ECSIT_HUMAN - dbPTM
ECSIT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECSIT_HUMAN
UniProt AC Q9BQ95
Protein Name Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
Gene Name ECSIT
Organism Homo sapiens (Human).
Sequence Length 431
Subcellular Localization Cytoplasm . Nucleus . Mitochondrion .
Protein Description Adapter protein of the Toll-like and IL-1 receptor signaling pathway that is involved in the activation of NF-kappa-B via MAP3K1. Promotes proteolytic activation of MAP3K1. Involved in the BMP signaling pathway. Required for normal embryonic development (By similarity).; Required for efficient assembly of mitochondrial NADH:ubiquinone oxidoreductase..
Protein Sequence MSWVQATLLARGLCRAWGGTCGAALTGTSISQVPRRLPRGLHCSAAAHSSEQSLVPSPPEPRQRPTKALVPFEDLFGQAPGGERDKASFLQTVQKFAEHSVRKRGHIDFIYLALRKMREYGVERDLAVYNQLLNIFPKEVFRPRNIIQRIFVHYPRQQECGIAVLEQMENHGVMPNKETEFLLIQIFGRKSYPMLKLVRLKLWFPRFMNVNPFPVPRDLPQDPVELAMFGLRHMEPDLSARVTIYQVPLPKDSTGAADPPQPHIVGIQSPDQQAALARHNPARPVFVEGPFSLWLRNKCVYYHILRADLLPPEEREVEETPEEWNLYYPMQLDLEYVRSGWDNYEFDINEVEEGPVFAMCMAGAHDQATMAKWIQGLQETNPTLAQIPVVFRLAGSTRELQTSSAGLEEPPLPEDHQEEDDNLQRQQQGQS
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
138UbiquitinationQLLNIFPKEVFRPRN
HHHCCCCHHHCCCHH
56.62-
192PhosphorylationQIFGRKSYPMLKLVR
EHHCCCCCHHHHHHH
8.8322461510
201AcetylationMLKLVRLKLWFPRFM
HHHHHHHHHHCCCCC
32.8625953088
201UbiquitinationMLKLVRLKLWFPRFM
HHHHHHHHHHCCCCC
32.86-
253PhosphorylationQVPLPKDSTGAADPP
ECCCCCCCCCCCCCC
34.5626471730
254PhosphorylationVPLPKDSTGAADPPQ
CCCCCCCCCCCCCCC
40.7626471730
267 (in isoform 2)Phosphorylation-2.2522210691
269PhosphorylationPHIVGIQSPDQQAAL
CCEEEECCHHHHHHH
28.6420068231

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
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:32296023

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECSIT_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 ECSIT_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIC60_HUMANIMMTphysical
16169070
SETB1_HUMANSETDB1physical
16169070
TRI59_HUMANTRIM59physical
22588174
MAVS_HUMANMAVSphysical
22588174
PAXI1_HUMANPAXIP1physical
21163940
BLMH_HUMANBLMHphysical
21163940
PSN2_HUMANPSEN2physical
21163940
PSN1_HUMANPSEN1physical
21163940
APOE_HUMANAPOEphysical
21163940
AP1M2_HUMANAP1M2physical
21163940
CP2CI_HUMANCYP2C18physical
21163940
DNJB1_HUMANDNAJB1physical
21163940
ELAV3_HUMANELAVL3physical
21163940
EXOC6_HUMANEXOC6physical
21163940
EXOS1_HUMANEXOSC1physical
21163940
SYFA_HUMANFARSAphysical
21163940
GCDH_HUMANGCDHphysical
21163940
IFIT5_HUMANIFIT5physical
21163940
LONM_HUMANLONP1physical
21163940
LOXL4_HUMANLOXL4physical
21163940
PRDX2_HUMANPRDX2physical
21163940
RD23A_HUMANRAD23Aphysical
21163940
RHEB_HUMANRHEBphysical
21163940
ECSIT_HUMANECSITphysical
21163940
FBXW4_HUMANFBXW4physical
21163940
CEP55_HUMANCEP55physical
21163940
STALP_HUMANSTAMBPL1physical
21163940
A4_HUMANAPPphysical
21163940
CP2C8_HUMANCYP2C8physical
21163940
CP2C9_HUMANCYP2C9physical
21163940
FXL12_HUMANFBXL12physical
21163940
IFIT3_HUMANIFIT3physical
21163940
P4K2A_HUMANPI4K2Aphysical
21163940
RAB3A_HUMANRAB3Aphysical
21163940
TF65_HUMANRELAphysical
25355951
NFKB1_HUMANNFKB1physical
25355951
M3K7_HUMANMAP3K7physical
25371197
NDUB1_HUMANNDUFB1physical
26186194
IF2M_HUMANMTIF2physical
26186194
NU4M_HUMANND4physical
26186194
CIA30_HUMANNDUFAF1physical
26186194
EFGM_HUMANGFM1physical
26186194
NDUS2_HUMANNDUFS2physical
26186194
ACADV_HUMANACADVLphysical
26186194
DECR_HUMANDECR1physical
26186194
NDUA3_HUMANNDUFA3physical
26186194
2ABD_HUMANPPP2R2Dphysical
26186194
NDUF4_HUMANNDUFAF4physical
26186194
ACAD9_HUMANACAD9physical
26186194
NDUB8_HUMANNDUFB8physical
26186194
CLPP_HUMANCLPPphysical
26186194
MGME1_HUMANMGME1physical
26186194
NU1M_HUMANND1physical
26186194
TR61B_HUMANTRMT61Bphysical
26186194
NDUA8_HUMANNDUFA8physical
26186194
COA1_HUMANCOA1physical
26186194
T126B_HUMANTMEM126Bphysical
26186194
NDUC2_HUMANNDUFC2physical
26186194
NDUS8_HUMANNDUFS8physical
26186194
NDUB5_HUMANNDUFB5physical
26186194
NNTM_HUMANNNTphysical
26186194
MRP7_HUMANABCC10physical
26186194
MGME1_HUMANMGME1physical
24344204
CIA30_HUMANNDUFAF1physical
24344204
TM186_HUMANTMEM186physical
24344204
ACAD9_HUMANACAD9physical
24344204
T126B_HUMANTMEM126Bphysical
24344204
TMM70_HUMANTMEM70physical
24344204
TIDC1_HUMANTIMMDC1physical
24344204
CP24A_HUMANCYP24A1physical
24344204
RT17_HUMANMRPS17physical
24344204
ITB1_HUMANITGB1physical
24344204
NDUF3_HUMANNDUFAF3physical
24344204
MCCB_HUMANMCCC2physical
24344204
ATD3B_HUMANATAD3Bphysical
24344204
SYIM_HUMANIARS2physical
24344204
KBL_HUMANGCATphysical
24344204
NDUS2_HUMANNDUFS2physical
24344204
NU4M_HUMANND4physical
24344204
NDUS1_HUMANNDUFS1physical
24344204
NDUBB_HUMANNDUFB11physical
24344204
ACAD9_HUMANACAD9physical
20816094
CIA30_HUMANNDUFAF1physical
20816094
ACAD9_HUMANACAD9physical
28514442
CIA30_HUMANNDUFAF1physical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
NDUB1_HUMANNDUFB1physical
28514442
NDUC2_HUMANNDUFC2physical
28514442
COA1_HUMANCOA1physical
28514442
MRP7_HUMANABCC10physical
28514442
NU4M_HUMANND4physical
28514442
NDUA3_HUMANNDUFA3physical
28514442
T126B_HUMANTMEM126Bphysical
28514442
NDUA8_HUMANNDUFA8physical
28514442
CLPP_HUMANCLPPphysical
28514442
IF2M_HUMANMTIF2physical
28514442
NDUB8_HUMANNDUFB8physical
28514442
NDUS8_HUMANNDUFS8physical
28514442
NU1M_HUMANND1physical
28514442
ACADV_HUMANACADVLphysical
28514442
EFGM_HUMANGFM1physical
28514442
NDUF4_HUMANNDUFAF4physical
28514442
MARF1_HUMANKIAA0430physical
27173435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECSIT_HUMAN

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Related Literatures of Post-Translational Modification

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