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O75340 (PDCD6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Programmed cell death protein 6
Alternative name(s):
Apoptosis-linked gene 2 protein
Probable calcium-binding protein ALG-2
Gene names
Name:PDCD6
Synonyms:ALG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. May mediate Ca2+-regulated signals along the death pathway By similarity. Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphoprylation of the Akt signaling pathway. Seems to play a role in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Isoform 2 has a lower Ca2+ affinity than isoform 1. Isoform 1 and, to a lesser extend, isoform 2, can stabilize SHISA5. Ref.11 Ref.14 Ref.16 Ref.17 Ref.20

Subunit structure

Isoform 1 and isoform 2 self-associate; probably forming homodimers. Interacts with SHISA5, PEF1, RBM22, PLSCR4, ANXA7, TSG101 and DAPK1. Interacts with PDCD6IP, SEC31A, ANXA11 (via N-terminus), PLSCR3 (via N-terminus) and MCOLN1; the interactions are calcium-dependent. Isoform 2 does not interact with SHISA5, PDCD6IP, TSG101, ANXA7 and ANXA11. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.20 Ref.22 Ref.23

Subcellular location

Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Endosome. Note: Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus. Translocated from the cytoplasm to the nucleus after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules. Ref.13 Ref.17 Ref.19

Sequence similarities

Contains 5 EF-hand domains.

Ontologies

Keywords
   Biological processAngiogenesis
Apoptosis
   Cellular componentEndoplasmic reticulum
Endosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandCalcium
Metal-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic signaling pathway

Traceable author statement PubMed 8560270. Source: ProtInc

cellular response to heat

Inferred from direct assay Ref.19. Source: UniProtKB

intracellular protein transport

Inferred from direct assay Ref.19. Source: UniProtKB

negative regulation of TOR signaling

Inferred from direct assay Ref.20. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from direct assay Ref.20. Source: UniProtKB

negative regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of angiogenesis

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of endothelial cell migration

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from direct assay Ref.20. Source: UniProtKB

response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

vascular endothelial growth factor receptor-2 signaling pathway

Inferred from direct assay Ref.20. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.19. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay Ref.19. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 17196169. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 17196169Ref.19. Source: UniProtKB

   Molecular_functionbinding, bridging

Inferred from mutant phenotype Ref.16. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-dependent protein binding

Inferred from physical interaction PubMed 17196169PubMed 17214967Ref.15. Source: UniProtKB

protein dimerization activity

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75340-1)

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.
Isoform 2 (identifier: O75340-2)

Also known as: ALG-2(delta)GF122;

The sequence of this isoform differs from the canonical sequence as follows:
     121-122: Missing.
Isoform 3 (identifier: O75340-3)

The sequence of this isoform differs from the canonical sequence as follows:
     70-191: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 191190Programmed cell death protein 6
PRO_0000073729

Regions

Domain23 – 5836EF-hand 1
Domain59 – 8931EF-hand 2
Domain90 – 12536EF-hand 3
Domain126 – 16136EF-hand 4
Domain162 – 19130EF-hand 5
Calcium binding36 – 47121
Calcium binding73 – 84122 Potential
Calcium binding103 – 114123
Calcium binding169 – 181134

Amino acid modifications

Modified residue21N-acetylalanine Ref.21

Natural variations

Alternative sequence70 – 191122Missing in isoform 3.
VSP_045542
Alternative sequence121 – 1222Missing in isoform 2.
VSP_045113
Natural variant1231G → C in a breast cancer sample; somatic mutation. Ref.24
VAR_035459

Experimental info

Mutagenesis471E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-114. Ref.13 Ref.15
Mutagenesis571W → A: Reduces the interaction with PDCD6IP and ANXA7. Ref.15
Mutagenesis601F → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. Ref.15
Mutagenesis911Y → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. Ref.15
Mutagenesis951W → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. Ref.15
Mutagenesis1141E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-47. Ref.13 Ref.15
Mutagenesis1221F → A: Increases interaction with PDCD6IP and ANXA7. Impairs interaction with ANXA11. Augments stauroporine-induced cell death. Ref.23
Mutagenesis1221F → G: Increases interaction with PDCD6IP. Impairs interaction with ANXA11. Ref.23
Mutagenesis1221F → S: Increases interaction with PDCD6IP. Impairs interaction with ANAX7 and ANXA11. Ref.23
Mutagenesis1221F → W: Impairs interaction with ANXA11. Ref.23
Mutagenesis1801Y → A: Abolishes the interaction with PDCD6IP, TSG101, ANXA7 and ANXA11. Ref.15

Secondary structure

............................ 191
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D0B5944CF3C696AD

FASTA19121,868
        10         20         30         40         50         60 
MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGTWTPF 

        70         80         90        100        110        120 
NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR TYDRDNSGMI DKNELKQALS 

       130        140        150        160        170        180 
GFGYRLSDQF HDILIRKFDR QGRGQIAFDD FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY 

       190 
EQYLSMVFSI V 

« Hide

Isoform 2 (ALG-2(delta)GF122) [UniParc].

Checksum: 8F93724C044DD93A
Show »

FASTA18921,664
Isoform 3 [UniParc].

Checksum: 8410709B76C52B47
Show »

FASTA697,349

References

« Hide 'large scale' references
[1]Ganjei J.K., D'Adamio L.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Urcelay E., Ibarreta D., Parrilla R., Ayuso M.S.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[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. expand/collapse author list , 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 1).
Tissue: Cerebellum.
[4]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS 1; 2 AND 3).
Tissue: Colon, Ovary and Placenta.
[8]"Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner."
Kitaura Y., Matsumoto S., Satoh H., Hitomi K., Maki M.
J. Biol. Chem. 276:14053-14058(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEF1.
[9]"Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized by dimerization through their fifth EF-hand regions."
Kitaura Y., Satoh H., Takahashi H., Shibata H., Maki M.
Arch. Biochem. Biophys. 399:12-18(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEF1.
[10]"ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner."
Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.
Biochem. Biophys. Res. Commun. 291:1166-1172(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANXA11.
[11]"Programmed cell death 6 (PDCD6) protein interacts with death-associated protein kinase 1 (DAPk1): additive effect on apoptosis via caspase-3 dependent pathway."
Lee J.H., Rho S.B., Chun T.
Biotechnol. Lett. 27:1011-1015(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DAPK1.
[12]"Nuclear translocation of the calcium-binding protein ALG-2 induced by the RNA-binding protein RBM22."
Montaville P., Dai Y., Cheung C.Y., Giller K., Becker S., Michalak M., Webb S.E., Miller A.L., Krebs J.
Biochim. Biophys. Acta 1763:1335-1343(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBM22.
[13]"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.
Mol. Biol. Cell 17:4876-4887(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEC31A AND PDCD6IP, MUTAGENESIS OF GLU-47 AND GLU-114, SUBCELLULAR LOCATION.
[14]"The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane."
Draeby I., Woods Y.L., la Cour J.M., Mollerup J., Bourdon J.C., Berchtold M.W.
Arch. Biochem. Biophys. 467:87-94(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH WITH SHISA5.
[15]"Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLSCR3; PLSCR4; PDCD6IP; ANXA7; ANXA11; SEC31A AND TSG101, MUTAGENESIS OF GLU-47; TRP-57; PHE-60; TYR-91; TRP-95; GLU-114 AND TYR-180.
[16]"Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101."
Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H., Shibata H., Maki M.
Biochem. Biophys. Res. Commun. 386:237-241(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1."
Vergarajauregui S., Martina J.A., Puertollano R.
J. Biol. Chem. 284:36357-36366(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MCOLN1.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7."
Janowicz A., Michalak M., Krebs J.
Biochim. Biophys. Acta 1813:1045-1049(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[20]"Programmed cell death 6 (PDCD6) inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of VEGFR-2."
Rho S.B., Song Y.J., Lim M.C., Lee S.H., Kim B.R., Park S.Y.
Cell. Signal. 24:131-139(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KDR.
[21]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[22]"Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide complex: Ca2+/EF3-driven arginine switch mechanism."
Suzuki H., Kawasaki M., Inuzuka T., Okumura M., Kakiuchi T., Shibata H., Wakatsuki S., Maki M.
Structure 16:1562-1573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-191 IN COMPLEXES WITH CALCIUM; ZINC AND PDCD6IP, SUBUNIT, INTERACTION WITH PDCD6IP.
[23]"Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition."
Inuzuka T., Suzuki H., Kawasaki M., Shibata H., Wakatsuki S., Maki M.
BMC Struct. Biol. 10:25-25(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-191, INTERACTION WITH PDCD6IP; TSG101; ANXA7 AND ANXA11, MUTAGENESIS OF PHE-122.
[24]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-123.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035606 mRNA. Translation: AAC27697.1.
U58773 mRNA. Translation: AAF14336.1.
AK315370 mRNA. Translation: BAG37763.1.
BT020072 mRNA. Translation: AAV38875.1.
AC010442 Genomic DNA. No translation available.
AC021087 Genomic DNA. No translation available.
AC118458 Genomic DNA. No translation available.
CH471235 Genomic DNA. Translation: EAW50991.1.
BC012384 mRNA. Translation: AAH12384.1.
BC106706 mRNA. Translation: AAI06707.1.
BC110291 mRNA. Translation: AAI10292.1.
CB991882 mRNA. No translation available.
RefSeqNP_001254485.1. NM_001267556.1.
NP_001254486.1. NM_001267557.1.
NP_001254487.1. NM_001267558.1.
NP_001254488.1. NM_001267559.1.
NP_037364.1. NM_013232.3.
UniGeneHs.50823.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZN8X-ray2.70A2-191[»]
2ZN9X-ray2.40A/B20-191[»]
2ZNDX-ray1.70A20-191[»]
2ZNEX-ray2.20A/B24-191[»]
2ZRSX-ray3.10A/B/C/D/E/F/G/H24-191[»]
2ZRTX-ray3.30A/B/C/D/E/F/G/H24-191[»]
3AAJX-ray2.40A/B24-191[»]
3AAKX-ray2.70A20-191[»]
ProteinModelPortalO75340.
SMRO75340. Positions 24-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115333. 34 interactions.
DIPDIP-33217N.
IntActO75340. 30 interactions.
MINTMINT-5000341.
STRING9606.ENSP00000323816.

PTM databases

PhosphoSiteO75340.

Proteomic databases

PRIDEO75340.

Protocols and materials databases

DNASU10016.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264933; ENSP00000264933; ENSG00000249915. [O75340-1]
ENST00000505221; ENSP00000422085; ENSG00000249915. [O75340-3]
ENST00000507528; ENSP00000423815; ENSG00000249915. [O75340-2]
GeneID10016.
KEGGhsa:10016.
UCSCuc003jat.1. human. [O75340-1]
uc003jau.2. human.

Organism-specific databases

CTD10016.
GeneCardsGC05P000258.
HGNCHGNC:8765. PDCD6.
HPAHPA047221.
MIM601057. gene.
neXtProtNX_O75340.
PharmGKBPA33115.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000231984.
HOVERGENHBG004492.
OMAFLWNIFQ.
OrthoDBEOG7RV9FM.
PhylomeDBO75340.
TreeFamTF314682.

Gene expression databases

ArrayExpressO75340.
BgeeO75340.
CleanExHS_ALG2.
HS_PDCD6.
GenevestigatorO75340.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 5 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDCD6. human.
EvolutionaryTraceO75340.
GeneWikiPDCD6.
GenomeRNAi10016.
NextBio37841.
PROO75340.
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Entry information

Entry namePDCD6_HUMAN
AccessionPrimary (citable) accession number: O75340
Secondary accession number(s): B2RD16 expand/collapse secondary AC list , E7ESR3, Q2YDC2, Q5TZS0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM