IRPL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IRPL1_HUMAN
• UniProt AC: Q9NZN1
• Protein Name: Interleukin-1 receptor accessory protein-like 1
• Gene Name: IL1RAPL1
• Organism: Homo sapiens (Human).
• Sequence Length: 696
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Cytoplasm . Cell projection, axon. Cell projection, dendrite. May localize to the cell body and growth cones of dendrite-like processes..
• Protein Description: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. [PubMed: 12783849 May activate the MAP kinase JNK]
• Protein Sequence: MKAPIPHLILLYATFTQSLKVVTKRGSADGCTDWSIDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYCMKVSISLTVGENDTGLCYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKECRTKTWRPSIVFKRDTLLIREVREDDIGNYTCELKYGGFVVRRTTELTVTAPLTDKPPKLLYPMESKLTIQETQLGDSANLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLIVDSVEEGDLGNYSCYVENGNGRRHASVLLHKRELMYTVELAGGLGAILLLLVCLVTIYKCYKIEIMLFYRNHFGAEELDGDNKDYDAYLSYTKVDPDQWNQETGEEERFALEILPDMLEKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVTGEIKVILIECSELRGIMNYQEVEALKHTIKLLTVIKWHGPKCNKLNSKFWKRLQYEMPFKRIEPITHEQALDVSEQGPFGELQTVSAISMAAATSTALATAHPDLRSTFHNTYHSQMRQKHYYRSYEYDVPPTGTLPLTSIGNQHTYCNIPMTLINGQRPQTKSSREQNPDEAHTNSAILPLLPRETSISSVIW

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
12	Phosphorylation	IPHLILLYATFTQSL CCCEEHHHHHHHCCC	10.51	24043423
14	Phosphorylation	HLILLYATFTQSLKV CEEHHHHHHHCCCEE	17.41	24043423
16	Phosphorylation	ILLYATFTQSLKVVT EHHHHHHHCCCEEEE	16.94	24043423
18	Phosphorylation	LYATFTQSLKVVTKR HHHHHHCCCEEEECC	27.40	24043423
63	N-linked_Glycosylation	FYGYIRTNYSLAQSA HHHHHHCCHHHHHHC	17.97	UniProtKB CARBOHYD
122	N-linked_Glycosylation	LYACVIRNSTYCMKV EEEEEECCCCEEEEE	27.81	UniProtKB CARBOHYD
138	N-linked_Glycosylation	ISLTVGENDTGLCYN EEEEECCCCCCCCCC	46.33	UniProtKB CARBOHYD
157	Phosphorylation	YFEKAELSKSKEISC HHHHHHHHCCCCCCC	26.79	26552605
159	Phosphorylation	EKAELSKSKEISCRD HHHHHHCCCCCCCCC	31.95	22964224
213	N-linked_Glycosylation	VREDDIGNYTCELKY ECHHHCCCEEEEEEE	29.31	UniProtKB CARBOHYD
228	Phosphorylation	GGFVVRRTTELTVTA CCEEEEEEEEEEEEE	17.66	-
264	N-linked_Glycosylation	TQLGDSANLTCRAFF EECCCCCCEEEEEEC	39.57	UniProtKB CARBOHYD
331	N-linked_Glycosylation	VEEGDLGNYSCYVEN CCCCCCCCEEEEEEC	32.61	UniProtKB CARBOHYD
478	Phosphorylation	KRLIIVMTPNYVVRR CCEEEEECCCHHHCC	9.48	-

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

Oops, there are no upstream regulatory protein records of IRPL1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IRPL1_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 IRPL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCS1_HUMAN	NCS1	physical	12783849

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.