Full text data of DERA
DERA
[Confidence: high (present in two of the MS resources)]
Putative deoxyribose-phosphate aldolase; DERA; 4.1.2.4 (2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Putative deoxyribose-phosphate aldolase; DERA; 4.1.2.4 (2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00219677
IPI00219677 CGI-26 protein CGI-26 protein membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a extracellular n/a found at its expected molecular weight found at molecular weight
IPI00219677 CGI-26 protein CGI-26 protein membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a extracellular n/a found at its expected molecular weight found at molecular weight
UniProt
Q9Y315
ID DEOC_HUMAN Reviewed; 318 AA.
AC Q9Y315; Q53HN9; Q6PHW2;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-2002, sequence version 2.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Putative deoxyribose-phosphate aldolase;
DE Short=DERA;
DE EC=4.1.2.4;
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;
DE AltName: Full=Phosphodeoxyriboaldolase;
DE Short=Deoxyriboaldolase;
GN Name=DERA; ORFNames=CGI-26;
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 [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes a reversible aldol reaction between
CC acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-
CC D-ribose 5-phosphate (By similarity).
CC -!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-
CC glyceraldehyde 3-phosphate + acetaldehyde.
CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC deoxy-alpha-D-ribose 1-phosphate: step 2/2.
CC -!- INTERACTION:
CC Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-1048152, EBI-1056358;
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27735.1; Type=Erroneous initiation;
CC Sequence=AAH56234.1; Type=Erroneous initiation;
CC Sequence=BAD96261.1; Type=Erroneous initiation;
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DR EMBL; AF132960; AAD27735.1; ALT_INIT; mRNA.
DR EMBL; AK222541; BAD96261.1; ALT_INIT; mRNA.
DR EMBL; BC056234; AAH56234.1; ALT_INIT; mRNA.
DR RefSeq; NP_057038.2; NM_015954.2.
DR UniGene; Hs.39429; -.
DR ProteinModelPortal; Q9Y315; -.
DR SMR; Q9Y315; 48-289.
DR STRING; 9606.ENSP00000416583; -.
DR PhosphoSite; Q9Y315; -.
DR DMDM; 24636817; -.
DR PaxDb; Q9Y315; -.
DR PRIDE; Q9Y315; -.
DR DNASU; 51071; -.
DR Ensembl; ENST00000428559; ENSP00000416583; ENSG00000023697.
DR GeneID; 51071; -.
DR KEGG; hsa:51071; -.
DR UCSC; uc001rde.3; human.
DR CTD; 51071; -.
DR GeneCards; GC12P016064; -.
DR HGNC; HGNC:24269; DERA.
DR neXtProt; NX_Q9Y315; -.
DR PharmGKB; PA134943367; -.
DR eggNOG; COG0274; -.
DR HOGENOM; HOG000241644; -.
DR HOVERGEN; HBG030164; -.
DR InParanoid; Q9Y315; -.
DR KO; K01619; -.
DR OMA; WKTGKKI; -.
DR OrthoDB; EOG7B5WWC; -.
DR PhylomeDB; Q9Y315; -.
DR SABIO-RK; Q9Y315; -.
DR UniPathway; UPA00002; UER00468.
DR GenomeRNAi; 51071; -.
DR NextBio; 53683; -.
DR PRO; PR:Q9Y315; -.
DR ArrayExpress; Q9Y315; -.
DR Bgee; Q9Y315; -.
DR CleanEx; HS_DERA; -.
DR Genevestigator; Q9Y315; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0046121; P:deoxyribonucleoside catabolic process; IDA:UniProtKB.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/lacD_aldolase.
DR PANTHER; PTHR10889; PTHR10889; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR TIGRFAMs; TIGR00126; deoC; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Lyase; Reference proteome; Schiff base.
FT CHAIN 1 318 Putative deoxyribose-phosphate aldolase.
FT /FTId=PRO_0000057310.
FT ACT_SITE 218 218 Schiff-base intermediate with
FT acetaldehyde (By similarity).
FT ACT_SITE 254 254 By similarity.
FT CONFLICT 159 159 N -> S (in Ref. 2; BAD96261).
FT CONFLICT 234 234 I -> T (in Ref. 2; BAD96261).
FT CONFLICT 240 240 I -> T (in Ref. 2; BAD96261).
SQ SEQUENCE 318 AA; 35231 MW; E9576567D0E5CBDE CRC64;
MSAHNRGTEL DLSWISKIQV NHPAVLRRAE QIQARRTVKK EWQAAWLLKA VTFIDLTTLS
GDDTSSNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPARVCDAV KALKAAGCNI
PVASVAAGFP AGQTHLKTRL EEIRLAVEDG ATEIDVVINR SLVLTGQWEA LYDEIRQFRK
ACGEAHLKTI LATGELGTLT NVYKASMIAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI
RDFFWKTGNK IGFKPAGGIR SAKDSLAWLS LVKEELGDEW LKPELFRIGA STLLSDIERQ
IYHHVTGRYA AYHDLPMS
//
ID DEOC_HUMAN Reviewed; 318 AA.
AC Q9Y315; Q53HN9; Q6PHW2;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-2002, sequence version 2.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Putative deoxyribose-phosphate aldolase;
DE Short=DERA;
DE EC=4.1.2.4;
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;
DE AltName: Full=Phosphodeoxyriboaldolase;
DE Short=Deoxyriboaldolase;
GN Name=DERA; ORFNames=CGI-26;
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 [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes a reversible aldol reaction between
CC acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-
CC D-ribose 5-phosphate (By similarity).
CC -!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-
CC glyceraldehyde 3-phosphate + acetaldehyde.
CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC deoxy-alpha-D-ribose 1-phosphate: step 2/2.
CC -!- INTERACTION:
CC Q9BRP4:PAAF1; NbExp=1; IntAct=EBI-1048152, EBI-1056358;
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27735.1; Type=Erroneous initiation;
CC Sequence=AAH56234.1; Type=Erroneous initiation;
CC Sequence=BAD96261.1; Type=Erroneous initiation;
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; AF132960; AAD27735.1; ALT_INIT; mRNA.
DR EMBL; AK222541; BAD96261.1; ALT_INIT; mRNA.
DR EMBL; BC056234; AAH56234.1; ALT_INIT; mRNA.
DR RefSeq; NP_057038.2; NM_015954.2.
DR UniGene; Hs.39429; -.
DR ProteinModelPortal; Q9Y315; -.
DR SMR; Q9Y315; 48-289.
DR STRING; 9606.ENSP00000416583; -.
DR PhosphoSite; Q9Y315; -.
DR DMDM; 24636817; -.
DR PaxDb; Q9Y315; -.
DR PRIDE; Q9Y315; -.
DR DNASU; 51071; -.
DR Ensembl; ENST00000428559; ENSP00000416583; ENSG00000023697.
DR GeneID; 51071; -.
DR KEGG; hsa:51071; -.
DR UCSC; uc001rde.3; human.
DR CTD; 51071; -.
DR GeneCards; GC12P016064; -.
DR HGNC; HGNC:24269; DERA.
DR neXtProt; NX_Q9Y315; -.
DR PharmGKB; PA134943367; -.
DR eggNOG; COG0274; -.
DR HOGENOM; HOG000241644; -.
DR HOVERGEN; HBG030164; -.
DR InParanoid; Q9Y315; -.
DR KO; K01619; -.
DR OMA; WKTGKKI; -.
DR OrthoDB; EOG7B5WWC; -.
DR PhylomeDB; Q9Y315; -.
DR SABIO-RK; Q9Y315; -.
DR UniPathway; UPA00002; UER00468.
DR GenomeRNAi; 51071; -.
DR NextBio; 53683; -.
DR PRO; PR:Q9Y315; -.
DR ArrayExpress; Q9Y315; -.
DR Bgee; Q9Y315; -.
DR CleanEx; HS_DERA; -.
DR Genevestigator; Q9Y315; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0046121; P:deoxyribonucleoside catabolic process; IDA:UniProtKB.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/lacD_aldolase.
DR PANTHER; PTHR10889; PTHR10889; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR TIGRFAMs; TIGR00126; deoC; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Lyase; Reference proteome; Schiff base.
FT CHAIN 1 318 Putative deoxyribose-phosphate aldolase.
FT /FTId=PRO_0000057310.
FT ACT_SITE 218 218 Schiff-base intermediate with
FT acetaldehyde (By similarity).
FT ACT_SITE 254 254 By similarity.
FT CONFLICT 159 159 N -> S (in Ref. 2; BAD96261).
FT CONFLICT 234 234 I -> T (in Ref. 2; BAD96261).
FT CONFLICT 240 240 I -> T (in Ref. 2; BAD96261).
SQ SEQUENCE 318 AA; 35231 MW; E9576567D0E5CBDE CRC64;
MSAHNRGTEL DLSWISKIQV NHPAVLRRAE QIQARRTVKK EWQAAWLLKA VTFIDLTTLS
GDDTSSNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPARVCDAV KALKAAGCNI
PVASVAAGFP AGQTHLKTRL EEIRLAVEDG ATEIDVVINR SLVLTGQWEA LYDEIRQFRK
ACGEAHLKTI LATGELGTLT NVYKASMIAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI
RDFFWKTGNK IGFKPAGGIR SAKDSLAWLS LVKEELGDEW LKPELFRIGA STLLSDIERQ
IYHHVTGRYA AYHDLPMS
//