IL1A_HUMAN - dbPTM
IL1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IL1A_HUMAN
UniProt AC P01583
Protein Name Interleukin-1 alpha
Gene Name IL1A
Organism Homo sapiens (Human).
Sequence Length 271
Subcellular Localization Secreted. The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.
Protein Description Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells..
Protein Sequence MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA
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
15PhosphorylationFEDLKNCYSENEEDS
HHHHHHHCCCCCCCC
28.5425002506
16PhosphorylationEDLKNCYSENEEDSS
HHHHHHCCCCCCCCC
35.8230108239
22PhosphorylationYSENEEDSSSIDHLS
CCCCCCCCCCCCEEE
29.3030108239
23PhosphorylationSENEEDSSSIDHLSL
CCCCCCCCCCCEEEE
43.5730108239
24PhosphorylationENEEDSSSIDHLSLN
CCCCCCCCCCEEEEC
35.6727794612
29PhosphorylationSSSIDHLSLNQKSFY
CCCCCEEEECCCCEE
23.1225002506
59PhosphorylationVSLSISETSKTSKLT
EEEEEECCCCCCCCC
28.82-
60PhosphorylationSLSISETSKTSKLTF
EEEEECCCCCCCCCC
29.86-
66PhosphorylationTSKTSKLTFKESMVV
CCCCCCCCCCCCEEE
36.08-
82N6-myristoyl lysineATNGKVLKKRRLSLS
EECCCEEEEECCCCC
47.42-
82MyristoylationATNGKVLKKRRLSLS
EECCCEEEEECCCCC
47.428346241
83MyristoylationTNGKVLKKRRLSLSQ
ECCCEEEEECCCCCC
38.298346241
83N6-myristoyl lysineTNGKVLKKRRLSLSQ
ECCCEEEEECCCCCC
38.29-
87PhosphorylationVLKKRRLSLSQSITD
EEEEECCCCCCCCCH
24.9428355574
89PhosphorylationKKRRLSLSQSITDDD
EEECCCCCCCCCHHH
20.6428176443
91PhosphorylationRRLSLSQSITDDDLE
ECCCCCCCCCHHHHH
24.8728176443
93PhosphorylationLSLSQSITDDDLEAI
CCCCCCCCHHHHHHH
38.3329507054
102N-linked_GlycosylationDDLEAIANDSEEEII
HHHHHHHCCCHHHCC
47.42UniProtKB CARBOHYD
104PhosphorylationLEAIANDSEEEIIKP
HHHHHCCCHHHCCCC
46.8726657352
141N-linked_GlycosylationFILNDALNQSIIRAN
HHHCHHHHHHHHHHC
34.96UniProtKB CARBOHYD
143PhosphorylationLNDALNQSIIRANDQ
HCHHHHHHHHHHCCH
20.9324719451
189PhosphorylationVILRISKTQLYVTAQ
EEEEECCCEEEEEEC
19.6022817900

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 IL1A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IL1A_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 IL1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NECD_HUMANNDNphysical
12913118
S10AD_HUMANS100A13physical
12746488
HAX1_HUMANHAX1physical
11554782
IL1A_HUMANIL1Aphysical
11554782
SPT7_YEASTSPT7physical
22879895
SPT8_YEASTSPT8physical
22879895
HFI1_YEASTHFI1physical
22879895
GCN5_YEASTGCN5physical
22879895
ADA2_YEASTADA2physical
22879895
NGG1_YEASTNGG1physical
22879895
AHC1_YEASTAHC1physical
22879895
IL1R2_HUMANIL1R2physical
25241761

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 IL1A_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"The 31-kDa precursor of interleukin 1 alpha is myristoylated onspecific lysines within the 16-kDa N-terminal propiece.";
Stevenson F.T., Bursten S.L., Fanton C., Locksley R.M., Lovett D.H.;
Proc. Natl. Acad. Sci. U.S.A. 90:7245-7249(1993).
Cited for: MYRISTOYLATION AT LYS-82 AND LYS-83.

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