LIME1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LIME1_HUMAN
• UniProt AC: Q9H400
• Protein Name: Lck-interacting transmembrane adapter 1
• Gene Name: LIME1
• Organism: Homo sapiens (Human).
• Sequence Length: 295
• Subcellular Localization: Cell membrane ; Single-pass type III membrane protein . Present in lipid rafts. Recruited to the immunological synapse upon conjugation of T-cell with antigen-presenting cell.
• Protein Description: Involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and TCR (T-cell antigen receptor)-mediated T-cell signaling in T-cells. In absence of TCR signaling, may be involved in CD4-mediated inhibition of T-cell activation. Couples activation of these receptors and their associated kinases with distal intracellular events such as calcium mobilization or MAPK activation through the recruitment of PLCG2, GRB2, GRAP2, and other signaling molecules..
• Protein Sequence: MGLPVSWAPPALWVLGCCALLLSLWALCTACRRPEDAVAPRKRARRQRARLQGSATAAEASLLRRTHLCSLSKSDTRLHELHRGPRSSRALRPASMDLLRPHWLEVSRDITGPQAAPSAFPHQELPRALPAAAATAGCAGLEATYSNVGLAALPGVSLAASPVVAEYARVQKRKGTHRSPQEPQQGKTEVTPAAQVDVLYSRVCKPKRRDPGPTTDPLDPKGQGAILALAGDLAYQTLPLRALDVDSGPLENVYESIRELGDPAGRSSTCGAGTPPASSCPSLGRGWRPLPASLP

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
28	S-palmitoylation	LLSLWALCTACRRPE HHHHHHHHHHCCCHH	1.43	14610046
31	S-palmitoylation	LWALCTACRRPEDAV HHHHHHHCCCHHHCC	1.72	14610046
54	Phosphorylation	QRARLQGSATAAEAS HHHHHHCCHHHHHHH	14.97	29978859
56	Phosphorylation	ARLQGSATAAEASLL HHHHCCHHHHHHHHH	28.26	29978859
61	Phosphorylation	SATAAEASLLRRTHL CHHHHHHHHHHHHCH	21.31	23401153
66	Phosphorylation	EASLLRRTHLCSLSK HHHHHHHHCHHHCCC	16.86	-
70	Phosphorylation	LRRTHLCSLSKSDTR HHHHCHHHCCCCCCH	41.88	23312004
72	Phosphorylation	RTHLCSLSKSDTRLH HHCHHHCCCCCCHHH	17.51	28348404
73	Ubiquitination	THLCSLSKSDTRLHE HCHHHCCCCCCHHHH	58.61	-
74	Phosphorylation	HLCSLSKSDTRLHEL CHHHCCCCCCHHHHH	40.62	23401153
87	Phosphorylation	ELHRGPRSSRALRPA HHHCCCCCCCCCCCC	27.58	24719451
88	Phosphorylation	LHRGPRSSRALRPAS HHCCCCCCCCCCCCC	23.89	24719451
95	Phosphorylation	SRALRPASMDLLRPH CCCCCCCCCHHHCCH	18.60	26657352
145	Phosphorylation	CAGLEATYSNVGLAA CCCCHHHHCCCCHHH	12.80	22817900
146	Phosphorylation	AGLEATYSNVGLAAL CCCHHHHCCCCHHHC	22.23	27642862
167	Phosphorylation	ASPVVAEYARVQKRK CCHHHHHHHHHHCCC	7.03	22817900
179	Phosphorylation	KRKGTHRSPQEPQQG CCCCCCCCCCCCCCC	24.27	24719451
200	Phosphorylation	AAQVDVLYSRVCKPK HHHHHHHEEECCCCC	8.35	27155012
201	Phosphorylation	AQVDVLYSRVCKPKR HHHHHHEEECCCCCC	17.68	21082442
205	Ubiquitination	VLYSRVCKPKRRDPG HHEEECCCCCCCCCC	51.20	-
207	Ubiquitination	YSRVCKPKRRDPGPT EEECCCCCCCCCCCC	45.63	-
235	Phosphorylation	ALAGDLAYQTLPLRA HHHCCHHHHCCCCCE	14.88	22817900
237	Phosphorylation	AGDLAYQTLPLRALD HCCHHHHCCCCCEEC	20.05	24719451
254	Phosphorylation	SGPLENVYESIRELG CCCHHHHHHHHHHHC	18.62	27273156
256	Phosphorylation	PLENVYESIRELGDP CHHHHHHHHHHHCCC	14.84	29978859
274	Phosphorylation	SSTCGAGTPPASSCP CCCCCCCCCCHHHCC	26.09	28985074
288	Methylation	PSLGRGWRPLPASLP CCCCCCCCCCCCCCC	26.21	115388705
293	Phosphorylation	GWRPLPASLP----- CCCCCCCCCC-----	38.95	24719451

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
254	Y	Phosphorylation	Kinase	LCK	P06239	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
28	C	Palmitoylation	Palmitoylation of Cys-28 and Cys-31 is required for raft targeting.	14610046
31	C	Palmitoylation	Palmitoylation of Cys-28 and Cys-31 is required for raft targeting.	14610046

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LIME1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRAF7_HUMAN	TRAF7	physical	26186194
TRAF7_HUMAN	TRAF7	physical	28514442
IDE_HUMAN	IDE	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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-200, AND MASSSPECTROMETRY.
PubMed: 18083107

"LIME: a new membrane raft-associated adaptor protein involved in CD4and CD8 coreceptor signaling.";
Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J.,Hilgert I., Paces J., Simeoni L., Kliche S., Merten C., Schraven B.,Horejsi V.;
J. Exp. Med. 198:1453-1462(2003).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,SUBCELLULAR LOCATION, INTERACTION WITH LCK AND CSK, PHOSPHORYLATION ATTYR-167; TYR-200 AND TYR-254, PALMITOYLATION AT CYS-28 AND CYS-31,MUTAGENESIS OF TYR-145; TYR-167; TYR-200; TYR-235 AND TYR-254, ANDFUNCTION.
PubMed: 14610046