IFI44_HUMAN - dbPTM
IFI44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFI44_HUMAN
UniProt AC Q8TCB0
Protein Name Interferon-induced protein 44
Gene Name IFI44
Organism Homo sapiens (Human).
Sequence Length 444
Subcellular Localization Cytoplasm .
Protein Description This protein aggregates to form microtubular structures..
Protein Sequence MAVTTRLTWLHEKILQNHFGGKRLSLLYKGSVHGFRNGVLLDRCCNQGPTLTVIYSEDHIIGAYAEESYQEGKYASIILFALQDTKISEWKLGLCTPETLFCCDVTKYNSPTNFQIDGRNRKVIMDLKTMENLGLAQNCTISIQDYEVFRCEDSLDERKIKGVIELRKSLLSALRTYEPYGSLVQQIRILLLGPIGAGKSSFFNSVRSVFQGHVTHQALVGTNTTGISEKYRTYSIRDGKDGKYLPFILCDSLGLSEKEGGLCRDDIFYILNGNIRDRYQFNPMESIKLNHHDYIDSPSLKDRIHCVAFVFDASSIQYFSSQMIVKIKRIRRELVNAGVVHVALLTHVDSMDLITKGDLIEIERCEPVRSKLEEVQRKLGFALSDISVVSNYSSEWELDPVKDVLILSALRRMLWAADDFLEDLPFEQIGNLREEIINCAQGKK
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
3 (in isoform 2)Phosphorylation-5.6129507054
14 (in isoform 2)Phosphorylation-4.3329507054
18UbiquitinationHEKILQNHFGGKRLS
HHHHHHHCCCCCEEE
15.12-
22UbiquitinationLQNHFGGKRLSLLYK
HHHCCCCCEEEEEEC
51.0129967540
107UbiquitinationLFCCDVTKYNSPTNF
EEEEECCCCCCCCCE
42.1321963094
108PhosphorylationFCCDVTKYNSPTNFQ
EEEECCCCCCCCCEE
16.1130108239
110PhosphorylationCDVTKYNSPTNFQID
EECCCCCCCCCEEEC
29.9730108239
161UbiquitinationSLDERKIKGVIELRK
CCCHHHHHHHHHHHH
50.6029967540
199UbiquitinationLGPIGAGKSSFFNSV
HCCCCCCHHHHHHHH
42.25-
205PhosphorylationGKSSFFNSVRSVFQG
CHHHHHHHHHHHHCC
17.4723186163
208PhosphorylationSFFNSVRSVFQGHVT
HHHHHHHHHHCCCCC
25.73-
215PhosphorylationSVFQGHVTHQALVGT
HHHCCCCCCEEEECC
11.55-
225PhosphorylationALVGTNTTGISEKYR
EEECCCCCCCCCEEE
34.29-
235PhosphorylationSEKYRTYSIRDGKDG
CCEEEEEEEEECCCC
15.5524719451
240UbiquitinationTYSIRDGKDGKYLPF
EEEEEECCCCCEECE
68.5430230243
269PhosphorylationLCRDDIFYILNGNIR
CCCCCEEEEECCCCC
12.58-
299PhosphorylationHDYIDSPSLKDRIHC
CCCCCCCCHHHHEEE
52.5929507054
301UbiquitinationYIDSPSLKDRIHCVA
CCCCCCHHHHEEEEE
49.6621963094
371UbiquitinationRCEPVRSKLEEVQRK
ECCCHHHHHHHHHHH
49.7229967540
392PhosphorylationDISVVSNYSSEWELD
HCEEEECCCCCCCCC
13.18-
408PhosphorylationVKDVLILSALRRMLW
HHHHHHHHHHHHHHH
20.4723403867
443MethylationIINCAQGKK------
HHHHHCCCC------
43.1423644510
443"N6,N6-dimethyllysine"IINCAQGKK------
HHHHHCCCC------
43.14-

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 IFI44_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFI44_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 IFI44_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of IFI44_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IFI44_HUMAN

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Related Literatures of Post-Translational Modification

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