCTION: Up-regulated in macrophages stimulated with IFNG, GPI-mucins
CC or bacterial lipopolysaccharides (LPS). {ECO:0000269|PubMed:12488504}.
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DR EMBL; AK056257; BAB71130.1; -; mRNA.
DR EMBL; AC006287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093747; AAY40982.1; -; Genomic_DNA.
DR EMBL; AC093618; AAY41054.1; -; Genomic_DNA.
DR EMBL; BC121003; AAI21004.1; -; mRNA.
DR EMBL; BC121004; AAI21005.1; -; mRNA.
DR CCDS; CCDS34022.1; -. [Q0VAM2-1]
DR CCDS; CCDS75151.1; -. [Q0VAM2-2]
DR CCDS; CCDS75152.1; -. [Q0VAM2-3]
DR RefSeq; NP_001287664.1; NM_001300735.1. [Q0VAM2-3]
DR RefSeq; NP_001287665.1; NM_001300736.1. [Q0VAM2-2]
DR RefSeq; NP_689758.1; NM_152545.2. [Q0VAM2-1]
DR RefSeq; XP_016863302.1; XM_017007813.1. [Q0VAM2-1]
DR AlphaFoldDB; Q0VAM2; -.
DR SMR; Q0VAM2; -.
DR BioGRID; 127476; 10.
DR IntAct; Q0VAM2; 6.
DR STRING; 9606.ENSP00000264400; -.
DR iPTMnet; Q0VAM2; -.
DR PhosphoSitePlus; Q0VAM2; -.
DR BioMuta; RASGEF1B; -.
DR DMDM; 156633611; -.
DR MassIVE; Q0VAM2; -.
DR MaxQB; Q0VAM2; -.
DR PaxDb; Q0VAM2; -.
DR PeptideAtlas; Q0VAM2; -.
DR PRIDE; Q0VAM2; -.
DR Antibodypedia; 25022; 86 antibodies from 21 providers.
DR DNASU; 153020; -.
DR Ensembl; ENST00000264400.7; ENSP00000264400.2; ENSG00000138670.19. [Q0VAM2-1]
DR Ensembl; ENST00000335927.11; ENSP00000338437.7; ENSG00000138670.19. [Q0VAM2-2]
DR Ensembl; ENST00000509081.5; ENSP00000425393.1; ENSG00000138670.19. [Q0VAM2-3]
DR GeneID; 153020; -.
DR KEGG; hsa:153020; -.
DR MANE-Select; ENST00000264400.7; ENSP00000264400.2; NM_152545.3; NP_689758.1.
DR UCSC; uc003hmi.2; human. [Q0VAM2-1]
DR CTD; 153020; -.
DR DisGeNET; 153020; -.
DR GeneCards; RASGEF1B; -.
DR HGNC; HGNC:24881; RASGEF1B.
DR HPA; ENSG00000138670; Low tissue specificity.
DR MIM; 614532; gene.
DR neXtProt; NX_Q0VAM2; -.
DR OpenTargets; ENSG00000138670; -.
DR PharmGKB; PA134927621; -.
DR VEuPathDB; HostDB:ENSG00000138670; -.
DR eggNOG; KOG3417; Eukaryota.
DR eggNOG; KOG3541; Eukaryota.
DR GeneTree; ENSGT00940000155816; -.
DR InParanoid; Q0VAM2; -.
DR OMA; THEYYPD; -.
DR OrthoDB; 533115at2759; -.
DR PhylomeDB; Q0VAM2; -.
DR TreeFam; TF313379; -.
DR PathwayCommons; Q0VAM2; -.
DR SignaLink; Q0VAM2; -.
DR SIGNOR; Q0VAM2; -.
DR BioGRID-ORCS; 153020; 10 hits in 1066 CRISPR screens.
DR ChiTaRS; RASGEF1B; human.
DR GenomeRNAi; 153020; -.
DR Pharos; Q0VAM2; Tbio.
DR PRO; PR:Q0VAM2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q0VAM2; protein.
DR Bgee; ENSG00000138670; Expressed in ganglionic eminence and 98 other tissues.
DR ExpressionAtlas; Q0VAM2; baseline and differential.
DR Genevisible; Q0VAM2; HS.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Guanine-nucleotide releasing factor;
KW Reference proteome.
FT CHAIN 1..473
FT /note="Ras-GEF domain-containing family member 1B"
FT /id="PRO_0000297638"
FT DOMAIN 34..164
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 204..452
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT VAR_SEQ 60..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027313"
FT VAR_SEQ 147
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027314"
SQ SEQUENCE 473 AA; 55359 MW; 8078400AD7B2CE94 CRC64;
MPQTPPFSAM FDSSGYNRNL YQSAEDSCGG LYYHDNNLLS GSLEALIQHL VPNVDYYPDR
TYIFTFLLSS RLFMHPYELM AKVCHLCVEH QRLSDPDSDK NQMRKIAPKI LQLLTEWTET
FPYDFRDERM MRNLKDLAHR IASGEEQTYR KNVQQMMQCL IRKLAALSQY EEVLAKISST
STDRLTVLKT KPQSIQRDII TVCNDPYTLA QQLTHIELER LNYIGPEEFV QAFVQKDPLD
NDKSCYSERK KTRNLEAYVE WFNRLSYLVA TEICMPVKKK HRARMIEYFI DVARECFNIG
NFNSLMAIIS GMNMSPVSRL KKTWAKVKTA KFDILEHQMD PSSNFYNYRT ALRGAAQRSL
TAHSSREKIV IPFFSLLIKD IYFLNEGCAN RLPNGHVNFE KFWELAKQVS EFMTWKQVEC
PFERDRKILQ YLLTVPVFSE DALYLASYES EGPENHIEKD RWKSLRSSLL GRV
