IL7RA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IL7RA_HUMAN
• UniProt AC: P16871
• Protein Name: Interleukin-7 receptor subunit alpha
• Gene Name: IL7R
• Organism: Homo sapiens (Human).
• Sequence Length: 459
• Subcellular Localization: Isoform 1: Cell membrane; Single-pass type I membrane protein.; Isoform 3: Cell membrane; Single-pass type I membrane protein.; Isoform 4: Secreted.
• Protein Description: Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP)..
• Protein Sequence: MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNTTNLEFEICGALVEVKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVIYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ

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
49	N-linked_Glycosylation	CYSQLEVNGSQHSLT EEEEEEECCCEEEEE	34.72	19141282
65	N-linked_Glycosylation	AFEDPDVNTTNLEFE EEECCCCCCCCEEEE	48.87	19141282
96	Phosphorylation	QEIYFIETKKFLLIG EEEEEEEECEEEEEC	34.42	26074081
151	N-linked_Glycosylation	NDFVVTFNTSHLQKK CCEEEEEEHHHHHHH	31.16	19141282
159	Phosphorylation	TSHLQKKYVKVLMHD HHHHHHHHHHHHHHH	16.73	26074081
169	Phosphorylation	VLMHDVAYRQEKDEN HHHHHHHHHCCCCCC	16.81	26074081
182	N-linked_Glycosylation	ENKWTHVNLSSTKLT CCCCEEEECCHHHHH	26.97	UniProtKB CARBOHYD
189	Phosphorylation	NLSSTKLTLLQRKLQ ECCHHHHHHHHHHHC	27.29	23612710
232	N-linked_Glycosylation	YFRTPEINNSSGEMD EECCCCCCCCCCCCC	40.44	UniProtKB CARBOHYD
233	N-linked_Glycosylation	FRTPEINNSSGEMDP ECCCCCCCCCCCCCH	43.12	UniProtKB CARBOHYD
282	Phosphorylation	SLPDHKKTLEHLCKK CCCCHHHHHHHHCCC	42.03	-
292	Ubiquitination	HLCKKPRKNLNVSFN HHCCCCCCCCCCCCC	74.45	-
297	Phosphorylation	PRKNLNVSFNPESFL CCCCCCCCCCHHHHH	20.45	25159151
337	Ubiquitination	QQLEESEKQRLGGDV HHHHHHHHHHCCCCC	50.42	21987572
346	Phosphorylation	RLGGDVQSPNCPSED HCCCCCCCCCCCCCC	20.23	25159151
365	Phosphorylation	PESFGRDSSLTCLAG CHHHCCCCCCEEECC	26.36	26657352
366	Phosphorylation	ESFGRDSSLTCLAGN HHHCCCCCCEEECCC	31.80	24114839
368	Phosphorylation	FGRDSSLTCLAGNVS HCCCCCCEEECCCCC	13.86	26657352
375	Phosphorylation	TCLAGNVSACDAPIL EEECCCCCCCCCCCC	27.46	21712546
449	Phosphorylation	GSNQEEAYVTMSSFY CCCCCEEEEEHHHHH	10.34	22817900

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
282	T	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IL7RA_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
346	Phosphorylation	356 (10)	I ⇒ V	rs3194051	Ulcerative colitis	21297633
365	Phosphorylation	356 (9)	I ⇒ V	rs3194051	Ulcerative colitis	21297633

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FYN_HUMAN	FYN	physical	7515933
KIT_HUMAN	KIT	physical	17554063
JAK3_HUMAN	JAK3	physical	17554063
CISH_HUMAN	CISH	physical	27596538

Drug and Disease Associations

• Kegg Disease
• H00091: T-B+Severe combined immunodeficiencies (SCIDs), including the following eight diseases: X-linked SCI
• OMIM Disease
• 608971: Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID)
• 612595: Multiple sclerosis 3 (MS3)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structural and biophysical studies of the human IL-7/IL-7Ralphacomplex.";
McElroy C.A., Dohm J.A., Walsh S.T.;
Structure 17:54-65(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-239 IN COMPLEX WITH IL7,SUBUNIT, GLYCOSYLATION AT ASN-49; ASN-65 AND ASN-151, AND DISULFIDEBONDS.
PubMed: 19141282

Phosphorylation

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159 AND TYR-169, ANDMASS SPECTROMETRY.
PubMed: 17924679