dbPTM

I13R2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	I13R2_HUMAN
UniProt AC	Q14627
Protein Name	Interleukin-13 receptor subunit alpha-2
Gene Name	IL13RA2
Organism	Homo sapiens (Human).
Sequence Length	380
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	Binds as a monomer with high affinity to interleukin-13 (IL13), but not to interleukin-4 (IL4)..
Protein Sequence	MAFVCLAIGCLYTFLISTTFGCTSSSDTEIKVNPPQDFEIVDPGYLGYLYLQWQPPLSLDHFKECTVEYELKYRNIGSETWKTIITKNLHYKDGFDLNKGIEAKIHTLLPWQCTNGSEVQSSWAETTYWISPQGIPETKVQDMDCVYYNWQYLLCSWKPGIGVLLDTNYNLFYWYEGLDHALQCVDYIKADGQNIGCRFPYLEASDYKDFYICVNGSSENKPIRSSYFTFQLQNIVKPLPPVYLTFTRESSCEIKLKWSIPLGPIPARCFDYEIEIREDDTTLVTATVENETYTLKTTNETRQLCFVVRSKVNIYCSDDGIWSEWSDKQCWEGEDLSKKTLLRFWLPFGFILILVIFVTGLLLRKPNTYPKMIPEFFCDT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
115	N-linked_Glycosylation	LLPWQCTNGSEVQSS ECCEECCCCCEEECC	60.67	UniProtKB CARBOHYD
215	N-linked_Glycosylation	KDFYICVNGSSENKP CCEEEEECCCCCCCC	39.97	20223216
290	N-linked_Glycosylation	LVTATVENETYTLKT EEEEEEECCEEEEEE	42.44	UniProtKB CARBOHYD
299	N-linked_Glycosylation	TYTLKTTNETRQLCF EEEEEECCCCEEEEE	54.60	UniProtKB CARBOHYD

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 I13R2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of I13R2_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 I13R2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TSH3_HUMAN	TSHZ3	physical	28514442
ENDD1_HUMAN	ENDOD1	physical	28514442
NEK6_HUMAN	NEK6	physical	28514442
CQ080_HUMAN	C17orf80	physical	28514442
SCMC3_HUMAN	SLC25A23	physical	28514442
RN5A_HUMAN	RNASEL	physical	28514442
MP2K7_HUMAN	MAP2K7	physical	28514442
STML1_HUMAN	STOML1	physical	28514442
ZN195_HUMAN	ZNF195	physical	28514442
SIA4B_HUMAN	ST3GAL2	physical	28514442
SAMD1_HUMAN	SAMD1	physical	28514442
MET15_HUMAN	METTL15	physical	28514442
PTPRF_HUMAN	PTPRF	physical	28514442
ULBP3_HUMAN	ULBP3	physical	28514442
DSCR3_HUMAN	DSCR3	physical	28514442
CHK1_HUMAN	CHEK1	physical	28514442
TV23C_HUMAN	TVP23C	physical	28514442
IPO11_HUMAN	IPO11	physical	28514442
KPCD2_HUMAN	PRKD2	physical	28514442
ORC5_HUMAN	ORC5	physical	28514442
PHLB3_HUMAN	PHLDB3	physical	28514442
SDK2_HUMAN	SDK2	physical	28514442
COMD3_HUMAN	COMMD3	physical	28514442
DHB11_HUMAN	HSD17B11	physical	28514442
BCD1_HUMAN	ZNHIT6	physical	28514442
ECM29_HUMAN	KIAA0368	physical	28514442
SCMC2_HUMAN	SLC25A25	physical	28514442
TPPC5_HUMAN	TRAPPC5	physical	28514442
PTPM1_HUMAN	PTPMT1	physical	28514442
ABHEA_HUMAN	ABHD14A	physical	28514442
GCN1_HUMAN	GCN1L1	physical	28514442
INT12_HUMAN	INTS12	physical	28514442
NEK7_HUMAN	NEK7	physical	28514442
MELK_HUMAN	MELK	physical	28514442
TNFL9_HUMAN	TNFSF9	physical	28514442
GLPK_HUMAN	GK	physical	28514442
B4GT5_HUMAN	B4GALT5	physical	28514442
SYMPK_HUMAN	SYMPK	physical	28514442
MTO1_HUMAN	MTO1	physical	28514442
KIRR1_HUMAN	KIRREL	physical	28514442
HXD13_HUMAN	HOXD13	physical	28514442
SIK2_HUMAN	SIK2	physical	28514442
JAK1_HUMAN	JAK1	physical	28514442
MTFR1_HUMAN	MTFR1	physical	28514442
MRRP3_HUMAN	KIAA0391	physical	28514442
HIP1R_HUMAN	HIP1R	physical	28514442
ZDH18_HUMAN	ZDHHC18	physical	28514442
NAMPT_HUMAN	NAMPT	physical	28514442
XRCC3_HUMAN	XRCC3	physical	28514442
SH3B4_HUMAN	SH3BP4	physical	28514442
MYO19_HUMAN	MYO19	physical	28514442
ANTR1_HUMAN	ANTXR1	physical	28514442
F207A_HUMAN	FAM207A	physical	28514442
S2546_HUMAN	SLC25A46	physical	28514442
PTPRS_HUMAN	PTPRS	physical	28514442
SYRM_HUMAN	RARS2	physical	28514442
GATB_HUMAN	GATB	physical	28514442
ARV1_HUMAN	ARV1	physical	28514442
GUF1_HUMAN	GUF1	physical	28514442
RPP29_HUMAN	POP4	physical	28514442
ECHD1_HUMAN	ECHDC1	physical	28514442
PALD_HUMAN	PALD1	physical	28514442
SGPL1_HUMAN	SGPL1	physical	28514442
LRFN1_HUMAN	LRFN1	physical	28514442
RFC4_HUMAN	RFC4	physical	28514442
LAR4B_HUMAN	LARP4B	physical	28514442
UCKL1_HUMAN	UCKL1	physical	28514442
TMED4_HUMAN	TMED4	physical	28514442
B4GT1_HUMAN	B4GALT1	physical	28514442
RICTR_HUMAN	RICTOR	physical	28514442
RFC5_HUMAN	RFC5	physical	28514442
TTK_HUMAN	TTK	physical	28514442
RAB3B_HUMAN	RAB3B	physical	28514442
RPTOR_HUMAN	RPTOR	physical	28514442
NOCT_HUMAN	CCRN4L	physical	28514442
ERF_HUMAN	ERF	physical	28514442
ELYS_HUMAN	AHCTF1	physical	28514442
SENP1_HUMAN	SENP1	physical	28514442
MA1A2_HUMAN	MAN1A2	physical	28514442
DAG1_HUMAN	DAG1	physical	28514442
ALG5_HUMAN	ALG5	physical	28514442
BDH_HUMAN	BDH1	physical	28514442
ADCK1_HUMAN	ADCK1	physical	28514442
AT12A_HUMAN	ATP12A	physical	28514442
INT7_HUMAN	INTS7	physical	28514442
MCU_HUMAN	MCU	physical	28514442
RB15B_HUMAN	RBM15B	physical	28514442
B4GT3_HUMAN	B4GALT3	physical	28514442
CAND1_HUMAN	CAND1	physical	28514442
DAAF5_HUMAN	DNAAF5	physical	28514442
KNTC1_HUMAN	KNTC1	physical	28514442
TM2D3_HUMAN	TM2D3	physical	28514442
SEM4C_HUMAN	SEMA4C	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.

Regulatory Network of I13R2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Molecular basis for shared cytokine recognition revealed in thestructure of an unusually high affinity complex between IL-13 and IL-13Ralpha2."; Lupardus P.J., Birnbaum M.E., Garcia K.C.; Structure 18:332-342(2010). Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH IL13, FUNCTION,DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-215.	20223216 [Abstract]