Full text data of CYTH1
CYTH1
(D17S811E, PSCD1)
[Confidence: low (only semi-automatic identification from reviews)]
Cytohesin-1 (PH, SEC7 and coiled-coil domain-containing protein 1; SEC7 homolog B2-1)
Cytohesin-1 (PH, SEC7 and coiled-coil domain-containing protein 1; SEC7 homolog B2-1)
UniProt
Q15438
ID CYH1_HUMAN Reviewed; 398 AA.
AC Q15438; A6NFW7; Q9P123; Q9P124;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Cytohesin-1;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 1;
DE AltName: Full=SEC7 homolog B2-1;
GN Name=CYTH1; Synonyms=D17S811E, PSCD1;
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].
RX PubMed=1511013; DOI=10.1016/0167-4781(92)90055-5;
RA Liu L., Pohajdak B.;
RT "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with
RT homology to yeast SEC7.";
RL Biochim. Biophys. Acta 1132:75-78(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-398, FUNCTION, AND ALTERNATIVE
RP SPLICING.
RX PubMed=10652308; DOI=10.1074/jbc.275.5.3221;
RA Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K.,
RA Kirby M., Moss J., Vaughan M.;
RT "Similarities in function and gene structure of cytohesin-4 and
RT cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation
RT factors.";
RL J. Biol. Chem. 275:3221-3230(2000).
RN [5]
RP INTERACTION WITH TRIM23.
RX PubMed=10748148; DOI=10.1074/jbc.M909642199;
RA Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W.,
RA Moss J., Vaughan M.;
RT "Specific functional interaction of human cytohesin-1 and ADP-
RT ribosylation factor domain protein (ARD1).";
RL J. Biol. Chem. 275:21331-21339(2000).
RN [6]
RP INTERACTION WITH CYTIP.
RX PubMed=11867758; DOI=10.1073/pnas.052712999;
RA Tang P., Cheng T.P., Agnello D., Wu C.-Y., Hissong B.D., Watford W.T.,
RA Ahn H.-J., Galon J., Moss J., Vaughan M., O'Shea J.J., Gadina M.;
RT "Cybr, a cytokine-inducible protein that binds cytohesin-1 and
RT regulates its activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2625-2629(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17398095; DOI=10.1016/j.cub.2007.03.007;
RA Hofmann I., Thompson A., Sanderson C.M., Munro S.;
RT "The Arl4 family of small G proteins can recruit the cytohesin Arf6
RT exchange factors to the plasma membrane.";
RL Curr. Biol. 17:711-716(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP STRUCTURE BY NMR OF 58-256, FUNCTION, AND MUTAGENESIS OF GLU-157;
RP TYR-187 AND MET-195.
RX PubMed=9653114; DOI=10.1073/pnas.95.14.7909;
RA Betz S.F., Schnuchel A., Wang H., Olejniczak E.T., Meadows R.P.,
RA Lipsky B.P., Harris E.A., Staunton D.E., Fesik S.W.;
RT "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its
RT interaction with the GTPase ADP ribosylation factor 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7909-7914(1998).
CC -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5.
CC Promotes the activation of ARF factors through replacement of GDP
CC with GTP.
CC -!- SUBUNIT: Interacts with TRIM23 and CYTIP.
CC -!- INTERACTION:
CC O60759:CYTIP; NbExp=2; IntAct=EBI-997830, EBI-997814;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cytoplasm, cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15438-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15438-2; Sequence=VSP_006034;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Binds via its PH domain to the inositol head group of
CC phosphatidylinositol 3,4,5-trisphosphate (By similarity).
CC -!- DOMAIN: Autoinhibited by its C-terminal basic region (By
CC similarity).
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 SEC7 domain.
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; M85169; AAA36602.1; -; mRNA.
DR EMBL; AC022966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038385; AAH38385.1; -; mRNA.
DR EMBL; BC050452; AAH50452.1; -; mRNA.
DR EMBL; AF125362; AAF37737.1; -; Genomic_DNA.
DR EMBL; AF125350; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125351; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125352; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125353; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125354; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125355; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125356; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125357; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125359; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125360; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125361; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125362; AAF37738.1; -; Genomic_DNA.
DR EMBL; AF125350; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125351; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125352; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125353; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125354; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125355; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125356; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125357; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125358; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125359; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125360; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125361; AAF37738.1; JOINED; Genomic_DNA.
DR PIR; S24168; S24168.
DR RefSeq; NP_004753.1; NM_004762.2.
DR RefSeq; NP_059430.2; NM_017456.2.
DR UniGene; Hs.191215; -.
DR PDB; 1BC9; NMR; -; A=58-248.
DR PDB; 4A4P; X-ray; 2.00 A; A/B=63-248.
DR PDBsum; 1BC9; -.
DR PDBsum; 4A4P; -.
DR ProteinModelPortal; Q15438; -.
DR SMR; Q15438; 58-391.
DR IntAct; Q15438; 2.
DR MINT; MINT-3031502; -.
DR STRING; 9606.ENSP00000354398; -.
DR PhosphoSite; Q15438; -.
DR DMDM; 2498175; -.
DR PaxDb; Q15438; -.
DR PRIDE; Q15438; -.
DR DNASU; 9267; -.
DR Ensembl; ENST00000361101; ENSP00000354398; ENSG00000108669.
DR Ensembl; ENST00000446868; ENSP00000389095; ENSG00000108669.
DR Ensembl; ENST00000591455; ENSP00000465665; ENSG00000108669.
DR GeneID; 9267; -.
DR KEGG; hsa:9267; -.
DR UCSC; uc010wtw.1; human.
DR CTD; 9267; -.
DR GeneCards; GC17M076670; -.
DR HGNC; HGNC:9501; CYTH1.
DR MIM; 182115; gene.
DR neXtProt; NX_Q15438; -.
DR PharmGKB; PA164718528; -.
DR eggNOG; COG5307; -.
DR HOGENOM; HOG000253023; -.
DR HOVERGEN; HBG002647; -.
DR OMA; SEFSMPE; -.
DR OrthoDB; EOG7RBZ9C; -.
DR ChiTaRS; CYTH1; human.
DR EvolutionaryTrace; Q15438; -.
DR GeneWiki; CYTH1; -.
DR GenomeRNAi; 9267; -.
DR NextBio; 34739; -.
DR PRO; PR:Q15438; -.
DR ArrayExpress; Q15438; -.
DR Bgee; Q15438; -.
DR CleanEx; HS_CYTH1; -.
DR Genevestigator; Q15438; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic to cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005923; C:tight junction; IEA:Ensembl.
DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR023394; Sec7_alpha_orthog.
DR InterPro; IPR000904; Sec7_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Coiled coil; Complete proteome; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Reference proteome.
FT CHAIN 1 398 Cytohesin-1.
FT /FTId=PRO_0000120194.
FT DOMAIN 73 202 SEC7.
FT DOMAIN 260 377 PH.
FT REGION 269 277 Phosphatidylinositol 3,4,5-trisphosphate
FT binding (By similarity).
FT REGION 388 396 C-terminal autoinhibitory region (By
FT similarity).
FT COILED 10 67 Potential.
FT BINDING 281 281 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT BINDING 292 292 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT BINDING 302 302 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT BINDING 351 351 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 273 273 Missing (in isoform 2).
FT /FTId=VSP_006034.
FT MUTAGEN 157 157 E->A,K: Reduces guanine exchange factor
FT activity by over 90%.
FT MUTAGEN 187 187 Y->A: Reduces guanine exchange factor
FT activity by over 90%.
FT MUTAGEN 195 195 M->A: Reduces guanine exchange factor
FT activity by over 90%.
FT CONFLICT 353 361 TVYRISAPT -> MFTGSQLRR (in Ref. 4;
FT AAF37737/AAF37738).
FT HELIX 64 75
FT HELIX 77 86
FT HELIX 94 103
FT HELIX 109 116
FT HELIX 121 133
FT TURN 137 139
FT HELIX 141 150
FT HELIX 158 175
FT HELIX 183 201
FT STRAND 203 205
FT HELIX 211 217
FT TURN 218 221
FT HELIX 229 241
FT STRAND 246 248
SQ SEQUENCE 398 AA; 46413 MW; 067FEE0FEA7A4C86 CRC64;
MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKDE IAEVANEIEN LGSTEERKNM
QRNKQVAMGR KKFNMDPKKG IQFLIENDLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD
EFNIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNNGVF
QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK
NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP
TPEEKEEWIK CIKAAISRDP FYEMLAARKK KVSSTKRH
//
ID CYH1_HUMAN Reviewed; 398 AA.
AC Q15438; A6NFW7; Q9P123; Q9P124;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Cytohesin-1;
DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 1;
DE AltName: Full=SEC7 homolog B2-1;
GN Name=CYTH1; Synonyms=D17S811E, PSCD1;
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].
RX PubMed=1511013; DOI=10.1016/0167-4781(92)90055-5;
RA Liu L., Pohajdak B.;
RT "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with
RT homology to yeast SEC7.";
RL Biochim. Biophys. Acta 1132:75-78(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-398, FUNCTION, AND ALTERNATIVE
RP SPLICING.
RX PubMed=10652308; DOI=10.1074/jbc.275.5.3221;
RA Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K.,
RA Kirby M., Moss J., Vaughan M.;
RT "Similarities in function and gene structure of cytohesin-4 and
RT cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation
RT factors.";
RL J. Biol. Chem. 275:3221-3230(2000).
RN [5]
RP INTERACTION WITH TRIM23.
RX PubMed=10748148; DOI=10.1074/jbc.M909642199;
RA Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W.,
RA Moss J., Vaughan M.;
RT "Specific functional interaction of human cytohesin-1 and ADP-
RT ribosylation factor domain protein (ARD1).";
RL J. Biol. Chem. 275:21331-21339(2000).
RN [6]
RP INTERACTION WITH CYTIP.
RX PubMed=11867758; DOI=10.1073/pnas.052712999;
RA Tang P., Cheng T.P., Agnello D., Wu C.-Y., Hissong B.D., Watford W.T.,
RA Ahn H.-J., Galon J., Moss J., Vaughan M., O'Shea J.J., Gadina M.;
RT "Cybr, a cytokine-inducible protein that binds cytohesin-1 and
RT regulates its activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2625-2629(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17398095; DOI=10.1016/j.cub.2007.03.007;
RA Hofmann I., Thompson A., Sanderson C.M., Munro S.;
RT "The Arl4 family of small G proteins can recruit the cytohesin Arf6
RT exchange factors to the plasma membrane.";
RL Curr. Biol. 17:711-716(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP STRUCTURE BY NMR OF 58-256, FUNCTION, AND MUTAGENESIS OF GLU-157;
RP TYR-187 AND MET-195.
RX PubMed=9653114; DOI=10.1073/pnas.95.14.7909;
RA Betz S.F., Schnuchel A., Wang H., Olejniczak E.T., Meadows R.P.,
RA Lipsky B.P., Harris E.A., Staunton D.E., Fesik S.W.;
RT "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its
RT interaction with the GTPase ADP ribosylation factor 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7909-7914(1998).
CC -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5.
CC Promotes the activation of ARF factors through replacement of GDP
CC with GTP.
CC -!- SUBUNIT: Interacts with TRIM23 and CYTIP.
CC -!- INTERACTION:
CC O60759:CYTIP; NbExp=2; IntAct=EBI-997830, EBI-997814;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cytoplasm, cytosol (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15438-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15438-2; Sequence=VSP_006034;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: Binds via its PH domain to the inositol head group of
CC phosphatidylinositol 3,4,5-trisphosphate (By similarity).
CC -!- DOMAIN: Autoinhibited by its C-terminal basic region (By
CC similarity).
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 SEC7 domain.
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; M85169; AAA36602.1; -; mRNA.
DR EMBL; AC022966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038385; AAH38385.1; -; mRNA.
DR EMBL; BC050452; AAH50452.1; -; mRNA.
DR EMBL; AF125362; AAF37737.1; -; Genomic_DNA.
DR EMBL; AF125350; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125351; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125352; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125353; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125354; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125355; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125356; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125357; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125359; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125360; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125361; AAF37737.1; JOINED; Genomic_DNA.
DR EMBL; AF125362; AAF37738.1; -; Genomic_DNA.
DR EMBL; AF125350; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125351; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125352; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125353; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125354; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125355; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125356; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125357; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125358; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125359; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125360; AAF37738.1; JOINED; Genomic_DNA.
DR EMBL; AF125361; AAF37738.1; JOINED; Genomic_DNA.
DR PIR; S24168; S24168.
DR RefSeq; NP_004753.1; NM_004762.2.
DR RefSeq; NP_059430.2; NM_017456.2.
DR UniGene; Hs.191215; -.
DR PDB; 1BC9; NMR; -; A=58-248.
DR PDB; 4A4P; X-ray; 2.00 A; A/B=63-248.
DR PDBsum; 1BC9; -.
DR PDBsum; 4A4P; -.
DR ProteinModelPortal; Q15438; -.
DR SMR; Q15438; 58-391.
DR IntAct; Q15438; 2.
DR MINT; MINT-3031502; -.
DR STRING; 9606.ENSP00000354398; -.
DR PhosphoSite; Q15438; -.
DR DMDM; 2498175; -.
DR PaxDb; Q15438; -.
DR PRIDE; Q15438; -.
DR DNASU; 9267; -.
DR Ensembl; ENST00000361101; ENSP00000354398; ENSG00000108669.
DR Ensembl; ENST00000446868; ENSP00000389095; ENSG00000108669.
DR Ensembl; ENST00000591455; ENSP00000465665; ENSG00000108669.
DR GeneID; 9267; -.
DR KEGG; hsa:9267; -.
DR UCSC; uc010wtw.1; human.
DR CTD; 9267; -.
DR GeneCards; GC17M076670; -.
DR HGNC; HGNC:9501; CYTH1.
DR MIM; 182115; gene.
DR neXtProt; NX_Q15438; -.
DR PharmGKB; PA164718528; -.
DR eggNOG; COG5307; -.
DR HOGENOM; HOG000253023; -.
DR HOVERGEN; HBG002647; -.
DR OMA; SEFSMPE; -.
DR OrthoDB; EOG7RBZ9C; -.
DR ChiTaRS; CYTH1; human.
DR EvolutionaryTrace; Q15438; -.
DR GeneWiki; CYTH1; -.
DR GenomeRNAi; 9267; -.
DR NextBio; 34739; -.
DR PRO; PR:Q15438; -.
DR ArrayExpress; Q15438; -.
DR Bgee; Q15438; -.
DR CleanEx; HS_CYTH1; -.
DR Genevestigator; Q15438; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic to cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005923; C:tight junction; IEA:Ensembl.
DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR023394; Sec7_alpha_orthog.
DR InterPro; IPR000904; Sec7_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Coiled coil; Complete proteome; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane;
KW Reference proteome.
FT CHAIN 1 398 Cytohesin-1.
FT /FTId=PRO_0000120194.
FT DOMAIN 73 202 SEC7.
FT DOMAIN 260 377 PH.
FT REGION 269 277 Phosphatidylinositol 3,4,5-trisphosphate
FT binding (By similarity).
FT REGION 388 396 C-terminal autoinhibitory region (By
FT similarity).
FT COILED 10 67 Potential.
FT BINDING 281 281 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT BINDING 292 292 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT BINDING 302 302 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT BINDING 351 351 Phosphatidylinositol 3,4,5-trisphosphate
FT (By similarity).
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 273 273 Missing (in isoform 2).
FT /FTId=VSP_006034.
FT MUTAGEN 157 157 E->A,K: Reduces guanine exchange factor
FT activity by over 90%.
FT MUTAGEN 187 187 Y->A: Reduces guanine exchange factor
FT activity by over 90%.
FT MUTAGEN 195 195 M->A: Reduces guanine exchange factor
FT activity by over 90%.
FT CONFLICT 353 361 TVYRISAPT -> MFTGSQLRR (in Ref. 4;
FT AAF37737/AAF37738).
FT HELIX 64 75
FT HELIX 77 86
FT HELIX 94 103
FT HELIX 109 116
FT HELIX 121 133
FT TURN 137 139
FT HELIX 141 150
FT HELIX 158 175
FT HELIX 183 201
FT STRAND 203 205
FT HELIX 211 217
FT TURN 218 221
FT HELIX 229 241
FT STRAND 246 248
SQ SEQUENCE 398 AA; 46413 MW; 067FEE0FEA7A4C86 CRC64;
MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKDE IAEVANEIEN LGSTEERKNM
QRNKQVAMGR KKFNMDPKKG IQFLIENDLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD
EFNIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNNGVF
QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK
NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP
TPEEKEEWIK CIKAAISRDP FYEMLAARKK KVSSTKRH
//
MIM
182115
*RECORD*
*FIELD* NO
182115
*FIELD* TI
*182115 CYTOHESIN 1; CYTH1
;;PLECKSTRIN HOMOLOGY, SEC7, AND COILED-COIL DOMAINS PROTEIN 1; PSCD1;;
read moreSEC7, YEAST, HOMOLOG OF; SEC7;;
D17S811E
*FIELD* TX
CLONING
One of the major mediators of the inborn or 'natural' immune system is
the natural killer (NK) cell. Dixon et al. (1993) prepared a subtractive
cDNA library from human NK cells and characterized 13 unique clones. A
clone named B2-1 was highly expressed in both NK and T cells, but was
very weakly expressed or absent in several other cell lines. The deduced
protein was highly homologous to the yeast protein SEC7, which is
located in the Golgi apparatus and is thought to be involved in
transporting proteins through the Golgi complex. B2-1 was the only known
human protein with significant homology to SEC7 and may be one of the
human equivalents of the yeast secretory proteins.
Using a yeast 2-hybrid screen of a T-cell leukemia cell line with the
intracellular portion of CD18 (ITGB2; 600065) as bait, Kolanus et al.
(1996) isolated a cDNA encoding cytohesin-1 (PSCD1) and a partial cDNA
encoding PSCD2L (602488), which they designated cts18.1. PSCD1 is 88%
identical to the PSCD2L fragment. The predicted 398-amino acid PSCD1
protein contains a central 200-residue SEC7 domain and a C-terminal
pleckstrin homology (PH) domain. Western blot analysis showed expression
of a 47-kD protein, particularly, but not exclusively, in lymphoid
cells.
GENE FUNCTION
Kolanus et al. (1996) found that overexpression of a full-length PSCD1
protein or of the SEC7 domain only induced CD18-dependent binding to
ICAM1 (147840), whereas the PSCD1 PH domain specifically inhibited
adhesion. Binding analysis indicated that the SEC7 domain, but not the
PH domain, interacts with the cytoplasmic domain of CD18 but not with
other cell surface receptors or protein-tyrosine kinases tested. Kolanus
et al. (1996) concluded that PSCD1 specifically regulates the adhesive
function of beta-2 integrins in lymphocytes.
The induction of a transformed cellular phenotype by viruses requires
the modulation of signaling pathways through viral proteins. Kliche et
al. (2001) showed that the phenotypic changes induced by the kaposin A
protein of human herpesvirus-8 are mediated through its direct
interaction with cytohesin-1, a guanine nucleotide exchange factor (GEF)
for ARF GTPases (e.g., ARF1; 103180) and regulator of integrin-mediated
cell adhesion. Focus formation, stress fiber dissolution, and activation
of the ERK1 (601795)/ERK2 (176948) mitogen-activated protein kinase
(MAPK) signal cascade were reverted by a cytohesin-1 glu157-to-lys
mutant, which is deficient in catalyzing guanine nucleotide exchange.
Furthermore, liposome-embedded kaposin A was found to specifically
stimulate cytohesin-1-dependent GTP binding of myristoylated ARF1 in
vitro.
Hafner et al. (2006) used an aptamer displacement screen to identify
SecinH3, a small Sec7 domain-specific molecular antagonist of
cytohesins. The cytohesins are a class of BFA-resistant small GEFs for
ADP-ribosylation factors (ARFs), which regulate cytoskeletal
organization, integrin activation, or integrin signaling. The
application of SecinH3 in human liver cells showed that insulin receptor
complex-associated cytohesins are required for insulin signaling.
SecinH3-treated mice showed increased expression of gluconeogenic genes,
reduced expression of glycolytic, fatty acid, and ketone body metabolism
genes in the liver, reduced liver glycogen stores, and a compensatory
increase in plasma insulin. Thus, Hafner et al. (2006) concluded that
cytohesin inhibition results in hepatic insulin resistance.
Vitale et al. (2000) found that cytohesin-1 interacted with ARF domain
protein-1 (ARD1, or TRIM23; 601747) in a yeast 2-hybrid screen of a
human liver cDNA library. ARD1-GDP interacted well with cytohesin-1 but
poorly with cytohesin-2 (PSCD2; 602488), and cytohesin-1 accelerated
binding of a nonhydrolyzable GTP analog to ARD1. Mutation analysis
showed that the effector region of the ARF domain of ARD1 interacted
with the Sec7 domain of cytohesin-1. Physical association between these
domains was highly dependent on experimental conditions, and a free
Mg(2+) concentration that favored nucleotide release from ARD1 and
accumulation of the nucleotide-free ARD1 form also favored interaction
between ARD1 and cytohesin-1. In transfected COS-7 cells, cytohesin-1
was distributed throughout the cell and was also present in the nucleus.
ARD1 associated with vesicular structures concentrated around the
nucleus and scattered throughout the cytoplasm, corresponding to Golgi
and lysosomes, respectively. A constitutively GDP-bound form of ARD1
showed a similar distribution, whereas a constitutively GTP-bound form
of ARD1 was concentrated close to the nucleus in a Golgi-like
distribution only. When ARD1 or its GDP- and GTP-bound forms were
coexpressed with cytohesin-1, only the GDP-bound form showed any change
in distribution or colocalization with cytohesin-1. In 90% of cells
coexpressing the proteins, the GDP-bound form of ARD1 was distributed
throughout the cell, except for the nucleus, and largely colocalized
with cytohesin-1. In less than 10% of cells coexpressing the proteins,
the GDP-bound form of ARD1 and cytohesin-1 colocalized in lysosomes.
GENE STRUCTURE
By genomic sequence analysis, Ogasawara et al. (2000) determined that
the PSCD1 gene contains at least 14 exons, including a 3-bp exon 10 also
present in PSCD2 and PSCD3 (605081) but not in PSCD4 (606514) that
results in the insertion of a single glycine into the variable loop
between the first and second beta sheets in the pleckstrin homology
domain.
MAPPING
Dixon et al. (1993) showed by PCR analysis of a human/rodent hybrid
panel that the B2-1 gene is located on chromosome 17. Fluorescence in
situ hybridization localized the gene to 17q25.
*FIELD* RF
1. Dixon, B.; Mansour, M.; Pohajdak, B.: Assignment of human B2-1
gene (D17S811E) to chromosome 17qter by PCR analysis of somatic cell
hybrids and fluorescence in situ hybridization. Cytogenet. Cell Genet. 63:
42-44, 1993.
2. Hafner, M.; Schmitz, A.; Grune, I.; Srivatsan, S. G.; Paul, B.;
Kolanus, W.; Quast, T.; Kremmer, E.; Bauer, I.; Famulok, M.: Inhibition
of cytohesins by SecinH3 leads to hepatic insulin resistance. Nature 444:
941-944, 2006.
3. Kliche, S.; Nagel, W.; Kremmer, E.; Atzler, C.; Ege, A.; Knorr,
T.; Koszinowski, U.; Kolanus, W.; Haas, J.: Signaling by human herpesvirus
8 kaposin A through direct membrane recruitment of cytohesin-1. Molec.
Cell 7: 833-843, 2001.
4. Kolanus, W.; Nagel, W.; Schiller, B.; Zeitlmann, L.; Godar, S.;
Stockinger, H.; Seed, B.: Alpha-L-beta-2 integrin/LFA-1 binding to
ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell 86:
233-242, 1996.
5. Ogasawara, M.; Kim, S.-C.; Adamik, R.; Togawa, A.; Ferrans, V.
J.; Takeda, K.; Kirby, M.; Moss, J.; Vaughan, M.: Similarities in
function and gene structure of cytohesin-4 and cytohesin-1, guanine
nucleotide-exchange proteins for ADP-ribosylation factors. J. Biol.
Chem. 275: 3221-3230, 2000.
6. Vitale, N.; Pacheco-Rodriguez, G.; Ferrans, V. J.; Riemenschneider,
W.; Moss, J.; Vaughan, M.: Specific functional interaction of human
cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). J.
Biol. Chem. 275: 21331-21339, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 3/15/2007
Ada Hamosh - updated: 2/1/2007
Paul J. Converse - updated: 2/20/2002
Paul J. Converse - updated: 11/27/2001
Stylianos E. Antonarakis - updated: 8/7/2001
*FIELD* CD
Victor A. McKusick: 5/27/1993
*FIELD* ED
alopez: 02/06/2013
terry: 1/29/2013
terry: 9/7/2010
mgross: 10/1/2009
mgross: 3/15/2007
alopez: 2/5/2007
terry: 2/1/2007
alopez: 12/31/2003
terry: 12/30/2003
mgross: 2/20/2002
alopez: 11/27/2001
mgross: 8/7/2001
mgross: 1/20/2000
carol: 5/4/1999
carol: 5/27/1993
*RECORD*
*FIELD* NO
182115
*FIELD* TI
*182115 CYTOHESIN 1; CYTH1
;;PLECKSTRIN HOMOLOGY, SEC7, AND COILED-COIL DOMAINS PROTEIN 1; PSCD1;;
read moreSEC7, YEAST, HOMOLOG OF; SEC7;;
D17S811E
*FIELD* TX
CLONING
One of the major mediators of the inborn or 'natural' immune system is
the natural killer (NK) cell. Dixon et al. (1993) prepared a subtractive
cDNA library from human NK cells and characterized 13 unique clones. A
clone named B2-1 was highly expressed in both NK and T cells, but was
very weakly expressed or absent in several other cell lines. The deduced
protein was highly homologous to the yeast protein SEC7, which is
located in the Golgi apparatus and is thought to be involved in
transporting proteins through the Golgi complex. B2-1 was the only known
human protein with significant homology to SEC7 and may be one of the
human equivalents of the yeast secretory proteins.
Using a yeast 2-hybrid screen of a T-cell leukemia cell line with the
intracellular portion of CD18 (ITGB2; 600065) as bait, Kolanus et al.
(1996) isolated a cDNA encoding cytohesin-1 (PSCD1) and a partial cDNA
encoding PSCD2L (602488), which they designated cts18.1. PSCD1 is 88%
identical to the PSCD2L fragment. The predicted 398-amino acid PSCD1
protein contains a central 200-residue SEC7 domain and a C-terminal
pleckstrin homology (PH) domain. Western blot analysis showed expression
of a 47-kD protein, particularly, but not exclusively, in lymphoid
cells.
GENE FUNCTION
Kolanus et al. (1996) found that overexpression of a full-length PSCD1
protein or of the SEC7 domain only induced CD18-dependent binding to
ICAM1 (147840), whereas the PSCD1 PH domain specifically inhibited
adhesion. Binding analysis indicated that the SEC7 domain, but not the
PH domain, interacts with the cytoplasmic domain of CD18 but not with
other cell surface receptors or protein-tyrosine kinases tested. Kolanus
et al. (1996) concluded that PSCD1 specifically regulates the adhesive
function of beta-2 integrins in lymphocytes.
The induction of a transformed cellular phenotype by viruses requires
the modulation of signaling pathways through viral proteins. Kliche et
al. (2001) showed that the phenotypic changes induced by the kaposin A
protein of human herpesvirus-8 are mediated through its direct
interaction with cytohesin-1, a guanine nucleotide exchange factor (GEF)
for ARF GTPases (e.g., ARF1; 103180) and regulator of integrin-mediated
cell adhesion. Focus formation, stress fiber dissolution, and activation
of the ERK1 (601795)/ERK2 (176948) mitogen-activated protein kinase
(MAPK) signal cascade were reverted by a cytohesin-1 glu157-to-lys
mutant, which is deficient in catalyzing guanine nucleotide exchange.
Furthermore, liposome-embedded kaposin A was found to specifically
stimulate cytohesin-1-dependent GTP binding of myristoylated ARF1 in
vitro.
Hafner et al. (2006) used an aptamer displacement screen to identify
SecinH3, a small Sec7 domain-specific molecular antagonist of
cytohesins. The cytohesins are a class of BFA-resistant small GEFs for
ADP-ribosylation factors (ARFs), which regulate cytoskeletal
organization, integrin activation, or integrin signaling. The
application of SecinH3 in human liver cells showed that insulin receptor
complex-associated cytohesins are required for insulin signaling.
SecinH3-treated mice showed increased expression of gluconeogenic genes,
reduced expression of glycolytic, fatty acid, and ketone body metabolism
genes in the liver, reduced liver glycogen stores, and a compensatory
increase in plasma insulin. Thus, Hafner et al. (2006) concluded that
cytohesin inhibition results in hepatic insulin resistance.
Vitale et al. (2000) found that cytohesin-1 interacted with ARF domain
protein-1 (ARD1, or TRIM23; 601747) in a yeast 2-hybrid screen of a
human liver cDNA library. ARD1-GDP interacted well with cytohesin-1 but
poorly with cytohesin-2 (PSCD2; 602488), and cytohesin-1 accelerated
binding of a nonhydrolyzable GTP analog to ARD1. Mutation analysis
showed that the effector region of the ARF domain of ARD1 interacted
with the Sec7 domain of cytohesin-1. Physical association between these
domains was highly dependent on experimental conditions, and a free
Mg(2+) concentration that favored nucleotide release from ARD1 and
accumulation of the nucleotide-free ARD1 form also favored interaction
between ARD1 and cytohesin-1. In transfected COS-7 cells, cytohesin-1
was distributed throughout the cell and was also present in the nucleus.
ARD1 associated with vesicular structures concentrated around the
nucleus and scattered throughout the cytoplasm, corresponding to Golgi
and lysosomes, respectively. A constitutively GDP-bound form of ARD1
showed a similar distribution, whereas a constitutively GTP-bound form
of ARD1 was concentrated close to the nucleus in a Golgi-like
distribution only. When ARD1 or its GDP- and GTP-bound forms were
coexpressed with cytohesin-1, only the GDP-bound form showed any change
in distribution or colocalization with cytohesin-1. In 90% of cells
coexpressing the proteins, the GDP-bound form of ARD1 was distributed
throughout the cell, except for the nucleus, and largely colocalized
with cytohesin-1. In less than 10% of cells coexpressing the proteins,
the GDP-bound form of ARD1 and cytohesin-1 colocalized in lysosomes.
GENE STRUCTURE
By genomic sequence analysis, Ogasawara et al. (2000) determined that
the PSCD1 gene contains at least 14 exons, including a 3-bp exon 10 also
present in PSCD2 and PSCD3 (605081) but not in PSCD4 (606514) that
results in the insertion of a single glycine into the variable loop
between the first and second beta sheets in the pleckstrin homology
domain.
MAPPING
Dixon et al. (1993) showed by PCR analysis of a human/rodent hybrid
panel that the B2-1 gene is located on chromosome 17. Fluorescence in
situ hybridization localized the gene to 17q25.
*FIELD* RF
1. Dixon, B.; Mansour, M.; Pohajdak, B.: Assignment of human B2-1
gene (D17S811E) to chromosome 17qter by PCR analysis of somatic cell
hybrids and fluorescence in situ hybridization. Cytogenet. Cell Genet. 63:
42-44, 1993.
2. Hafner, M.; Schmitz, A.; Grune, I.; Srivatsan, S. G.; Paul, B.;
Kolanus, W.; Quast, T.; Kremmer, E.; Bauer, I.; Famulok, M.: Inhibition
of cytohesins by SecinH3 leads to hepatic insulin resistance. Nature 444:
941-944, 2006.
3. Kliche, S.; Nagel, W.; Kremmer, E.; Atzler, C.; Ege, A.; Knorr,
T.; Koszinowski, U.; Kolanus, W.; Haas, J.: Signaling by human herpesvirus
8 kaposin A through direct membrane recruitment of cytohesin-1. Molec.
Cell 7: 833-843, 2001.
4. Kolanus, W.; Nagel, W.; Schiller, B.; Zeitlmann, L.; Godar, S.;
Stockinger, H.; Seed, B.: Alpha-L-beta-2 integrin/LFA-1 binding to
ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell 86:
233-242, 1996.
5. Ogasawara, M.; Kim, S.-C.; Adamik, R.; Togawa, A.; Ferrans, V.
J.; Takeda, K.; Kirby, M.; Moss, J.; Vaughan, M.: Similarities in
function and gene structure of cytohesin-4 and cytohesin-1, guanine
nucleotide-exchange proteins for ADP-ribosylation factors. J. Biol.
Chem. 275: 3221-3230, 2000.
6. Vitale, N.; Pacheco-Rodriguez, G.; Ferrans, V. J.; Riemenschneider,
W.; Moss, J.; Vaughan, M.: Specific functional interaction of human
cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). J.
Biol. Chem. 275: 21331-21339, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 3/15/2007
Ada Hamosh - updated: 2/1/2007
Paul J. Converse - updated: 2/20/2002
Paul J. Converse - updated: 11/27/2001
Stylianos E. Antonarakis - updated: 8/7/2001
*FIELD* CD
Victor A. McKusick: 5/27/1993
*FIELD* ED
alopez: 02/06/2013
terry: 1/29/2013
terry: 9/7/2010
mgross: 10/1/2009
mgross: 3/15/2007
alopez: 2/5/2007
terry: 2/1/2007
alopez: 12/31/2003
terry: 12/30/2003
mgross: 2/20/2002
alopez: 11/27/2001
mgross: 8/7/2001
mgross: 1/20/2000
carol: 5/4/1999
carol: 5/27/1993