Full text data of AGFG2
AGFG2
(HRBL, RABR)
[Confidence: low (only semi-automatic identification from reviews)]
Arf-GAP domain and FG repeat-containing protein 2 (HIV-1 Rev-binding protein-like protein; Rev/Rex activation domain-binding protein related; RAB-R)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Arf-GAP domain and FG repeat-containing protein 2 (HIV-1 Rev-binding protein-like protein; Rev/Rex activation domain-binding protein related; RAB-R)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95081
ID AGFG2_HUMAN Reviewed; 481 AA.
AC O95081; O75429; Q96AB9; Q96GL4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-JUN-2004, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Arf-GAP domain and FG repeat-containing protein 2;
DE AltName: Full=HIV-1 Rev-binding protein-like protein;
DE AltName: Full=Rev/Rex activation domain-binding protein related;
DE Short=RAB-R;
GN Name=AGFG2; Synonyms=HRBL, RABR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9303539;
RA Salcini A.E., Confalonieri S., Doria M., Santolini E., Tassi E.,
RA Minenkova O., Cesareni G., Pelicci P.G., Di Fiore P.P.;
RT "Binding specificity and in vivo targets of the EH domain, a novel
RT protein-protein interaction module.";
RL Genes Dev. 11:2239-2249(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-481.
RX PubMed=9799793;
RA Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA Tsui L.-C., Rosenthal A.;
RT "Large-scale sequencing of two regions in human chromosome 7q22:
RT analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci
RT reveals 17 genes.";
RL Genome Res. 8:1060-1073(1998).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBUNIT: Interacts with EPS15R (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95081-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95081-2; Sequence=VSP_010667, VSP_010668;
CC -!- DOMAIN: Contains FG repeats and 4 N-P-F repeats.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78803.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF015042; AAD01550.1; -; mRNA.
DR EMBL; BC009393; AAH09393.1; -; mRNA.
DR EMBL; BC017329; AAH17329.1; -; mRNA.
DR EMBL; AF053356; AAC78803.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_006067.3; NM_006076.4.
DR UniGene; Hs.521083; -.
DR ProteinModelPortal; O95081; -.
DR SMR; O95081; 14-155.
DR IntAct; O95081; 1.
DR MINT; MINT-6630281; -.
DR STRING; 9606.ENSP00000300176; -.
DR PhosphoSite; O95081; -.
DR PaxDb; O95081; -.
DR PRIDE; O95081; -.
DR Ensembl; ENST00000262935; ENSP00000262935; ENSG00000106351.
DR Ensembl; ENST00000300176; ENSP00000300176; ENSG00000106351.
DR Ensembl; ENST00000430857; ENSP00000394453; ENSG00000106351.
DR GeneID; 3268; -.
DR KEGG; hsa:3268; -.
DR UCSC; uc003uvf.3; human.
DR CTD; 3268; -.
DR GeneCards; GC07P100136; -.
DR HGNC; HGNC:5177; AGFG2.
DR HPA; HPA019689; -.
DR MIM; 604019; gene.
DR neXtProt; NX_O95081; -.
DR PharmGKB; PA29451; -.
DR eggNOG; NOG293564; -.
DR HOGENOM; HOG000253009; -.
DR HOVERGEN; HBG006551; -.
DR InParanoid; O95081; -.
DR OMA; SSQVTPF; -.
DR OrthoDB; EOG7W9RW0; -.
DR GeneWiki; HRBL; -.
DR GenomeRNAi; 3268; -.
DR NextBio; 12977; -.
DR PRO; PR:O95081; -.
DR ArrayExpress; O95081; -.
DR Bgee; O95081; -.
DR CleanEx; HS_AGFG2; -.
DR Genevestigator; O95081; -.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR InterPro; IPR001164; ArfGAP.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Metal-binding;
KW Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1 481 Arf-GAP domain and FG repeat-containing
FT protein 2.
FT /FTId=PRO_0000204828.
FT DOMAIN 27 153 Arf-GAP.
FT ZN_FING 47 70 C4-type.
FT COMPBIAS 367 427 Pro-rich.
FT MOD_RES 173 173 N6-acetyllysine.
FT VAR_SEQ 145 155 YVPPDQVKGPT -> PDTFPRRLCQL (in isoform
FT 2).
FT /FTId=VSP_010667.
FT VAR_SEQ 157 481 Missing (in isoform 2).
FT /FTId=VSP_010668.
FT VARIANT 365 365 T -> N (in dbSNP:rs34731997).
FT /FTId=VAR_050566.
FT CONFLICT 96 96 V -> L (in Ref. 1; AAD01550).
FT CONFLICT 124 124 D -> N (in Ref. 1; AAD01550).
FT CONFLICT 206 206 Q -> H (in Ref. 3; AAC78803).
FT CONFLICT 349 349 M -> T (in Ref. 2; AAH17329).
SQ SEQUENCE 481 AA; 48963 MW; A89202A0F0924FE2 CRC64;
MVMAAKKGPG PGGGVSGGKA EAEAASEVWC RRVRELGGCS QAGNRHCFEC AQRGVTYVDI
TVGSFVCTTC SGLLRGLNPP HRVKSISMTT FTEPEVVFLQ SRGNEVCRKI WLGLFDARTS
LVPDSRDPQK VKEFLQEKYE KKRWYVPPDQ VKGPTYTKGS ASTPVQGSIP EGKPLRTLLG
DPAPSLSVAA STSSQPVSQS HARTSQARST QPPPHSSVKK ASTDLLADIG GDPFAAPQMA
PAFAAFPAFG GQTPSQGGFA NFDAFSSGPS SSVFGSLPPA GQASFQAQPT PAGSSQGTPF
GATPLAPASQ PNSLADVGSF LGPGVPAAGV PSSLFGMAGQ VPPLQSVTMG GGGGSSTGLA
FGAFTNPFTA PAAQSPLPST NPFQPNGLAP GPGFGMSSAG PGFPQAVPPT GAFASSFPAP
LFPPQTPLVQ QQNGSSFGDL GSAKLGQRPL SQPAGISTNP FMTGPSSSPF ASKPPTTNPF
L
//
ID AGFG2_HUMAN Reviewed; 481 AA.
AC O95081; O75429; Q96AB9; Q96GL4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-JUN-2004, sequence version 2.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Arf-GAP domain and FG repeat-containing protein 2;
DE AltName: Full=HIV-1 Rev-binding protein-like protein;
DE AltName: Full=Rev/Rex activation domain-binding protein related;
DE Short=RAB-R;
GN Name=AGFG2; Synonyms=HRBL, RABR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9303539;
RA Salcini A.E., Confalonieri S., Doria M., Santolini E., Tassi E.,
RA Minenkova O., Cesareni G., Pelicci P.G., Di Fiore P.P.;
RT "Binding specificity and in vivo targets of the EH domain, a novel
RT protein-protein interaction module.";
RL Genes Dev. 11:2239-2249(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-481.
RX PubMed=9799793;
RA Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA Tsui L.-C., Rosenthal A.;
RT "Large-scale sequencing of two regions in human chromosome 7q22:
RT analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci
RT reveals 17 genes.";
RL Genome Res. 8:1060-1073(1998).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBUNIT: Interacts with EPS15R (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95081-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95081-2; Sequence=VSP_010667, VSP_010668;
CC -!- DOMAIN: Contains FG repeats and 4 N-P-F repeats.
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78803.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF015042; AAD01550.1; -; mRNA.
DR EMBL; BC009393; AAH09393.1; -; mRNA.
DR EMBL; BC017329; AAH17329.1; -; mRNA.
DR EMBL; AF053356; AAC78803.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_006067.3; NM_006076.4.
DR UniGene; Hs.521083; -.
DR ProteinModelPortal; O95081; -.
DR SMR; O95081; 14-155.
DR IntAct; O95081; 1.
DR MINT; MINT-6630281; -.
DR STRING; 9606.ENSP00000300176; -.
DR PhosphoSite; O95081; -.
DR PaxDb; O95081; -.
DR PRIDE; O95081; -.
DR Ensembl; ENST00000262935; ENSP00000262935; ENSG00000106351.
DR Ensembl; ENST00000300176; ENSP00000300176; ENSG00000106351.
DR Ensembl; ENST00000430857; ENSP00000394453; ENSG00000106351.
DR GeneID; 3268; -.
DR KEGG; hsa:3268; -.
DR UCSC; uc003uvf.3; human.
DR CTD; 3268; -.
DR GeneCards; GC07P100136; -.
DR HGNC; HGNC:5177; AGFG2.
DR HPA; HPA019689; -.
DR MIM; 604019; gene.
DR neXtProt; NX_O95081; -.
DR PharmGKB; PA29451; -.
DR eggNOG; NOG293564; -.
DR HOGENOM; HOG000253009; -.
DR HOVERGEN; HBG006551; -.
DR InParanoid; O95081; -.
DR OMA; SSQVTPF; -.
DR OrthoDB; EOG7W9RW0; -.
DR GeneWiki; HRBL; -.
DR GenomeRNAi; 3268; -.
DR NextBio; 12977; -.
DR PRO; PR:O95081; -.
DR ArrayExpress; O95081; -.
DR Bgee; O95081; -.
DR CleanEx; HS_AGFG2; -.
DR Genevestigator; O95081; -.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR InterPro; IPR001164; ArfGAP.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Metal-binding;
KW Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1 481 Arf-GAP domain and FG repeat-containing
FT protein 2.
FT /FTId=PRO_0000204828.
FT DOMAIN 27 153 Arf-GAP.
FT ZN_FING 47 70 C4-type.
FT COMPBIAS 367 427 Pro-rich.
FT MOD_RES 173 173 N6-acetyllysine.
FT VAR_SEQ 145 155 YVPPDQVKGPT -> PDTFPRRLCQL (in isoform
FT 2).
FT /FTId=VSP_010667.
FT VAR_SEQ 157 481 Missing (in isoform 2).
FT /FTId=VSP_010668.
FT VARIANT 365 365 T -> N (in dbSNP:rs34731997).
FT /FTId=VAR_050566.
FT CONFLICT 96 96 V -> L (in Ref. 1; AAD01550).
FT CONFLICT 124 124 D -> N (in Ref. 1; AAD01550).
FT CONFLICT 206 206 Q -> H (in Ref. 3; AAC78803).
FT CONFLICT 349 349 M -> T (in Ref. 2; AAH17329).
SQ SEQUENCE 481 AA; 48963 MW; A89202A0F0924FE2 CRC64;
MVMAAKKGPG PGGGVSGGKA EAEAASEVWC RRVRELGGCS QAGNRHCFEC AQRGVTYVDI
TVGSFVCTTC SGLLRGLNPP HRVKSISMTT FTEPEVVFLQ SRGNEVCRKI WLGLFDARTS
LVPDSRDPQK VKEFLQEKYE KKRWYVPPDQ VKGPTYTKGS ASTPVQGSIP EGKPLRTLLG
DPAPSLSVAA STSSQPVSQS HARTSQARST QPPPHSSVKK ASTDLLADIG GDPFAAPQMA
PAFAAFPAFG GQTPSQGGFA NFDAFSSGPS SSVFGSLPPA GQASFQAQPT PAGSSQGTPF
GATPLAPASQ PNSLADVGSF LGPGVPAAGV PSSLFGMAGQ VPPLQSVTMG GGGGSSTGLA
FGAFTNPFTA PAAQSPLPST NPFQPNGLAP GPGFGMSSAG PGFPQAVPPT GAFASSFPAP
LFPPQTPLVQ QQNGSSFGDL GSAKLGQRPL SQPAGISTNP FMTGPSSSPF ASKPPTTNPF
L
//
MIM
604019
*RECORD*
*FIELD* NO
604019
*FIELD* TI
*604019 HIV-1 REV-BINDING PROTEIN-LIKE; HRBL
;;REV/REX ACTIVATION DOMAIN-BINDING PROTEIN-RELATED; RABR
read more*FIELD* TX
Salcini et al. (1997) determined that the EH protein-protein interaction
domains from EPS15 (600051) and mouse Eps15R bind in vitro to peptides
containing an asn-pro-phe (NPF) motif. By screening a human fibroblast
expression library with a chimeric glutathione S-transferase-EH-domain
protein, the authors identified cDNAs encoding NUMB (603728), NUMBR
(604018), RAB (600862), RABR, and 3 other proteins that interact with EH
domains. The predicted 481-amino acid RABR protein shares 46% identity
with RAB. Both RAB and RABR contain a zinc finger region near the N
terminus, several phe-gly (FG) motifs characteristic of nucleoporin-like
proteins, and 4 NPF motifs located in the C-terminal half.
*FIELD* RF
1. Salcini, A. E.; Confalonieri, S.; Doria, M.; Santolini, E.; Tassi,
E.; Minenkova, O.; Cesareni, G.; Pelicci, P. G.; Di Fiore, P. P.:
Binding specificity and in vivo targets of the EH domain, a novel
protein-protein interaction module. Genes Dev. 11: 2239-2249, 1997.
*FIELD* CD
Rebekah S. Rasooly: 7/14/1999
*FIELD* ED
carol: 09/18/2008
mgross: 7/15/1999
*RECORD*
*FIELD* NO
604019
*FIELD* TI
*604019 HIV-1 REV-BINDING PROTEIN-LIKE; HRBL
;;REV/REX ACTIVATION DOMAIN-BINDING PROTEIN-RELATED; RABR
read more*FIELD* TX
Salcini et al. (1997) determined that the EH protein-protein interaction
domains from EPS15 (600051) and mouse Eps15R bind in vitro to peptides
containing an asn-pro-phe (NPF) motif. By screening a human fibroblast
expression library with a chimeric glutathione S-transferase-EH-domain
protein, the authors identified cDNAs encoding NUMB (603728), NUMBR
(604018), RAB (600862), RABR, and 3 other proteins that interact with EH
domains. The predicted 481-amino acid RABR protein shares 46% identity
with RAB. Both RAB and RABR contain a zinc finger region near the N
terminus, several phe-gly (FG) motifs characteristic of nucleoporin-like
proteins, and 4 NPF motifs located in the C-terminal half.
*FIELD* RF
1. Salcini, A. E.; Confalonieri, S.; Doria, M.; Santolini, E.; Tassi,
E.; Minenkova, O.; Cesareni, G.; Pelicci, P. G.; Di Fiore, P. P.:
Binding specificity and in vivo targets of the EH domain, a novel
protein-protein interaction module. Genes Dev. 11: 2239-2249, 1997.
*FIELD* CD
Rebekah S. Rasooly: 7/14/1999
*FIELD* ED
carol: 09/18/2008
mgross: 7/15/1999