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Q96F86

- EDC3_HUMAN

UniProt

Q96F86 - EDC3_HUMAN

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Protein

Enhancer of mRNA-decapping protein 3

Gene

EDC3

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

Functioni

Binds single-stranded RNA. In the process of mRNA degradation, may play a role in mRNA decapping. May play a role in spermiogenesis and oogenesis.3 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. RNA metabolic process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
Enhancer of mRNA-decapping protein 3
Alternative name(s):
LSM16 homolog
YjeF N-terminal domain-containing protein 2
Short name:
YjeF_N2
Short name:
hYjeF_N2
YjeF domain-containing protein 1
Gene namesi
Name:EDC3
Synonyms:LSM16, YJDC, YJEFN2
ORF Names:PP844
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:26114. EDC3.

Subcellular locationi

CytoplasmP-body 1 Publication
Note: Processing bodies (PB).

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi204 – 2041F → A: Abolishes interaction with DDX6; when associated with A-206. 1 Publication
Mutagenesisi206 – 2061F → A: Abolishes interaction with DDX6; when associated with A-204. 1 Publication
Mutagenesisi306 – 3061E → A: Abolishes homodimerization and RNA binding; when associated with A-310. 1 Publication
Mutagenesisi310 – 3101V → A: Abolishes homodimerization and RNA binding; when associated with A-306. 1 Publication

Organism-specific databases

PharmGKBiPA142670551.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Enhancer of mRNA-decapping protein 3PRO_0000119054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Phosphoserine2 Publications
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei161 – 1611Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96F86.
PaxDbiQ96F86.
PeptideAtlasiQ96F86.
PRIDEiQ96F86.

PTM databases

PhosphoSiteiQ96F86.

Expressioni

Tissue specificityi

Expressed in theca and granulosa cells in ovary, and in spermatids of the meiotic division part II and apical membrane of Sertoli cells in testis (at protein level). Also expressed in brain and mammary gland.1 Publication

Gene expression databases

BgeeiQ96F86.
CleanExiHS_EDC3.
ExpressionAtlasiQ96F86. baseline and differential.
GenevestigatoriQ96F86.

Organism-specific databases

HPAiHPA040650.
HPA044206.

Interactioni

Subunit structurei

Homodimer (via YjeF N-terminal domain). Forms a complex with DCP1A, DCP2, DDX6 and EDC4/HEDLS, within this complex directly interacts with DCP1A and DDX6. Interacts with ZFP36.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-997311,EBI-997311
DCP1BQ8IZD43EBI-997311,EBI-521595
DDX6P261962EBI-997311,EBI-351257
ZFP36P266512EBI-997311,EBI-374248

Protein-protein interaction databases

BioGridi123144. 20 interactions.
DIPiDIP-35516N.
IntActiQ96F86. 15 interactions.
MINTiMINT-5005528.
STRINGi9606.ENSP00000320503.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi9 – 135Combined sources
Turni16 – 183Combined sources
Beta strandi20 – 2910Combined sources
Turni30 – 334Combined sources
Beta strandi34 – 429Combined sources
Beta strandi48 – 558Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 667Combined sources
Helixi206 – 2105Combined sources
Helixi215 – 22511Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi278 – 2803Combined sources
Helixi284 – 29613Combined sources
Helixi301 – 31919Combined sources
Beta strandi336 – 3416Combined sources
Helixi345 – 35915Combined sources
Beta strandi363 – 3675Combined sources
Helixi376 – 38510Combined sources
Beta strandi391 – 3944Combined sources
Helixi396 – 3983Combined sources
Beta strandi405 – 4106Combined sources
Helixi419 – 4213Combined sources
Helixi423 – 43513Combined sources
Beta strandi439 – 4435Combined sources
Beta strandi456 – 4638Combined sources
Helixi469 – 4713Combined sources
Beta strandi473 – 4775Combined sources
Helixi483 – 4886Combined sources
Turni496 – 4994Combined sources
Beta strandi501 – 5066Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VC8X-ray1.31A1-82[»]
2WAXX-ray2.30B/D192-228[»]
2WAYX-ray2.30B/D192-228[»]
3D3JX-ray2.80A203-508[»]
3D3KX-ray2.20A/B/C/D250-508[»]
ProteinModelPortaliQ96F86.
SMRiQ96F86. Positions 3-74, 197-226, 258-507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96F86.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 22837DFDFPROSITE-ProRule annotationAdd
BLAST
Domaini283 – 487205YjeF N-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7979Required for P-body targeting and interaction with DCP1ABy similarityAdd
BLAST
Regioni191 – 296106Required for interaction with DDX6By similarityAdd
BLAST

Domaini

The DFDF domain is unstructured by itself. It assumes a helical fold upon interaction with DDX6.1 Publication

Sequence similaritiesi

Belongs to the EDC3 family.Curated
Contains 1 DFDF domain.PROSITE-ProRule annotation
Contains 1 YjeF N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG271303.
GeneTreeiENSGT00390000016435.
HOGENOMiHOG000231481.
HOVERGENiHBG079428.
InParanoidiQ96F86.
KOiK12615.
OMAiPEVTFRA.
OrthoDBiEOG7H793B.
PhylomeDBiQ96F86.
TreeFamiTF324695.

Family and domain databases

Gene3Di3.40.50.10260. 1 hit.
InterProiIPR025762. DFDF.
IPR019050. FDF_dom.
IPR025609. Lsm14_N.
IPR004443. YjeF_N_dom.
[Graphical view]
PfamiPF09532. FDF. 1 hit.
PF12701. LSM14. 1 hit.
PF03853. YjeF_N. 1 hit.
[Graphical view]
SUPFAMiSSF64153. SSF64153. 1 hit.
PROSITEiPS51512. DFDF. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96F86-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP
60 70 80 90 100
EVTFRAGDIT ELKILEIPGP GDNQHFGDLH QTELGPSGAG CQVGINQNGT
110 120 130 140 150
GKFVKKPASS SSAPQNIPKR TDVKSQDVAV SPQQQQCSKS YVDRHMESLS
160 170 180 190 200
QSKSFRRRHN SWSSSSRHPN QATPKKSGLK NGQMKNKDDE CFGDDIEEIP
210 220 230 240 250
DTDFDFEGNL ALFDKAAVFE EIDTYERRSG TRSRGIPNER PTRYRHDENI
260 270 280 290 300
LESEPIVYRR IIVPHNVSKE FCTDSGLVVP SISYELHKKL LSVAEKHGLT
310 320 330 340 350
LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG
360 370 380 390 400
ISCGRHLANH DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLKDLP
410 420 430 440 450
TSPVDLVINC LDCPENVFLR DQPWYKAAVA WANQNRAPVL SIDPPVHEVE
460 470 480 490 500
QGIDAKWSLA LGLPLPLGEH AGRIYLCDIG IPQQVFQEVG INYHSPFGCK

FVIPLHSA
Length:508
Mass (Da):56,078
Last modified:December 1, 2001 - v1
Checksum:i95346F484FCFC3EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741Q → R in BAB15001. (PubMed:14702039)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193058 mRNA. Translation: AAG22486.1.
AK024781 mRNA. Translation: BAB15001.1.
AK056339 mRNA. Translation: BAG51682.1.
CH471136 Genomic DNA. Translation: EAW99316.1.
CH471136 Genomic DNA. Translation: EAW99317.1.
CH471136 Genomic DNA. Translation: EAW99318.1.
CH471136 Genomic DNA. Translation: EAW99319.1.
BC011534 mRNA. Translation: AAH11534.1.
BC021271 mRNA. Translation: AAH21271.1.
CCDSiCCDS10267.1.
RefSeqiNP_001135915.1. NM_001142443.1.
NP_001135916.1. NM_001142444.1.
NP_079359.2. NM_025083.3.
UniGeneiHs.682454.
Hs.96852.

Genome annotation databases

EnsembliENST00000315127; ENSP00000320503; ENSG00000179151.
ENST00000426797; ENSP00000401343; ENSG00000179151.
ENST00000568176; ENSP00000455580; ENSG00000179151.
GeneIDi80153.
KEGGihsa:80153.
UCSCiuc002aym.3. human.

Polymorphism databases

DMDMi74731669.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF193058 mRNA. Translation: AAG22486.1 .
AK024781 mRNA. Translation: BAB15001.1 .
AK056339 mRNA. Translation: BAG51682.1 .
CH471136 Genomic DNA. Translation: EAW99316.1 .
CH471136 Genomic DNA. Translation: EAW99317.1 .
CH471136 Genomic DNA. Translation: EAW99318.1 .
CH471136 Genomic DNA. Translation: EAW99319.1 .
BC011534 mRNA. Translation: AAH11534.1 .
BC021271 mRNA. Translation: AAH21271.1 .
CCDSi CCDS10267.1.
RefSeqi NP_001135915.1. NM_001142443.1.
NP_001135916.1. NM_001142444.1.
NP_079359.2. NM_025083.3.
UniGenei Hs.682454.
Hs.96852.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VC8 X-ray 1.31 A 1-82 [» ]
2WAX X-ray 2.30 B/D 192-228 [» ]
2WAY X-ray 2.30 B/D 192-228 [» ]
3D3J X-ray 2.80 A 203-508 [» ]
3D3K X-ray 2.20 A/B/C/D 250-508 [» ]
ProteinModelPortali Q96F86.
SMRi Q96F86. Positions 3-74, 197-226, 258-507.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123144. 20 interactions.
DIPi DIP-35516N.
IntActi Q96F86. 15 interactions.
MINTi MINT-5005528.
STRINGi 9606.ENSP00000320503.

PTM databases

PhosphoSitei Q96F86.

Polymorphism databases

DMDMi 74731669.

Proteomic databases

MaxQBi Q96F86.
PaxDbi Q96F86.
PeptideAtlasi Q96F86.
PRIDEi Q96F86.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315127 ; ENSP00000320503 ; ENSG00000179151 .
ENST00000426797 ; ENSP00000401343 ; ENSG00000179151 .
ENST00000568176 ; ENSP00000455580 ; ENSG00000179151 .
GeneIDi 80153.
KEGGi hsa:80153.
UCSCi uc002aym.3. human.

Organism-specific databases

CTDi 80153.
GeneCardsi GC15M074922.
HGNCi HGNC:26114. EDC3.
HPAi HPA040650.
HPA044206.
MIMi 609842. gene.
neXtProti NX_Q96F86.
PharmGKBi PA142670551.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271303.
GeneTreei ENSGT00390000016435.
HOGENOMi HOG000231481.
HOVERGENi HBG079428.
InParanoidi Q96F86.
KOi K12615.
OMAi PEVTFRA.
OrthoDBi EOG7H793B.
PhylomeDBi Q96F86.
TreeFami TF324695.

Enzyme and pathway databases

Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

ChiTaRSi EDC3. human.
EvolutionaryTracei Q96F86.
GeneWikii EDC3.
GenomeRNAii 80153.
NextBioi 70444.
PROi Q96F86.
SOURCEi Search...

Gene expression databases

Bgeei Q96F86.
CleanExi HS_EDC3.
ExpressionAtlasi Q96F86. baseline and differential.
Genevestigatori Q96F86.

Family and domain databases

Gene3Di 3.40.50.10260. 1 hit.
InterProi IPR025762. DFDF.
IPR019050. FDF_dom.
IPR025609. Lsm14_N.
IPR004443. YjeF_N_dom.
[Graphical view ]
Pfami PF09532. FDF. 1 hit.
PF12701. LSM14. 1 hit.
PF03853. YjeF_N. 1 hit.
[Graphical view ]
SUPFAMi SSF64153. SSF64153. 1 hit.
PROSITEi PS51512. DFDF. 1 hit.
PS51385. YJEF_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Eye and Placenta.
  5. "Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping."
    Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.
    Mol. Cell 20:905-915(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DCP1A; DCP2; DDX6; EDC4 AND ZFP36, SUBCELLULAR LOCATION, FUNCTION.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and hYjeF_N3 comprise the YjeF_N domain protein family in humans with a role in spermiogenesis and oogenesis."
    Rudolph C., Sigruener A., Hartmann A., Orso E., Bals-Pratsch M., Gronwald W., Seifert B., Kalbitzer H.R., Verdorfer I., Luetjens C.M., Ortmann O., Bornstein S.R., Schmitz G.
    Horm. Metab. Res. 39:322-335(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-138 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 1-82.
  15. "Crystal structure of human Edc3 and its functional implications."
    Ling S.H., Decker C.J., Walsh M.A., She M., Parker R., Song H.
    Mol. Cell. Biol. 28:5965-5976(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 250-508, FUNCTION, RNA-BINDING, SUBUNIT, CIRCULAR DICHROISM, MUTAGENESIS OF GLU-306 AND VAL-310.
  16. "Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B."
    Tritschler F., Braun J.E., Eulalio A., Truffault V., Izaurralde E., Weichenrieder O.
    Mol. Cell 33:661-668(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 192-228 IN COMPLEX WITH DDX6, INTERACTION WITH DDX6, MUTAGENESIS OF PHE-204 AND PHE-206, DOMAIN.

Entry informationi

Entry nameiEDC3_HUMAN
AccessioniPrimary (citable) accession number: Q96F86
Secondary accession number(s): B3KPH0, D3DW61, Q9H797
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 116 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 15
    Human chromosome 15: 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

External Data

Dasty 3