Full text data of DPH3
DPH3
(DESR1, ZCSL2)
[Confidence: low (only semi-automatic identification from reviews)]
DPH3 homolog (CSL-type zinc finger-containing protein 2; DelGEF-interacting protein 1; DelGIP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DPH3 homolog (CSL-type zinc finger-containing protein 2; DelGEF-interacting protein 1; DelGIP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96FX2
ID DPH3_HUMAN Reviewed; 82 AA.
AC Q96FX2;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=DPH3 homolog;
DE AltName: Full=CSL-type zinc finger-containing protein 2;
DE AltName: Full=DelGEF-interacting protein 1;
DE Short=DelGIP1;
GN Name=DPH3; Synonyms=DESR1, ZCSL2;
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), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH GNEFR.
RX PubMed=14980502; DOI=10.1016/j.yexcr.2003.09.033;
RA Sjoelinder M., Uhlmann J., Ponstingl H.;
RT "Characterisation of an evolutionary conserved protein interacting
RT with the putative guanine nucleotide exchange factor DelGEF and
RT modulating secretion.";
RL Exp. Cell Res. 294:68-76(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14527407; DOI=10.1016/j.molcel.2003.08.003;
RA Liu S., Leppla S.H.;
RT "Retroviral insertional mutagenesis identifies a small protein
RT required for synthesis of diphthamide, the target of bacterial ADP-
RT ribosylating toxins.";
RL Mol. Cell 12:603-613(2003).
RN [5]
RP STRUCTURE BY NMR OF 1-81 IN COMPLEX WITH ZINC IONS.
RX PubMed=18214955; DOI=10.1002/prot.21915;
RA Wu F., Zhang J., Sun J., Huang H., Ji P., Chu W., Yu M., Yang F.,
RA Wu Z., Wu J., Shi Y.;
RT "Solution structure of human DESR1, a CSL zinc-binding protein.";
RL Proteins 71:514-518(2008).
CC -!- FUNCTION: Essential for the first step in the synthesis of
CC diphthamide, a post-translational modification of histidine which
CC occurs in elongation factor 2 (EEF2) and which can be ADP-
CC ribosylated by diphtheria toxin and by Pseudomonas exotoxin A
CC (Eta) (By similarity).
CC -!- FUNCTION: Down-regulation increases extracellular release of
CC proteoglycans, indicating a possible role in the secretion
CC process. Stimulates binding of GNEFR to SEC5.
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- INTERACTION:
CC Q9UGK8:SERGEF; NbExp=3; IntAct=EBI-465363, EBI-465368;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96FX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FX2-2; Sequence=VSP_012411;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in small
CC intestine, spleen, thymus, heart, liver and lung.
CC -!- SIMILARITY: Belongs to the DPH3 family.
CC -!- SIMILARITY: Contains 1 DPH-type zinc finger.
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; AK022970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC010181; AAH10181.1; -; mRNA.
DR RefSeq; NP_001040899.1; NM_001047434.2.
DR RefSeq; NP_996662.1; NM_206831.2.
DR UniGene; Hs.388087; -.
DR PDB; 2JR7; NMR; -; A=1-81.
DR PDBsum; 2JR7; -.
DR ProteinModelPortal; Q96FX2; -.
DR SMR; Q96FX2; 1-81.
DR IntAct; Q96FX2; 3.
DR STRING; 9606.ENSP00000419599; -.
DR DMDM; 29611922; -.
DR PRIDE; Q96FX2; -.
DR DNASU; 285381; -.
DR Ensembl; ENST00000383775; ENSP00000373285; ENSG00000154813.
DR Ensembl; ENST00000488423; ENSP00000419599; ENSG00000154813.
DR GeneID; 285381; -.
DR KEGG; hsa:285381; -.
DR UCSC; uc003cau.3; human.
DR CTD; 285381; -.
DR GeneCards; GC03M016298; -.
DR HGNC; HGNC:27717; DPH3.
DR HPA; HPA035287; -.
DR MIM; 608959; gene.
DR neXtProt; NX_Q96FX2; -.
DR PharmGKB; PA162384061; -.
DR eggNOG; COG5216; -.
DR HOGENOM; HOG000190740; -.
DR HOVERGEN; HBG056007; -.
DR InParanoid; Q96FX2; -.
DR KO; K15455; -.
DR OMA; PCGDRFL; -.
DR OrthoDB; EOG7BZVWK; -.
DR PhylomeDB; Q96FX2; -.
DR UniPathway; UPA00559; -.
DR EvolutionaryTrace; Q96FX2; -.
DR GenomeRNAi; 285381; -.
DR NextBio; 95485; -.
DR PRO; PR:Q96FX2; -.
DR Bgee; Q96FX2; -.
DR CleanEx; HS_DPH3; -.
DR Genevestigator; Q96FX2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR GO; GO:0051099; P:positive regulation of binding; IDA:UniProtKB.
DR InterPro; IPR007872; Znf_DHP.
DR Pfam; PF05207; zf-CSL; 1.
DR PROSITE; PS51074; ZF_DPH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1 82 DPH3 homolog.
FT /FTId=PRO_0000082620.
FT ZN_FING 4 60 DPH-type.
FT VAR_SEQ 36 60 Missing (in isoform 2).
FT /FTId=VSP_012411.
FT STRAND 7 9
FT TURN 10 12
FT STRAND 13 15
FT TURN 17 19
FT STRAND 20 25
FT STRAND 29 35
FT HELIX 36 41
FT STRAND 45 47
FT TURN 49 51
FT STRAND 54 58
FT HELIX 61 64
SQ SEQUENCE 82 AA; 9240 MW; 7AC8F3FFF8CE766C CRC64;
MAVFHDEVEI EDFQYDEDSE TYFYPCPCGD NFSITKEDLE NGEDVATCPS CSLIIKVIYD
KDQFVCGETV PAPSANKELV KC
//
ID DPH3_HUMAN Reviewed; 82 AA.
AC Q96FX2;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=DPH3 homolog;
DE AltName: Full=CSL-type zinc finger-containing protein 2;
DE AltName: Full=DelGEF-interacting protein 1;
DE Short=DelGIP1;
GN Name=DPH3; Synonyms=DESR1, ZCSL2;
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), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH GNEFR.
RX PubMed=14980502; DOI=10.1016/j.yexcr.2003.09.033;
RA Sjoelinder M., Uhlmann J., Ponstingl H.;
RT "Characterisation of an evolutionary conserved protein interacting
RT with the putative guanine nucleotide exchange factor DelGEF and
RT modulating secretion.";
RL Exp. Cell Res. 294:68-76(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14527407; DOI=10.1016/j.molcel.2003.08.003;
RA Liu S., Leppla S.H.;
RT "Retroviral insertional mutagenesis identifies a small protein
RT required for synthesis of diphthamide, the target of bacterial ADP-
RT ribosylating toxins.";
RL Mol. Cell 12:603-613(2003).
RN [5]
RP STRUCTURE BY NMR OF 1-81 IN COMPLEX WITH ZINC IONS.
RX PubMed=18214955; DOI=10.1002/prot.21915;
RA Wu F., Zhang J., Sun J., Huang H., Ji P., Chu W., Yu M., Yang F.,
RA Wu Z., Wu J., Shi Y.;
RT "Solution structure of human DESR1, a CSL zinc-binding protein.";
RL Proteins 71:514-518(2008).
CC -!- FUNCTION: Essential for the first step in the synthesis of
CC diphthamide, a post-translational modification of histidine which
CC occurs in elongation factor 2 (EEF2) and which can be ADP-
CC ribosylated by diphtheria toxin and by Pseudomonas exotoxin A
CC (Eta) (By similarity).
CC -!- FUNCTION: Down-regulation increases extracellular release of
CC proteoglycans, indicating a possible role in the secretion
CC process. Stimulates binding of GNEFR to SEC5.
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- INTERACTION:
CC Q9UGK8:SERGEF; NbExp=3; IntAct=EBI-465363, EBI-465368;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96FX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FX2-2; Sequence=VSP_012411;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in small
CC intestine, spleen, thymus, heart, liver and lung.
CC -!- SIMILARITY: Belongs to the DPH3 family.
CC -!- SIMILARITY: Contains 1 DPH-type zinc finger.
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; AK022970; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC010181; AAH10181.1; -; mRNA.
DR RefSeq; NP_001040899.1; NM_001047434.2.
DR RefSeq; NP_996662.1; NM_206831.2.
DR UniGene; Hs.388087; -.
DR PDB; 2JR7; NMR; -; A=1-81.
DR PDBsum; 2JR7; -.
DR ProteinModelPortal; Q96FX2; -.
DR SMR; Q96FX2; 1-81.
DR IntAct; Q96FX2; 3.
DR STRING; 9606.ENSP00000419599; -.
DR DMDM; 29611922; -.
DR PRIDE; Q96FX2; -.
DR DNASU; 285381; -.
DR Ensembl; ENST00000383775; ENSP00000373285; ENSG00000154813.
DR Ensembl; ENST00000488423; ENSP00000419599; ENSG00000154813.
DR GeneID; 285381; -.
DR KEGG; hsa:285381; -.
DR UCSC; uc003cau.3; human.
DR CTD; 285381; -.
DR GeneCards; GC03M016298; -.
DR HGNC; HGNC:27717; DPH3.
DR HPA; HPA035287; -.
DR MIM; 608959; gene.
DR neXtProt; NX_Q96FX2; -.
DR PharmGKB; PA162384061; -.
DR eggNOG; COG5216; -.
DR HOGENOM; HOG000190740; -.
DR HOVERGEN; HBG056007; -.
DR InParanoid; Q96FX2; -.
DR KO; K15455; -.
DR OMA; PCGDRFL; -.
DR OrthoDB; EOG7BZVWK; -.
DR PhylomeDB; Q96FX2; -.
DR UniPathway; UPA00559; -.
DR EvolutionaryTrace; Q96FX2; -.
DR GenomeRNAi; 285381; -.
DR NextBio; 95485; -.
DR PRO; PR:Q96FX2; -.
DR Bgee; Q96FX2; -.
DR CleanEx; HS_DPH3; -.
DR Genevestigator; Q96FX2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050709; P:negative regulation of protein secretion; IDA:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR GO; GO:0051099; P:positive regulation of binding; IDA:UniProtKB.
DR InterPro; IPR007872; Znf_DHP.
DR Pfam; PF05207; zf-CSL; 1.
DR PROSITE; PS51074; ZF_DPH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1 82 DPH3 homolog.
FT /FTId=PRO_0000082620.
FT ZN_FING 4 60 DPH-type.
FT VAR_SEQ 36 60 Missing (in isoform 2).
FT /FTId=VSP_012411.
FT STRAND 7 9
FT TURN 10 12
FT STRAND 13 15
FT TURN 17 19
FT STRAND 20 25
FT STRAND 29 35
FT HELIX 36 41
FT STRAND 45 47
FT TURN 49 51
FT STRAND 54 58
FT HELIX 61 64
SQ SEQUENCE 82 AA; 9240 MW; 7AC8F3FFF8CE766C CRC64;
MAVFHDEVEI EDFQYDEDSE TYFYPCPCGD NFSITKEDLE NGEDVATCPS CSLIIKVIYD
KDQFVCGETV PAPSANKELV KC
//
MIM
608959
*RECORD*
*FIELD* NO
608959
*FIELD* TI
*608959 DPH3, S. CEREVISIAE, HOMOLOG OF; DPH3
;;KTI11, S. CEREVISIAE, HOMOLOG OF; KTI11;;
read moreZINC FINGER, CSL DOMAIN-CONTAINING 2; ZCSL2;;
DEAFNESS LOCUS PUTATIVE GUANINE NUCLEOTIDE EXCHANGE FACTOR-INTERACTING
PROTEIN 1; DELGIP1;;
DELGEF-INTERACTING PROTEIN 1;;
DESR1
*FIELD* TX
CLONING
Using retroviral insertional mutagenesis, Liu and Leppla (2003) rendered
Chinese hamster ovary (CHO) cells resistant to several bacterial
ADP-ribosylating toxins. PCR analysis of flanking sequence of the
retroviral insertion identified a disrupted gene that the authors named
'diphtheria toxin (DT) and Pseudomonas exotoxin A (ETA) sensitivity
required gene-1' (DESR1). BLAST analysis using hamster DESR1 as query
identified DESR1 homologs in human, mouse, C. elegans, D. melanogaster,
and yeast. The human DESR1 gene encodes 2 cDNAs of 0.7 and 3.1 kb,
resulting from alternative 3-prime untranslated regions, both of which
encode a predicted 82-residue protein. BLAST analysis also identified a
57-amino acid DESR1 splice variant that lacks exon 2. Transfection of
the 82-residue human DESR1 cDNA into the original CHO cells rendered
resistant by gene disruption restored bacterial toxin sensitivity, while
the 57-residue DESR1 isoform had no effect. Northern blot analysis
showed ubiquitous expression of 1- and 3-kb DESR1 transcripts in adult
tissues.
Using yeast 2-hybrid analysis with the guanine nucleotide exchange
factor DELGEF (606051) as bait, Sjolinder et al. (2004) cloned DESR1,
which they named DELGEF-interacting protein-1 (DELGIP1). The interaction
between DESR1 and DELGEF was confirmed by coimmunoprecipitation. The
DESR1 gene encodes a highly acidic protein of 9.2 kD molecular mass, and
comparative sequence analysis of DESR1 homologs revealed a putative
Zn-binding motif. Immunofluorescence studies in COS cells transfected
with DESR1-FLAG constructs showed that DESR1 localizes to the nucleus
and the cytoplasm.
GENE FUNCTION
Using a variety of in vivo assays, Liu and Leppla (2003) showed that
DESR1 is required for the first step in the posttranslational
modification of EF2 (130610), which yields diphthamide, the target
molecule for DT and ETA. KTI11, the yeast homolog of DESR1, is also
required for diphthamide synthesis, and Liu and Leppla (2003) noted the
role of KTI11 in numerous other cell processes.
Using antisense oligonucleotides, Sjolinder et al. (2004) showed that
downregulation of DESR1 in HeLa cells causes an increase of proteoglycan
secretion. GST pull-down assays showed that DESR1 increases the binding
of DELGEF to human Sec5 (EXOC2; 615329).
GENE STRUCTURE
Using genomic sequence analysis, Liu and Leppla (2003) showed that the
DESR1 gene contains 3 exons.
MAPPING
By genomic sequence analysis, Liu and Leppla (2003) mapped the DESR1
gene to human chromosome 14.
*FIELD* RF
1. Liu, S.; Leppla, S. H.: Retroviral insertional mutagenesis identifies
a small protein required for synthesis of diphthamide, the target
of bacterial ADP-ribosylating toxins. Molec. Cell 12: 603-613, 2003.
2. Sjolinder, M.; Uhlmann, J.; Ponstingl, H.: Characterisation of
an evolutionarily conserved protein interacting with the putative
guanine nucleotide exchange factor DelGEF and modulating secretion. Exp.
Cell Res. 294: 68-76, 2004.
*FIELD* CD
Laura L. Baxter: 10/5/2004
*FIELD* ED
alopez: 07/24/2013
mgross: 6/5/2007
alopez: 10/5/2004
*RECORD*
*FIELD* NO
608959
*FIELD* TI
*608959 DPH3, S. CEREVISIAE, HOMOLOG OF; DPH3
;;KTI11, S. CEREVISIAE, HOMOLOG OF; KTI11;;
read moreZINC FINGER, CSL DOMAIN-CONTAINING 2; ZCSL2;;
DEAFNESS LOCUS PUTATIVE GUANINE NUCLEOTIDE EXCHANGE FACTOR-INTERACTING
PROTEIN 1; DELGIP1;;
DELGEF-INTERACTING PROTEIN 1;;
DESR1
*FIELD* TX
CLONING
Using retroviral insertional mutagenesis, Liu and Leppla (2003) rendered
Chinese hamster ovary (CHO) cells resistant to several bacterial
ADP-ribosylating toxins. PCR analysis of flanking sequence of the
retroviral insertion identified a disrupted gene that the authors named
'diphtheria toxin (DT) and Pseudomonas exotoxin A (ETA) sensitivity
required gene-1' (DESR1). BLAST analysis using hamster DESR1 as query
identified DESR1 homologs in human, mouse, C. elegans, D. melanogaster,
and yeast. The human DESR1 gene encodes 2 cDNAs of 0.7 and 3.1 kb,
resulting from alternative 3-prime untranslated regions, both of which
encode a predicted 82-residue protein. BLAST analysis also identified a
57-amino acid DESR1 splice variant that lacks exon 2. Transfection of
the 82-residue human DESR1 cDNA into the original CHO cells rendered
resistant by gene disruption restored bacterial toxin sensitivity, while
the 57-residue DESR1 isoform had no effect. Northern blot analysis
showed ubiquitous expression of 1- and 3-kb DESR1 transcripts in adult
tissues.
Using yeast 2-hybrid analysis with the guanine nucleotide exchange
factor DELGEF (606051) as bait, Sjolinder et al. (2004) cloned DESR1,
which they named DELGEF-interacting protein-1 (DELGIP1). The interaction
between DESR1 and DELGEF was confirmed by coimmunoprecipitation. The
DESR1 gene encodes a highly acidic protein of 9.2 kD molecular mass, and
comparative sequence analysis of DESR1 homologs revealed a putative
Zn-binding motif. Immunofluorescence studies in COS cells transfected
with DESR1-FLAG constructs showed that DESR1 localizes to the nucleus
and the cytoplasm.
GENE FUNCTION
Using a variety of in vivo assays, Liu and Leppla (2003) showed that
DESR1 is required for the first step in the posttranslational
modification of EF2 (130610), which yields diphthamide, the target
molecule for DT and ETA. KTI11, the yeast homolog of DESR1, is also
required for diphthamide synthesis, and Liu and Leppla (2003) noted the
role of KTI11 in numerous other cell processes.
Using antisense oligonucleotides, Sjolinder et al. (2004) showed that
downregulation of DESR1 in HeLa cells causes an increase of proteoglycan
secretion. GST pull-down assays showed that DESR1 increases the binding
of DELGEF to human Sec5 (EXOC2; 615329).
GENE STRUCTURE
Using genomic sequence analysis, Liu and Leppla (2003) showed that the
DESR1 gene contains 3 exons.
MAPPING
By genomic sequence analysis, Liu and Leppla (2003) mapped the DESR1
gene to human chromosome 14.
*FIELD* RF
1. Liu, S.; Leppla, S. H.: Retroviral insertional mutagenesis identifies
a small protein required for synthesis of diphthamide, the target
of bacterial ADP-ribosylating toxins. Molec. Cell 12: 603-613, 2003.
2. Sjolinder, M.; Uhlmann, J.; Ponstingl, H.: Characterisation of
an evolutionarily conserved protein interacting with the putative
guanine nucleotide exchange factor DelGEF and modulating secretion. Exp.
Cell Res. 294: 68-76, 2004.
*FIELD* CD
Laura L. Baxter: 10/5/2004
*FIELD* ED
alopez: 07/24/2013
mgross: 6/5/2007
alopez: 10/5/2004