EF1B_HUMAN - dbPTM
EF1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1B_HUMAN
UniProt AC P24534
Protein Name Elongation factor 1-beta
Gene Name EEF1B2
Organism Homo sapiens (Human).
Sequence Length 225
Subcellular Localization
Protein Description EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP..
Protein Sequence MGFGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPADLCHALRWYNHIKSYEKEKASLPGVKKALGKYGPADVEDTTGSGATDSKDDDDIDLFGSDDEEESEEAKRLREERLAQYESKKAKKPALVAKSSILLDVKPWDDETDMAKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDYVQSMDVAAFNKI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Acetylation-MGFGDLKSPAGLQV
-CCCCCCCCHHHHHH		60.1619608861
7Ubiquitination-MGFGDLKSPAGLQV
-CCCCCCCCHHHHHH		60.1621890473
7Succinylation-MGFGDLKSPAGLQV
-CCCCCCCCHHHHHH		60.1623954790
7Methylation-MGFGDLKSPAGLQV
-CCCCCCCCHHHHHH		60.1619608861
8PhosphorylationMGFGDLKSPAGLQVL
CCCCCCCCHHHHHHH		27.5528355574
18PhosphorylationGLQVLNDYLADKSYI
HHHHHHHHHCCHHHC		11.6128152594
28PhosphorylationDKSYIEGYVPSQADV
CHHHCCCCCCCHHCE		9.0828450419
31PhosphorylationYIEGYVPSQADVAVF
HCCCCCCCHHCEEEE		28.1428464451
42PhosphorylationVAVFEAVSSPPPADL
EEEEEECCCCCCHHH		44.1425159151
43PhosphorylationAVFEAVSSPPPADLC
EEEEECCCCCCHHHH		34.5225159151
50GlutathionylationSPPPADLCHALRWYN
CCCCHHHHHHHHHHH		1.4922555962
60AcetylationLRWYNHIKSYEKEKA
HHHHHHHHHHHHHHC		39.1623236377
60UbiquitinationLRWYNHIKSYEKEKA
HHHHHHHHHHHHHHC		39.1621890473
60SuccinylationLRWYNHIKSYEKEKA
HHHHHHHHHHHHHHC		39.1623954790
66AcetylationIKSYEKEKASLPGVK
HHHHHHHHCCCCCHH		55.1025953088
68PhosphorylationSYEKEKASLPGVKKA
HHHHHHCCCCCHHHH		46.2830387612
73AcetylationKASLPGVKKALGKYG
HCCCCCHHHHHHCCC		37.9426051181
78UbiquitinationGVKKALGKYGPADVE
CHHHHHHCCCCCCCC		48.1321906983
78AcetylationGVKKALGKYGPADVE
CHHHHHHCCCCCCCC		48.1327452117
79PhosphorylationVKKALGKYGPADVED
HHHHHHCCCCCCCCC		26.9223927012
87PhosphorylationGPADVEDTTGSGATD
CCCCCCCCCCCCCCC		21.3923927012
88PhosphorylationPADVEDTTGSGATDS
CCCCCCCCCCCCCCC		41.4925159151
90PhosphorylationDVEDTTGSGATDSKD
CCCCCCCCCCCCCCC		24.1423927012
93PhosphorylationDTTGSGATDSKDDDD
CCCCCCCCCCCCCCC		44.3129255136
95PhosphorylationTGSGATDSKDDDDID
CCCCCCCCCCCCCCC		33.3619664994
106PhosphorylationDDIDLFGSDDEEESE
CCCCCCCCCCHHHHH		34.2619664994
112PhosphorylationGSDDEEESEEAKRLR
CCCCHHHHHHHHHHH		43.9722167270
126PhosphorylationREERLAQYESKKAKK
HHHHHHHHHHHCCCC		19.3017287340
128PhosphorylationERLAQYESKKAKKPA
HHHHHHHHHCCCCCC		34.2317287340
129UbiquitinationRLAQYESKKAKKPAL
HHHHHHHHCCCCCCE		44.82-
129AcetylationRLAQYESKKAKKPAL
HHHHHHHHCCCCCCE		44.8223749302
130UbiquitinationLAQYESKKAKKPALV
HHHHHHHCCCCCCEE		74.78-
132UbiquitinationQYESKKAKKPALVAK
HHHHHCCCCCCEEEE		69.07-
133AcetylationYESKKAKKPALVAKS
HHHHCCCCCCEEEEC		40.1426051181
133UbiquitinationYESKKAKKPALVAKS
HHHHCCCCCCEEEEC		40.1421906983
140PhosphorylationKPALVAKSSILLDVK
CCCEEEECCEECCCC		16.9325159151
141PhosphorylationPALVAKSSILLDVKP
CCEEEECCEECCCCC		19.2925159151
147UbiquitinationSSILLDVKPWDDETD
CCEECCCCCCCCCCC		39.8021906983
147SumoylationSSILLDVKPWDDETD
CCEECCCCCCCCCCC		39.8028112733
147AcetylationSSILLDVKPWDDETD
CCEECCCCCCCCCCC		39.8023236377
153PhosphorylationVKPWDDETDMAKLEE
CCCCCCCCCHHHHHH		37.7622817901
157AcetylationDDETDMAKLEECVRS
CCCCCHHHHHHHHHH		50.2026051181
161GlutathionylationDMAKLEECVRSIQAD
CHHHHHHHHHHHHHC		1.9422555962
164PhosphorylationKLEECVRSIQADGLV
HHHHHHHHHHHCCCE		9.9221712546
174PhosphorylationADGLVWGSSKLVPVG
HCCCEECCCCEEEEC		14.4825159151
175PhosphorylationDGLVWGSSKLVPVGY
CCCEECCCCEEEECC		26.5228450419
176UbiquitinationGLVWGSSKLVPVGYG
CCEECCCCEEEECCC		56.0221906983
176AcetylationGLVWGSSKLVPVGYG
CCEECCCCEEEECCC		56.0223954790
182PhosphorylationSKLVPVGYGIKKLQI
CCEEEECCCEEEEEE		18.8625394399
185MalonylationVPVGYGIKKLQIQCV
EEECCCEEEEEEEEE		42.9726320211
185UbiquitinationVPVGYGIKKLQIQCV
EEECCCEEEEEEEEE		42.9721890473
185AcetylationVPVGYGIKKLQIQCV
EEECCCEEEEEEEEE		42.9723954790
186UbiquitinationPVGYGIKKLQIQCVV
EECCCEEEEEEEEEE		43.64-
213PhosphorylationQITAFEDYVQSMDVA
HHHHHHHHHHHCCHH		8.00-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of EF1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1B_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of EF1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1G_HUMANEEF1Gphysical
16189514
EF1B_HUMANEEF1B2physical
10094407
EF1G_HUMANEEF1Gphysical
16169070
SYHC_HUMANHARSphysical
11829477
A4_HUMANAPPphysical
21832049
EF1G_HUMANEEF1Gphysical
22939629
RS2_HUMANRPS2physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
STRP1_HUMANSTRIP1physical
22939629
TPR_HUMANTPRphysical
22939629
NU153_HUMANNUP153physical
22939629
PLOD3_HUMANPLOD3physical
22939629
SNRPA_HUMANSNRPAphysical
22939629
STRN4_HUMANSTRN4physical
22939629
T2FA_HUMANGTF2F1physical
22939629
SRSF9_HUMANSRSF9physical
22939629
UBQL2_HUMANUBQLN2physical
22939629
QCR6_HUMANUQCRHphysical
22939629
DNJA1_HUMANDNAJA1physical
22863883
EF1D_HUMANEEF1Dphysical
22863883
EF1G_HUMANEEF1Gphysical
22863883
SYVC_HUMANVARSphysical
22863883
EF1G_HUMANEEF1Gphysical
25416956
AHNK_HUMANAHNAKphysical
26344197
ATLA3_HUMANATL3physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
KMT2D_HUMANKMT2Dphysical
26344197
SYVC_HUMANVARSphysical
26344197
EF1G_HUMANEEF1Gphysical
21516116
TCTP_HUMANTPT1physical
25635048
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7 AND LYS-60, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-95 AND SER-106,AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-95; SER-106 ANDSER-112, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-95 AND SER-106,AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93; SER-95; SER-106;TYR-126; SER-128 AND SER-141, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-106, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.

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