PDCD5_HUMAN
ID PDCD5_HUMAN Reviewed; 125 AA.
AC O14737; B4DE64; Q53YC9; Q6IB70;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 cell
RT line TF-1, could enhance apoptosis of some tumor cells induced by growth
RT factor withdrawal.";
RL Biochem. Biophys. Res. Commun. 254:203-210(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
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 [22]
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 protein.";
RL Arch. Biochem. Biophys. 486:141-149(2009).
CC -!- FUNCTION: May function in the process of apoptosis.
CC -!- INTERACTION:
CC O14737; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-712290, EBI-79165;
CC O14737; Q9NS91: RAD18; NbExp=3; IntAct=EBI-712290, EBI-2339393;
CC O14737; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-712290, EBI-17716262;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14737-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14737-2; Sequence=VSP_056203;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in heart, testis,
CC kidney, pituitary gland, adrenal gland and placenta.
CC -!- DEVELOPMENTAL STAGE: Expression in fetal tissues is significantly lower
CC than in adult tissues.
CC -!- INDUCTION: Activated in cells undergoing apoptosis.
CC -!- SIMILARITY: Belongs to the PDCD5 family. {ECO:0000305}.
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DR EMBL; AF014955; AAD11579.1; -; mRNA.
DR EMBL; BT006694; AAP35340.1; -; mRNA.
DR EMBL; AK293486; BAG56975.1; -; mRNA.
DR EMBL; CR456934; CAG33215.1; -; mRNA.
DR EMBL; AC008474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015519; AAH15519.1; -; mRNA.
DR CCDS; CCDS12423.1; -. [O14737-1]
DR PIR; JG0192; JG0192.
DR RefSeq; NP_004699.1; NM_004708.3. [O14737-1]
DR RefSeq; XP_005259449.1; XM_005259392.4. [O14737-2]
DR PDB; 1YYB; NMR; -; A=1-26.
DR PDB; 2CRU; NMR; -; A=9-113.
DR PDB; 2K6B; NMR; -; A=2-112.
DR PDBsum; 1YYB; -.
DR PDBsum; 2CRU; -.
DR PDBsum; 2K6B; -.
DR AlphaFoldDB; O14737; -.
DR BMRB; O14737; -.
DR SMR; O14737; -.
DR BioGRID; 114588; 50.
DR DIP; DIP-50602N; -.
DR IntAct; O14737; 39.
DR MINT; O14737; -.
DR STRING; 9606.ENSP00000466214; -.
DR iPTMnet; O14737; -.
DR MetOSite; O14737; -.
DR PhosphoSitePlus; O14737; -.
DR BioMuta; PDCD5; -.
DR EPD; O14737; -.
DR jPOST; O14737; -.
DR MassIVE; O14737; -.
DR MaxQB; O14737; -.
DR PaxDb; O14737; -.
DR PeptideAtlas; O14737; -.
DR PRIDE; O14737; -.
DR ProteomicsDB; 3922; -.
DR ProteomicsDB; 48199; -. [O14737-1]
DR TopDownProteomics; O14737-1; -. [O14737-1]
DR Antibodypedia; 15598; 248 antibodies from 31 providers.
DR DNASU; 9141; -.
DR Ensembl; ENST00000419343.7; ENSP00000476525.1; ENSG00000105185.12. [O14737-2]
DR Ensembl; ENST00000590247.7; ENSP00000466214.1; ENSG00000105185.12. [O14737-1]
DR GeneID; 9141; -.
DR KEGG; hsa:9141; -.
DR MANE-Select; ENST00000590247.7; ENSP00000466214.1; NM_004708.4; NP_004699.1.
DR UCSC; uc002ntl.4; human. [O14737-1]
DR CTD; 9141; -.
DR DisGeNET; 9141; -.
DR GeneCards; PDCD5; -.
DR HGNC; HGNC:8764; PDCD5.
DR HPA; ENSG00000105185; Low tissue specificity.
DR MIM; 604583; gene.
DR neXtProt; NX_O14737; -.
DR OpenTargets; ENSG00000105185; -.
DR PharmGKB; PA33114; -.
DR VEuPathDB; HostDB:ENSG00000105185; -.
DR eggNOG; KOG3431; Eukaryota.
DR GeneTree; ENSGT00390000011085; -.
DR InParanoid; O14737; -.
DR OMA; KPQFGEQ; -.
DR OrthoDB; 1645187at2759; -.
DR PhylomeDB; O14737; -.
DR PathwayCommons; O14737; -.
DR SignaLink; O14737; -.
DR SIGNOR; O14737; -.
DR BioGRID-ORCS; 9141; 320 hits in 1080 CRISPR screens.
DR ChiTaRS; PDCD5; human.
DR EvolutionaryTrace; O14737; -.
DR GeneWiki; PDCD5; -.
DR GenomeRNAi; 9141; -.
DR Pharos; O14737; Tbio.
DR PRO; PR:O14737; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14737; protein.
DR Bgee; ENSG00000105185; Expressed in right testis and 195 other tissues.
DR ExpressionAtlas; O14737; baseline and differential.
DR Genevisible; O14737; HS.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:1903645; P:negative regulation of chaperone-mediated protein folding; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:1903638; P:positive regulation of protein insertion into mitochondrial outer membrane; IMP:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
DR Gene3D; 1.10.8.140; -; 1.
DR InterPro; IPR002836; PDCD5-like.
DR InterPro; IPR036883; PDCD5-like_sf.
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; Alternative splicing; Apoptosis;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..125
FT /note="Programmed cell death protein 5"
FT /id="PRO_0000121545"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 89..125
FT /note="EQGLIEILKKVSQQTEKTTTVKFNRRKVMDSDEDDDY -> LDSLEELYCYL
FT LYQNMASKGQLHLHWITEFLLTLRRNCWRE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056203"
FT CONFLICT 104
FT /note="E -> K (in Ref. 4; CAG33215)"
FT /evidence="ECO:0000305"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:1YYB"
FT HELIX 26..47
FT /evidence="ECO:0007829|PDB:2CRU"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:2CRU"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:2CRU"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:2CRU"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2K6B"
SQ SEQUENCE 125 AA; 14285 MW; 9569E0679C3DC20D CRC64;
MADEELEALR RQRLAELQAK HGDPGDAAQQ EAKHREAEMR NSILAQVLDQ SARARLSNLA
LVKPEKTKAV ENYLIQMARY GQLSEKVSEQ GLIEILKKVS QQTEKTTTVK FNRRKVMDSD
EDDDY
