dbPTM

IL1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IL1B_HUMAN
UniProt AC	P01584
Protein Name	Interleukin-1 beta {ECO:0000303\|PubMed:1919436}
Gene Name	IL1B {ECO:0000312\|HGNC:HGNC:5992}
Organism	Homo sapiens (Human).
Sequence Length	269
Subcellular Localization	Cytoplasm, cytosol . Lysosome . Secreted, exosome . Secreted . The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. IL1B la
Protein Description	Potent proinflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. [PubMed: 10653850]
Protein Sequence	MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	Ubiquitination	FFEADGPKQMKCSFQ EEECCCCCCCCEEEC	69.43	32015554
59	Acetylation	ISDHHYSKGFRQAAS ECCCCCCCCHHHHHH	55.70	26210075
133	Phosphorylation	LRDSQQKSLVMSGPY ECHHHHCEEEEECCC	23.12	24961811
140	Phosphorylation	SLVMSGPYELKALHL EEEEECCCEEEEEEE	37.10	-
161	Phosphorylation	QQVVFSMSFVQGEES HEEEEEEEEECCCCC	22.52	23532336
184	Phosphorylation	GLKEKNLYLSCVLKD ECCCCCEEEEEEECC	13.13	25404012
186	Phosphorylation	KEKNLYLSCVLKDDK CCCCEEEEEEECCCC	6.66	25404012
200	Phosphorylation	KPTLQLESVDPKNYP CCCEEEEECCCCCCC	40.17	24719451
206	Phosphorylation	ESVDPKNYPKKKMEK EECCCCCCCCHHHHH	23.66	24719451
269	Phosphorylation	FTMQFVSS------- HHHEECCC-------	38.65	-

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 IL1B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IL1B_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 IL1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JIP2_HUMAN	MAPK8IP2	genetic	10756100
ZN675_HUMAN	ZNF675	genetic	11751921
UBE2N_HUMAN	UBE2N	genetic	11057907
IL1R1_HUMAN	IL1R1	physical	7878046
EGR1_HUMAN	EGR1	physical	22455954
SP1_HUMAN	SP1	physical	22455954
A4_HUMAN	APP	physical	21832049
A2MG_HUMAN	A2M	physical	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
DB06168	Canakinumab
DB05260	Gallium nitrate
DB01017	Minocycline
DB06372	Rilonacept

Regulatory Network of IL1B_HUMAN

Related Literatures of Post-Translational Modification