dbPTM

IL12B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IL12B_HUMAN
UniProt AC	P29460
Protein Name	Interleukin-12 subunit beta
Gene Name	IL12B
Organism	Homo sapiens (Human).
Sequence Length	328
Subcellular Localization	Secreted.
Protein Description	Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC.; Associates with IL23A to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis..
Protein Sequence	MCHQQLVISWFSLVFLASPLVAIWELKKDVYVVELDWYPDAPGEMVVLTCDTPEEDGITWTLDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSHSLLLLHKKEDGIWSTDILKDQKEPKNKTFLRCEAKNYSGRFTCWWLTTISTDLTFSVKSSRGSSDPQGVTCGAATLSAERVRGDNKEYEYSVECQEDSACPAAEESLPIEVMVDAVHKLKYENYTSSFFIRDIIKPDPPKNLQLKPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKSKREKKDRVFTDKTSATVICRKNASISVRAQDRYYSSSWSEWASVPCS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
135	N-linked_Glycosylation	FLRCEAKNYSGRFTC EEEEEEECCCCCEEE	43.16	UniProtKB CARBOHYD
141	Phosphorylation	KNYSGRFTCWWLTTI ECCCCCEEEEEEEEE	13.07	29759185
146	Phosphorylation	RFTCWWLTTISTDLT CEEEEEEEEEECEEE	14.36	29759185
147	Phosphorylation	FTCWWLTTISTDLTF EEEEEEEEEECEEEE	15.68	29759185
162	Phosphorylation	SVKSSRGSSDPQGVT EEECCCCCCCCCCCC	30.38	18491316
163	Phosphorylation	VKSSRGSSDPQGVTC EECCCCCCCCCCCCC	57.01	18491316
169	Phosphorylation	SSDPQGVTCGAATLS CCCCCCCCCCEEEEE	16.43	-
174	Phosphorylation	GVTCGAATLSAERVR CCCCCEEEEEEEECC	22.25	-
176	Phosphorylation	TCGAATLSAERVRGD CCCEEEEEEEECCCC	24.59	24719451
220	Phosphorylation	DAVHKLKYENYTSSF ECHHHHCCCCCCCEE	21.61	30576142
222	N-linked_Glycosylation	VHKLKYENYTSSFFI HHHHCCCCCCCEEEE	42.14	10899108
226	Phosphorylation	KYENYTSSFFIRDII CCCCCCCEEEEEHHC	19.17	30576142
314	Phosphorylation	SVRAQDRYYSSSWSE EEEEECCCCCCCHHH	18.91	-
319	C-linked_Glycosylation	DRYYSSSWSEWASVP CCCCCCCHHHCCCCC	11.39	10207176

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 IL12B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IL12B_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 IL12B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
IL23A_HUMAN	IL23A	physical	11114383
ERP44_HUMAN	ERP44	physical	16467190

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614890	Immunodeficiency 29 (IMD29)
612599	Psoriasis 11 (PSORS11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IL12B_HUMAN

Related Literatures of Post-Translational Modification

C-linked Glycosylation
Reference	PubMed
"Recombinant human interleukin-12 is the second example of a C-mannosylated protein."; Doucey M.A., Hess D., Blommers M.J., Hofsteenge J.; Glycobiology 9:435-441(1999). Cited for: GLYCOSYLATION AT TRP-319.	10207176 [Abstract]
N-linked Glycosylation
Reference	PubMed
"Charged residues dominate a unique interlocking topography in theheterodimeric cytokine interleukin-12."; Yoon C., Johnston S.C., Tang J., Stahl M., Tobin J.F., Somers W.S.; EMBO J. 19:3530-3541(2000). Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-328 ALONE AND IN COMPLEXWITH IL12A, GLYCOSYLATION AT ASN-222, AND DISULFIDE BONDS.	10899108 [Abstract]