SLAF5_HUMAN - dbPTM
SLAF5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SLAF5_HUMAN
UniProt AC Q9UIB8
Protein Name SLAM family member 5
Gene Name CD84
Organism Homo sapiens (Human).
Sequence Length 345
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (By similarity). Increases proliferative responses of activated T-cells and SH2D1A/SAP does not seem be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A-dependent pathway. May serve as a marker for hematopoietic progenitor cells. [PubMed: 11564780]
Protein Sequence MAQHHLWILLLCLQTWPEAAGKDSEIFTVNGILGESVTFPVNIQEPRQVKIIAWTSKTSVAYVTPGDSETAPVVTVTHRNYYERIHALGPNYNLVISDLRMEDAGDYKADINTQADPYTTTKRYNLQIYRRLGKPKITQSLMASVNSTCNVTLTCSVEKEEKNVTYNWSPLGEEGNVLQIFQTPEDQELTYTCTAQNPVSNNSDSISARQLCADIAMGFRTHHTGLLSVLAMFFLLVLILSSVFLFRLFKRRQGRIFPEGSCLNTFTKNPYAASKKTIYTYIMASRNTQPAESRIYDEILQSKVLPSKEEPVNTVYSEVQFADKMGKASTQDSKPPGTSSYEIVI
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 Orthologous
Protein Cluster
36O-linked_GlycosylationVNGILGESVTFPVNI
EECEECCCEEECCCC		25.34OGP
38O-linked_GlycosylationGILGESVTFPVNIQE
CEECCCEEECCCCCC		31.34OGP
58PhosphorylationIIAWTSKTSVAYVTP
EEEEECCCEEEEECC		28.35-
97PhosphorylationPNYNLVISDLRMEDA
CCCEEEEEECCHHHC		24.1024719451
108UbiquitinationMEDAGDYKADINTQA
HHHCCCCCCCCCCCC		44.3024816145
122UbiquitinationADPYTTTKRYNLQIY
CCCCCCCHHHHHHHH		51.2829967540
148 (in isoform 7)Phosphorylation-11.6927155012
150N-linked_GlycosylationASVNSTCNVTLTCSV
HHCCCCCCEEEEEEE		29.87UniProtKB CARBOHYD
172UbiquitinationTYNWSPLGEEGNVLQ
EEEEEECCCCCCEEE		34.0029967540
177UbiquitinationPLGEEGNVLQIFQTP
ECCCCCCEEEEEECC		6.4729967540
228PhosphorylationTHHTGLLSVLAMFFL
HHHHHHHHHHHHHHH		21.81-
262 (in isoform 3)Phosphorylation-5.0927155012
262 (in isoform 5)Phosphorylation-5.09-
265 (in isoform 5)Phosphorylation-21.52-
277PhosphorylationPYAASKKTIYTYIMA
CCCCCCHHHHEEHHH		23.9728796482
279PhosphorylationAASKKTIYTYIMASR
CCCCHHHHEEHHHCC		9.9522115753
280PhosphorylationASKKTIYTYIMASRN
CCCHHHHEEHHHCCC		11.6128796482
281PhosphorylationSKKTIYTYIMASRNT
CCHHHHEEHHHCCCC		3.3228796482
285PhosphorylationIYTYIMASRNTQPAE
HHEEHHHCCCCCCCH		14.5328796482
286UbiquitinationYTYIMASRNTQPAES
HEEHHHCCCCCCCHH		40.4529967540
288PhosphorylationYIMASRNTQPAESRI
EHHHCCCCCCCHHHH		34.5229978859
291UbiquitinationASRNTQPAESRIYDE
HCCCCCCCHHHHHHH		19.9929967540
293PhosphorylationRNTQPAESRIYDEIL
CCCCCCHHHHHHHHH		26.5329978859
296PhosphorylationQPAESRIYDEILQSK
CCCHHHHHHHHHHCC		13.3523401153
297UbiquitinationPAESRIYDEILQSKV
CCHHHHHHHHHHCCC		33.8029967540
302UbiquitinationIYDEILQSKVLPSKE
HHHHHHHCCCCCCCC		22.6829967540
302PhosphorylationIYDEILQSKVLPSKE
HHHHHHHCCCCCCCC		22.6827535140
303UbiquitinationYDEILQSKVLPSKEE
HHHHHHCCCCCCCCC		34.5329967540
307PhosphorylationLQSKVLPSKEEPVNT
HHCCCCCCCCCCCCH		48.8424719451
308UbiquitinationQSKVLPSKEEPVNTV
HCCCCCCCCCCCCHH		65.2429967540
314PhosphorylationSKEEPVNTVYSEVQF
CCCCCCCHHHHHHHH		22.5128796482
314O-linked_GlycosylationSKEEPVNTVYSEVQF
CCCCCCCHHHHHHHH		22.51OGP
316PhosphorylationEEPVNTVYSEVQFAD
CCCCCHHHHHHHHHH		9.3223401153
317PhosphorylationEPVNTVYSEVQFADK
CCCCHHHHHHHHHHH		27.2728796482
339PhosphorylationDSKPPGTSSYEIVI-
CCCCCCCCCCEEEC-		36.5228796482
340PhosphorylationSKPPGTSSYEIVI--
CCCCCCCCCEEEC--		26.9928796482
341PhosphorylationKPPGTSSYEIVI---
CCCCCCCCEEEC---		14.9417563375
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
296YPhosphorylationKinaseLYNP07948
Uniprot
341YPhosphorylationKinaseFESP07332
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLAF5_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

Oops, there are no SNP-PTM records of SLAF5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLAF5_HUMANCD84physical
11564780
SH21A_HUMANSH2D1Aphysical
12115647
SH21B_HUMANSH2D1Bphysical
12115647
PTN11_HUMANPTPN11physical
11689425
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.
Regulatory Network of SLAF5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-279; SER-285 ANDTYR-316, AND MASS SPECTROMETRY.
"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-279 AND TYR-296, ANDMASS SPECTROMETRY.
"Platelet aggregation induces platelet aggregate stability via SLAMfamily receptor signaling.";
Nanda N., Andre P., Bao M., Clauser K., Deguzman F., Howie D.,Conley P.B., Terhorst C., Phillips D.R.;
Blood 106:3028-3034(2005).
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-296 AND TYR-316, AND IDENTIFICATIONBY MASS SPECTROMETRY.

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