IRPL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IRPL2_HUMAN
• UniProt AC: Q9NP60
• Protein Name: X-linked interleukin-1 receptor accessory protein-like 2
• Gene Name: IL1RAPL2
• Organism: Homo sapiens (Human).
• Sequence Length: 686
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Sequence: MKPPFLLALVVCSVVSTNLKMVSKRNSVDGCIDWSVDLKTYMALAGEPVRVKCALFYSYIRTNYSTAQSTGLRLMWYKNKGDLEEPIIFSEVRMSKEEDSIWFHSAEAQDSGFYTCVLRNSTYCMKVSMSLTVAENESGLCYNSRIRYLEKSEVTKRKEISCPDMDDFKKSDQEPDVVWYKECKPKMWRSIIIQKGNALLIQEVQEEDGGNYTCELKYEGKLVRRTTELKVTALLTDKPPKPLFPMENQPSVIDVQLGKPLNIPCKAFFGFSGESGPMIYWMKGEKFIEELAGHIREGEIRLLKEHLGEKEVELALIFDSVVEADLANYTCHVENRNGRKHASVLLRKKDLIYKIELAGGLGAIFLLLVLLVVIYKCYNIELMLFYRQHFGADETNDDNKEYDAYLSYTKVDQDTLDCDNPEEEQFALEVLPDVLEKHYGYKLFIPERDLIPSGTYMEDLTRYVEQSRRLIIVLTPDYILRRGWSIFELESRLHNMLVSGEIKVILIECTELKGKVNCQEVESLKRSIKLLSLIKWKGSKSSKLNSKFWKHLVYEMPIKKKEMLPRCHVLDSAEQGLFGELQPIPSIAMTSTSATLVSSQADLPEFHPSDSMQIRHCCRGYKHEIPATTLPVPSLGNHHTYCNLPLTLLNGQLPLNNTLKDTQEFHRNSSLLPLSSKELSFTSDIW

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
23	Phosphorylation	STNLKMVSKRNSVDG HCCCCCCCCCCCCCC	23.54	-
27	Phosphorylation	KMVSKRNSVDGCIDW CCCCCCCCCCCEEEE	26.14	-
35	Phosphorylation	VDGCIDWSVDLKTYM CCCEEEEEEEHHHHH	11.29	-
63	N-linked_Glycosylation	FYSYIRTNYSTAQST HHHHHHCCCCCHHHH	20.93	UniProtKB CARBOHYD
78	Sumoylation	GLRLMWYKNKGDLEE CCEEEEECCCCCCCC	36.35	-
78	Sumoylation	GLRLMWYKNKGDLEE CCEEEEECCCCCCCC	36.35	-
90	Phosphorylation	LEEPIIFSEVRMSKE CCCCEEEEEEECCCC	25.44	24719451
120	N-linked_Glycosylation	FYTCVLRNSTYCMKV EEEEEEECCCEEEEE	34.25	UniProtKB CARBOHYD
122	Phosphorylation	TCVLRNSTYCMKVSM EEEEECCCEEEEEEE	25.04	-
136	N-linked_Glycosylation	MSLTVAENESGLCYN EEEEEEECCCCCCCH	38.71	UniProtKB CARBOHYD
170	Acetylation	PDMDDFKKSDQEPDV CCHHHHHHCCCCCCC	60.29	11791563
211	N-linked_Glycosylation	VQEEDGGNYTCELKY EEEHHCCCEEEEEEE	34.17	UniProtKB CARBOHYD
226	Phosphorylation	EGKLVRRTTELKVTA CCEEEEEEEEEEEEE	17.66	23898821
227	Phosphorylation	GKLVRRTTELKVTAL CEEEEEEEEEEEEEE	37.19	23898821
232	Phosphorylation	RTTELKVTALLTDKP EEEEEEEEEEECCCC	15.25	23898821
275	Phosphorylation	FFGFSGESGPMIYWM EEECCCCCCCEEEEE	52.28	27732954
280	Phosphorylation	GESGPMIYWMKGEKF CCCCCEEEEEECHHH	8.00	27732954
328	N-linked_Glycosylation	VVEADLANYTCHVEN HHHHHHHHCEEEEEC	39.69	UniProtKB CARBOHYD
343	Phosphorylation	RNGRKHASVLLRKKD CCCCEEEEEEEECCC	17.02	20230923
408	Phosphorylation	EYDAYLSYTKVDQDT EEEEEEEEEEECCCC	14.16	-
409	Phosphorylation	YDAYLSYTKVDQDTL EEEEEEEEEECCCCC	22.63	-
455	Phosphorylation	RDLIPSGTYMEDLTR HHCCCCCCCHHHHHH	24.83	-
456	Phosphorylation	DLIPSGTYMEDLTRY HCCCCCCCHHHHHHH	11.30	-
532	Phosphorylation	KRSIKLLSLIKWKGS HHHHHHHHHHCCCCC	38.18	24719451
541	Phosphorylation	IKWKGSKSSKLNSKF HCCCCCCCHHCCHHH	34.11	-
542	Phosphorylation	KWKGSKSSKLNSKFW CCCCCCCHHCCHHHH	44.92	-
543	Acetylation	WKGSKSSKLNSKFWK CCCCCCHHCCHHHHH	59.80	12653657
547	Acetylation	KSSKLNSKFWKHLVY CCHHCCHHHHHHHHH	54.92	12653667
560	Acetylation	VYEMPIKKKEMLPRC HHHCCCCHHHHCCCC	55.47	7851367
561	Acetylation	YEMPIKKKEMLPRCH HHCCCCHHHHCCCCE	43.27	7851377
609	Phosphorylation	DLPEFHPSDSMQIRH CCCCCCCCCCHHHHH	33.47	21601212

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

Oops, there are no upstream regulatory protein records of IRPL2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IRPL2_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 IRPL2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of IRPL2_HUMAN !!

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.