MCA3_HUMAN - dbPTM
MCA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCA3_HUMAN
UniProt AC O43324
Protein Name Eukaryotic translation elongation factor 1 epsilon-1
Gene Name EEF1E1
Organism Homo sapiens (Human).
Sequence Length 174
Subcellular Localization Cytoplasm . Cytoplasm, cytosol . Nucleus . Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage.
Protein Description Positive modulator of ATM response to DNA damage..
Protein Sequence MAAAAELSLLEKSLGLSKGNKYSAQGERQIPVLQTNNGPSLTGLTTIAAHLVKQANKEYLLGSTAEEKAIVQQWLEYRVTQVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADILLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH
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
2Acetylation------MAAAAELSL
------CCHHHHHHH		13.05-
8PhosphorylationMAAAAELSLLEKSLG
CCHHHHHHHHHHHHC		23.5520068231
12UbiquitinationAELSLLEKSLGLSKG
HHHHHHHHHHCCCCC		51.4522817900
12AcetylationAELSLLEKSLGLSKG
HHHHHHHHHHCCCCC		51.4519608861
122-HydroxyisobutyrylationAELSLLEKSLGLSKG
HHHHHHHHHHCCCCC		51.45-
12UbiquitinationAELSLLEKSLGLSKG
HHHHHHHHHHCCCCC		51.4521890473
13PhosphorylationELSLLEKSLGLSKGN
HHHHHHHHHCCCCCC		20.4924719451
17PhosphorylationLEKSLGLSKGNKYSA
HHHHHCCCCCCCCCC		36.4028674151
18UbiquitinationEKSLGLSKGNKYSAQ
HHHHCCCCCCCCCCC		72.1127667366
21AcetylationLGLSKGNKYSAQGER
HCCCCCCCCCCCCCE		49.6123749302
22PhosphorylationGLSKGNKYSAQGERQ
CCCCCCCCCCCCCEE		17.1524719451
23PhosphorylationLSKGNKYSAQGERQI
CCCCCCCCCCCCEEC		18.7424719451
35PhosphorylationRQIPVLQTNNGPSLT
EECCEEECCCCCCCC		26.8726846344
40PhosphorylationLQTNNGPSLTGLTTI
EECCCCCCCCHHHHH		39.7126846344
42PhosphorylationTNNGPSLTGLTTIAA
CCCCCCCCHHHHHHH		34.1926846344
45PhosphorylationGPSLTGLTTIAAHLV
CCCCCHHHHHHHHHH		19.9426846344
46PhosphorylationPSLTGLTTIAAHLVK
CCCCHHHHHHHHHHH		17.4226846344
53UbiquitinationTIAAHLVKQANKEYL
HHHHHHHHHHCHHHH		50.4821906983
57AcetylationHLVKQANKEYLLGST
HHHHHHCHHHHCCCC		51.2326051181
57UbiquitinationHLVKQANKEYLLGST
HHHHHHCHHHHCCCC		51.2321906983
59PhosphorylationVKQANKEYLLGSTAE
HHHHCHHHHCCCCHH		14.6120071362
63PhosphorylationNKEYLLGSTAEEKAI
CHHHHCCCCHHHHHH		25.1420071362
68UbiquitinationLGSTAEEKAIVQQWL
CCCCHHHHHHHHHHH		34.6121963094
88UbiquitinationQVDGHSSKNDIHTLL
EECCCCCHHHHHHHH		62.7527667366
93PhosphorylationSSKNDIHTLLKDLNS
CCHHHHHHHHHHHHH		33.8320873877
96AcetylationNDIHTLLKDLNSYLE
HHHHHHHHHHHHHHC		64.3826822725
96UbiquitinationNDIHTLLKDLNSYLE
HHHHHHHHHHHHHHC		64.38-
101PhosphorylationLLKDLNSYLEDKVYL
HHHHHHHHHCCCEEE		17.03-
136AcetylationVDLTVQEKEKYLNVS
HCCCHHHHHHHHCHH		42.2726051181
138UbiquitinationLTVQEKEKYLNVSRW
CCHHHHHHHHCHHHH		67.1329901268
1382-HydroxyisobutyrylationLTVQEKEKYLNVSRW
CCHHHHHHHHCHHHH		67.13-
138MalonylationLTVQEKEKYLNVSRW
CCHHHHHHHHCHHHH		67.1326320211
138AcetylationLTVQEKEKYLNVSRW
CCHHHHHHHHCHHHH		67.1319608861
160PhosphorylationPGIRQHLSSVVFIKN
CCHHHHHHEEEEEEC		20.9722210691
161PhosphorylationGIRQHLSSVVFIKNR
CHHHHHHEEEEEECC		28.7622210691
166AcetylationLSSVVFIKNRLYTNS
HHEEEEEECCCCCCC		25.2619608861
168MethylationSVVFIKNRLYTNSH-
EEEEEECCCCCCCC-		24.86-
170PhosphorylationVFIKNRLYTNSH---
EEEECCCCCCCC---		10.7129496907
171PhosphorylationFIKNRLYTNSH----
EEECCCCCCCC----		34.5329514088
173PhosphorylationKNRLYTNSH------
ECCCCCCCC------		23.8325849741
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 MCA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCA3_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 MCA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYEP_HUMANEPRSphysical
22939629
SYK_HUMANKARSphysical
22939629
SYIC_HUMANIARSphysical
22939629
SYDC_HUMANDARSphysical
22939629
SYMC_HUMANMARSphysical
22939629
SYQ_HUMANQARSphysical
22939629
SYRC_HUMANRARSphysical
22939629
AIMP1_HUMANAIMP1physical
22863883
AIMP2_HUMANAIMP2physical
22863883
SYDC_HUMANDARSphysical
22863883
IF2G_HUMANEIF2S3physical
22863883
ROA2_HUMANHNRNPA2B1physical
22863883
SYIC_HUMANIARSphysical
22863883
IQGA1_HUMANIQGAP1physical
22863883
CCAR2_HUMANCCAR2physical
22863883
SYMC_HUMANMARSphysical
22863883
SYQ_HUMANQARSphysical
22863883
RL13_HUMANRPL13physical
22863883
RL21_HUMANRPL21physical
22863883
RL23A_HUMANRPL23Aphysical
22863883
RL24_HUMANRPL24physical
22863883
RL26_HUMANRPL26physical
22863883
RL27A_HUMANRPL27Aphysical
22863883
RL36_HUMANRPL36physical
22863883
CACO2_HUMANCALCOCO2physical
25416956
NAT9_HUMANNAT9physical
25416956
AIMP1_HUMANAIMP1physical
26344197
SYLC_HUMANLARSphysical
26344197
RNH2C_HUMANRNASEH2Cphysical
26344197
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 MCA3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-12; LYS-138 AND LYS-166, ANDMASS SPECTROMETRY.

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