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Reviewed, UniProtKB/Swiss-Prot O75340 (PDCD6_HUMAN)

Last modified June 16, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

Interacts with PEF1. Interacts with SEC31A and PDCD6IP in a calcium-dependent manner. Interacts with RBM22. Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Note: Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus. Ref.9

Sequence similarities

Contains 5 EF-hand domains.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentEndoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandCalcium
   Technical term3D-structure
Gene Ontology (GO)
   Biological processapoptosis

Inferred from electronic annotation. Source: UniProtKB-KW

induction of apoptosis by extracellular signals

Traceable author statement. Source: ProtInc

response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-dependent protein binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191Programmed 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 Potential
Calcium binding73 – 84122 Potential
Calcium binding103 – 114123 Potential

Natural variations

Natural variant1231G → C in a breast cancer sample; somatic mutation. Ref.11
VAR_035459

Experimental info

Mutagenesis471E → A: Loss of interaction with SEC31A and loss of localization to the endoplasmic reticulum; when associated with A-114. Ref.9
Mutagenesis1141E → A: Loss of interaction with SEC31A and loss if localization to the endoplasmic reticulum; when associated with A-47. Ref.9

Sequences

Sequence LengthMass (Da)Tools
O75340-1 [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

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].
[2]Urcelay E., Ibarreta D., Parrilla R., Ayuso M.S.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[6]"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: 11278427] [Abstract]
Cited for: INTERACTION WITH PEF1.
[7]"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: 11883899] [Abstract]
Cited for: INTERACTION WITH PEF1.
[8]"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: 17045351] [Abstract]
Cited for: INTERACTION WITH RBM22.
[9]"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: 16957052] [Abstract]
Cited for: INTERACTION WITH SEC31A AND PDCD6IP, MUTAGENESIS OF GLU-47 AND GLU-114, SUBCELLULAR LOCATION.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-123.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF035606 mRNA. Translation: AAC27697.1.
U58773 mRNA. Translation: AAF14336.1.
AK315370 mRNA. Translation: BAG37763.1.
BT020072 mRNA. Translation: AAV38875.1.
BC012384 mRNA. Translation: AAH12384.1.
BC106706 mRNA. Translation: AAI06707.1.
IPIIPI00025277.
RefSeqNP_037364.1.
UniGeneHs.50823

3D structure databases

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[»]
SMRO75340. Positions 20-188.
ModBaseSearch...

Protein-protein interaction databases

IntActO75340. 13 interactions.

PTM databases

PhosphoSiteO75340.

Proteomic databases

PRIDEO75340.

Genome annotation databases

EnsemblENSG00000063438. Homo sapiens. [Contig view]
GeneID10016.
KEGGhsa:10016.

Organism-specific databases

GeneCardsGC05P000324.
HGNCHGNC:8765. PDCD6.
MIM601057. gene.
PharmGKBPA33115.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO75340.
OMAO75340. ISDNELQ.

Gene expression databases

ArrayExpressO75340.
BgeeO75340.
CleanExHS_ALG2.
HS_PDCD6.
GermOnlineENSG00000063438. Homo sapiens.

Family and domain databases

InterProIPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF00036. efhand. 2 hits.
[Graphical view]
ProDomPD000012. EF-hand. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00054. EFh. 5 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio37841.
SOURCESearch...

Entry information

Entry namePDCD6_HUMAN
AccessionPrimary (citable) accession number: O75340
Secondary accession number(s): B2RD16, Q5TZS0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 5

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents