LENG8_HUMAN - dbPTM
LENG8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LENG8_HUMAN
UniProt AC Q96PV6
Protein Name Leukocyte receptor cluster member 8
Gene Name LENG8
Organism Homo sapiens (Human).
Sequence Length 800
Subcellular Localization
Protein Description
Protein Sequence MAANVGDQRSTDWSSQYSMVAGAGRENGMETPMHENPEWEKARQALASISKSGAAGGSAKSSSNGPVASAQYVSQAEASALQQQQYYQWYQQYNYAYPYSYYYPMSMYQSYGSPSQYGMAGSYGSATPQQPSAPQHQGTLNQPPVPGMDESMSYQAPPQQLPSAQPPQPSNPPHGAHTLNSGPQPGTAPATQHSQAGPATGQAYGPHTYTEPAKPKKGQQLWNRMKPAPGTGGLKFNIQKRPFAVTTQSFGSNAEGQHSGFGPQPNPEKVQNHSGSSARGNLSGKPDDWPQDMKEYVERCFTACESEEDKDRTEKLLKEVLQARLQDGSAYTIDWSREPLPGLTREPVAESPKKKRWEAASSLHPPRGAGSATRGGGAPSQRGTPGAGGAGRARGNSFTKFGNRNVFMKDNSSSSSTDSRSRSSSRSPTRHFRRSDSHSDSDSSYSGNECHPVGRRNPPPKGRGGRGAHMDRGRGRAQRGKRHDLAPTKRSRKKMAALECEDPERELKKQKRAARFQHGHSRRLRLEPLVLQMSSLESSGADPDWQELQIVGTCPDITKHYLRLTCAPDPSTVRPVAVLKKSLCMVKCHWKEKQDYAFACEQMKSIRQDLTVQGIRTEFTVEVYETHARIALEKGDHEEFNQCQTQLKSLYAENLPGNVGEFTAYRILYYIFTKNSGDITTELAYLTRELKADPCVAHALALRTAWALGNYHRFFRLYCHAPCMSGYLVDKFADRERKVALKAMIKTFRPALPVSYLQAELAFEGEAACRAFLEPLGLAYTGPDNSSIDCRLSLAQLSAF
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
2Acetylation------MAANVGDQR
------CCCCCCCCC		14.0322814378
15PhosphorylationQRSTDWSSQYSMVAG
CCCCCHHHHHHCCCC		28.9628796482
17PhosphorylationSTDWSSQYSMVAGAG
CCCHHHHHHCCCCCC		10.7328796482
18PhosphorylationTDWSSQYSMVAGAGR
CCHHHHHHCCCCCCC		10.1128796482
31PhosphorylationGRENGMETPMHENPE
CCCCCCCCCCCCCHH		19.6124719451
48PhosphorylationKARQALASISKSGAA
HHHHHHHHHHHCCCC		28.3928555341
58PhosphorylationKSGAAGGSAKSSSNG
HCCCCCCCCCCCCCC		31.44-
61PhosphorylationAAGGSAKSSSNGPVA
CCCCCCCCCCCCCCC		38.42-
62PhosphorylationAGGSAKSSSNGPVAS
CCCCCCCCCCCCCCC		27.41-
63PhosphorylationGGSAKSSSNGPVASA
CCCCCCCCCCCCCCH		53.55-
69PhosphorylationSSNGPVASAQYVSQA
CCCCCCCCHHEECHH		19.01-
209 (in isoform 1)O-linked_Glycosylation-18.7131492838
210O-linked_GlycosylationAYGPHTYTEPAKPKK
CCCCCCCCCCCCCCC		18.6731492838
212PhosphorylationGPHTYTEPAKPKKGQ
CCCCCCCCCCCCCCH		29.4928555341
248MethylationRPFAVTTQSFGSNAE
CCEEEEECCCCCCCC		41.7323644510
248AcetylationRPFAVTTQSFGSNAE
CCEEEEECCCCCCCC		41.7326051181
257MethylationFGSNAEGQHSGFGPQ
CCCCCCCCCCCCCCC		54.9323644510
281SumoylationSGSSARGNLSGKPDD
CCCCCCCCCCCCCCC		57.10-
292PhosphorylationKPDDWPQDMKEYVER
CCCCCCHHHHHHHHH		26.7923090842
294PhosphorylationDDWPQDMKEYVERCF
CCCCHHHHHHHHHHH		13.1123090842
295PhosphorylationDWPQDMKEYVERCFT
CCCHHHHHHHHHHHH		16.5122199227
299PhosphorylationDMKEYVERCFTACES
HHHHHHHHHHHHHHC		24.0230576142
307PhosphorylationCFTACESEEDKDRTE
HHHHHHCCCCHHHHH		38.6122617229
314PhosphorylationEEDKDRTEKLLKEVL
CCCHHHHHHHHHHHH		32.0823401153
324PhosphorylationLKEVLQARLQDGSAY
HHHHHHHHCCCCCEE		40.2424719451
337MethylationAYTIDWSREPLPGLT
EEEEECCCCCCCCCC		41.2830987797
345MethylationEPLPGLTREPVAESP
CCCCCCCCCCCCCCC		56.1282955227
351PhosphorylationTREPVAESPKKKRWE
CCCCCCCCCCHHHHH		32.1923186163
355MethylationVAESPKKKRWEAASS
CCCCCCHHHHHHHHC		22.15-
357MethylationESPKKKRWEAASSLH
CCCCHHHHHHHHCCC		43.39-
360PhosphorylationKKKRWEAASSLHPPR
CHHHHHHHHCCCCCC		36.8024719451
363AcetylationRWEAASSLHPPRGAG
HHHHHHCCCCCCCCC		49.6225953088
363MethylationRWEAASSLHPPRGAG
HHHHHHCCCCCCCCC		49.62-
375PhosphorylationGAGSATRGGGAPSQR
CCCCCCCCCCCCCCC		41.5522210691
376PhosphorylationAGSATRGGGAPSQRG
CCCCCCCCCCCCCCC		40.2622964224
377PhosphorylationGSATRGGGAPSQRGT
CCCCCCCCCCCCCCC		28.2922210691
378PhosphorylationSATRGGGAPSQRGTP
CCCCCCCCCCCCCCC		38.9222964224
379PhosphorylationATRGGGAPSQRGTPG
CCCCCCCCCCCCCCC		37.8822964224
380PhosphorylationTRGGGAPSQRGTPGA
CCCCCCCCCCCCCCC		39.6822964224
382PhosphorylationGGGAPSQRGTPGAGG
CCCCCCCCCCCCCCC		32.0422964224
384PhosphorylationGAPSQRGTPGAGGAG
CCCCCCCCCCCCCCC		40.2322964224
387PhosphorylationSQRGTPGAGGAGRAR
CCCCCCCCCCCCCCC		28.7622210691
388PhosphorylationQRGTPGAGGAGRARG
CCCCCCCCCCCCCCC		37.7222210691
398PhosphorylationGRARGNSFTKFGNRN
CCCCCCCCCCCCCCC		38.9320873877
400PhosphorylationARGNSFTKFGNRNVF
CCCCCCCCCCCCCEE		26.5729214152
402PhosphorylationGNSFTKFGNRNVFMK
CCCCCCCCCCCEEEC		42.6430576142
404PhosphorylationSFTKFGNRNVFMKDN
CCCCCCCCCEEECCC		42.2720873877
406PhosphorylationTKFGNRNVFMKDNSS
CCCCCCCEEECCCCC		34.8230576142
407PhosphorylationKFGNRNVFMKDNSSS
CCCCCCEEECCCCCC		28.4530576142
408PhosphorylationFGNRNVFMKDNSSSS
CCCCCEEECCCCCCC		25.2520873877
409PhosphorylationGNRNVFMKDNSSSSS
CCCCEEECCCCCCCC		36.7730576142
435MethylationPTRHFRRSDSHSDSD
CCCCCCCCCCCCCCC		29.18-
451PhosphorylationSYSGNECHPVGRRNP
CCCCCCCCCCCCCCC		33.2220068231
452AcetylationYSGNECHPVGRRNPP
CCCCCCCCCCCCCCC		47.5225953088
474AcetylationGAHMDRGRGRAQRGK
CCCCCCCCCHHHHCC		53.54-
498PhosphorylationSRKKMAALECEDPER
HHHHHHHHHCCCHHH		30.7116674116
528PhosphorylationSRRLRLEPLVLQMSS
HHHHCCCCEEHHHHH		10.5329083192
534PhosphorylationEPLVLQMSSLESSGA
CCEEHHHHHHHHCCC		47.0929083192
535PhosphorylationPLVLQMSSLESSGAD
CEEHHHHHHHHCCCC		26.3929083192
543AcetylationLESSGADPDWQELQI
HHHCCCCCCHHHEEE		33.4526051181
567AcetylationHYLRLTCAPDPSTVR
HHHHHEECCCCCCCC		42.2825953088
568PhosphorylationYLRLTCAPDPSTVRP
HHHHEECCCCCCCCH		20.0526074081
574PhosphorylationAPDPSTVRPVAVLKK
CCCCCCCCHHHHHHH		21.0526074081
580PhosphorylationVRPVAVLKKSLCMVK
CCHHHHHHHHEEEEE		33.2626074081
583PhosphorylationVAVLKKSLCMVKCHW
HHHHHHHEEEEEECC		14.9926074081
587PhosphorylationKKSLCMVKCHWKEKQ
HHHEEEEEECCCCCH		11.1226074081
589PhosphorylationSLCMVKCHWKEKQDY
HEEEEEECCCCCHHH		11.8026074081
597AcetylationWKEKQDYAFACEQMK
CCCCHHHHHHHHHHH		71.1826051181
639PhosphorylationLEKGDHEEFNQCQTQ
HHCCCHHHHHHHHHH		39.1222817900
643PhosphorylationDHEEFNQCQTQLKSL
CHHHHHHHHHHHHHH		20.9620068231
644PhosphorylationHEEFNQCQTQLKSLY
HHHHHHHHHHHHHHH		29.3620068231
648PhosphorylationNQCQTQLKSLYAENL
HHHHHHHHHHHHHCC		22.6420068231
650PhosphorylationCQTQLKSLYAENLPG
HHHHHHHHHHHCCCC		14.9320068231
676PhosphorylationYYIFTKNSGDITTEL
HHHHCCCCCCHHHHH		23.2620068231
680PhosphorylationTKNSGDITTELAYLT
CCCCCCHHHHHHHHH		4.5220068231
681PhosphorylationKNSGDITTELAYLTR
CCCCCHHHHHHHHHH		4.3020068231
687PhosphorylationTTELAYLTRELKADP
HHHHHHHHHHHCCCH		3.2018452278
770PhosphorylationFEGEAACRAFLEPLG
HCCHHHHHHHHHCCC		28.8015302935
776PhosphorylationCRAFLEPLGLAYTGP
HHHHHHCCCCEECCC		28.8715302935
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 LENG8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LENG8_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 LENG8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MISSL_HUMANMAPK1IP1Lphysical
19060904
DMRTB_HUMANDMRTB1physical
19060904
KDM1A_HUMANKDM1Aphysical
23455924
ANM5_HUMANPRMT5physical
23455924
ANM6_HUMANPRMT6physical
23455924
SMYD1_HUMANSMYD1physical
23455924
SUV91_HUMANSUV39H1physical
23455924
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 LENG8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-770 AND SER-776, ANDMASS SPECTROMETRY.

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