AMPL_HUMAN - dbPTM
AMPL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPL_HUMAN
UniProt AC P28838
Protein Name Cytosol aminopeptidase
Gene Name LAP3
Organism Homo sapiens (Human).
Sequence Length 519
Subcellular Localization Cytoplasm.
Protein Description Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides..
Protein Sequence MFLLPLPAAGRVVVRRLAVRRFGSRSLSTADMTKGLVLGIYSKEKEDDVPQFTSAGENFDKLLAGKLRETLNISGPPLKAGKTRTFYGLHQDFPSVVLVGLGKKAAGIDEQENWHEGKENIRAAVAAGCRQIQDLELSSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKMAVSAKLYGSGDQEAWQKGVLFASGQNLARQLMETPANEMTPTRFAEIIEKNLKSASSKTEVHIRPKSWIEEQAMGSFLSVAKGSDEPPVFLEIHYKGSPNANEPPLVFVGKGITFDSGGISIKASANMDLMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRAKNGKTIQVDNTDAEGRLILADALCYAHTFNPKVILNAATLTGAMDVALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLFEHYTRQVVDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGVMTNKDEVPYLRKGMTGRPTRTLIEFLLRFSQDNA
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
24PhosphorylationLAVRRFGSRSLSTAD
HHHHHHCCCCCCHHH		18.9132645325
26PhosphorylationVRRFGSRSLSTADMT
HHHHCCCCCCHHHCC		28.5020068231
28PhosphorylationRFGSRSLSTADMTKG
HHCCCCCCHHHCCCC		23.8528450419
29PhosphorylationFGSRSLSTADMTKGL
HCCCCCCHHHCCCCE		31.7828450419
33PhosphorylationSLSTADMTKGLVLGI
CCCHHHCCCCEEEEE		23.6228985074
41PhosphorylationKGLVLGIYSKEKEDD
CCEEEEEEECCCCCC		16.3420068231
42PhosphorylationGLVLGIYSKEKEDDV
CEEEEEEECCCCCCC		32.2020068231
45SuccinylationLGIYSKEKEDDVPQF
EEEEECCCCCCCCCC		70.90-
45SuccinylationLGIYSKEKEDDVPQF
EEEEECCCCCCCCCC		70.90-
45AcetylationLGIYSKEKEDDVPQF
EEEEECCCCCCCCCC		70.9025038526
45UbiquitinationLGIYSKEKEDDVPQF
EEEEECCCCCCCCCC		70.9029967540
53PhosphorylationEDDVPQFTSAGENFD
CCCCCCCCCCCCCHH		16.6628857561
54PhosphorylationDDVPQFTSAGENFDK
CCCCCCCCCCCCHHH		35.2528857561
61UbiquitinationSAGENFDKLLAGKLR
CCCCCHHHHHHHHHH		41.0629967540
61SuccinylationSAGENFDKLLAGKLR
CCCCCHHHHHHHHHH		41.06-
61SuccinylationSAGENFDKLLAGKLR
CCCCCHHHHHHHHHH		41.06-
61AcetylationSAGENFDKLLAGKLR
CCCCCHHHHHHHHHH		41.0625953088
66UbiquitinationFDKLLAGKLRETLNI
HHHHHHHHHHHHCCC		38.4727667366
79UbiquitinationNISGPPLKAGKTRTF
CCCCCCCCCCCEEEE		61.9524816145
79AcetylationNISGPPLKAGKTRTF
CCCCCCCCCCCEEEE		61.9525953088
103AcetylationVVLVGLGKKAAGIDE
EEEEECCCCCCCCCC		44.262403929
1032-HydroxyisobutyrylationVVLVGLGKKAAGIDE
EEEEECCCCCCCCCC		44.26-
103SuccinylationVVLVGLGKKAAGIDE
EEEEECCCCCCCCCC		44.26-
103SuccinylationVVLVGLGKKAAGIDE
EEEEECCCCCCCCCC		44.26-
104AcetylationVLVGLGKKAAGIDEQ
EEEECCCCCCCCCCC		41.4911790729
118UbiquitinationQENWHEGKENIRAAV
CCCCHHHHHHHHHHH		44.6029967540
138PhosphorylationQIQDLELSSVEVDPC
EEECEECCEEEEECC		23.9828102081
139PhosphorylationIQDLELSSVEVDPCG
EECEECCEEEEECCC		34.6228102081
157 (in isoform 2)Ubiquitination-3.7621890473
160PhosphorylationEGAVLGLYEYDDLKQ
HCCEEEEEECCHHHH		15.6228102081
170AcetylationDDLKQKKKMAVSAKL
CHHHHHHHHHHEEEH		38.8425038526
180PhosphorylationVSAKLYGSGDQEAWQ
HEEEHHCCCCHHHHH		26.1625850435
188 (in isoform 1)Ubiquitination-40.0421890473
188UbiquitinationGDQEAWQKGVLFASG
CCHHHHHHCEEEECH		40.0422817900
190 (in isoform 2)Ubiquitination-5.2421890473
194PhosphorylationQKGVLFASGQNLARQ
HHCEEEECHHHHHHH		33.3128258704
203SulfoxidationQNLARQLMETPANEM
HHHHHHHHCCCHHHC		4.0030846556
205PhosphorylationLARQLMETPANEMTP
HHHHHHCCCHHHCCH		17.4627251275
210SulfoxidationMETPANEMTPTRFAE
HCCCHHHCCHHHHHH		5.6630846556
211PhosphorylationETPANEMTPTRFAEI
CCCHHHCCHHHHHHH		18.4823917254
213PhosphorylationPANEMTPTRFAEIIE
CHHHCCHHHHHHHHH		29.2923186163
221AcetylationRFAEIIEKNLKSASS
HHHHHHHHHHHCCCC		58.1119608861
221SuccinylationRFAEIIEKNLKSASS
HHHHHHHHHHHCCCC		58.11-
221SuccinylationRFAEIIEKNLKSASS
HHHHHHHHHHHCCCC		58.11-
221MalonylationRFAEIIEKNLKSASS
HHHHHHHHHHHCCCC		58.1126320211
221UbiquitinationRFAEIIEKNLKSASS
HHHHHHHHHHHCCCC		58.1122817900
221 (in isoform 1)Ubiquitination-58.1121890473
224UbiquitinationEIIEKNLKSASSKTE
HHHHHHHHCCCCCCE		54.0622817900
224SuccinylationEIIEKNLKSASSKTE
HHHHHHHHCCCCCCE		54.0623954790
225PhosphorylationIIEKNLKSASSKTEV
HHHHHHHCCCCCCEE		36.2329116813
227PhosphorylationEKNLKSASSKTEVHI
HHHHHCCCCCCEEEE		39.1829116813
228PhosphorylationKNLKSASSKTEVHIR
HHHHCCCCCCEEEEC		43.2323312004
229UbiquitinationNLKSASSKTEVHIRP
HHHCCCCCCEEEECC		46.3327667366
230PhosphorylationLKSASSKTEVHIRPK
HHCCCCCCEEEECCC		45.2328857561
237AcetylationTEVHIRPKSWIEEQA
CEEEECCCHHHHHHH		48.8825038526
238PhosphorylationEVHIRPKSWIEEQAM
EEEECCCHHHHHHHH		35.6522617229
250PhosphorylationQAMGSFLSVAKGSDE
HHHHHHHHHCCCCCC		20.3024719451
267AcetylationVFLEIHYKGSPNANE
EEEEEEECCCCCCCC		38.4625038526
285PhosphorylationVFVGKGITFDSGGIS
EEEECCEEECCCCEE		30.0220068231
288PhosphorylationGKGITFDSGGISIKA
ECCEEECCCCEEEEE		34.4320068231
292PhosphorylationTFDSGGISIKASANM
EECCCCEEEEEECCC		22.7024719451
296PhosphorylationGGISIKASANMDLMR
CCEEEEEECCCCCCC		18.3820068231
311PhosphorylationADMGGAATICSAIVS
CCCCHHHHHHHHHHH		23.2120068231
314PhosphorylationGGAATICSAIVSAAK
CHHHHHHHHHHHHHH		19.7220068231
318PhosphorylationTICSAIVSAAKLNLP
HHHHHHHHHHHCCCC		19.1820068231
335GlutathionylationIIGLAPLCENMPSGK
EEEEHHHHHCCCCCC		3.2822555962
345UbiquitinationMPSGKANKPGDVVRA
CCCCCCCCCCCEEEE		56.06-
356UbiquitinationVVRAKNGKTIQVDNT
EEEECCCCEEEECCC		52.4224816145
356AcetylationVVRAKNGKTIQVDNT
EEEECCCCEEEECCC		52.4225953088
363PhosphorylationKTIQVDNTDAEGRLI
CEEEECCCCCCCCEE		31.93-
376GlutathionylationLILADALCYAHTFNP
EEHHHHHHHHHCCCH		2.7822555962
377PhosphorylationILADALCYAHTFNPK
EHHHHHHHHHCCCHH		11.4129496907
424 (in isoform 2)Ubiquitination-44.2221890473
445 (in isoform 2)Ubiquitination-2.1121890473
455UbiquitinationADVNNIGKYRSAGAC
CCCCCCCCCCCCCHH		33.4222817900
455SuccinylationADVNNIGKYRSAGAC
CCCCCCCCCCCCCHH		33.4221906983
455 (in isoform 1)Ubiquitination-33.4221890473
455SuccinylationADVNNIGKYRSAGAC
CCCCCCCCCCCCCHH		33.42-
455AcetylationADVNNIGKYRSAGAC
CCCCCCCCCCCCCHH		33.4225953088
456PhosphorylationDVNNIGKYRSAGACT
CCCCCCCCCCCCHHH		12.4620090780
458PhosphorylationNNIGKYRSAGACTAA
CCCCCCCCCCHHHHH		28.1528857561
469AcetylationCTAAAFLKEFVTHPK
HHHHHHHHHHHHCCC		42.5326051181
469UbiquitinationCTAAAFLKEFVTHPK
HHHHHHHHHHHHCCC		42.53-
476 (in isoform 1)Ubiquitination-49.7821890473
476UbiquitinationKEFVTHPKWAHLDIA
HHHHHCCCCCCEEEE		49.7821890473
476AcetylationKEFVTHPKWAHLDIA
HHHHHCCCCCCEEEE		49.7825038526
476SuccinylationKEFVTHPKWAHLDIA
HHHHHCCCCCCEEEE		49.782189047
476SuccinylationKEFVTHPKWAHLDIA
HHHHHCCCCCCEEEE		49.78-
486SulfoxidationHLDIAGVMTNKDEVP
CEEEEEEECCCCCCC		3.1530846556
489AcetylationIAGVMTNKDEVPYLR
EEEEECCCCCCCCCC		46.2125038526
489SuccinylationIAGVMTNKDEVPYLR
EEEEECCCCCCCCCC		46.21-
489SuccinylationIAGVMTNKDEVPYLR
EEEEECCCCCCCCCC		46.21-
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 AMPL_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPL_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 AMPL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
AASD1_HUMANAARSD1physical
22863883
AGFG1_HUMANAGFG1physical
22863883
HEM2_HUMANALADphysical
22863883
ARPC2_HUMANARPC2physical
22863883
OGT1_HUMANOGTphysical
22863883
SH3G1_HUMANSH3GL1physical
22863883
SHLB1_HUMANSH3GLB1physical
22863883
TPRKB_HUMANTPRKBphysical
22863883
FUBP1_HUMANFUBP1physical
26344197
MIF_HUMANMIFphysical
26344197
PRDX1_HUMANPRDX1physical
26344197
PRDX2_HUMANPRDX2physical
26344197
TKT_HUMANTKTphysical
26344197
SYVC_HUMANVARSphysical
26344197
RAB7A_HUMANRAB7Aphysical
26496610
RBM39_HUMANRBM39physical
26496610
NO40_HUMANZCCHC17physical
26496610
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 AMPL_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-221, AND MASS SPECTROMETRY.

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