IFRD1_HUMAN - dbPTM
IFRD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFRD1_HUMAN
UniProt AC O00458
Protein Name Interferon-related developmental regulator 1
Gene Name IFRD1
Organism Homo sapiens (Human).
Sequence Length 451
Subcellular Localization
Protein Description Could play a role in regulating gene activity in the proliferative and/or differentiative pathways induced by NGF. May be an autocrine factor that attenuates or amplifies the initial ligand-induced signal (By similarity)..
Protein Sequence MPKNKKRNTPHRGSSAGGGGSGAAAATAATAGGQHRNVQPFSDEDASIETMSHCSGYSDPSSFAEDGPEVLDEEGTQEDLEYKLKGLIDLTLDKSAKTRQAALEGIKNALASKMLYEFILERRMTLTDSIERCLKKGKSDEQRAAAALASVLCIQLGPGIESEEILKTLGPILKKIICDGSASMQARQTCATCFGVCCFIATDDITELYSTLECLENIFTKSYLKEKDTTVICSTPNTVLHISSLLAWTLLLTICPINEVKKKLEMHFHKLPSLLSCDDVNMRIAAGESLALLFELARGIESDFFYEDMESLTQMLRALATDGNKHRAKVDKRKQRSVFRDVLRAVEERDFPTETIKFGPERMYIDCWVKKHTYDTFKEVLGSGMQYHLQSNEFLRNVFELGPPVMLDAATLKTMKISRFERHLYNSAAFKARTKARSKCRDKRADVGEFF
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
9PhosphorylationPKNKKRNTPHRGSSA
CCCCCCCCCCCCCCC
25.2229978859
14PhosphorylationRNTPHRGSSAGGGGS
CCCCCCCCCCCCCHH
19.5725159151
15PhosphorylationNTPHRGSSAGGGGSG
CCCCCCCCCCCCHHH
33.4825159151
21PhosphorylationSSAGGGGSGAAAATA
CCCCCCHHHHHHHHH
28.6525159151
27PhosphorylationGSGAAAATAATAGGQ
HHHHHHHHHHHCCCC
16.4626699800
30PhosphorylationAAAATAATAGGQHRN
HHHHHHHHCCCCCCC
24.3027080861
94UbiquitinationLIDLTLDKSAKTRQA
HHHHHCCCCHHHHHH
56.26-
107UbiquitinationQAALEGIKNALASKM
HHHHHHHHHHHHHHH
47.20-
116PhosphorylationALASKMLYEFILERR
HHHHHHHHHHHHHHC
12.8019664994
162PhosphorylationQLGPGIESEEILKTL
HHCCCCCHHHHHHHH
38.31-
174UbiquitinationKTLGPILKKIICDGS
HHHHHHHHHHHCCCC
42.5221890473
174UbiquitinationKTLGPILKKIICDGS
HHHHHHHHHHHCCCC
42.5221890473
175UbiquitinationTLGPILKKIICDGSA
HHHHHHHHHHCCCCH
33.5821890473
175UbiquitinationTLGPILKKIICDGSA
HHHHHHHHHHCCCCH
33.5821890473
325UbiquitinationALATDGNKHRAKVDK
HHHHCCCCHHHHCCH
39.74-
357UbiquitinationDFPTETIKFGPERMY
CCCCCCEECCCCCEE
52.25-
371UbiquitinationYIDCWVKKHTYDTFK
EEEEEEEHHCHHHHH
31.40-
416UbiquitinationAATLKTMKISRFERH
HHHHHHHCCHHHHHH
42.64-
425PhosphorylationSRFERHLYNSAAFKA
HHHHHHHHHHHHHHH
10.8423312004
427PhosphorylationFERHLYNSAAFKART
HHHHHHHHHHHHHHH
13.8622817900
431UbiquitinationLYNSAAFKARTKARS
HHHHHHHHHHHHHHH
32.03-

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 IFRD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFRD1_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 IFRD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
12198164
MEF2C_HUMANMEF2Cphysical
15743821
IFRD1_HUMANIFRD1physical
15743821
HDAC4_HUMANHDAC4physical
15743821

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 IFRD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.

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