Full text data of PDCD5
PDCD5
(TFAR19)
[Confidence: low (only semi-automatic identification from reviews)]
Programmed cell death protein 5 (TF-1 cell apoptosis-related protein 19; Protein TFAR19)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Programmed cell death protein 5 (TF-1 cell apoptosis-related protein 19; Protein TFAR19)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O14737
ID PDCD5_HUMAN Reviewed; 125 AA.
AC O14737; Q53YC9; Q6IB70;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Programmed cell death protein 5;
DE AltName: Full=TF-1 cell apoptosis-related protein 19;
DE Short=Protein TFAR19;
GN Name=PDCD5; Synonyms=TFAR19;
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].
RC TISSUE=Erythroleukemia;
RX PubMed=9920759; DOI=10.1006/bbrc.1998.9893;
RA Liu H.T., Wang Y.G., Zhang Y.M., Song Q.S., Di C.H., Chen G., Tang J.,
RA Ma D.L.;
RT "TFAR19, a novel apoptosis-related gene cloned from human leukemia
RT cell line TF-1, could enhance apoptosis of some tumor cells induced by
RT growth factor withdrawal.";
RL Biochem. Biophys. Res. Commun. 254:203-210(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP SPECTROMETRY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [16]
RP STRUCTURE BY NMR OF 9-113.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of programmed cell death 5.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [17]
RP STRUCTURE BY NMR OF 2-112.
RX PubMed=19358820; DOI=10.1016/j.abb.2009.03.018;
RA Yao H., Xu L., Feng Y., Liu D., Chen Y., Wang J.;
RT "Structure-function correlation of human programmed cell death 5
RT protein.";
RL Arch. Biochem. Biophys. 486:141-149(2009).
CC -!- FUNCTION: May function in the process of apoptosis.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart,
CC testis, kidney, pituitary gland, adrenal gland and placenta.
CC -!- DEVELOPMENTAL STAGE: Expression in fetal tissues is significantly
CC lower than in adult tissues.
CC -!- INDUCTION: Activated in cells undergoing apoptosis.
CC -!- SIMILARITY: Belongs to the PDCD5 family.
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; AF014955; AAD11579.1; -; mRNA.
DR EMBL; BT006694; AAP35340.1; -; mRNA.
DR EMBL; CR456934; CAG33215.1; -; mRNA.
DR EMBL; BC015519; AAH15519.1; -; mRNA.
DR PIR; JG0192; JG0192.
DR RefSeq; NP_004699.1; NM_004708.3.
DR UniGene; Hs.443831; -.
DR PDB; 1YYB; NMR; -; A=2-26.
DR PDB; 2CRU; NMR; -; A=9-112.
DR PDB; 2K6B; NMR; -; A=2-112.
DR PDBsum; 1YYB; -.
DR PDBsum; 2CRU; -.
DR PDBsum; 2K6B; -.
DR ProteinModelPortal; O14737; -.
DR SMR; O14737; 2-112.
DR DIP; DIP-50602N; -.
DR IntAct; O14737; 14.
DR MINT; MINT-5002173; -.
DR STRING; 9606.ENSP00000221784; -.
DR PhosphoSite; O14737; -.
DR PaxDb; O14737; -.
DR PeptideAtlas; O14737; -.
DR PRIDE; O14737; -.
DR DNASU; 9141; -.
DR Ensembl; ENST00000590247; ENSP00000466214; ENSG00000105185.
DR GeneID; 9141; -.
DR KEGG; hsa:9141; -.
DR UCSC; uc002ntm.3; human.
DR CTD; 9141; -.
DR GeneCards; GC19P033072; -.
DR HGNC; HGNC:8764; PDCD5.
DR HPA; HPA018471; -.
DR MIM; 604583; gene.
DR neXtProt; NX_O14737; -.
DR PharmGKB; PA33114; -.
DR eggNOG; COG2118; -.
DR HOGENOM; HOG000194121; -.
DR HOVERGEN; HBG053536; -.
DR InParanoid; O14737; -.
DR KO; K06875; -.
DR OMA; RMAQMGQ; -.
DR OrthoDB; EOG7G7KS0; -.
DR PhylomeDB; O14737; -.
DR EvolutionaryTrace; O14737; -.
DR GeneWiki; PDCD5; -.
DR GenomeRNAi; 9141; -.
DR NextBio; 34283; -.
DR PRO; PR:O14737; -.
DR ArrayExpress; O14737; -.
DR Bgee; O14737; -.
DR CleanEx; HS_PDCD5; -.
DR Genevestigator; O14737; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR Gene3D; 1.10.8.140; -; 1.
DR InterPro; IPR002836; PDCD5-related.
DR PANTHER; PTHR10840; PTHR10840; 1.
DR Pfam; PF01984; dsDNA_bind; 1.
DR PIRSF; PIRSF015730; TFAR19; 1.
DR SUPFAM; SSF46950; SSF46950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 125 Programmed cell death protein 5.
FT /FTId=PRO_0000121545.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 63 63 N6-acetyllysine.
FT MOD_RES 119 119 Phosphoserine.
FT CONFLICT 104 104 E -> K (in Ref. 3; CAG33215).
FT HELIX 2 19
FT HELIX 26 47
FT HELIX 50 62
FT HELIX 64 80
FT HELIX 89 99
FT STRAND 100 102
SQ SEQUENCE 125 AA; 14285 MW; 9569E0679C3DC20D CRC64;
MADEELEALR RQRLAELQAK HGDPGDAAQQ EAKHREAEMR NSILAQVLDQ SARARLSNLA
LVKPEKTKAV ENYLIQMARY GQLSEKVSEQ GLIEILKKVS QQTEKTTTVK FNRRKVMDSD
EDDDY
//
ID PDCD5_HUMAN Reviewed; 125 AA.
AC O14737; Q53YC9; Q6IB70;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Programmed cell death protein 5;
DE AltName: Full=TF-1 cell apoptosis-related protein 19;
DE Short=Protein TFAR19;
GN Name=PDCD5; Synonyms=TFAR19;
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].
RC TISSUE=Erythroleukemia;
RX PubMed=9920759; DOI=10.1006/bbrc.1998.9893;
RA Liu H.T., Wang Y.G., Zhang Y.M., Song Q.S., Di C.H., Chen G., Tang J.,
RA Ma D.L.;
RT "TFAR19, a novel apoptosis-related gene cloned from human leukemia
RT cell line TF-1, could enhance apoptosis of some tumor cells induced by
RT growth factor withdrawal.";
RL Biochem. Biophys. Res. Commun. 254:203-210(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP SPECTROMETRY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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 [16]
RP STRUCTURE BY NMR OF 9-113.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of programmed cell death 5.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [17]
RP STRUCTURE BY NMR OF 2-112.
RX PubMed=19358820; DOI=10.1016/j.abb.2009.03.018;
RA Yao H., Xu L., Feng Y., Liu D., Chen Y., Wang J.;
RT "Structure-function correlation of human programmed cell death 5
RT protein.";
RL Arch. Biochem. Biophys. 486:141-149(2009).
CC -!- FUNCTION: May function in the process of apoptosis.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart,
CC testis, kidney, pituitary gland, adrenal gland and placenta.
CC -!- DEVELOPMENTAL STAGE: Expression in fetal tissues is significantly
CC lower than in adult tissues.
CC -!- INDUCTION: Activated in cells undergoing apoptosis.
CC -!- SIMILARITY: Belongs to the PDCD5 family.
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; AF014955; AAD11579.1; -; mRNA.
DR EMBL; BT006694; AAP35340.1; -; mRNA.
DR EMBL; CR456934; CAG33215.1; -; mRNA.
DR EMBL; BC015519; AAH15519.1; -; mRNA.
DR PIR; JG0192; JG0192.
DR RefSeq; NP_004699.1; NM_004708.3.
DR UniGene; Hs.443831; -.
DR PDB; 1YYB; NMR; -; A=2-26.
DR PDB; 2CRU; NMR; -; A=9-112.
DR PDB; 2K6B; NMR; -; A=2-112.
DR PDBsum; 1YYB; -.
DR PDBsum; 2CRU; -.
DR PDBsum; 2K6B; -.
DR ProteinModelPortal; O14737; -.
DR SMR; O14737; 2-112.
DR DIP; DIP-50602N; -.
DR IntAct; O14737; 14.
DR MINT; MINT-5002173; -.
DR STRING; 9606.ENSP00000221784; -.
DR PhosphoSite; O14737; -.
DR PaxDb; O14737; -.
DR PeptideAtlas; O14737; -.
DR PRIDE; O14737; -.
DR DNASU; 9141; -.
DR Ensembl; ENST00000590247; ENSP00000466214; ENSG00000105185.
DR GeneID; 9141; -.
DR KEGG; hsa:9141; -.
DR UCSC; uc002ntm.3; human.
DR CTD; 9141; -.
DR GeneCards; GC19P033072; -.
DR HGNC; HGNC:8764; PDCD5.
DR HPA; HPA018471; -.
DR MIM; 604583; gene.
DR neXtProt; NX_O14737; -.
DR PharmGKB; PA33114; -.
DR eggNOG; COG2118; -.
DR HOGENOM; HOG000194121; -.
DR HOVERGEN; HBG053536; -.
DR InParanoid; O14737; -.
DR KO; K06875; -.
DR OMA; RMAQMGQ; -.
DR OrthoDB; EOG7G7KS0; -.
DR PhylomeDB; O14737; -.
DR EvolutionaryTrace; O14737; -.
DR GeneWiki; PDCD5; -.
DR GenomeRNAi; 9141; -.
DR NextBio; 34283; -.
DR PRO; PR:O14737; -.
DR ArrayExpress; O14737; -.
DR Bgee; O14737; -.
DR CleanEx; HS_PDCD5; -.
DR Genevestigator; O14737; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR Gene3D; 1.10.8.140; -; 1.
DR InterPro; IPR002836; PDCD5-related.
DR PANTHER; PTHR10840; PTHR10840; 1.
DR Pfam; PF01984; dsDNA_bind; 1.
DR PIRSF; PIRSF015730; TFAR19; 1.
DR SUPFAM; SSF46950; SSF46950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 125 Programmed cell death protein 5.
FT /FTId=PRO_0000121545.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 63 63 N6-acetyllysine.
FT MOD_RES 119 119 Phosphoserine.
FT CONFLICT 104 104 E -> K (in Ref. 3; CAG33215).
FT HELIX 2 19
FT HELIX 26 47
FT HELIX 50 62
FT HELIX 64 80
FT HELIX 89 99
FT STRAND 100 102
SQ SEQUENCE 125 AA; 14285 MW; 9569E0679C3DC20D CRC64;
MADEELEALR RQRLAELQAK HGDPGDAAQQ EAKHREAEMR NSILAQVLDQ SARARLSNLA
LVKPEKTKAV ENYLIQMARY GQLSEKVSEQ GLIEILKKVS QQTEKTTTVK FNRRKVMDSD
EDDDY
//
MIM
604583
*RECORD*
*FIELD* NO
604583
*FIELD* TI
*604583 PROGRAMMED CELL DEATH 5; PDCD5
;;TF1 CELL APOPTOSIS-RELATED GENE 19; TFAR19
read more*FIELD* TX
Using cDNA-representative differences analysis (Lisitsyn et al., 1993),
Liu et al. (1999) identified a novel gene, designated TFAR19, from TF1
cells (a human premyeloid cell line established from a patient with
erythroleukemia) undergoing apoptosis after the withdrawal of GM-CSF
from the culture medium. This TFAR19 gene encodes a protein of 125 amino
acids, with an ATG initiation codon at nucleotides 25-27. It contains a
cAMP- and cGMP-dependent protein kinase phosphorylation site, multiple
protein kinase C phosphorylation sites, and a casein kinase II
phosphorylation site. It shares significant homology to the
corresponding proteins of species ranging from yeast to mice. The TFAR19
protein product is predicted to localize in the nucleus. Dot blot
analysis showed that TFAR19 is ubiquitously expressed, but is most
prominent in heart, testis, kidney, pituitary gland, adrenal gland, and
placenta. Expression in fetal tissues is significantly lower than that
in adult tissues. The expression of TFAR19 is upregulated in tumor cells
undergoing apoptosis and enhances apoptosis triggered by growth factor
or serum deprivation.
*FIELD* RF
1. Lisitsyn, N.; Lisitsyn, N.; Wigler, M.: Cloning the differences
between two complex genomes. Science 259: 946-951, 1993.
2. Liu, H.; Wang, Y.; Zhang, Y.; Song, Q.; Di, C.; Chen, G.; Tang,
J.; Ma, D.: TFAR19, a novel apoptosis-related gene cloned from human
leukemia cell line TF-1, could enhance apoptosis of some tumor cells
induced by growth factor withdrawal. Biochem. Biophys. Res. Commun. 254:
203-210, 1999.
*FIELD* CD
Wilson H. Y. Lo: 2/19/2000
*FIELD* ED
carol: 02/19/2000
*RECORD*
*FIELD* NO
604583
*FIELD* TI
*604583 PROGRAMMED CELL DEATH 5; PDCD5
;;TF1 CELL APOPTOSIS-RELATED GENE 19; TFAR19
read more*FIELD* TX
Using cDNA-representative differences analysis (Lisitsyn et al., 1993),
Liu et al. (1999) identified a novel gene, designated TFAR19, from TF1
cells (a human premyeloid cell line established from a patient with
erythroleukemia) undergoing apoptosis after the withdrawal of GM-CSF
from the culture medium. This TFAR19 gene encodes a protein of 125 amino
acids, with an ATG initiation codon at nucleotides 25-27. It contains a
cAMP- and cGMP-dependent protein kinase phosphorylation site, multiple
protein kinase C phosphorylation sites, and a casein kinase II
phosphorylation site. It shares significant homology to the
corresponding proteins of species ranging from yeast to mice. The TFAR19
protein product is predicted to localize in the nucleus. Dot blot
analysis showed that TFAR19 is ubiquitously expressed, but is most
prominent in heart, testis, kidney, pituitary gland, adrenal gland, and
placenta. Expression in fetal tissues is significantly lower than that
in adult tissues. The expression of TFAR19 is upregulated in tumor cells
undergoing apoptosis and enhances apoptosis triggered by growth factor
or serum deprivation.
*FIELD* RF
1. Lisitsyn, N.; Lisitsyn, N.; Wigler, M.: Cloning the differences
between two complex genomes. Science 259: 946-951, 1993.
2. Liu, H.; Wang, Y.; Zhang, Y.; Song, Q.; Di, C.; Chen, G.; Tang,
J.; Ma, D.: TFAR19, a novel apoptosis-related gene cloned from human
leukemia cell line TF-1, could enhance apoptosis of some tumor cells
induced by growth factor withdrawal. Biochem. Biophys. Res. Commun. 254:
203-210, 1999.
*FIELD* CD
Wilson H. Y. Lo: 2/19/2000
*FIELD* ED
carol: 02/19/2000