EIF3H_HUMAN - dbPTM
EIF3H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EIF3H_HUMAN
UniProt AC O15372
Protein Name Eukaryotic translation initiation factor 3 subunit H {ECO:0000255|HAMAP-Rule:MF_03007}
Gene Name EIF3H {ECO:0000255|HAMAP-Rule:MF_03007}
Organism Homo sapiens (Human).
Sequence Length 352
Subcellular Localization Cytoplasm .
Protein Description Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. [PubMed: 17581632]
Protein Sequence MASRKEGTGSTATSSSSTAGAAGKGKGKGGSGDSAVKQVQIDGLVVLKIIKHYQEEGQGTEVVQGVLLGLVVEDRLEITNCFPFPQHTEDDADFDEVQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASSNHLGKNLQLLMDRVDEMSQDIVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPPQPPARMDSLLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN
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
3Phosphorylation-----MASRKEGTGS
-----CCCCCCCCCC		42.4623401153
5Ubiquitination---MASRKEGTGSTA
---CCCCCCCCCCCC		58.9821890473
8PhosphorylationMASRKEGTGSTATSS
CCCCCCCCCCCCCCC		29.1129255136
10PhosphorylationSRKEGTGSTATSSSS
CCCCCCCCCCCCCCC		18.0829255136
11PhosphorylationRKEGTGSTATSSSST
CCCCCCCCCCCCCCC		34.9929255136
13O-linked_GlycosylationEGTGSTATSSSSTAG
CCCCCCCCCCCCCCC		29.2728510447
13PhosphorylationEGTGSTATSSSSTAG
CCCCCCCCCCCCCCC		29.2729255136
14PhosphorylationGTGSTATSSSSTAGA
CCCCCCCCCCCCCCC		26.2625262027
14O-linked_GlycosylationGTGSTATSSSSTAGA
CCCCCCCCCCCCCCC		26.2628510447
15PhosphorylationTGSTATSSSSTAGAA
CCCCCCCCCCCCCCC		24.7729255136
16PhosphorylationGSTATSSSSTAGAAG
CCCCCCCCCCCCCCC		31.3229255136
17PhosphorylationSTATSSSSTAGAAGK
CCCCCCCCCCCCCCC		24.9929255136
17O-linked_GlycosylationSTATSSSSTAGAAGK
CCCCCCCCCCCCCCC		24.9928510447
18O-linked_GlycosylationTATSSSSTAGAAGKG
CCCCCCCCCCCCCCC		30.9328510447
18PhosphorylationTATSSSSTAGAAGKG
CCCCCCCCCCCCCCC		30.9325262027
19UbiquitinationATSSSSTAGAAGKGK
CCCCCCCCCCCCCCC		13.9421890473
24UbiquitinationSTAGAAGKGKGKGGS
CCCCCCCCCCCCCCC		53.3621906983
24AcetylationSTAGAAGKGKGKGGS
CCCCCCCCCCCCCCC		53.3626051181
26AcetylationAGAAGKGKGKGGSGD
CCCCCCCCCCCCCCC		62.0230588437
28AcetylationAAGKGKGKGGSGDSA
CCCCCCCCCCCCCCC		64.6826051181
28UbiquitinationAAGKGKGKGGSGDSA
CCCCCCCCCCCCCCC		64.6821890473
31PhosphorylationKGKGKGGSGDSAVKQ
CCCCCCCCCCCCCEE		48.3628985074
37UbiquitinationGSGDSAVKQVQIDGL
CCCCCCCEEEEECCE		44.4621906983
38UbiquitinationSGDSAVKQVQIDGLV
CCCCCCEEEEECCEE		26.2521890473
42UbiquitinationAVKQVQIDGLVVLKI
CCEEEEECCEEEEEH		27.5521890473
51UbiquitinationLVVLKIIKHYQEEGQ
EEEEEHHHHHHHCCC		39.4721890473
101SulfoxidationFDEVQYQMEMMRSLR
HHHHHHHHHHHHHCC		2.7928465586
104SulfoxidationVQYQMEMMRSLRHVN
HHHHHHHHHHCCCCC		1.3528465586
130PhosphorylationTYYGSFVTRALLDSQ
HCCHHHHHHHHHCCC		14.2824719451
156UbiquitinationVLIYDPIKTAQGSLS
EEEECCCCCCCCCCH		43.10-
161PhosphorylationPIKTAQGSLSLKAYR
CCCCCCCCCHHHHEE		11.6024719451
163PhosphorylationKTAQGSLSLKAYRLT
CCCCCCCHHHHEECC		29.5327067055
165AcetylationAQGSLSLKAYRLTPK
CCCCCHHHHEECCHH		39.7426051181
165UbiquitinationAQGSLSLKAYRLTPK
CCCCCHHHHEECCHH		39.7421906983
1652-HydroxyisobutyrylationAQGSLSLKAYRLTPK
CCCCCHHHHEECCHH		39.74-
172UbiquitinationKAYRLTPKLMEVCKE
HHEECCHHHHHHHHH		56.05-
172AcetylationKAYRLTPKLMEVCKE
HHEECCHHHHHHHHH		56.0525953088
178UbiquitinationPKLMEVCKEKDFSPE
HHHHHHHHHCCCCHH		73.33-
178AcetylationPKLMEVCKEKDFSPE
HHHHHHHHHCCCCHH		73.3326051181
179UbiquitinationKLMEVCKEKDFSPEA
HHHHHHHHCCCCHHH		53.3721890473
1802-HydroxyisobutyrylationLMEVCKEKDFSPEAL
HHHHHHHCCCCHHHH		49.95-
180AcetylationLMEVCKEKDFSPEAL
HHHHHHHCCCCHHHH		49.9525953088
180UbiquitinationLMEVCKEKDFSPEAL
HHHHHHHCCCCHHHH		49.95-
183PhosphorylationVCKEKDFSPEALKKA
HHHHCCCCHHHHHHC		31.7829255136
188UbiquitinationDFSPEALKKANITFE
CCCHHHHHHCCEEEE		57.8121906983
189UbiquitinationFSPEALKKANITFEY
CCHHHHHHCCEEEEE		47.73-
202UbiquitinationEYMFEEVPIVIKNSH
EECCCCCCEEEECHH		20.5721890473
220AcetylationVLMWELEKKSAVADK
HHHHHHHHCCCCCCH		65.7325953088
220UbiquitinationVLMWELEKKSAVADK
HHHHHHHHCCCCCCH		65.7321906983
221MalonylationLMWELEKKSAVADKH
HHHHHHHCCCCCCHH		33.9826320211
221UbiquitinationLMWELEKKSAVADKH
HHHHHHHCCCCCCHH		33.98-
227AcetylationKKSAVADKHELLSLA
HCCCCCCHHHHHHHH		29.2823749302
227UbiquitinationKKSAVADKHELLSLA
HCCCCCCHHHHHHHH		29.2821890473
2272-HydroxyisobutyrylationKKSAVADKHELLSLA
HCCCCCCHHHHHHHH		29.28-
232PhosphorylationADKHELLSLASSNHL
CCHHHHHHHHHCCCH		34.2223312004
234UbiquitinationKHELLSLASSNHLGK
HHHHHHHHHCCCHHH		13.9221890473
235PhosphorylationHELLSLASSNHLGKN
HHHHHHHHCCCHHHH		36.6524275569
236PhosphorylationELLSLASSNHLGKNL
HHHHHHHCCCHHHHH		23.7423312004
241UbiquitinationASSNHLGKNLQLLMD
HHCCCHHHHHHHHHH		61.9321906983
247SulfoxidationGKNLQLLMDRVDEMS
HHHHHHHHHHHHHHH		4.1521406390
253SulfoxidationLMDRVDEMSQDIVKY
HHHHHHHHHHHHHHH		3.6421406390
254PhosphorylationMDRVDEMSQDIVKYN
HHHHHHHHHHHHHHH		23.7421815630
255UbiquitinationDRVDEMSQDIVKYNT
HHHHHHHHHHHHHHH		43.0421890473
259UbiquitinationEMSQDIVKYNTYMRN
HHHHHHHHHHHHHCC		32.8721890473
260PhosphorylationMSQDIVKYNTYMRNT
HHHHHHHHHHHHCCC		11.2226074081
262PhosphorylationQDIVKYNTYMRNTSK
HHHHHHHHHHCCCCH		18.6629978859
263PhosphorylationDIVKYNTYMRNTSKQ
HHHHHHHHHCCCCHH		7.1629978859
267PhosphorylationYNTYMRNTSKQQQQK
HHHHHCCCCHHHHHH		27.2626074081
268PhosphorylationNTYMRNTSKQQQQKH
HHHHCCCCHHHHHHH		31.8326074081
273UbiquitinationNTSKQQQQKHQYQQR
CCCHHHHHHHHHHHH		40.6421890473
274UbiquitinationTSKQQQQKHQYQQRR
CCHHHHHHHHHHHHH		28.4721906983
274AcetylationTSKQQQQKHQYQQRR
CCHHHHHHHHHHHHH		28.4726210075
277PhosphorylationQQQQKHQYQQRRQQE
HHHHHHHHHHHHHHH		13.3126074081
288UbiquitinationRQQENMQRQSRGEPP
HHHHHHHHHHCCCCC		26.1821890473
290PhosphorylationQENMQRQSRGEPPLP
HHHHHHHHCCCCCCC		44.4327050516
303UbiquitinationLPEEDLSKLFKPPQP
CCHHHHHHHCCCCCC		66.3021890473
303SumoylationLPEEDLSKLFKPPQP
CCHHHHHHHCCCCCC		66.3028112733
306UbiquitinationEDLSKLFKPPQPPAR
HHHHHHCCCCCCCCC		67.25-
306MalonylationEDLSKLFKPPQPPAR
HHHHHHCCCCCCCCC		67.2526320211
316PhosphorylationQPPARMDSLLIAGQI
CCCCCCHHEEHHHHH		18.7427251275
320UbiquitinationRMDSLLIAGQINTYC
CCHHEEHHHHHHHHH		12.1021890473
331UbiquitinationNTYCQNIKEFTAQNL
HHHHCCHHHHHHHHH		55.0921906983
340UbiquitinationFTAQNLGKLFMAQAL
HHHHHHHHHHHHHHH		41.542190698
345UbiquitinationLGKLFMAQALQEYNN
HHHHHHHHHHHHHCC		30.7121890473
350PhosphorylationMAQALQEYNN-----
HHHHHHHHCC-----		13.6728796482
354UbiquitinationLQEYNN---------
HHHHCC---------		21890473
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 EIF3H_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EIF3H_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 EIF3H_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ABI3_HUMANABI3physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
EIF3G_HUMANEIF3Gphysical
9822659
AGRB1_HUMANBAI1physical
19615732
CSK21_HUMANCSNK2A1physical
19615732
CSK22_HUMANCSNK2A2physical
19615732
CSK2B_HUMANCSNK2Bphysical
19615732
IF4G1_HUMANEIF4G1physical
19615732
EIF3E_HUMANEIF3Ephysical
19615732
ABCE1_HUMANABCE1physical
19615732
EIF3A_HUMANEIF3Aphysical
19615732
EIF3B_HUMANEIF3Bphysical
19615732
EIF3C_HUMANEIF3Cphysical
19615732
EIF3D_HUMANEIF3Dphysical
19615732
EIF3F_HUMANEIF3Fphysical
19615732
EIF3G_HUMANEIF3Gphysical
19615732
EIF3I_HUMANEIF3Iphysical
19615732
EIF3J_HUMANEIF3Jphysical
19615732
IF4G3_HUMANEIF4G3physical
19615732
ARPC5_HUMANARPC5physical
19615732
EIF3M_HUMANEIF3Mphysical
19615732
EIF3K_HUMANEIF3Kphysical
19615732
EIF3L_HUMANEIF3Lphysical
19615732
PRC2B_HUMANPRRC2Bphysical
19615732
TM203_HUMANTMEM203physical
19615732
EIF3B_HUMANEIF3Bphysical
18599441
EIF3K_HUMANEIF3Kphysical
22939629
EIF3I_HUMANEIF3Iphysical
22939629
EIF3M_HUMANEIF3Mphysical
22939629
EIF3L_HUMANEIF3Lphysical
22939629
POL_HV1H2gag-polphysical
20016921
ABI3_HUMANABI3physical
19060904
EIF3A_HUMANEIF3Aphysical
22863883
EIF3C_HUMANEIF3Cphysical
22863883
EIF3D_HUMANEIF3Dphysical
22863883
EIF3E_HUMANEIF3Ephysical
22863883
RS20_HUMANRPS20physical
22863883
RS9_HUMANRPS9physical
22863883
YTHD2_HUMANYTHDF2physical
22863883
ABI2_HUMANABI2physical
25416956
VINEX_HUMANSORBS3physical
25416956
ABI3_HUMANABI3physical
25416956
EIF3B_HUMANEIF3Bphysical
26186194
EIF3K_HUMANEIF3Kphysical
26186194
EIF3A_HUMANEIF3Aphysical
26186194
PRC2B_HUMANPRRC2Bphysical
26186194
EIFCL_HUMANEIF3CLphysical
26186194
EIF3C_HUMANEIF3Cphysical
26186194
EIF3M_HUMANEIF3Mphysical
26186194
EIF3L_HUMANEIF3Lphysical
26186194
EIF3D_HUMANEIF3Dphysical
26186194
EIF3E_HUMANEIF3Ephysical
26186194
CSN5_HUMANCOPS5physical
26344197
EIF3B_HUMANEIF3Bphysical
26344197
EIF3C_HUMANEIF3Cphysical
26344197
EIFCL_HUMANEIF3CLphysical
26344197
EIF3D_HUMANEIF3Dphysical
26344197
EIF3F_HUMANEIF3Fphysical
26344197
EIF3K_HUMANEIF3Kphysical
26344197
EIF3M_HUMANEIF3Mphysical
26344197
NP1L1_HUMANNAP1L1physical
26344197
PDCD4_HUMANPDCD4physical
26344197
EIF3M_HUMANEIF3Mphysical
28514442
EIF3E_HUMANEIF3Ephysical
28514442
EIF3L_HUMANEIF3Lphysical
28514442
EIFCL_HUMANEIF3CLphysical
28514442
PRC2B_HUMANPRRC2Bphysical
28514442
EIF3A_HUMANEIF3Aphysical
28514442
EIF3C_HUMANEIF3Cphysical
28514442
EIF3D_HUMANEIF3Dphysical
28514442
EIF3B_HUMANEIF3Bphysical
28514442
EIF3K_HUMANEIF3Kphysical
28514442
IF4A1_HUMANEIF4A1physical
28514442
PSD12_HUMANPSMD12physical
28514442
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 EIF3H_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-183, AND MASSSPECTROMETRY.
"Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry.";
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
Mol. Cell. Proteomics 6:1135-1146(2007).
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, PHOSPHORYLATION AT SER-183, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-10 AND THR-11,AND MASS SPECTROMETRY.
"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-183, AND MASSSPECTROMETRY.

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