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Protein

Elongation factor 2

Gene

Eef2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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: MGI
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: MGI
  4. protein kinase binding Source: MGI
  5. translation activator activity Source: MGI
  6. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. hematopoietic progenitor cell differentiation Source: MGI
  2. positive regulation of gene expression Source: MGI
  3. positive regulation of translation Source: MGI
  4. translational elongation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_311765. Peptide chain elongation.
REACT_333333. Synthesis of diphthamide-EEF2.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Gene namesi
Name:Eef2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:95288. Eef2.

Subcellular locationi

Cytoplasm. Nucleus By similarity
Note: Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.By similarity

GO - Cellular componenti

  1. aggresome Source: MGI
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: MGI
  4. membrane Source: MGI
  5. nucleus Source: MGI
  6. plasma membrane Source: MGI
  7. polysome Source: MGI
  8. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 858857Elongation factor 2PRO_0000091002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphothreonineBy similarity
Modified residuei57 – 571Phosphothreonine; by EEF2KBy similarity
Modified residuei59 – 591PhosphothreonineBy similarity
Modified residuei152 – 1521N6-succinyllysine1 Publication
Modified residuei235 – 2351N6-acetyllysineBy similarity
Modified residuei239 – 2391N6-acetyllysine1 Publication
Modified residuei265 – 2651Phosphotyrosine; by CSKBy similarity
Modified residuei272 – 2721N6-acetyllysine; alternate1 Publication
Modified residuei272 – 2721N6-succinyllysine; alternate1 Publication
Modified residuei275 – 2751N6-acetyllysine1 Publication
Cross-linki322 – 322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei373 – 3731Phosphotyrosine; by CSKBy similarity
Modified residuei435 – 4351PhosphothreonineBy similarity
Modified residuei439 – 4391N6-acetyllysine1 Publication
Modified residuei445 – 4451N6-acetyllysine1 Publication
Modified residuei502 – 5021PhosphoserineBy similarity
Modified residuei525 – 5251N6,N6,N6-trimethyllysine; by EEF2KMTBy similarity
Cross-linki529 – 529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei572 – 5721N6-succinyllysine1 Publication
Modified residuei595 – 5951Phosphoserine; by CDK2By similarity
Modified residuei619 – 6191N6-acetyllysine1 Publication
Modified residuei715 – 7151DiphthamideBy similarity

Post-translational modificationi

Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage, and nuclear translocation if the C-terminal fragment.By similarity
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
Proteolytically processed at two sites following phosphorylation by CSK.By similarity
SUMOytated following phosphorylation by CSK, promotes proteolytic cleavage.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP58252.
PaxDbiP58252.
PRIDEiP58252.

2D gel databases

COMPLUYEAST-2DPAGEP58252.
REPRODUCTION-2DPAGEP58252.

PTM databases

PhosphoSiteiP58252.

Expressioni

Gene expression databases

BgeeiP58252.
CleanExiMM_EEF2.
ExpressionAtlasiP58252. baseline and differential.
GenevestigatoriP58252.

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.By similarity

Protein-protein interaction databases

BioGridi199387. 10 interactions.
IntActiP58252. 11 interactions.
MINTiMINT-1862939.

Structurei

3D structure databases

ProteinModelPortaliP58252.
SMRiP58252. 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.
InParanoidiP58252.
KOiK03234.
OMAiKMAPEEF.
OrthoDBiEOG7WDN1S.
PhylomeDBiP58252.
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.

P58252-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR
60 70 80 90 100
AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI
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 EGQLSAAERA
260 270 280 290 300
KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV
310 320 330 340 350
FDAIMNFRKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL
360 370 380 390 400
LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK
410 420 430 440 450
MVPTSDKGRF YAFGRVFSGV 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 EVSARQELKA 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):95,314
Last modified:January 23, 2007 - v2
Checksum:i0569DFFB9B1DB5F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040474 mRNA. Translation: BAC30601.1.
AK077866 mRNA. Translation: BAC37041.1.
AK087985 mRNA. Translation: BAC40076.1.
AK145545 mRNA. Translation: BAE26498.1.
AK146947 mRNA. Translation: BAE27556.1.
AK151487 mRNA. Translation: BAE30440.1.
AK151812 mRNA. Translation: BAE30710.1.
AK151945 mRNA. Translation: BAE30820.1.
AK152146 mRNA. Translation: BAE30983.1.
AK152447 mRNA. Translation: BAE31226.1.
AK152587 mRNA. Translation: BAE31336.1.
AK152826 mRNA. Translation: BAE31527.1.
AK153275 mRNA. Translation: BAE31861.1.
AK155325 mRNA. Translation: BAE33192.1.
AK159806 mRNA. Translation: BAE35386.1.
AK163063 mRNA. Translation: BAE37177.1.
AK166212 mRNA. Translation: BAE38631.1.
AK166596 mRNA. Translation: BAE38882.1.
AK166747 mRNA. Translation: BAE38989.1.
AK166751 mRNA. Translation: BAE38992.1.
AK166851 mRNA. Translation: BAE39070.1.
AK166968 mRNA. Translation: BAE39151.1.
AK167093 mRNA. Translation: BAE39249.1.
AK167109 mRNA. Translation: BAE39257.1.
AK167115 mRNA. Translation: BAE39263.1.
AK167221 mRNA. Translation: BAE39346.1.
AK168794 mRNA. Translation: BAE40627.1.
AK168827 mRNA. Translation: BAE40654.1.
AK168874 mRNA. Translation: BAE40692.1.
AK169013 mRNA. Translation: BAE40810.1.
BC007152 mRNA. Translation: AAH07152.1.
CCDSiCCDS35993.1.
RefSeqiNP_031933.1. NM_007907.2.
UniGeneiMm.326799.
Mm.482883.
Mm.486637.

Genome annotation databases

EnsembliENSMUST00000047864; ENSMUSP00000046101; ENSMUSG00000034994.
GeneIDi13629.
KEGGimmu:13629.
UCSCiuc007gge.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040474 mRNA. Translation: BAC30601.1.
AK077866 mRNA. Translation: BAC37041.1.
AK087985 mRNA. Translation: BAC40076.1.
AK145545 mRNA. Translation: BAE26498.1.
AK146947 mRNA. Translation: BAE27556.1.
AK151487 mRNA. Translation: BAE30440.1.
AK151812 mRNA. Translation: BAE30710.1.
AK151945 mRNA. Translation: BAE30820.1.
AK152146 mRNA. Translation: BAE30983.1.
AK152447 mRNA. Translation: BAE31226.1.
AK152587 mRNA. Translation: BAE31336.1.
AK152826 mRNA. Translation: BAE31527.1.
AK153275 mRNA. Translation: BAE31861.1.
AK155325 mRNA. Translation: BAE33192.1.
AK159806 mRNA. Translation: BAE35386.1.
AK163063 mRNA. Translation: BAE37177.1.
AK166212 mRNA. Translation: BAE38631.1.
AK166596 mRNA. Translation: BAE38882.1.
AK166747 mRNA. Translation: BAE38989.1.
AK166751 mRNA. Translation: BAE38992.1.
AK166851 mRNA. Translation: BAE39070.1.
AK166968 mRNA. Translation: BAE39151.1.
AK167093 mRNA. Translation: BAE39249.1.
AK167109 mRNA. Translation: BAE39257.1.
AK167115 mRNA. Translation: BAE39263.1.
AK167221 mRNA. Translation: BAE39346.1.
AK168794 mRNA. Translation: BAE40627.1.
AK168827 mRNA. Translation: BAE40654.1.
AK168874 mRNA. Translation: BAE40692.1.
AK169013 mRNA. Translation: BAE40810.1.
BC007152 mRNA. Translation: AAH07152.1.
CCDSiCCDS35993.1.
RefSeqiNP_031933.1. NM_007907.2.
UniGeneiMm.326799.
Mm.482883.
Mm.486637.

3D structure databases

ProteinModelPortaliP58252.
SMRiP58252. Positions 3-858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199387. 10 interactions.
IntActiP58252. 11 interactions.
MINTiMINT-1862939.

PTM databases

PhosphoSiteiP58252.

2D gel databases

COMPLUYEAST-2DPAGEP58252.
REPRODUCTION-2DPAGEP58252.

Proteomic databases

MaxQBiP58252.
PaxDbiP58252.
PRIDEiP58252.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047864; ENSMUSP00000046101; ENSMUSG00000034994.
GeneIDi13629.
KEGGimmu:13629.
UCSCiuc007gge.2. mouse.

Organism-specific databases

CTDi1938.
MGIiMGI:95288. Eef2.

Phylogenomic databases

eggNOGiCOG0480.
GeneTreeiENSGT00770000120583.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiP58252.
KOiK03234.
OMAiKMAPEEF.
OrthoDBiEOG7WDN1S.
PhylomeDBiP58252.
TreeFamiTF300575.

Enzyme and pathway databases

ReactomeiREACT_311765. Peptide chain elongation.
REACT_333333. Synthesis of diphthamide-EEF2.

Miscellaneous databases

ChiTaRSiEef2. mouse.
NextBioi284312.
PROiP58252.
SOURCEiSearch...

Gene expression databases

BgeeiP58252.
CleanExiMM_EEF2.
ExpressionAtlasiP58252. baseline and differential.
GenevestigatoriP58252.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Forelimb, Kidney, Liver, Mammary gland and Thymus.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.
    Submitted (JAN-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10 AND 499-506, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic fibroblast.
  4. Lubec G., Klug S., Sunyer B., Chen W.-Q.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-10; 33-50; 163-180; 240-249; 288-308; 416-426; 581-594; 606-625; 668-688; 717-726; 728-739; 768-801 AND 846-858, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: ISGYLATION.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-272; LYS-275; LYS-439; LYS-445 AND LYS-619, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-152; LYS-272 AND LYS-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiEF2_MOUSE
AccessioniPrimary (citable) accession number: P58252
Secondary accession number(s): Q544E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.