Full text data of AGFG1
AGFG1
(HRB, RAB, RIP)
[Confidence: low (only semi-automatic identification from reviews)]
Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein; Nucleoporin-like protein RIP; Rev-interacting protein; Rev/Rex activation domain-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Arf-GAP domain and FG repeat-containing protein 1 (HIV-1 Rev-binding protein; Nucleoporin-like protein RIP; Rev-interacting protein; Rev/Rex activation domain-binding protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P52594
ID AGFG1_HUMAN Reviewed; 562 AA.
AC P52594; B3KUL1; E9PHX7; Q15277; Q4VAS0; Q4VAS1; Q4VAS3; Q53QT8;
read moreAC Q53R11;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Arf-GAP domain and FG repeat-containing protein 1;
DE AltName: Full=HIV-1 Rev-binding protein;
DE AltName: Full=Nucleoporin-like protein RIP;
DE AltName: Full=Rev-interacting protein;
DE AltName: Full=Rev/Rex activation domain-binding protein;
GN Name=AGFG1; Synonyms=HRB, RAB, RIP;
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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
RP INTERACTION WITH HIV-1 REV AND HTLV-1 REX, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=7634337; DOI=10.1016/0092-8674(95)90437-9;
RA Bogerd H.P., Fridell R.A., Madore S., Cullen B.R.;
RT "Identification of a novel cellular cofactor for the Rev/Rex class of
RT retroviral regulatory proteins.";
RL Cell 82:485-494(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HIV-1
RP REV.
RC TISSUE=Placenta;
RX PubMed=7637788; DOI=10.1038/376530a0;
RA Fritz C.C., Zapp M.L., Green M.R.;
RT "A human nucleoporin-like protein that specifically interacts with HIV
RT Rev.";
RL Nature 376:530-533(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Testis;
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 [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH EPS15, AND FUNCTION.
RX PubMed=10613896; DOI=10.1083/jcb.147.7.1379;
RA Doria M., Salcini A.E., Colombo E., Parslow T.G., Pelicci P.G.,
RA Di Fiore P.P.;
RT "The eps15 homology (EH) domain-based interaction between eps15 and
RT hrb connects the molecular machinery of endocytosis to that of
RT nucleocytosolic transport.";
RL J. Cell Biol. 147:1379-1384(1999).
RN [7]
RP FUNCTION.
RX PubMed=14701878; DOI=10.1101/gad.1149704;
RA Sanchez-Velar N., Udofia E.B., Yu Z., Zapp M.L.;
RT "hRIP, a cellular cofactor for Rev function, promotes release of HIV
RT RNAs from the perinuclear region.";
RL Genes Dev. 18:23-34(2004).
RN [8]
RP FUNCTION.
RX PubMed=15749819; DOI=10.1073/pnas.0408889102;
RA Yu Z., Sanchez-Velar N., Catrina I.E., Kittler E.L., Udofia E.B.,
RA Zapp M.L.;
RT "The cellular HIV-1 Rev cofactor hRIP is required for viral
RT replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4027-4032(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [18]
RP STRUCTURE BY NMR OF 14-134.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ARFGAP domain of human RIP.";
RL Submitted (DEC-2006) to the PDB data bank.
CC -!- FUNCTION: Required for vesicle docking or fusion during acrosome
CC biogenesis (By similarity). May play a role in RNA trafficking or
CC localization. In case of infection by HIV-1, acts as a cofactor
CC for viral Rev and promotes movement of Rev-responsive element-
CC containing RNAs from the nuclear periphery to the cytoplasm. This
CC step is essential for HIV-1 replication.
CC -!- SUBUNIT: Interacts with EPS15R and EPS15. Interacts with FCHO1.
CC -!- INTERACTION:
CC P51809:VAMP7; NbExp=7; IntAct=EBI-996560, EBI-1052205;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasmic vesicle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P52594-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52594-2; Sequence=VSP_017600;
CC Name=3;
CC IsoId=P52594-3; Sequence=VSP_017601;
CC Name=4;
CC IsoId=P52594-4; Sequence=VSP_046185, VSP_046186, VSP_017601;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: Contains FG repeats. The FG repeat region is required for
CC acting as a cofactor of HIV-1 Rev.
CC -!- PTM: O-glycosylated (By similarity).
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
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DR EMBL; L42025; AAC37580.1; -; Genomic_DNA.
DR EMBL; X89478; CAA61667.1; -; mRNA.
DR EMBL; AK097451; BAG53473.1; -; mRNA.
DR EMBL; AC105286; AAX93270.1; -; Genomic_DNA.
DR EMBL; AC097662; AAY24254.1; -; Genomic_DNA.
DR EMBL; BC030592; AAH30592.1; -; mRNA.
DR EMBL; BC096272; AAH96272.1; -; mRNA.
DR EMBL; BC096273; AAH96273.1; -; mRNA.
DR EMBL; BC096274; AAH96274.1; -; mRNA.
DR EMBL; BC096275; AAH96275.1; -; mRNA.
DR PIR; A57088; A57088.
DR RefSeq; NP_001128659.1; NM_001135187.1.
DR RefSeq; NP_001128660.1; NM_001135188.1.
DR RefSeq; NP_001128661.1; NM_001135189.1.
DR RefSeq; NP_004495.2; NM_004504.4.
DR UniGene; Hs.352962; -.
DR PDB; 2D9L; NMR; -; A=14-134.
DR PDB; 2OLM; X-ray; 1.48 A; A=4-141.
DR PDB; 2VX8; X-ray; 2.20 A; A/B/C/D=136-176.
DR PDBsum; 2D9L; -.
DR PDBsum; 2OLM; -.
DR PDBsum; 2VX8; -.
DR ProteinModelPortal; P52594; -.
DR SMR; P52594; 14-134, 153-186.
DR DIP; DIP-35546N; -.
DR IntAct; P52594; 4.
DR MINT; MINT-1651458; -.
DR STRING; 9606.ENSP00000397094; -.
DR PhosphoSite; P52594; -.
DR DMDM; 26007019; -.
DR PaxDb; P52594; -.
DR PRIDE; P52594; -.
DR Ensembl; ENST00000310078; ENSP00000312059; ENSG00000173744.
DR Ensembl; ENST00000373671; ENSP00000362775; ENSG00000173744.
DR Ensembl; ENST00000409171; ENSP00000387218; ENSG00000173744.
DR GeneID; 3267; -.
DR KEGG; hsa:3267; -.
DR UCSC; uc002vpd.2; human.
DR CTD; 3267; -.
DR GeneCards; GC02P228336; -.
DR HGNC; HGNC:5175; AGFG1.
DR HPA; HPA008741; -.
DR MIM; 600862; gene.
DR neXtProt; NX_P52594; -.
DR PharmGKB; PA29449; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG006551; -.
DR KO; K15044; -.
DR OrthoDB; EOG7W9RW0; -.
DR PhylomeDB; P52594; -.
DR ChiTaRS; AGFG1; human.
DR EvolutionaryTrace; P52594; -.
DR GeneWiki; HRB_(gene); -.
DR GenomeRNAi; 3267; -.
DR NextBio; 12971; -.
DR PRO; PR:P52594; -.
DR ArrayExpress; P52594; -.
DR Bgee; P52594; -.
DR CleanEx; HS_AGFG1; -.
DR Genevestigator; P52594; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:ProtInc.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 3D-structure; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Developmental protein; Differentiation;
KW DNA-binding; Glycoprotein; Metal-binding; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1 562 Arf-GAP domain and FG repeat-containing
FT protein 1.
FT /FTId=PRO_0000204904.
FT DOMAIN 11 135 Arf-GAP.
FT ZN_FING 29 52 C4-type.
FT MOD_RES 177 177 Phosphothreonine.
FT MOD_RES 181 181 Phosphoserine.
FT CARBOHYD 367 367 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 15 Missing (in isoform 4).
FT /FTId=VSP_046185.
FT VAR_SEQ 232 271 Missing (in isoform 2).
FT /FTId=VSP_017600.
FT VAR_SEQ 272 272 G -> AFRMLSSSCSFGEFTSAFPLQATHS (in
FT isoform 4).
FT /FTId=VSP_046186.
FT VAR_SEQ 513 514 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_017601.
FT CONFLICT 25 25 H -> R (in Ref. 2; CAA61667).
FT CONFLICT 429 429 A -> R (in Ref. 2; CAA61667).
FT CONFLICT 542 542 F -> S (in Ref. 3; BAG53473).
FT HELIX 4 21
FT HELIX 24 27
FT TURN 30 32
FT STRAND 39 41
FT TURN 42 45
FT STRAND 46 48
FT HELIX 50 56
FT STRAND 59 61
FT STRAND 65 67
FT TURN 68 70
FT HELIX 75 83
FT HELIX 85 93
FT TURN 94 96
FT TURN 99 101
FT HELIX 110 121
FT HELIX 130 134
FT STRAND 157 159
FT HELIX 160 164
SQ SEQUENCE 562 AA; 58260 MW; 9A2242217F53B4D9 CRC64;
MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN
PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK
YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGDSAPT LHLNKGTPSQ
SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF
ANFDAFGQSS GSSNFGGFPT ASHSPFQPQT TGGSAASVNA NFAHFDNFPK SSSADFGTFN
TSQSHQTASA VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV
VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA SSNVFGTVPV VASAQTQPAS
SSVPAPFGAT PSTNPFVAAA GPSVASSTNP FQTNARGATA ATFGTASMSM PTGFGTPAPY
SLPTSFSGSF QQPAFPAQAA FPQQTAFSQQ PNGAGFAAFG QTKPVVTPFG QVAAAGVSSN
PFMTGAPTGQ FPTGSSSTNP FL
//
ID AGFG1_HUMAN Reviewed; 562 AA.
AC P52594; B3KUL1; E9PHX7; Q15277; Q4VAS0; Q4VAS1; Q4VAS3; Q53QT8;
read moreAC Q53R11;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Arf-GAP domain and FG repeat-containing protein 1;
DE AltName: Full=HIV-1 Rev-binding protein;
DE AltName: Full=Nucleoporin-like protein RIP;
DE AltName: Full=Rev-interacting protein;
DE AltName: Full=Rev/Rex activation domain-binding protein;
GN Name=AGFG1; Synonyms=HRB, RAB, RIP;
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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1),
RP INTERACTION WITH HIV-1 REV AND HTLV-1 REX, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=7634337; DOI=10.1016/0092-8674(95)90437-9;
RA Bogerd H.P., Fridell R.A., Madore S., Cullen B.R.;
RT "Identification of a novel cellular cofactor for the Rev/Rex class of
RT retroviral regulatory proteins.";
RL Cell 82:485-494(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HIV-1
RP REV.
RC TISSUE=Placenta;
RX PubMed=7637788; DOI=10.1038/376530a0;
RA Fritz C.C., Zapp M.L., Green M.R.;
RT "A human nucleoporin-like protein that specifically interacts with HIV
RT Rev.";
RL Nature 376:530-533(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Testis;
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 [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH EPS15, AND FUNCTION.
RX PubMed=10613896; DOI=10.1083/jcb.147.7.1379;
RA Doria M., Salcini A.E., Colombo E., Parslow T.G., Pelicci P.G.,
RA Di Fiore P.P.;
RT "The eps15 homology (EH) domain-based interaction between eps15 and
RT hrb connects the molecular machinery of endocytosis to that of
RT nucleocytosolic transport.";
RL J. Cell Biol. 147:1379-1384(1999).
RN [7]
RP FUNCTION.
RX PubMed=14701878; DOI=10.1101/gad.1149704;
RA Sanchez-Velar N., Udofia E.B., Yu Z., Zapp M.L.;
RT "hRIP, a cellular cofactor for Rev function, promotes release of HIV
RT RNAs from the perinuclear region.";
RL Genes Dev. 18:23-34(2004).
RN [8]
RP FUNCTION.
RX PubMed=15749819; DOI=10.1073/pnas.0408889102;
RA Yu Z., Sanchez-Velar N., Catrina I.E., Kittler E.L., Udofia E.B.,
RA Zapp M.L.;
RT "The cellular HIV-1 Rev cofactor hRIP is required for viral
RT replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4027-4032(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
RN [18]
RP STRUCTURE BY NMR OF 14-134.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ARFGAP domain of human RIP.";
RL Submitted (DEC-2006) to the PDB data bank.
CC -!- FUNCTION: Required for vesicle docking or fusion during acrosome
CC biogenesis (By similarity). May play a role in RNA trafficking or
CC localization. In case of infection by HIV-1, acts as a cofactor
CC for viral Rev and promotes movement of Rev-responsive element-
CC containing RNAs from the nuclear periphery to the cytoplasm. This
CC step is essential for HIV-1 replication.
CC -!- SUBUNIT: Interacts with EPS15R and EPS15. Interacts with FCHO1.
CC -!- INTERACTION:
CC P51809:VAMP7; NbExp=7; IntAct=EBI-996560, EBI-1052205;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasmic vesicle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P52594-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52594-2; Sequence=VSP_017600;
CC Name=3;
CC IsoId=P52594-3; Sequence=VSP_017601;
CC Name=4;
CC IsoId=P52594-4; Sequence=VSP_046185, VSP_046186, VSP_017601;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DOMAIN: Contains FG repeats. The FG repeat region is required for
CC acting as a cofactor of HIV-1 Rev.
CC -!- PTM: O-glycosylated (By similarity).
CC -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC -----------------------------------------------------------------------
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DR EMBL; L42025; AAC37580.1; -; Genomic_DNA.
DR EMBL; X89478; CAA61667.1; -; mRNA.
DR EMBL; AK097451; BAG53473.1; -; mRNA.
DR EMBL; AC105286; AAX93270.1; -; Genomic_DNA.
DR EMBL; AC097662; AAY24254.1; -; Genomic_DNA.
DR EMBL; BC030592; AAH30592.1; -; mRNA.
DR EMBL; BC096272; AAH96272.1; -; mRNA.
DR EMBL; BC096273; AAH96273.1; -; mRNA.
DR EMBL; BC096274; AAH96274.1; -; mRNA.
DR EMBL; BC096275; AAH96275.1; -; mRNA.
DR PIR; A57088; A57088.
DR RefSeq; NP_001128659.1; NM_001135187.1.
DR RefSeq; NP_001128660.1; NM_001135188.1.
DR RefSeq; NP_001128661.1; NM_001135189.1.
DR RefSeq; NP_004495.2; NM_004504.4.
DR UniGene; Hs.352962; -.
DR PDB; 2D9L; NMR; -; A=14-134.
DR PDB; 2OLM; X-ray; 1.48 A; A=4-141.
DR PDB; 2VX8; X-ray; 2.20 A; A/B/C/D=136-176.
DR PDBsum; 2D9L; -.
DR PDBsum; 2OLM; -.
DR PDBsum; 2VX8; -.
DR ProteinModelPortal; P52594; -.
DR SMR; P52594; 14-134, 153-186.
DR DIP; DIP-35546N; -.
DR IntAct; P52594; 4.
DR MINT; MINT-1651458; -.
DR STRING; 9606.ENSP00000397094; -.
DR PhosphoSite; P52594; -.
DR DMDM; 26007019; -.
DR PaxDb; P52594; -.
DR PRIDE; P52594; -.
DR Ensembl; ENST00000310078; ENSP00000312059; ENSG00000173744.
DR Ensembl; ENST00000373671; ENSP00000362775; ENSG00000173744.
DR Ensembl; ENST00000409171; ENSP00000387218; ENSG00000173744.
DR GeneID; 3267; -.
DR KEGG; hsa:3267; -.
DR UCSC; uc002vpd.2; human.
DR CTD; 3267; -.
DR GeneCards; GC02P228336; -.
DR HGNC; HGNC:5175; AGFG1.
DR HPA; HPA008741; -.
DR MIM; 600862; gene.
DR neXtProt; NX_P52594; -.
DR PharmGKB; PA29449; -.
DR eggNOG; COG5347; -.
DR HOVERGEN; HBG006551; -.
DR KO; K15044; -.
DR OrthoDB; EOG7W9RW0; -.
DR PhylomeDB; P52594; -.
DR ChiTaRS; AGFG1; human.
DR EvolutionaryTrace; P52594; -.
DR GeneWiki; HRB_(gene); -.
DR GenomeRNAi; 3267; -.
DR NextBio; 12971; -.
DR PRO; PR:P52594; -.
DR ArrayExpress; P52594; -.
DR Bgee; P52594; -.
DR CleanEx; HS_AGFG1; -.
DR Genevestigator; P52594; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006406; P:mRNA export from nucleus; TAS:ProtInc.
DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 3D-structure; Alternative splicing; Complete proteome;
KW Cytoplasmic vesicle; Developmental protein; Differentiation;
KW DNA-binding; Glycoprotein; Metal-binding; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1 562 Arf-GAP domain and FG repeat-containing
FT protein 1.
FT /FTId=PRO_0000204904.
FT DOMAIN 11 135 Arf-GAP.
FT ZN_FING 29 52 C4-type.
FT MOD_RES 177 177 Phosphothreonine.
FT MOD_RES 181 181 Phosphoserine.
FT CARBOHYD 367 367 O-linked (GlcNAc) (By similarity).
FT VAR_SEQ 1 15 Missing (in isoform 4).
FT /FTId=VSP_046185.
FT VAR_SEQ 232 271 Missing (in isoform 2).
FT /FTId=VSP_017600.
FT VAR_SEQ 272 272 G -> AFRMLSSSCSFGEFTSAFPLQATHS (in
FT isoform 4).
FT /FTId=VSP_046186.
FT VAR_SEQ 513 514 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_017601.
FT CONFLICT 25 25 H -> R (in Ref. 2; CAA61667).
FT CONFLICT 429 429 A -> R (in Ref. 2; CAA61667).
FT CONFLICT 542 542 F -> S (in Ref. 3; BAG53473).
FT HELIX 4 21
FT HELIX 24 27
FT TURN 30 32
FT STRAND 39 41
FT TURN 42 45
FT STRAND 46 48
FT HELIX 50 56
FT STRAND 59 61
FT STRAND 65 67
FT TURN 68 70
FT HELIX 75 83
FT HELIX 85 93
FT TURN 94 96
FT TURN 99 101
FT HELIX 110 121
FT HELIX 130 134
FT STRAND 157 159
FT HELIX 160 164
SQ SEQUENCE 562 AA; 58260 MW; 9A2242217F53B4D9 CRC64;
MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN
PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK
YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGDSAPT LHLNKGTPSQ
SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF
ANFDAFGQSS GSSNFGGFPT ASHSPFQPQT TGGSAASVNA NFAHFDNFPK SSSADFGTFN
TSQSHQTASA VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV
VSVPSQSSAS SDKYAALAEL DSVFSSAATS SNAYTSTSNA SSNVFGTVPV VASAQTQPAS
SSVPAPFGAT PSTNPFVAAA GPSVASSTNP FQTNARGATA ATFGTASMSM PTGFGTPAPY
SLPTSFSGSF QQPAFPAQAA FPQQTAFSQQ PNGAGFAAFG QTKPVVTPFG QVAAAGVSSN
PFMTGAPTGQ FPTGSSSTNP FL
//
MIM
600862
*RECORD*
*FIELD* NO
600862
*FIELD* TI
*600862 HIV-1 REV-BINDING PROTEIN; HRB
;;REV-INTERACTING PROTEIN; RIP;;
REV/REX ACTIVATION DOMAIN-BINDING PROTEIN; RAB
read more*FIELD* TX
CLONING
Using the yeast 2-hybrid screening system to identify proteins that
interact with the Rev protein of HIV-1 and which thereby assist in HIV
replication, Fritz et al. (1995) identified a novel cDNA, which they
designated Rev-interacting protein (RIP). A partial clone from the
initial screen was used to obtain a full-length 2.4-kb RIP cDNA. The
authors found that the predicted 562-amino acid protein is related to
the nucleoporins (e.g., 114350), a class of proteins that mediate
nucleocytoplasmic transport. The protein was detected in the nuclear
extract of HeLa cells and by immunofluorescence on the nuclear surface.
Expression studies showed that recombinant RIP did indeed lead to
increased Rev activity.
Bogerd et al. (1995) also cloned the HRB gene using a yeast 2-hybrid
screen to identify proteins that interact with the activation domains of
Rev and the equivalent regulatory protein from human T-cell leukemia
virus type 1 (HTLV1), Rex. They designated the protein RAB for 'Rev/Rex
activation domain-binding protein.' By SDS-PAGE, human, mouse, quail,
and frog RAB migrated as an approximately 60-kD protein. The RAB gene
was expressed as a major 2.8-kb and a minor 4.6-kb mRNA in all tissues
examined.
GENE FUNCTION
Salcini et al. (1997) reported that both the RAB and RABR (604018)
proteins bind to the EH protein-protein interaction domain found in
EPS15 (600051) and other proteins. Coimmunoprecipitation studies
demonstrated that RAB and EPS15 are associated in vivo.
Bogerd et al. (1995) showed that RAB binds to the Rev activation domain
in vitro and in vivo and also to functionally equivalent domains in Rex
and in other Rev proteins from diverse viruses.
By ablating RIP activity with a dominant-negative mutant or RNA
interference, Sanchez-Velar et al. (2004) analyzed the role of RIP in
Rev-directed RNA movement by RNA in situ hybridization. In the absence
of functional RIP, Rev-directed RNAs mislocalized and aberrantly
accumulated at the nuclear periphery, where RIP is localized. In
contrast, in the absence of Rev or a Rev cofactor, Rev-directed RNAs
remained nuclear. The RNA mislocalization pattern was specific to viral
RNA. The intracellular distribution patterns of cellular mRNA, nuclear
proteins, and cellular proteins containing a nuclear export signal were
unaffected. Sanchez-Velar et al. (2004) concluded that RIP is a cellular
Rev cofactor essential for the nuclear export of viral RNAs.
MAPPING
Jones et al. (1997) used fluorescence in situ hybridization to map the
RIP gene to human chromosome 2q36.
ANIMAL MODEL
Kang-Decker et al. (2001) generated mice deficient in HRB by targeted
disruption. Male mice with a null mutation in Hrb were infertile and
displayed round-headed spermatozoa that lacked an acrosome. In wildtype
spermatids, Hrb was associated with the cytosolic surface of
proacrosomic transport vesicles that fuse to create a single large
acrosomic vesicle at step 3 of spermiogenesis. Although proacrosomic
vesicles form in spermatids that lack Hrb, the vesicles are unable to
fuse, blocking acrosome development at step 2. Kang-Decker et al. (2001)
concluded that HRB is required for docking and/or fusion of proacrosomic
vesicles during acrosome biogenesis.
*FIELD* RF
1. Bogerd, H. P.; Fridell, R. A.; Madore, S.; Cullen, B. R.: Identification
of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory
proteins. Cell 82: 485-494, 1995.
2. Fritz, C. C.; Zapp, M. L.; Green, M. R.: A human nucleoporin-like
protein that specifically interacts with HIV Rev. Nature 376: 530-533,
1995.
3. Jones, T.; Sheer, D.; Bevec, D.; Kappel, B.; Hauber, J.; Steinkasserer,
A.: The human HIV-1 Rev binding-protein hRIP/Rab (HRB) maps to chromosome
2q36. Genomics 40: 198-199, 1997.
4. Kang-Decker, N.; Mantchev, G. T.; Juneja, S. C.; McNiven, M. A.;
van Deursen, J. M. A.: Lack of acrosome formation in Hrb-deficient
mice. Science 294: 1531-1533, 2001.
5. 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.
6. Sanchez-Velar, N.; Udofia, E. B.; Yu, Z.; Zapp, M. L.: hRIP, a
cellular cofactor for Rev function, promotes release of HIV RNAs from
the perinuclear region. Genes Dev. 18: 23-34, 2004.
*FIELD* CN
Patricia A. Hartz - updated: 2/25/2004
Ada Hamosh - updated: 11/26/2001
Rebekah S. Rasooly - updated: 7/15/1999
Rebekah S. Rasooly - updated: 4/24/1998
Rebekah S. Rasooly - updated: 3/4/1998
*FIELD* CD
Alan F. Scott: 10/15/1995
*FIELD* ED
carol: 02/25/2004
carol: 2/25/2004
alopez: 11/26/2001
terry: 11/26/2001
mgross: 7/15/1999
alopez: 6/11/1999
carol: 5/24/1999
dkim: 12/2/1998
psherman: 4/28/1998
psherman: 4/24/1998
alopez: 3/4/1998
mark: 2/19/1997
mark: 4/7/1996
mark: 10/15/1995
*RECORD*
*FIELD* NO
600862
*FIELD* TI
*600862 HIV-1 REV-BINDING PROTEIN; HRB
;;REV-INTERACTING PROTEIN; RIP;;
REV/REX ACTIVATION DOMAIN-BINDING PROTEIN; RAB
read more*FIELD* TX
CLONING
Using the yeast 2-hybrid screening system to identify proteins that
interact with the Rev protein of HIV-1 and which thereby assist in HIV
replication, Fritz et al. (1995) identified a novel cDNA, which they
designated Rev-interacting protein (RIP). A partial clone from the
initial screen was used to obtain a full-length 2.4-kb RIP cDNA. The
authors found that the predicted 562-amino acid protein is related to
the nucleoporins (e.g., 114350), a class of proteins that mediate
nucleocytoplasmic transport. The protein was detected in the nuclear
extract of HeLa cells and by immunofluorescence on the nuclear surface.
Expression studies showed that recombinant RIP did indeed lead to
increased Rev activity.
Bogerd et al. (1995) also cloned the HRB gene using a yeast 2-hybrid
screen to identify proteins that interact with the activation domains of
Rev and the equivalent regulatory protein from human T-cell leukemia
virus type 1 (HTLV1), Rex. They designated the protein RAB for 'Rev/Rex
activation domain-binding protein.' By SDS-PAGE, human, mouse, quail,
and frog RAB migrated as an approximately 60-kD protein. The RAB gene
was expressed as a major 2.8-kb and a minor 4.6-kb mRNA in all tissues
examined.
GENE FUNCTION
Salcini et al. (1997) reported that both the RAB and RABR (604018)
proteins bind to the EH protein-protein interaction domain found in
EPS15 (600051) and other proteins. Coimmunoprecipitation studies
demonstrated that RAB and EPS15 are associated in vivo.
Bogerd et al. (1995) showed that RAB binds to the Rev activation domain
in vitro and in vivo and also to functionally equivalent domains in Rex
and in other Rev proteins from diverse viruses.
By ablating RIP activity with a dominant-negative mutant or RNA
interference, Sanchez-Velar et al. (2004) analyzed the role of RIP in
Rev-directed RNA movement by RNA in situ hybridization. In the absence
of functional RIP, Rev-directed RNAs mislocalized and aberrantly
accumulated at the nuclear periphery, where RIP is localized. In
contrast, in the absence of Rev or a Rev cofactor, Rev-directed RNAs
remained nuclear. The RNA mislocalization pattern was specific to viral
RNA. The intracellular distribution patterns of cellular mRNA, nuclear
proteins, and cellular proteins containing a nuclear export signal were
unaffected. Sanchez-Velar et al. (2004) concluded that RIP is a cellular
Rev cofactor essential for the nuclear export of viral RNAs.
MAPPING
Jones et al. (1997) used fluorescence in situ hybridization to map the
RIP gene to human chromosome 2q36.
ANIMAL MODEL
Kang-Decker et al. (2001) generated mice deficient in HRB by targeted
disruption. Male mice with a null mutation in Hrb were infertile and
displayed round-headed spermatozoa that lacked an acrosome. In wildtype
spermatids, Hrb was associated with the cytosolic surface of
proacrosomic transport vesicles that fuse to create a single large
acrosomic vesicle at step 3 of spermiogenesis. Although proacrosomic
vesicles form in spermatids that lack Hrb, the vesicles are unable to
fuse, blocking acrosome development at step 2. Kang-Decker et al. (2001)
concluded that HRB is required for docking and/or fusion of proacrosomic
vesicles during acrosome biogenesis.
*FIELD* RF
1. Bogerd, H. P.; Fridell, R. A.; Madore, S.; Cullen, B. R.: Identification
of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory
proteins. Cell 82: 485-494, 1995.
2. Fritz, C. C.; Zapp, M. L.; Green, M. R.: A human nucleoporin-like
protein that specifically interacts with HIV Rev. Nature 376: 530-533,
1995.
3. Jones, T.; Sheer, D.; Bevec, D.; Kappel, B.; Hauber, J.; Steinkasserer,
A.: The human HIV-1 Rev binding-protein hRIP/Rab (HRB) maps to chromosome
2q36. Genomics 40: 198-199, 1997.
4. Kang-Decker, N.; Mantchev, G. T.; Juneja, S. C.; McNiven, M. A.;
van Deursen, J. M. A.: Lack of acrosome formation in Hrb-deficient
mice. Science 294: 1531-1533, 2001.
5. 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.
6. Sanchez-Velar, N.; Udofia, E. B.; Yu, Z.; Zapp, M. L.: hRIP, a
cellular cofactor for Rev function, promotes release of HIV RNAs from
the perinuclear region. Genes Dev. 18: 23-34, 2004.
*FIELD* CN
Patricia A. Hartz - updated: 2/25/2004
Ada Hamosh - updated: 11/26/2001
Rebekah S. Rasooly - updated: 7/15/1999
Rebekah S. Rasooly - updated: 4/24/1998
Rebekah S. Rasooly - updated: 3/4/1998
*FIELD* CD
Alan F. Scott: 10/15/1995
*FIELD* ED
carol: 02/25/2004
carol: 2/25/2004
alopez: 11/26/2001
terry: 11/26/2001
mgross: 7/15/1999
alopez: 6/11/1999
carol: 5/24/1999
dkim: 12/2/1998
psherman: 4/28/1998
psherman: 4/24/1998
alopez: 3/4/1998
mark: 2/19/1997
mark: 4/7/1996
mark: 10/15/1995