NTAL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NTAL_HUMAN
• UniProt AC: Q9GZY6
• Protein Name: Linker for activation of T-cells family member 2
• Gene Name: LAT2
• Organism: Homo sapiens (Human).
• Sequence Length: 243
• Subcellular Localization: Cell membrane ; Single-pass type III membrane protein . Present in lipid rafts.
• Protein Description: Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2..
• Protein Sequence: MSSGTELLWPGAALLVLLGVAASLCVRCSRPGAKRSEKIYQQRSLREDQQSFTGSRTYSLVGQAWPGPLADMAPTRKDKLLQFYPSLEDPASSRYQNFSKGSRHGSEEAYIDPIAMEYYNWGRFSKPPEDDDANSYENVLICKQKTTETGAQQEGIGGLCRGDLSLSLALKTGPTSGLCPSASPEEDEESEDYQNSASIHQWRESRKVMGQLQREASPGPVGSPDEEDGEPDYVNGEVAATEA

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	VLLGVAASLCVRCSR HHHHHHHHHHHHCCC	16.74	24719451
25	S-palmitoylation	LGVAASLCVRCSRPG HHHHHHHHHHCCCCC	1.35	12486104
28	S-palmitoylation	AASLCVRCSRPGAKR HHHHHHHCCCCCCCH	1.70	12486104
38	Ubiquitination	PGAKRSEKIYQQRSL CCCCHHHHHHHHHCH	48.21	25015289
40	Phosphorylation	AKRSEKIYQQRSLRE CCHHHHHHHHHCHHH	15.06	17993265
44	Phosphorylation	EKIYQQRSLREDQQS HHHHHHHCHHHHHHH	27.69	23401153
51	Phosphorylation	SLREDQQSFTGSRTY CHHHHHHHHHCCCEE	21.10	23401153
53	Phosphorylation	REDQQSFTGSRTYSL HHHHHHHHCCCEEEE	39.22	30266825
55	Phosphorylation	DQQSFTGSRTYSLVG HHHHHHCCCEEEECC	20.56	28450419
57	Phosphorylation	QSFTGSRTYSLVGQA HHHHCCCEEEECCEE	21.11	28450419
58	Phosphorylation	SFTGSRTYSLVGQAW HHHCCCEEEECCEEC	10.01	17993265
59	Phosphorylation	FTGSRTYSLVGQAWP HHCCCEEEECCEECC	18.90	23401153
77	Ubiquitination	ADMAPTRKDKLLQFY HHCCCCCHHHHHHHC	62.79	23000965
77 (in isoform 2)	Ubiquitination	-	62.79	21890473
77 (in isoform 1)	Ubiquitination	-	62.79	21890473
79	Ubiquitination	MAPTRKDKLLQFYPS CCCCCHHHHHHHCCC	54.88	23000965
79 (in isoform 2)	Ubiquitination	-	54.88	21890473
79 (in isoform 1)	Ubiquitination	-	54.88	21890473
84	Phosphorylation	KDKLLQFYPSLEDPA HHHHHHHCCCCCCCC	4.48	29978859
86	Phosphorylation	KLLQFYPSLEDPASS HHHHHCCCCCCCCHH	32.77	23401153
92	Phosphorylation	PSLEDPASSRYQNFS CCCCCCCHHHCCCCC	22.27	29523821
93	Phosphorylation	SLEDPASSRYQNFSK CCCCCCHHHCCCCCC	36.79	29523821
95	Phosphorylation	EDPASSRYQNFSKGS CCCCHHHCCCCCCCC	15.12	17993265
99	Phosphorylation	SSRYQNFSKGSRHGS HHHCCCCCCCCCCCC	43.59	24719451
100	Ubiquitination	SRYQNFSKGSRHGSE HHCCCCCCCCCCCCC	57.69	25015289
102	Phosphorylation	YQNFSKGSRHGSEEA CCCCCCCCCCCCCCC	25.49	28188228
106	Phosphorylation	SKGSRHGSEEAYIDP CCCCCCCCCCCCCCH	26.58	23401153
110	Phosphorylation	RHGSEEAYIDPIAME CCCCCCCCCCHHHHH	14.77	28450419
118	Phosphorylation	IDPIAMEYYNWGRFS CCHHHHHHHCCCCCC	6.76	30576142
119	Phosphorylation	DPIAMEYYNWGRFSK CHHHHHHHCCCCCCC	7.37	17993265
125	Phosphorylation	YYNWGRFSKPPEDDD HHCCCCCCCCCCCCC	42.78	23684312
126	Ubiquitination	YNWGRFSKPPEDDDA HCCCCCCCCCCCCCC	62.98	-
135	Phosphorylation	PEDDDANSYENVLIC CCCCCCCCCCCEEEE	35.23	23401153
136	Phosphorylation	EDDDANSYENVLICK CCCCCCCCCCEEEEE	16.01	12486104
145	Ubiquitination	NVLICKQKTTETGAQ CEEEEEEECCCCCCC	42.80	25015289
165	Phosphorylation	GLCRGDLSLSLALKT CCCCCCEEEEEEECC	22.20	30266825
167	Phosphorylation	CRGDLSLSLALKTGP CCCCEEEEEEECCCC	14.28	23401153
175	Phosphorylation	LALKTGPTSGLCPSA EEECCCCCCCCCCCC	36.45	30108239
176	Phosphorylation	ALKTGPTSGLCPSAS EECCCCCCCCCCCCC	32.66	30108239
181	Phosphorylation	PTSGLCPSASPEEDE CCCCCCCCCCCCCCC	40.14	28450419
183	Phosphorylation	SGLCPSASPEEDEES CCCCCCCCCCCCCCC	36.86	28450419
190	Phosphorylation	SPEEDEESEDYQNSA CCCCCCCCHHHCCHH	33.45	23401153
193	Phosphorylation	EDEESEDYQNSASIH CCCCCHHHCCHHHHH	12.92	12486104
196	Phosphorylation	ESEDYQNSASIHQWR CCHHHCCHHHHHHHH	14.10	23401153
198	Phosphorylation	EDYQNSASIHQWRES HHHCCHHHHHHHHHH	22.03	28450419
205	Phosphorylation	SIHQWRESRKVMGQL HHHHHHHHHHHHHHH	28.91	-
217	Phosphorylation	GQLQREASPGPVGSP HHHHHHCCCCCCCCC	26.15	22115753
223	Phosphorylation	ASPGPVGSPDEEDGE CCCCCCCCCCCCCCC	29.43	29052541
233	Phosphorylation	EEDGEPDYVNGEVAA CCCCCCCCCCCEEEE	13.41	12486104
241	Phosphorylation	VNGEVAATEA----- CCCEEEECCC-----	23.78	22115753

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
95	Y	Phosphorylation	Kinase	LYN	P07948	PSP
110	Y	Phosphorylation	Kinase	KIT	P10721	PSP
110	Y	Phosphorylation	Kinase	LYN	P07948	PSP
118	Y	Phosphorylation	Kinase	KIT	P10721	PSP
118	Y	Phosphorylation	Kinase	LYN	P07948	PSP
119	Y	Phosphorylation	Kinase	LYN	P07948	PSP
136	Y	Phosphorylation	Kinase	SYK	P43405	PSP
136	Y	Phosphorylation	Kinase	LYN	P07948	PSP
193	Y	Phosphorylation	Kinase	SYK	P43405	PSP
233	Y	Phosphorylation	Kinase	SYK	P43405	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NTAL_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 NTAL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRB2_HUMAN	GRB2	physical	12514734
PLCG1_HUMAN	PLCG1	physical	12514734
PLCG2_HUMAN	PLCG2	physical	12514734

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-135, AND MASSSPECTROMETRY.
PubMed: 19369195

"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASSSPECTROMETRY.
PubMed: 19367720

"The importance of three membrane-distal tyrosines in the adaptorprotein NTAL/LAB.";
Koonpaew S., Janssen E., Zhu M., Zhang W.;
J. Biol. Chem. 279:11229-11235(2004).
Cited for: MUTAGENESIS OF TYR-58; TYR-84; TYR-95; TYR-110; TYR-118; TYR-136;TYR-193 AND TYR-233, PHOSPHORYLATION AT TYR-136; TYR-193 AND TYR-233,AND INTERACTION WITH GRB2.
PubMed: 14722116

"Non-T cell activation linker (NTAL): a transmembrane adaptor proteininvolved in immunoreceptor signaling.";
Brdicka T., Imrich M., Angelisova P., Brdickova N., Horvath O.,Spicka J., Hilgert I., Luskova P., Draber P., Novak P., Engels N.,Wienands J., Simeoni L., Oesterreicher J., Aguado E., Malissen M.,Schraven B., Horejsi V.;
J. Exp. Med. 196:1617-1626(2002).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASSSPECTROMETRY, INTERACTION WITH GRB2; SOS1; GAB1 AND CBL, TISSUESPECIFICITY, PALMITOYLATION AT CYS-25 AND CYS-28, SUBCELLULARLOCATION, PHOSPHORYLATION AT TYR-136; TYR-193 AND TYR-233,UBIQUITINATION, AND FUNCTION.
PubMed: 12486104