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P13639

- EF2_HUMAN

UniProt

P13639 - EF2_HUMAN

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Protein

Elongation factor 2

Gene

EEF2

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

Functioni

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338GTPBy similarity
Nucleotide bindingi104 – 1085GTPBy similarity
Nucleotide bindingi158 – 1614GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: Ensembl
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB
  4. protein kinase binding Source: UniProt
  5. translation activator activity Source: UniProt
  6. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. cellular protein metabolic process Source: Reactome
  3. gene expression Source: Reactome
  4. hematopoietic progenitor cell differentiation Source: Ensembl
  5. positive regulation of gene expression Source: UniProt
  6. positive regulation of translation Source: UniProt
  7. translation Source: Reactome
  8. translational elongation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1404. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Gene namesi
Name:EEF2
Synonyms:EF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:3214. EEF2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProt
  5. polysome Source: Ensembl
  6. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 26 (SCA26) [MIM:609306]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti596 – 5961P → H in SCA26; compromises the mechanics of translocation. 1 Publication
VAR_070792

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MIMi609306. phenotype.
Orphaneti101112. Spinocerebellar ataxia type 26.
PharmGKBiPA27650.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 858857Elongation factor 2PRO_0000091000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541Phosphothreonine1 Publication
Modified residuei57 – 571Phosphothreonine2 Publications
Modified residuei59 – 591Phosphothreonine2 Publications
Modified residuei152 – 1521N6-succinyllysineBy similarity
Modified residuei235 – 2351N6-acetyllysine1 Publication
Modified residuei239 – 2391N6-acetyllysine1 Publication
Modified residuei272 – 2721N6-acetyllysine; alternate1 Publication
Modified residuei272 – 2721N6-succinyllysine; alternateBy similarity
Modified residuei275 – 2751N6-acetyllysine1 Publication
Modified residuei435 – 4351Phosphothreonine2 Publications
Modified residuei439 – 4391N6-acetyllysineBy similarity
Modified residuei445 – 4451N6-acetyllysine1 Publication
Modified residuei502 – 5021Phosphoserine1 Publication
Modified residuei572 – 5721N6-succinyllysineBy similarity
Modified residuei619 – 6191N6-acetyllysineBy similarity
Modified residuei715 – 7151DiphthamideBy similarity

Post-translational modificationi

Phosphorylation by EF-2 kinase completely inactivates EF-2.3 Publications
Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis (By similarity).By similarity
ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP13639.
PaxDbiP13639.
PeptideAtlasiP13639.
PRIDEiP13639.

2D gel databases

REPRODUCTION-2DPAGEIPI00186290.

PTM databases

PhosphoSiteiP13639.

Expressioni

Gene expression databases

BgeeiP13639.
CleanExiHS_EEF2.
ExpressionAtlasiP13639. baseline and differential.
GenevestigatoriP13639.

Organism-specific databases

HPAiCAB007795.

Interactioni

Subunit structurei

Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Akt2Q608232EBI-352560,EBI-400263From a different organism.

Protein-protein interaction databases

BioGridi108258. 123 interactions.
IntActiP13639. 48 interactions.
MINTiMINT-4999025.
STRINGi9606.ENSP00000307940.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00z1-858[»]
ProteinModelPortaliP13639.
SMRiP13639. Positions 3-858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 362346tr-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0480.
GeneTreeiENSGT00770000120583.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiP13639.
KOiK03234.
OMAiRWAPVPE.
OrthoDBiEOG7WDN1S.
PhylomeDBiP13639.
TreeFamiTF300575.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13639-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR
60 70 80 90 100
AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI
110 120 130 140 150
NLIDSPGHVD FSSEVTAALR VTDGALVVVD CVSGVCVQTE TVLRQAIAER
160 170 180 190 200
IKPVLMMNKM DRALLELQLE PEELYQTFQR IVENVNVIIS TYGEGESGPM
210 220 230 240 250
GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG EGQLGPAERA
260 270 280 290 300
KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV
310 320 330 340 350
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL
360 370 380 390 400
LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK
410 420 430 440 450
MVPTSDKGRF YAFGRVFSGL VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT
460 470 480 490 500
ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEH AHNMRVMKFS
510 520 530 540 550
VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE SGEHIIAGAG
560 570 580 590 600
ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
610 620 630 640 650
RLYMKARPFP DGLAEDIDKG EVSARQELKQ RARYLAEKYE WDVAEARKIW
660 670 680 690 700
CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV
710 720 730 740 750
RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ
760 770 780 790 800
CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL
810 820 830 840 850
RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA

LDNFLDKL
Length:858
Mass (Da):95,338
Last modified:January 23, 2007 - v4
Checksum:i78BD1710236C0D9C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti596 – 5961P → H in SCA26; compromises the mechanics of translocation. 1 Publication
VAR_070792

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51466 mRNA. Translation: CAA35829.1.
Z11692 mRNA. Translation: CAA77750.1.
AY942181 mRNA. Translation: AAX34409.1.
CH471139 Genomic DNA. Translation: EAW69274.1.
CH471139 Genomic DNA. Translation: EAW69275.1.
BC126259 mRNA. Translation: AAI26260.1.
BC136313 mRNA. Translation: AAI36314.1.
M19997 mRNA. Translation: AAA50388.1.
CCDSiCCDS12117.1.
PIRiS18294. EFHU2.
RefSeqiNP_001952.1. NM_001961.3.
UniGeneiHs.515070.

Genome annotation databases

EnsembliENST00000309311; ENSP00000307940; ENSG00000167658.
GeneIDi1938.
KEGGihsa:1938.
UCSCiuc002lze.3. human.

Polymorphism databases

DMDMi119172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51466 mRNA. Translation: CAA35829.1 .
Z11692 mRNA. Translation: CAA77750.1 .
AY942181 mRNA. Translation: AAX34409.1 .
CH471139 Genomic DNA. Translation: EAW69274.1 .
CH471139 Genomic DNA. Translation: EAW69275.1 .
BC126259 mRNA. Translation: AAI26260.1 .
BC136313 mRNA. Translation: AAI36314.1 .
M19997 mRNA. Translation: AAA50388.1 .
CCDSi CCDS12117.1.
PIRi S18294. EFHU2.
RefSeqi NP_001952.1. NM_001961.3.
UniGenei Hs.515070.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3A electron microscopy 5.00 z 1-858 [» ]
ProteinModelPortali P13639.
SMRi P13639. Positions 3-858.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108258. 123 interactions.
IntActi P13639. 48 interactions.
MINTi MINT-4999025.
STRINGi 9606.ENSP00000307940.

Chemistry

ChEMBLi CHEMBL1795108.

PTM databases

PhosphoSitei P13639.

Polymorphism databases

DMDMi 119172.

2D gel databases

REPRODUCTION-2DPAGE IPI00186290.

Proteomic databases

MaxQBi P13639.
PaxDbi P13639.
PeptideAtlasi P13639.
PRIDEi P13639.

Protocols and materials databases

DNASUi 1938.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309311 ; ENSP00000307940 ; ENSG00000167658 .
GeneIDi 1938.
KEGGi hsa:1938.
UCSCi uc002lze.3. human.

Organism-specific databases

CTDi 1938.
GeneCardsi GC19M003976.
HGNCi HGNC:3214. EEF2.
HPAi CAB007795.
MIMi 130610. gene.
609306. phenotype.
neXtProti NX_P13639.
Orphaneti 101112. Spinocerebellar ataxia type 26.
PharmGKBi PA27650.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0480.
GeneTreei ENSGT00770000120583.
HOGENOMi HOG000231589.
HOVERGENi HBG001838.
InParanoidi P13639.
KOi K03234.
OMAi RWAPVPE.
OrthoDBi EOG7WDN1S.
PhylomeDBi P13639.
TreeFami TF300575.

Enzyme and pathway databases

Reactomei REACT_1404. Peptide chain elongation.

Miscellaneous databases

ChiTaRSi EEF2. human.
GeneWikii EEF2.
GenomeRNAii 1938.
NextBioi 7853.
PROi P13639.
SOURCEi Search...

Gene expression databases

Bgeei P13639.
CleanExi HS_EEF2.
ExpressionAtlasi P13639. baseline and differential.
Genevestigatori P13639.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view ]
Pfami PF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view ]
PRINTSi PR00315. ELONGATNFCT.
SMARTi SM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells."
    Rapp G., Klaudiny J., Hagendorff G., Luck M.R., Heinz K.
    Biol. Chem. Hoppe-Seyler 370:1071-1075(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  2. "Construction of a plasmid containing the complete coding region of human elongation factor 2."
    Hanes J., Freudenstein J., Rapp G., Scheit K.H.
    Biol. Chem. Hoppe-Seyler 373:201-204(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Ustek D., Bektas M., Cakiris A., Oku B., Bermek E.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peripheral blood.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2."
    Rapp G., Mucha J., Einspanier R., Luck M., Scheit K.H.
    Biol. Chem. Hoppe-Seyler 369:247-250(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-858.
  7. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 796-801, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. Bienvenut W.V.
    Submitted (AUG-2001) to UniProtKB
    Cited for: CLEAVAGE OF INITIATOR METHIONINE.
  9. Cited for: ISGYLATION.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay."
    Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.
    Genes Dev. 23:1091-1105(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SURF COMPLEX.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235; LYS-239; LYS-272; LYS-275 AND LYS-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 THR-57; THR-59 AND THR-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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 THR-54; THR-57 AND THR-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult."
    Hekman K.E., Yu G.Y., Brown C.D., Zhu H., Du X., Gervin K., Undlien D.E., Peterson A., Stevanin G., Clark H.B., Pulst S.M., Bird T.D., White K.P., Gomez C.M.
    Hum. Mol. Genet. 21:5472-5483(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SCA26 HIS-596, CHARACTERIZATION OF VARIANT SCA26 HIS-596.

Entry informationi

Entry nameiEF2_HUMAN
AccessioniPrimary (citable) accession number: P13639
Secondary accession number(s): B2RMP5, D6W618, Q58J86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 165 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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