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Protein

Programmed cell death protein 5

Gene

PDCD5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May function in the process of apoptosis.

GO - Molecular functioni

  • acetyltransferase activator activity Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • DNA binding Source: InterPro
  • heparin binding Source: UniProtKB

GO - Biological processi

  • cellular response to transforming growth factor beta stimulus Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of chaperone-mediated protein folding Source: UniProtKB
  • positive regulation of apoptotic process Source: FlyBase
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of protein import into mitochondrial outer membrane Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Programmed cell death protein 5
Alternative name(s):
TF-1 cell apoptosis-related protein 19
Short name:
Protein TFAR19
Gene namesi
Name:PDCD5
Synonyms:TFAR19
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:8764. PDCD5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33114.

Polymorphism and mutation databases

BioMutaiPDCD5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 125124Programmed cell death protein 5PRO_0000121545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei63 – 631N6-acetyllysineCombined sources
Modified residuei119 – 1191PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO14737.
MaxQBiO14737.
PaxDbiO14737.
PeptideAtlasiO14737.
PRIDEiO14737.
TopDownProteomicsiO14737-1. [O14737-1]

PTM databases

iPTMnetiO14737.
PhosphoSiteiO14737.

Expressioni

Tissue specificityi

Widely expressed. Highest levels in heart, testis, kidney, pituitary gland, adrenal gland and placenta.

Developmental stagei

Expression in fetal tissues is significantly lower than in adult tissues.

Inductioni

Activated in cells undergoing apoptosis.

Gene expression databases

BgeeiO14737.
CleanExiHS_PDCD5.
ExpressionAtlasiO14737. baseline and differential.
GenevisibleiO14737. HS.

Organism-specific databases

HPAiHPA018471.

Interactioni

GO - Molecular functioni

  • beta-tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114588. 26 interactions.
DIPiDIP-50602N.
IntActiO14737. 19 interactions.
MINTiMINT-5002173.
STRINGi9606.ENSP00000466214.

Structurei

Secondary structure

1
125
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1918Combined sources
Helixi26 – 4722Combined sources
Helixi50 – 6213Combined sources
Helixi64 – 8017Combined sources
Helixi89 – 9911Combined sources
Beta strandi100 – 1023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YYBNMR-A1-26[»]
2CRUNMR-A9-113[»]
2K6BNMR-A2-112[»]
ProteinModelPortaliO14737.
SMRiO14737. Positions 2-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14737.

Family & Domainsi

Sequence similaritiesi

Belongs to the PDCD5 family.Curated

Phylogenomic databases

eggNOGiKOG3431. Eukaryota.
COG2118. LUCA.
GeneTreeiENSGT00390000011085.
HOGENOMiHOG000194121.
HOVERGENiHBG053536.
InParanoidiO14737.
KOiK06875.
OMAiQQLVMLA.
OrthoDBiEOG7G7KS0.
PhylomeDBiO14737.

Family and domain databases

Gene3Di1.10.8.140. 1 hit.
InterProiIPR002836. PDCD5-related.
[Graphical view]
PANTHERiPTHR10840. PTHR10840. 1 hit.
PfamiPF01984. dsDNA_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF015730. TFAR19. 1 hit.
SUPFAMiSSF46950. SSF46950. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O14737-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADEELEALR RQRLAELQAK HGDPGDAAQQ EAKHREAEMR NSILAQVLDQ
60 70 80 90 100
SARARLSNLA LVKPEKTKAV ENYLIQMARY GQLSEKVSEQ GLIEILKKVS
110 120
QQTEKTTTVK FNRRKVMDSD EDDDY
Length:125
Mass (Da):14,285
Last modified:January 23, 2007 - v3
Checksum:i9569E0679C3DC20D
GO
Isoform 2 (identifier: O14737-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     89-125: EQGLIEILKK...VMDSDEDDDY → LDSLEELYCY...LTLRRNCWRE

Note: No experimental confirmation available.
Show »
Length:129
Mass (Da):14,997
Checksum:i222EF19836188BA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041E → K in CAG33215 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei89 – 12537EQGLI…EDDDY → LDSLEELYCYLLYQNMASKG QLHLHWITEFLLTLRRNCWR E in isoform 2. 1 PublicationVSP_056203Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014955 mRNA. Translation: AAD11579.1.
BT006694 mRNA. Translation: AAP35340.1.
AK293486 mRNA. Translation: BAG56975.1.
CR456934 mRNA. Translation: CAG33215.1.
AC008474 Genomic DNA. No translation available.
BC015519 mRNA. Translation: AAH15519.1.
CCDSiCCDS12423.1. [O14737-1]
PIRiJG0192.
RefSeqiNP_004699.1. NM_004708.3. [O14737-1]
XP_005259449.1. XM_005259392.3. [O14737-2]
UniGeneiHs.443831.

Genome annotation databases

EnsembliENST00000419343; ENSP00000476525; ENSG00000105185. [O14737-2]
ENST00000590247; ENSP00000466214; ENSG00000105185. [O14737-1]
GeneIDi9141.
KEGGihsa:9141.
UCSCiuc002ntl.4. human. [O14737-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014955 mRNA. Translation: AAD11579.1.
BT006694 mRNA. Translation: AAP35340.1.
AK293486 mRNA. Translation: BAG56975.1.
CR456934 mRNA. Translation: CAG33215.1.
AC008474 Genomic DNA. No translation available.
BC015519 mRNA. Translation: AAH15519.1.
CCDSiCCDS12423.1. [O14737-1]
PIRiJG0192.
RefSeqiNP_004699.1. NM_004708.3. [O14737-1]
XP_005259449.1. XM_005259392.3. [O14737-2]
UniGeneiHs.443831.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YYBNMR-A1-26[»]
2CRUNMR-A9-113[»]
2K6BNMR-A2-112[»]
ProteinModelPortaliO14737.
SMRiO14737. Positions 2-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114588. 26 interactions.
DIPiDIP-50602N.
IntActiO14737. 19 interactions.
MINTiMINT-5002173.
STRINGi9606.ENSP00000466214.

PTM databases

iPTMnetiO14737.
PhosphoSiteiO14737.

Polymorphism and mutation databases

BioMutaiPDCD5.

Proteomic databases

EPDiO14737.
MaxQBiO14737.
PaxDbiO14737.
PeptideAtlasiO14737.
PRIDEiO14737.
TopDownProteomicsiO14737-1. [O14737-1]

Protocols and materials databases

DNASUi9141.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000419343; ENSP00000476525; ENSG00000105185. [O14737-2]
ENST00000590247; ENSP00000466214; ENSG00000105185. [O14737-1]
GeneIDi9141.
KEGGihsa:9141.
UCSCiuc002ntl.4. human. [O14737-1]

Organism-specific databases

CTDi9141.
GeneCardsiPDCD5.
HGNCiHGNC:8764. PDCD5.
HPAiHPA018471.
MIMi604583. gene.
neXtProtiNX_O14737.
PharmGKBiPA33114.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3431. Eukaryota.
COG2118. LUCA.
GeneTreeiENSGT00390000011085.
HOGENOMiHOG000194121.
HOVERGENiHBG053536.
InParanoidiO14737.
KOiK06875.
OMAiQQLVMLA.
OrthoDBiEOG7G7KS0.
PhylomeDBiO14737.

Miscellaneous databases

EvolutionaryTraceiO14737.
GeneWikiiPDCD5.
GenomeRNAii9141.
NextBioi34283.
PROiO14737.
SOURCEiSearch...

Gene expression databases

BgeeiO14737.
CleanExiHS_PDCD5.
ExpressionAtlasiO14737. baseline and differential.
GenevisibleiO14737. HS.

Family and domain databases

Gene3Di1.10.8.140. 1 hit.
InterProiIPR002836. PDCD5-related.
[Graphical view]
PANTHERiPTHR10840. PTHR10840. 1 hit.
PfamiPF01984. dsDNA_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF015730. TFAR19. 1 hit.
SUPFAMiSSF46950. SSF46950. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Liu H.T., Wang Y.G., Zhang Y.M., Song Q.S., Di C.H., Chen G., Tang J., Ma D.L.
    Biochem. Biophys. Res. Commun. 254:203-210(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Erythroleukemia.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Platelet.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Solution structure of programmed cell death 5."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 9-113.
  21. "Structure-function correlation of human programmed cell death 5 protein."
    Yao H., Xu L., Feng Y., Liu D., Chen Y., Wang J.
    Arch. Biochem. Biophys. 486:141-149(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-112.

Entry informationi

Entry nameiPDCD5_HUMAN
AccessioniPrimary (citable) accession number: O14737
Secondary accession number(s): B4DE64, Q53YC9, Q6IB70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.