CLM7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CLM7_HUMAN
• UniProt AC: A8K4G0
• Protein Name: CMRF35-like molecule 7
• Gene Name: CD300LB
• Organism: Homo sapiens (Human).
• Sequence Length: 201
• Subcellular Localization: Cell membrane; Single-pass type I membrane protein.
• Protein Description: Acts as an activating immune receptor through its interaction with ITAM-bearing adapter TYROBP, and also independently by recruitment of GRB2..
• Protein Sequence: MWLPPALLLLSLSGCFSIQGPESVRAPEQGSLTVQCHYKQGWETYIKWWCRGVRWDTCKILIETRGSEQGEKSDRVSIKDNQKDRTFTVTMEGLRRDDADVYWCGIERRGPDLGTQVKVIVDPEGAASTTASSPTNSNMAVFIGSHKRNHYMLLVFVKVPILLILVTAILWLKGSQRVPEEPGEQPIYMNFSEPLTKDMAT

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
86	Phosphorylation	KDNQKDRTFTVTMEG CCCCCCCEEEEEEEC	33.52	26270265
88	Phosphorylation	NQKDRTFTVTMEGLR CCCCCEEEEEEECCC	17.91	26270265
90	Phosphorylation	KDRTFTVTMEGLRRD CCCEEEEEEECCCCC	13.37	26270265
188	Phosphorylation	EPGEQPIYMNFSEPL CCCCCCCEECCCCCC	7.84	16920917

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
188	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CLM7_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 CLM7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049

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

"Analysis of mouse LMIR5/CLM-7 as an activating receptor: differentialregulation of LMIR5/CLM-7 in mouse versus human cells.";
Yamanishi Y., Kitaura J., Izawa K., Matsuoka T., Oki T., Lu Y.,Shibata F., Yamazaki S., Kumagai H., Nakajima H., Maeda-Yamamoto M.,Tybulewicz V.L.J., Takai T., Kitamura T.;
Blood 111:688-698(2008).
Cited for: PHOSPHORYLATION AT TYR-188, INTERACTION WITH TYROBP, AND FUNCTION.
PubMed: 17928527

"Molecular and functional characterization of CD300b, a new activatingimmunoglobulin receptor able to transduce signals through twodifferent pathways.";
Martinez-Barriocanal A., Sayos J.;
J. Immunol. 177:2819-2830(2006).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,PHOSPHORYLATION AT TYR-188, MUTAGENESIS OF LYS-158 AND TYR-188, ANDINTERACTION WITH TYROBP.
PubMed: 16920917