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Protein

Elongation factor 1-beta

Gene

EEF1B2

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

Functioni

EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.

GO - Molecular functioni

  1. translation elongation factor activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. translation Source: Reactome
  4. translational elongation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1477. Eukaryotic Translation Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 1-beta
Short name:
EF-1-beta
Gene namesi
Name:EEF1B2
Synonyms:EEF1B, EF1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3208. EEF1B2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. eukaryotic translation elongation factor 1 complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27644.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 225224Elongation factor 1-betaPRO_0000155021Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71N6-acetyllysine1 Publication
Modified residuei8 – 81Phosphoserine3 Publications
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei93 – 931Phosphothreonine1 Publication
Modified residuei95 – 951Phosphoserine4 Publications
Modified residuei106 – 1061Phosphoserine11 Publications

Post-translational modificationi

Phosphorylation affects the GDP/GTP exchange rate.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP24534.
PaxDbiP24534.
PeptideAtlasiP24534.
PRIDEiP24534.

2D gel databases

DOSAC-COBS-2DPAGEP24534.
OGPiP24534.
SWISS-2DPAGEP24534.

PTM databases

PhosphoSiteiP24534.

Miscellaneous databases

PMAP-CutDBP24534.

Expressioni

Inductioni

By homocysteine (HC), may mediate accelerated synthesis of free thiol-containing proteins in response to HC-induced oxidative stress.1 Publication

Gene expression databases

BgeeiP24534.
CleanExiHS_EEF1B2.
ExpressionAtlasiP24534. baseline.
GenevestigatoriP24534.

Organism-specific databases

HPAiCAB012477.
HPA035029.

Interactioni

Subunit structurei

EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.

Binary interactionsi

WithEntry#Exp.IntActNotes
EEF1GP266413EBI-354334,EBI-351467

Protein-protein interaction databases

BioGridi108253. 52 interactions.
IntActiP24534. 23 interactions.
MINTiMINT-4999956.
STRINGi9606.ENSP00000236957.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi140 – 15011Combined sources
Helixi155 – 16410Combined sources
Beta strandi171 – 18313Combined sources
Beta strandi185 – 1939Combined sources
Helixi200 – 2078Combined sources
Turni211 – 2133Combined sources
Beta strandi214 – 2207Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B64NMR-A136-225[»]
ProteinModelPortaliP24534.
SMRiP24534. Positions 136-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24534.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8483GST C-terminalAdd
BLAST

Sequence similaritiesi

Belongs to the EF-1-beta/EF-1-delta family.Curated
Contains 1 GST C-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG2092.
GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207273.
HOVERGENiHBG000787.
InParanoidiP24534.
KOiK03232.
OMAiIASYEAE.
OrthoDBiEOG7RZ5QW.
PhylomeDBiP24534.
TreeFamiTF313134.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC
60 70 80 90 100
HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD
110 120 130 140 150
IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD
160 170 180 190 200
DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT
210 220
DMLEEQITAF EDYVQSMDVA AFNKI
Length:225
Mass (Da):24,764
Last modified:January 23, 2007 - v3
Checksum:iCDE763ADBF127822
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60489 mRNA. Translation: CAA43019.1.
X60656 mRNA. Translation: CAA43063.1.
BT007079 mRNA. Translation: AAP35742.1.
CR456825 mRNA. Translation: CAG33106.1.
AK291910 mRNA. Translation: BAF84599.1.
AC007383 Genomic DNA. Translation: AAY15062.1.
CH471063 Genomic DNA. Translation: EAW70381.1.
BC000211 mRNA. Translation: AAH00211.1.
BC004931 mRNA. Translation: AAH04931.1.
BC067787 mRNA. Translation: AAH67787.1.
CCDSiCCDS2367.1.
PIRiS25432.
RefSeqiNP_001032752.1. NM_001037663.1.
NP_001950.1. NM_001959.3.
NP_066944.1. NM_021121.3.
UniGeneiHs.421608.

Genome annotation databases

EnsembliENST00000236957; ENSP00000236957; ENSG00000114942.
ENST00000392221; ENSP00000376055; ENSG00000114942.
ENST00000392222; ENSP00000376056; ENSG00000114942.
GeneIDi1933.
KEGGihsa:1933.
UCSCiuc002vbf.1. human.

Polymorphism databases

DMDMi119163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60489 mRNA. Translation: CAA43019.1.
X60656 mRNA. Translation: CAA43063.1.
BT007079 mRNA. Translation: AAP35742.1.
CR456825 mRNA. Translation: CAG33106.1.
AK291910 mRNA. Translation: BAF84599.1.
AC007383 Genomic DNA. Translation: AAY15062.1.
CH471063 Genomic DNA. Translation: EAW70381.1.
BC000211 mRNA. Translation: AAH00211.1.
BC004931 mRNA. Translation: AAH04931.1.
BC067787 mRNA. Translation: AAH67787.1.
CCDSiCCDS2367.1.
PIRiS25432.
RefSeqiNP_001032752.1. NM_001037663.1.
NP_001950.1. NM_001959.3.
NP_066944.1. NM_021121.3.
UniGeneiHs.421608.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B64NMR-A136-225[»]
ProteinModelPortaliP24534.
SMRiP24534. Positions 136-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108253. 52 interactions.
IntActiP24534. 23 interactions.
MINTiMINT-4999956.
STRINGi9606.ENSP00000236957.

PTM databases

PhosphoSiteiP24534.

Polymorphism databases

DMDMi119163.

2D gel databases

DOSAC-COBS-2DPAGEP24534.
OGPiP24534.
SWISS-2DPAGEP24534.

Proteomic databases

MaxQBiP24534.
PaxDbiP24534.
PeptideAtlasiP24534.
PRIDEiP24534.

Protocols and materials databases

DNASUi1933.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236957; ENSP00000236957; ENSG00000114942.
ENST00000392221; ENSP00000376055; ENSG00000114942.
ENST00000392222; ENSP00000376056; ENSG00000114942.
GeneIDi1933.
KEGGihsa:1933.
UCSCiuc002vbf.1. human.

Organism-specific databases

CTDi1933.
GeneCardsiGC02P207024.
HGNCiHGNC:3208. EEF1B2.
HPAiCAB012477.
HPA035029.
MIMi600655. gene.
neXtProtiNX_P24534.
PharmGKBiPA27644.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2092.
GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207273.
HOVERGENiHBG000787.
InParanoidiP24534.
KOiK03232.
OMAiIASYEAE.
OrthoDBiEOG7RZ5QW.
PhylomeDBiP24534.
TreeFamiTF313134.

Enzyme and pathway databases

ReactomeiREACT_1477. Eukaryotic Translation Elongation.

Miscellaneous databases

ChiTaRSiEEF1B2. human.
EvolutionaryTraceiP24534.
GeneWikiiEEF1B2.
GenomeRNAii1933.
NextBioi7829.
PMAP-CutDBP24534.
PROiP24534.
SOURCEiSearch...

Gene expression databases

BgeeiP24534.
CleanExiHS_EEF1B2.
ExpressionAtlasiP24534. baseline.
GenevestigatoriP24534.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of human elongation factor-1 beta cDNA."
    Sanders J., Maassen J.A., Amons R., Moeller W.
    Nucleic Acids Res. 19:4551-4551(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin fibroblast.
  2. "Human elongation factor 1 beta: cDNA and derived amino acid sequence."
    von der Kammer H., Klaudiny J., Zimmer M., Scheit K.H.
    Biochem. Biophys. Res. Commun. 177:312-317(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovarian granulosa cell.
  3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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].
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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, Eye and Pancreas.
  9. "Human liver protein map: a reference database established by microsequencing and gel comparison."
    Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
    Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-11.
    Tissue: Liver.
  10. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 8-22; 140-157 AND 164-176, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 55-60; 79-85; 123-127 AND 164-175.
    Tissue: Keratinocyte.
  12. "Induction of acute translational response genes by homocysteine. Elongation factors-1alpha, -beta, and -delta."
    Chacko G., Ling Q., Hajjar K.A.
    J. Biol. Chem. 273:19840-19846(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HOMOCYSTEINE.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  15. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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].
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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-8; SER-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "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-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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-8; THR-93; SER-95 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEF1B_HUMAN
AccessioniPrimary (citable) accession number: P24534
Secondary accession number(s): A8K795, Q6IBH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 171 of the entry and version 3 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 2
    Human chromosome 2: 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

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.