LY9_HUMAN - dbPTM
LY9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LY9_HUMAN
UniProt AC Q9HBG7
Protein Name T-lymphocyte surface antigen Ly-9
Gene Name LY9
Organism Homo sapiens (Human).
Sequence Length 655
Subcellular Localization Membrane
Single-pass type I membrane protein. Cell membrane .
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. May participate in adhesion reactions between T lymphocytes and accessory cells by homophilic interaction. Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A. [PubMed: 22184727 Promotes recruitment of RORC to the IL-17 promoter]
Protein Sequence MVAPKSHTDDWAPGPFSSKPQRSQLQIFSSVLQTSLLFLLMGLRASGKDSAPTVVSGILGGSVTLPLNISVDTEIENVIWIGPKNALAFARPKENVTIMVKSYLGRLDITKWSYSLCISNLTLNDAGSYKAQINQRNFEVTTEEEFTLFVYEQLQEPQVTMKSVKVSENFSCNITLMCSVKGAEKSVLYSWTPREPHASESNGGSILTVSRTPCDPDLPYICTAQNPVSQRSSLPVHVGQFCTDPGASRGGTTGETVVGVLGEPVTLPLALPACRDTEKVVWLFNTSIISKEREEAATADPLIKSRDPYKNRVWVSSQDCSLKISQLKIEDAGPYHAYVCSEASSVTSMTHVTLLIYRRLRKPKITWSLRHSEDGICRISLTCSVEDGGNTVMYTWTPLQKEAVVSQGESHLNVSWRSSENHPNLTCTASNPVSRSSHQFLSENICSGPERNTKLWIGLFLMVCLLCVGIFSWCIWKRKGRCSVPAFCSSQAEAPADTPEPTAGHTLYSVLSQGYEKLDTPLRPARQQPTPTSDSSSDSNLTTEEDEDRPEVHKPISGRYEVFDQVTQEGAGHDPAPEGQADYDPVTPYVTEVESVVGENTMYAQVFNLQGKTPVSQKEESSATIYCSIRKPQVVPPPQQNDLEIPESPTYENFT
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
34PhosphorylationIFSSVLQTSLLFLLM
HHHHHHHHHHHHHHH		19.7226552605
35PhosphorylationFSSVLQTSLLFLLMG
HHHHHHHHHHHHHHH		15.3226552605
46PhosphorylationLLMGLRASGKDSAPT
HHHHHHHCCCCCCCC		39.6826552605
68N-linked_GlycosylationGSVTLPLNISVDTEI
CEEEEECEEEECCCE		23.66UniProtKB CARBOHYD
95N-linked_GlycosylationAFARPKENVTIMVKS
EECCCCCCEEEEEEH		42.2119349973
95N-linked_GlycosylationAFARPKENVTIMVKS
EECCCCCCEEEEEEH		42.2119349973
97PhosphorylationARPKENVTIMVKSYL
CCCCCCEEEEEEHHH		18.2225690035
102PhosphorylationNVTIMVKSYLGRLDI
CEEEEEEHHHCCCCC		17.7429759185
103PhosphorylationVTIMVKSYLGRLDIT
EEEEEEHHHCCCCCH		13.8823532336
110PhosphorylationYLGRLDITKWSYSLC
HHCCCCCHHHEEEEE		26.5729759185
120N-linked_GlycosylationSYSLCISNLTLNDAG
EEEEEEECCEECCCC		19.68UniProtKB CARBOHYD
159 (in isoform 4)Phosphorylation-9.1527251275
160PhosphorylationQLQEPQVTMKSVKVS
HHCCCEEEEEEEEEC		17.40-
163PhosphorylationEPQVTMKSVKVSENF
CCEEEEEEEEECCCC		19.15-
169N-linked_GlycosylationKSVKVSENFSCNITL
EEEEECCCCCCEEEE		26.99UniProtKB CARBOHYD
173N-linked_GlycosylationVSENFSCNITLMCSV
ECCCCCCEEEEEEEE		29.13UniProtKB CARBOHYD
186PhosphorylationSVKGAEKSVLYSWTP
EECCCCEEEEEEECC		14.62-
248PhosphorylationFCTDPGASRGGTTGE
EECCCCCCCCCCCCC		37.06-
285N-linked_GlycosylationEKVVWLFNTSIISKE
HHEEEEEECCCCCHH		30.6519349973
285N-linked_GlycosylationEKVVWLFNTSIISKE
HHEEEEEECCCCCHH		30.6519349973
287PhosphorylationVVWLFNTSIISKERE
EEEEEECCCCCHHHH		21.0124719451
298O-linked_GlycosylationKEREEAATADPLIKS
HHHHHHHHCCCCCCC		38.34OGP
304UbiquitinationATADPLIKSRDPYKN
HHCCCCCCCCCCCCC		47.31-
309PhosphorylationLIKSRDPYKNRVWVS
CCCCCCCCCCCEEEE		25.7818083107
325PhosphorylationQDCSLKISQLKIEDA
CCCEEEEEECEECCC		28.0724719451
368PhosphorylationRKPKITWSLRHSEDG
CCCCEEEEEECCCCC		13.5824719451
406PhosphorylationLQKEAVVSQGESHLN
CCCEEEECCCCCCCE		26.3525850435
410PhosphorylationAVVSQGESHLNVSWR
EEECCCCCCCEEEEE		39.8525850435
413N-linked_GlycosylationSQGESHLNVSWRSSE
CCCCCCCEEEEECCC		21.98UniProtKB CARBOHYD
415PhosphorylationGESHLNVSWRSSENH
CCCCCEEEEECCCCC		18.7225850435
424N-linked_GlycosylationRSSENHPNLTCTASN
ECCCCCCCCEEEECC		40.19UniProtKB CARBOHYD
508PhosphorylationPTAGHTLYSVLSQGY
CCCCHHHHHHHHCCH		9.63-
509PhosphorylationTAGHTLYSVLSQGYE
CCCHHHHHHHHCCHH		21.50-
512PhosphorylationHTLYSVLSQGYEKLD
HHHHHHHHCCHHCCC		21.28-
515PhosphorylationYSVLSQGYEKLDTPL
HHHHHCCHHCCCCCC		11.40-
520PhosphorylationQGYEKLDTPLRPARQ
CCHHCCCCCCCCCCC		34.36-
560PhosphorylationHKPISGRYEVFDQVT
CCCCCCCEEEEEHHC		21.70-
583PhosphorylationAPEGQADYDPVTPYV
CCCCCCCCCCCCCCE		25.76-
589PhosphorylationDYDPVTPYVTEVESV
CCCCCCCCEEEEEEE		15.61-
603PhosphorylationVVGENTMYAQVFNLQ
ECCCCCEEEEEEECC		7.5810970093
613PhosphorylationVFNLQGKTPVSQKEE
EEECCCCCCCCCCCC		35.4324706070
616PhosphorylationLQGKTPVSQKEESSA
CCCCCCCCCCCCCCC		36.4224706070
621PhosphorylationPVSQKEESSATIYCS
CCCCCCCCCCEEEEE		26.7726552605
622PhosphorylationVSQKEESSATIYCSI
CCCCCCCCCEEEEEE		32.4826552605
624PhosphorylationQKEESSATIYCSIRK
CCCCCCCEEEEEECC		17.9028796482
626PhosphorylationEESSATIYCSIRKPQ
CCCCCEEEEEECCCC		3.9328796482
628PhosphorylationSSATIYCSIRKPQVV
CCCEEEEEECCCCCC		14.4128796482
648PhosphorylationNDLEIPESPTYENFT
CCCCCCCCCCCCCCC		19.7228796482
650PhosphorylationLEIPESPTYENFT--
CCCCCCCCCCCCC--		53.3928796482
651PhosphorylationEIPESPTYENFT---
CCCCCCCCCCCC---		16.5628796482
655PhosphorylationSPTYENFT-------
CCCCCCCC-------		49.6528796482
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

Oops, there are no upstream regulatory protein records of LY9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LY9_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 LY9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2M1_HUMANAP2M1physical
12621057
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 LY9_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-285, AND MASSSPECTROMETRY.

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