NEUL_HUMAN - dbPTM
NEUL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEUL_HUMAN
UniProt AC Q9BYT8
Protein Name Neurolysin, mitochondrial
Gene Name NLN
Organism Homo sapiens (Human).
Sequence Length 704
Subcellular Localization Mitochondrion intermembrane space. Cytoplasm.
Protein Description Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A..
Protein Sequence MIARCLLAVRSLRRVGGSRILLRMTLGREVMSPLQAMSSYTVAGRNVLRWDLSPEQIKTRTEELIVQTKQVYDAVGMLGIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMRGDIFERIVHLQETCDLGKIKPEARRYLEKSIKMGKRNGLHLPEQVQNEIKSMKKRMSELCIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDDKYKITLKYPHYFPVMKKCCIPETRRRMEMAFNTRCKEENTIILQQLLPLRTKVAKLLGYSTHADFVLEMNTAKSTSRVTAFLDDLSQKLKPLGEAEREFILNLKKKECKDRGFEYDGKINAWDLYYYMTQTEELKYSIDQEFLKEYFPIEVVTEGLLNTYQELLGLSFEQMTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMAVAALVVNFSQPVAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDVDSLRRLSKHYKDGSPIADDLLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNTSLDAASEYAKYCSEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLHNFLKREPNQKAFLMSRGLHAP
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
11PhosphorylationRCLLAVRSLRRVGGS
HHHHHHHHHHHHCCH		21.45-
18PhosphorylationSLRRVGGSRILLRMT
HHHHHCCHHHEEEHH		15.3724719451
25PhosphorylationSRILLRMTLGREVMS
HHHEEEHHCCCHHCC		21.4524719451
32PhosphorylationTLGREVMSPLQAMSS
HCCCHHCCHHHHHHC		27.8625159151
41PhosphorylationLQAMSSYTVAGRNVL
HHHHHCCEECCCCEE		13.0620068231
53PhosphorylationNVLRWDLSPEQIKTR
CEECCCCCHHHHHHC		24.7419664994
58AcetylationDLSPEQIKTRTEELI
CCCHHHHHHCHHHHH		31.4825038526
58UbiquitinationDLSPEQIKTRTEELI
CCCHHHHHHCHHHHH		31.4821906983
59PhosphorylationLSPEQIKTRTEELIV
CCHHHHHHCHHHHHH		44.4423312004
61PhosphorylationPEQIKTRTEELIVQT
HHHHHHCHHHHHHHH		38.76-
113PhosphorylationLDFPQHVSSDKEVRA
CCCCCCCCCCHHHHH		30.6025690035
114PhosphorylationDFPQHVSSDKEVRAA
CCCCCCCCCHHHHHH		52.1725690035
116UbiquitinationPQHVSSDKEVRAAST
CCCCCCCHHHHHHCH		61.12-
1162-HydroxyisobutyrylationPQHVSSDKEVRAAST
CCCCCCCHHHHHHCH		61.12-
137PhosphorylationSRFDIEMSMRGDIFE
HHHCCCHHHCCCHHH		7.7926126808
148UbiquitinationDIFERIVHLQETCDL
CHHHHHHHHHHHCCC		21.3024816145
157UbiquitinationQETCDLGKIKPEARR
HHHCCCCCCCHHHHH		55.65-
168UbiquitinationEARRYLEKSIKMGKR
HHHHHHHHHHHHHHH		55.6929967540
171UbiquitinationRYLEKSIKMGKRNGL
HHHHHHHHHHHHCCC		49.0024816145
216PhosphorylationDDTFLVFSKAELGAL
CCCEEEEEHHHHCCC		24.3921712546
233UbiquitinationDFIDSLEKTDDDKYK
HHHHHHHCCCCCCEE		63.6529967540
242PhosphorylationDDDKYKITLKYPHYF
CCCCEEEEEECCCCH		17.0424719451
253AcetylationPHYFPVMKKCCIPET
CCCHHHCHHHCCHHH		42.7825953088
254UbiquitinationHYFPVMKKCCIPETR
CCHHHCHHHCCHHHH		19.08-
297PhosphorylationVAKLLGYSTHADFVL
HHHHHCCCCCCHHHE		16.3622210691
304UbiquitinationSTHADFVLEMNTAKS
CCCCHHHEEECCCCC		5.3724816145
308PhosphorylationDFVLEMNTAKSTSRV
HHHEEECCCCCCHHH		33.8720068231
311PhosphorylationLEMNTAKSTSRVTAF
EEECCCCCCHHHHHH		29.2020068231
312PhosphorylationEMNTAKSTSRVTAFL
EECCCCCCHHHHHHH		21.6122210691
313PhosphorylationMNTAKSTSRVTAFLD
ECCCCCCHHHHHHHH		31.6620068231
316PhosphorylationAKSTSRVTAFLDDLS
CCCCHHHHHHHHHHH		15.5820068231
323PhosphorylationTAFLDDLSQKLKPLG
HHHHHHHHHHCCCCC		32.0620068231
327MalonylationDDLSQKLKPLGEAER
HHHHHHCCCCCHHHH		45.2732601280
327UbiquitinationDDLSQKLKPLGEAER
HHHHHHCCCCCHHHH		45.2724816145
341UbiquitinationREFILNLKKKECKDR
HHHHHHCCHHHHHCC		61.8029967540
3412-HydroxyisobutyrylationREFILNLKKKECKDR
HHHHHHCCHHHHHCC		61.80-
404PhosphorylationYQELLGLSFEQMTDA
HHHHHCCCHHHHCCC		25.5726074081
409PhosphorylationGLSFEQMTDAHVWNK
CCCHHHHCCCEECCC		29.7226074081
417PhosphorylationDAHVWNKSVTLYTVK
CCEECCCCEEEEEEC		19.6826074081
419PhosphorylationHVWNKSVTLYTVKDK
EECCCCEEEEEECCC		22.5726074081
421PhosphorylationWNKSVTLYTVKDKAT
CCCCEEEEEECCCCC		10.5026074081
422PhosphorylationNKSVTLYTVKDKATG
CCCEEEEEECCCCCC		24.9626074081
424AcetylationSVTLYTVKDKATGEV
CEEEEEECCCCCCCE		45.7930584335
428PhosphorylationYTVKDKATGEVLGQF
EEECCCCCCCEEEEE		39.3526074081
436PhosphorylationGEVLGQFYLDLYPRE
CCEEEEEEHCCCCCC		7.45-
440PhosphorylationGQFYLDLYPREGKYN
EEEEHCCCCCCCCCC		10.4228152594
485PhosphorylationQPVAGRPSLLRHDEV
CCCCCCHHHHCCHHH		38.3822912867
542UbiquitinationWVWDVDSLRRLSKHY
CCCCHHHHHHHHHHC		2.9821963094
550SuccinylationRRLSKHYKDGSPIAD
HHHHHHCCCCCCCHH		56.1623954790
550MalonylationRRLSKHYKDGSPIAD
HHHHHHCCCCCCCHH		56.1626320211
550UbiquitinationRRLSKHYKDGSPIAD
HHHHHHCCCCCCCHH		56.1629967540
560UbiquitinationSPIADDLLEKLVASR
CCCHHHHHHHHHHHH		7.5921963094
562UbiquitinationIADDLLEKLVASRLV
CHHHHHHHHHHHHHH		48.5121906983
565UbiquitinationDLLEKLVASRLVNTG
HHHHHHHHHHHHHCC		10.2021963094
571PhosphorylationVASRLVNTGLLTLRQ
HHHHHHHCCHHHHHH		23.0221406692
575PhosphorylationLVNTGLLTLRQIVLS
HHHCCHHHHHHHHHH		25.57-
583UbiquitinationLRQIVLSKVDQSLHT
HHHHHHHHCCHHCCC		45.7421963094
598PhosphorylationNTSLDAASEYAKYCS
CCCHHHHHHHHHHHH		32.6229523821
623UbiquitinationTNMPATFGHLAGGYD
CCCCCCHHHHHCCCC		15.5621963094
641UbiquitinationYGYLWSEVFSMDMFY
HHHHHHHHCCHHHHH		3.4321963094
646UbiquitinationSEVFSMDMFYSCFKK
HHHCCHHHHHHHHHH		2.2621963094
653MalonylationMFYSCFKKEGIMNPE
HHHHHHHHCCCCCHH		40.7032601280
664UbiquitinationMNPEVGMKYRNLILK
CCHHHHHHHHCEECC		34.8221963094
664AcetylationMNPEVGMKYRNLILK
CCHHHHHHHHCEECC		34.8219608861
664MalonylationMNPEVGMKYRNLILK
CCHHHHHHHHCEECC		34.8226320211
665PhosphorylationNPEVGMKYRNLILKP
CHHHHHHHHCEECCC		8.8826356563
675PhosphorylationLILKPGGSLDGMDML
EECCCCCCCCHHHHH		29.2426356563
687AcetylationDMLHNFLKREPNQKA
HHHHHHHHCCCCCCH		51.0525953088
693AcetylationLKREPNQKAFLMSRG
HHCCCCCCHHHHHCC		47.9825953088
693MalonylationLKREPNQKAFLMSRG
HHCCCCCCHHHHHCC		47.9826320211
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 NEUL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEUL_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 NEUL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SYNE1_HUMANSYNE1physical
26344197
MBP_HUMANMBPphysical
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.
Regulatory Network of NEUL_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-664, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY.

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