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O75340

- PDCD6_HUMAN

UniProt

O75340 - PDCD6_HUMAN

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Protein
Programmed cell death protein 6
Gene
PDCD6, ALG2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 SHISA5.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi36 – 47121
Add
BLAST
Calcium bindingi73 – 84122 Reviewed prediction
Add
BLAST
Calcium bindingi103 – 114123
Add
BLAST
Calcium bindingi169 – 181134
Add
BLAST

GO - Molecular functioni

  1. binding, bridging Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. calcium-dependent cysteine-type endopeptidase activity Source: RefGenome
  4. calcium-dependent protein binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. protein dimerization activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  2. angiogenesis Source: UniProtKB-KW
  3. apoptotic signaling pathway Source: ProtInc
  4. cellular response to heat Source: UniProtKB
  5. intracellular protein transport Source: UniProtKB
  6. negative regulation of TOR signaling Source: UniProtKB
  7. negative regulation of protein kinase B signaling Source: UniProtKB
  8. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  9. positive regulation of angiogenesis Source: UniProtKB
  10. positive regulation of endothelial cell migration Source: UniProtKB
  11. positive regulation of endothelial cell proliferation Source: UniProtKB
  12. proteolysis Source: RefGenome
  13. response to calcium ion Source: UniProtKB
  14. vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Apoptosis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Programmed cell death protein 6
Alternative name(s):
Apoptosis-linked gene 2 protein
Probable calcium-binding protein ALG-2
Gene namesi
Name:PDCD6
Synonyms:ALG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:8765. PDCD6.

Subcellular locationi

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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. endosome Source: UniProtKB-SubCell
  6. extracellular vesicular exosome Source: UniProt
  7. nuclear membrane Source: UniProtKB-SubCell
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-114. 2 Publications
Mutagenesisi57 – 571W → A: Reduces the interaction with PDCD6IP and ANXA7. 1 Publication
Mutagenesisi60 – 601F → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. 1 Publication
Mutagenesisi91 – 911Y → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. 1 Publication
Mutagenesisi95 – 951W → A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11. 1 Publication
Mutagenesisi114 – 1141E → A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-47. 2 Publications
Mutagenesisi122 – 1221F → A: Increases interaction with PDCD6IP and ANXA7. Impairs interaction with ANXA11. Augments stauroporine-induced cell death. 1 Publication
Mutagenesisi122 – 1221F → G: Increases interaction with PDCD6IP. Impairs interaction with ANXA11. 1 Publication
Mutagenesisi122 – 1221F → S: Increases interaction with PDCD6IP. Impairs interaction with ANAX7 and ANXA11. 1 Publication
Mutagenesisi122 – 1221F → W: Impairs interaction with ANXA11. 1 Publication
Mutagenesisi180 – 1801Y → A: Abolishes the interaction with PDCD6IP, TSG101, ANXA7 and ANXA11. 1 Publication

Organism-specific databases

PharmGKBiPA33115.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 191190Programmed cell death protein 6
PRO_0000073729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO75340.
PRIDEiO75340.

PTM databases

PhosphoSiteiO75340.

Expressioni

Gene expression databases

ArrayExpressiO75340.
BgeeiO75340.
CleanExiHS_ALG2.
HS_PDCD6.
GenevestigatoriO75340.

Organism-specific databases

HPAiHPA047221.

Interactioni

Subunit structurei

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 ANXA11.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAPK1P533553EBI-352915,EBI-358616
KDRP359684EBI-352915,EBI-1005487
PDCD6IPQ8WUM45EBI-352915,EBI-310624
PLSCR3Q9NRY69EBI-352915,EBI-750734
PTPN23Q9H3S73EBI-352915,EBI-724478
SEC31AO949796EBI-352915,EBI-1767898

Protein-protein interaction databases

BioGridi115333. 35 interactions.
DIPiDIP-33217N.
IntActiO75340. 30 interactions.
MINTiMINT-5000341.
STRINGi9606.ENSP00000323816.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 3510
Beta strandi36 – 405
Beta strandi41 – 433
Helixi45 – 517
Beta strandi55 – 584
Helixi62 – 7211
Beta strandi74 – 807
Helixi82 – 10221
Beta strandi107 – 1104
Helixi112 – 12110
Helixi128 – 13811
Beta strandi143 – 1475
Helixi148 – 16821
Beta strandi172 – 1743
Helixi180 – 1889

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO75340.
SMRiO75340. Positions 24-191.

Miscellaneous databases

EvolutionaryTraceiO75340.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 5836EF-hand 1
Add
BLAST
Domaini59 – 8931EF-hand 2
Add
BLAST
Domaini90 – 12536EF-hand 3
Add
BLAST
Domaini126 – 16136EF-hand 4
Add
BLAST
Domaini162 – 19130EF-hand 5
Add
BLAST

Sequence similaritiesi

Contains 5 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000231984.
HOVERGENiHBG004492.
OMAiFLWNIFQ.
OrthoDBiEOG7RV9FM.
PhylomeDBiO75340.
TreeFamiTF314682.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 5 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75340-1) [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

MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ    50
ALSNGTWTPF NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR 100
TYDRDNSGMI DKNELKQALS GFGYRLSDQF HDILIRKFDR QGRGQIAFDD 150
FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY EQYLSMVFSI V 191
Length:191
Mass (Da):21,868
Last modified:November 1, 1998 - v1
Checksum:iD0B5944CF3C696AD
GO
Isoform 2 (identifier: O75340-2) [UniParc]FASTAAdd to Basket

Also known as: ALG-2(delta)GF122

The sequence of this isoform differs from the canonical sequence as follows:
     121-122: Missing.

Show »
Length:189
Mass (Da):21,664
Checksum:i8F93724C044DD93A
GO
Isoform 3 (identifier: O75340-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     70-191: Missing.

Note: No experimental confirmation available.

Show »
Length:69
Mass (Da):7,349
Checksum:i8410709B76C52B47
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti123 – 1231G → C in a breast cancer sample; somatic mutation. 1 Publication
VAR_035459

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei70 – 191122Missing in isoform 3.
VSP_045542Add
BLAST
Alternative sequencei121 – 1222Missing in isoform 2.
VSP_045113

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3854.1. [O75340-1]
CCDS58940.1. [O75340-2]
CCDS58941.1. [O75340-3]
RefSeqiNP_001254485.1. NM_001267556.1. [O75340-2]
NP_001254486.1. NM_001267557.1.
NP_001254487.1. NM_001267558.1.
NP_001254488.1. NM_001267559.1. [O75340-3]
NP_037364.1. NM_013232.3. [O75340-1]
UniGeneiHs.50823.

Genome annotation databases

EnsembliENST00000264933; ENSP00000264933; ENSG00000249915. [O75340-1]
ENST00000505221; ENSP00000422085; ENSG00000249915. [O75340-3]
ENST00000507528; ENSP00000423815; ENSG00000249915. [O75340-2]
GeneIDi10016.
KEGGihsa:10016.
UCSCiuc003jat.1. human. [O75340-1]
uc003jau.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS3854.1. [O75340-1 ]
CCDS58940.1. [O75340-2 ]
CCDS58941.1. [O75340-3 ]
RefSeqi NP_001254485.1. NM_001267556.1. [O75340-2 ]
NP_001254486.1. NM_001267557.1.
NP_001254487.1. NM_001267558.1.
NP_001254488.1. NM_001267559.1. [O75340-3 ]
NP_037364.1. NM_013232.3. [O75340-1 ]
UniGenei Hs.50823.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali O75340.
SMRi O75340. Positions 24-191.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115333. 35 interactions.
DIPi DIP-33217N.
IntActi O75340. 30 interactions.
MINTi MINT-5000341.
STRINGi 9606.ENSP00000323816.

PTM databases

PhosphoSitei O75340.

Proteomic databases

MaxQBi O75340.
PRIDEi O75340.

Protocols and materials databases

DNASUi 10016.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264933 ; ENSP00000264933 ; ENSG00000249915 . [O75340-1 ]
ENST00000505221 ; ENSP00000422085 ; ENSG00000249915 . [O75340-3 ]
ENST00000507528 ; ENSP00000423815 ; ENSG00000249915 . [O75340-2 ]
GeneIDi 10016.
KEGGi hsa:10016.
UCSCi uc003jat.1. human. [O75340-1 ]
uc003jau.2. human.

Organism-specific databases

CTDi 10016.
GeneCardsi GC05P000258.
HGNCi HGNC:8765. PDCD6.
HPAi HPA047221.
MIMi 601057. gene.
neXtProti NX_O75340.
PharmGKBi PA33115.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000231984.
HOVERGENi HBG004492.
OMAi FLWNIFQ.
OrthoDBi EOG7RV9FM.
PhylomeDBi O75340.
TreeFami TF314682.

Miscellaneous databases

ChiTaRSi PDCD6. human.
EvolutionaryTracei O75340.
GeneWikii PDCD6.
GenomeRNAii 10016.
NextBioi 37841.
PROi O75340.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75340.
Bgeei O75340.
CleanExi HS_ALG2.
HS_PDCD6.
Genevestigatori O75340.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF13499. EF-hand_7. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 5 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-123.

Entry informationi

Entry nameiPDCD6_HUMAN
AccessioniPrimary (citable) accession number: O75340
Secondary accession number(s): B2RD16
, E7ESR3, Q2YDC2, Q5TZS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 137 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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