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Q96F86

- EDC3_HUMAN

UniProt

Q96F86 - EDC3_HUMAN

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Protein
Enhancer of mRNA-decapping protein 3
Gene
EDC3, LSM16, YJDC, YJEFN2, PP844
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. RNA binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay 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
Note: Processing bodies (PB).1 Publication

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: UniProtKB-SubCell
  2. cytosol Source: Reactome
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 3
PRO_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

ArrayExpressiQ96F86.
BgeeiQ96F86.
CleanExiHS_EDC3.
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
DDX6P261962EBI-997311,EBI-351257
ZFP36P266512EBI-997311,EBI-374248

Protein-protein interaction databases

BioGridi123144. 15 interactions.
DIPiDIP-35516N.
IntActiQ96F86. 14 interactions.
MINTiMINT-5005528.
STRINGi9606.ENSP00000320503.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ96F86.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini192 – 22837DFDF
Add
BLAST
Domaini283 – 487205YjeF N-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7979Required for P-body targeting and interaction with DCP1A By similarity
Add
BLAST
Regioni191 – 296106Required for interaction with DDX6 By similarity
Add
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.
Contains 1 DFDF domain.

Phylogenomic databases

eggNOGiNOG271303.
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

MATDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP    50
EVTFRAGDIT ELKILEIPGP GDNQHFGDLH QTELGPSGAG CQVGINQNGT 100
GKFVKKPASS SSAPQNIPKR TDVKSQDVAV SPQQQQCSKS YVDRHMESLS 150
QSKSFRRRHN SWSSSSRHPN QATPKKSGLK NGQMKNKDDE CFGDDIEEIP 200
DTDFDFEGNL ALFDKAAVFE EIDTYERRSG TRSRGIPNER PTRYRHDENI 250
LESEPIVYRR IIVPHNVSKE FCTDSGLVVP SISYELHKKL LSVAEKHGLT 300
LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG 350
ISCGRHLANH DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLKDLP 400
TSPVDLVINC LDCPENVFLR DQPWYKAAVA WANQNRAPVL SIDPPVHEVE 450
QGIDAKWSLA LGLPLPLGEH AGRIYLCDIG IPQQVFQEVG INYHSPFGCK 500
FVIPLHSA 508
Length:508
Mass (Da):56,078
Last modified:December 1, 2001 - v1
Checksum:i95346F484FCFC3EA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741Q → R in BAB15001. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

Protein-protein interaction databases

BioGridi 123144. 15 interactions.
DIPi DIP-35516N.
IntActi Q96F86. 14 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.
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

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

Gene expression databases

ArrayExpressi Q96F86.
Bgeei Q96F86.
CleanExi HS_EDC3.
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: September 3, 2014
This is version 113 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

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