ILRL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ILRL2_HUMAN
• UniProt AC: Q9HB29
• Protein Name: Interleukin-1 receptor-like 2
• Gene Name: IL1RL2
• Organism: Homo sapiens (Human).
• Sequence Length: 575
• Subcellular Localization: Membrane; Single-pass type I membrane protein .
• Protein Description: Receptor for interleukin-36 (IL36A, IL36B and IL36G). After binding to interleukin-36 associates with the coreceptor IL1RAP to form the interleukin-36 receptor complex which mediates interleukin-36-dependent activation of NF-kappa-B, MAPK and other pathways (By similarity). The IL-36 signaling system is thought to be present in epithelial barriers and to take part in local inflammatory response; it is similar to the IL-1 system. Seems to be involved in skin inflammatory response by induction of the IL-23/IL-17/IL-22 pathway..
• Protein Sequence: MWSLLLCGLSIALPLSVTADGCKDIFMKNEILSASQPFAFNCTFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLTVFEKHWCDTSIGGLPNLSDEYKQILHLGKDDSLTCHLHFPKSCVLGPIKWYKDCNEIKGERFTVLETRLLVSNVSAEDRGNYACQAILTHSGKQYEVLNGITVSITERAGYGGSVPKIIYPKNHSIEVQLGTTLIVDCNVTDTKDNTNLRCWRVNNTLVDDYYDESKRIREGVETHVSFREHNLYTVNITFLEVKMEDYGLPFMCHAGVSTAYIILQLPAPDFRAYLIGGLIALVAVAVSVVYIYNIFKIDIVLWYRSAFHSTETIVDGKLYDAYVLYPKPHKESQRHAVDALVLNILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLLKNLSEEQIAVYSALIQDGMKVILIELEKIEDYTVMPESIQYIKQKHGAIRWHGDFTEQSQCMKTKFWKTVRYHMPPRRCRPFPPVQLLQHTPCYRTAGPELGSRRKKCTLTTG

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
41	N-linked_Glycosylation	ASQPFAFNCTFPPIT CCCCEEEEECCCCCC	22.08	UniProtKB CARBOHYD
59	N-linked_Glycosylation	VSVTWYKNSSKIPVS EEEEEEECCCCCCHH	35.50	UniProtKB CARBOHYD
109	N-linked_Glycosylation	SCHRIHVNLTVFEKH CCEEEEEEEEEEECE	18.81	UniProtKB CARBOHYD
127	N-linked_Glycosylation	TSIGGLPNLSDEYKQ CCCCCCCCCCHHHHH	58.16	UniProtKB CARBOHYD
184	N-linked_Glycosylation	ETRLLVSNVSAEDRG EEEEEECCCCHHHCC	25.04	UniProtKB CARBOHYD
234	N-linked_Glycosylation	PKIIYPKNHSIEVQL CEEEECCCCEEEEEE	29.63	UniProtKB CARBOHYD
250	N-linked_Glycosylation	TTLIVDCNVTDTKDN CEEEEECCCCCCCCC	34.95	UniProtKB CARBOHYD
266	N-linked_Glycosylation	NLRCWRVNNTLVDDY CEEEEEECCEEECCC	27.48	UniProtKB CARBOHYD
286	Phosphorylation	RIREGVETHVSFREH HHHCHHHHEEECCCC	25.77	27251275
289	Phosphorylation	EGVETHVSFREHNLY CHHHHEEECCCCCEE	15.81	27251275
299	N-linked_Glycosylation	EHNLYTVNITFLEVK CCCEEEEEEEEEEEE	21.56	UniProtKB CARBOHYD
369	Phosphorylation	DIVLWYRSAFHSTET CEEEEEHHHCCCCCE	21.42	22210691
373	Phosphorylation	WYRSAFHSTETIVDG EEHHHCCCCCEEECC	22.83	28060719
374	Phosphorylation	YRSAFHSTETIVDGK EHHHCCCCCEEECCE	28.69	28060719
376	Phosphorylation	SAFHSTETIVDGKLY HHCCCCCEEECCEEE	26.79	22210691
503	Phosphorylation	VMPESIQYIKQKHGA CCHHHHHHHHHHCCC	14.39	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ILRL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ILRL2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ILRL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POTEI_HUMAN	POTEI	physical	28514442
AUXI_HUMAN	DNAJC6	physical	28514442
MYO1F_HUMAN	MYO1F	physical	28514442
MICA1_HUMAN	MICAL1	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
GET4_HUMAN	GET4	physical	28514442

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.