O75340 (PDCD6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.11 Ref.15
Subunit structure	Self-associates By similarity. Homodimer. Interacts with PEF1. Interacts with RBM22. Interacts with PLSCR4, ANXA7 and TSG101. Interacts with SEC31A, PDCD6IP, and the N-termini of ANXA11 and PLSCR3 in a calcium-dependent manner. Interacts with DAPK1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18
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. 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
Sequence similarities	Contains 5 EF-hand domains.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Endoplasmic reticulum Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Calcium Metal-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara apoptotic signaling pathway Traceable author statement PubMed 8560270. Source: ProtInc cellular response to stress Inferred from direct assay Ref.17. Source: UniProtKB intracellular protein transport Inferred from direct assay Ref.17. Source: UniProtKB response to calcium ion Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasmic vesicle Inferred from direct assay Ref.17. Source: UniProtKB endoplasmic reticulum Inferred from direct assay PubMed 17196169. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 17196169Ref.17. Source: UniProtKB
Molecular_function	binding, bridging Inferred from mutant phenotype Ref.15. Source: UniProtKB calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DAPK1	P53355	3	EBI-352915,EBI-358616
PDCD6IP	Q8WUM4	5	EBI-352915,EBI-310624
PLSCR3	Q9NRY6	9	EBI-352915,EBI-750734
SEC31A	O94979	6	EBI-352915,EBI-1767898

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)

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 191

191

Programmed cell death protein 6

PRO_0000073729

Regions

Domain

23 – 58

36

EF-hand 1

Domain

59 – 89

31

EF-hand 2

Domain

90 – 125

36

EF-hand 3

Domain

126 – 161

36

EF-hand 4

Domain

162 – 191

30

EF-hand 5

Calcium binding

36 – 47

12

1

Calcium binding

73 – 84

12

2 Potential

Calcium binding

103 – 114

12

3

Calcium binding

169 – 181

13

4

Natural variations

Alternative sequence

70 – 191

122

Missing in isoform 3.

VSP_045542

Alternative sequence

121 – 122

2

Missing in isoform 2.

VSP_045113

Natural variant

123

1

G → C in a breast cancer sample; somatic mutation. Ref.19

VAR_035459

Experimental info

Mutagenesis

47

1

E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-114. Ref.13 Ref.14

Mutagenesis

57

1

W → A: Reduces the interaction with PDCD6IP and ANXA7. Ref.14

Mutagenesis

60

1

F → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. Ref.14

Mutagenesis

91

1

Y → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. Ref.14

Mutagenesis

95

1

W → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. Ref.14

Mutagenesis

114

1

E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-47. Ref.13 Ref.14

Mutagenesis

180

1

Y → A: Abolishes the interaction with PDCD6IP, TSG101, ANXA7 and ANXA11. Ref.14

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

191

Helix Strand Turn

Details...

Helix

26 – 35

10

Beta strand

36 – 40

5

Beta strand

41 – 43

3

Helix

45 – 51

7

Beta strand

55 – 58

4

Helix

62 – 72

11

Beta strand

74 – 80

7

Helix

82 – 102

21

Beta strand

107 – 110

4

Helix

112 – 121

10

Helix

128 – 138

11

Beta strand

143 – 147

5

Helix

148 – 168

21

Beta strand

172 – 174

3

Helix

180 – 188

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: D0B5944CF3C696AD	FASTA	191	21,868
	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
	Isoform 2 [UniParc]. Checksum: 8F93724C044DD93A	FASTA	189	21,664
	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 GYRLSDQFHD ILIRKFDRQG RGQIAFDDFI QGCIVLQRLT DIFRRYDTDQ DGWIQVSYEQ YLSMVFSIV
	Isoform 3 [UniParc]. Checksum: 8410709B76C52B47	FASTA	69	7,349
	10 20 30 40 50 60 MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGTWTPF NPVTVRSII

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[15]	"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.
[16]	"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].
[17]	"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.
[18]	"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.
[19]	"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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00025277.
IPI00967847.

RefSeq

NP_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.

UniGene

Hs.50823.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZN8	X-ray	2.70	A	2-191	[»]
2ZN9	X-ray	2.40	A/B	20-191	[»]
2ZND	X-ray	1.70	A	20-191	[»]
2ZNE	X-ray	2.20	A/B	24-191	[»]
2ZRS	X-ray	3.10	A/B/C/D/E/F/G/H	24-191	[»]
2ZRT	X-ray	3.30	A/B/C/D/E/F/G/H	24-191	[»]
3AAJ	X-ray	2.40	A/B	24-191	[»]
3AAK	X-ray	2.70	A	20-191	[»]

ProteinModelPortal

O75340.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33217N.

IntAct

O75340. 26 interactions.

MINT

MINT-5000341.

STRING

9606.ENSP00000323816.

PTM databases

PhosphoSite

O75340.

Proteomic databases

PRIDE

O75340.

Protocols and materials databases

DNASU

10016.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264933; ENSP00000264933; ENSG00000249915.
ENST00000505221; ENSP00000422085; ENSG00000249915.
ENST00000507528; ENSP00000423815; ENSG00000249915.

GeneID

10016.

KEGG

hsa:10016.

UCSC

uc003jat.1. human.

Organism-specific databases

CTD

10016.

GeneCards

GC05P000258.

HGNC

HGNC:8765. PDCD6.

MIM

601057. gene.

neXtProt

NX_O75340.

PharmGKB

PA33115.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HOG000231984.

HOVERGEN

HBG004492.

OMA

NGWITIN.

OrthoDB

EOG4H464S.

Gene expression databases

ArrayExpress

O75340.

Bgee

O75340.

CleanEx

HS_ALG2.
HS_PDCD6.

Genevestigator

O75340.

GermOnline

ENSG00000063438. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]

Pfam

PF13499. EF_hand_5. 1 hit.
[Graphical view]

SMART

SM00054. EFh. 5 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PDCD6. human.

EvolutionaryTrace

O75340.

GenomeRNAi

10016.

NextBio

37841.

SOURCE

Search...

Entry information

Entry name

PDCD6_HUMAN

Accession

Primary (citable) accession number: O75340
Secondary accession number(s): B2RD16 , E7ESR3, Q2YDC2, Q5TZS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.