LKHA4_HUMAN - dbPTM
LKHA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LKHA4_HUMAN
UniProt AC P09960
Protein Name Leukotriene A-4 hydrolase
Gene Name LTA4H
Organism Homo sapiens (Human).
Sequence Length 611
Subcellular Localization Cytoplasm.
Protein Description Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity..
Protein Sequence MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD
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
12PhosphorylationVDTCSLASPASVCRT
CCCCCCCCCHHHHCC
26.7125159151
15PhosphorylationCSLASPASVCRTKHL
CCCCCCHHHHCCCCE
25.7421815630
17GlutathionylationLASPASVCRTKHLHL
CCCCHHHHCCCCEEE
4.1822555962
20UbiquitinationPASVCRTKHLHLRCS
CHHHHCCCCEEEEEE
25.4721890473
20AcetylationPASVCRTKHLHLRCS
CHHHHCCCCEEEEEE
25.4726210075
20 (in isoform 1)Ubiquitination-25.4721890473
20 (in isoform 2)Ubiquitination-25.4721890473
20UbiquitinationPASVCRTKHLHLRCS
CHHHHCCCCEEEEEE
25.4722053931
27PhosphorylationKHLHLRCSVDFTRRT
CCEEEEEEEECCCCC
20.4927251275
31PhosphorylationLRCSVDFTRRTLTGT
EEEEEECCCCCCCEE
18.1225690035
34PhosphorylationSVDFTRRTLTGTAAL
EEECCCCCCCEEEEE
25.94-
42O-linked_GlycosylationLTGTAALTVQSQEDN
CCEEEEEEEECCCHH
16.2723301498
45O-linked_GlycosylationTAALTVQSQEDNLRS
EEEEEEECCCHHHHH
31.0723301498
49UbiquitinationTVQSQEDNLRSLVLD
EEECCCHHHHHEEEE
36.2821890473
49AcetylationTVQSQEDNLRSLVLD
EEECCCHHHHHEEEE
36.2819608861
49UbiquitinationTVQSQEDNLRSLVLD
EEECCCHHHHHEEEE
36.2819608861
58AcetylationRSLVLDTKDLTIEKV
HHEEEECCCCEEEEE
50.8623236377
58UbiquitinationRSLVLDTKDLTIEKV
HHEEEECCCCEEEEE
50.86-
582-HydroxyisobutyrylationRSLVLDTKDLTIEKV
HHEEEECCCCEEEEE
50.86-
58SuccinylationRSLVLDTKDLTIEKV
HHEEEECCCCEEEEE
50.8623954790
64UbiquitinationTKDLTIEKVVINGQE
CCCCEEEEEEECCEE
37.64-
73AcetylationVINGQEVKYALGERQ
EECCEEEEEEECCCC
24.8519608861
73UbiquitinationVINGQEVKYALGERQ
EECCEEEEEEECCCC
24.8573
73 (in isoform 2)Ubiquitination-24.8521890473
73 (in isoform 1)Ubiquitination-24.8521890473
74PhosphorylationINGQEVKYALGERQS
ECCEEEEEEECCCCC
16.5426437602
81PhosphorylationYALGERQSYKGSPME
EEECCCCCCCCCCCE
34.7325159151
83UbiquitinationLGERQSYKGSPMEIS
ECCCCCCCCCCCEEE
59.15-
85PhosphorylationERQSYKGSPMEISLP
CCCCCCCCCCEEEEE
19.5422210691
87SulfoxidationQSYKGSPMEISLPIA
CCCCCCCCEEEEEEE
8.3830846556
90PhosphorylationKGSPMEISLPIALSK
CCCCCEEEEEEEECC
18.1329396449
96PhosphorylationISLPIALSKNQEIVI
EEEEEEECCCCEEEE
22.1229396449
106PhosphorylationQEIVIEISFETSPKS
CEEEEEEEEECCCCC
12.3023663014
110PhosphorylationIEISFETSPKSSALQ
EEEEEECCCCCCCCC
24.1123663014
127UbiquitinationTPEQTSGKEHPYLFS
CCCCCCCCCCCCHHH
53.25-
150PhosphorylationAILPCQDTPSVKLTY
EEEECCCCCCEEEEE
7.5023403867
152PhosphorylationLPCQDTPSVKLTYTA
EECCCCCCEEEEEEE
33.7023403867
154UbiquitinationCQDTPSVKLTYTAEV
CCCCCCEEEEEEEEE
39.18-
156PhosphorylationDTPSVKLTYTAEVSV
CCCCEEEEEEEEEEC
17.0728152594
157PhosphorylationTPSVKLTYTAEVSVP
CCCEEEEEEEEEECC
17.8728152594
158PhosphorylationPSVKLTYTAEVSVPK
CCEEEEEEEEEECCH
15.8828152594
162PhosphorylationLTYTAEVSVPKELVA
EEEEEEEECCHHHHH
24.9823403867
171SulfoxidationPKELVALMSAIRDGE
CHHHHHHHHHHHCCC
1.5130846556
172PhosphorylationKELVALMSAIRDGET
HHHHHHHHHHHCCCC
22.7620068231
186PhosphorylationTPDPEDPSRKIYKFI
CCCCCCCCHHHHHHH
59.5321712546
188UbiquitinationDPEDPSRKIYKFIQK
CCCCCCHHHHHHHHC
55.51-
191UbiquitinationDPSRKIYKFIQKVPI
CCCHHHHHHHHCCCC
39.19-
195AcetylationKIYKFIQKVPIPCYL
HHHHHHHCCCCCHHH
45.2021466224
212PhosphorylationLVVGALESRQIGPRT
HHHHHHHHCCCCCCE
30.2719690332
225UbiquitinationRTLVWSEKEQVEKSA
CEEEECCHHHHHHHH
48.18-
225AcetylationRTLVWSEKEQVEKSA
CEEEECCHHHHHHHH
48.1825953088
230UbiquitinationSEKEQVEKSAYEFSE
CCHHHHHHHHHCCCH
41.3421906983
230 (in isoform 2)Ubiquitination-41.3421890473
230 (in isoform 1)Ubiquitination-41.3421890473
231PhosphorylationEKEQVEKSAYEFSET
CHHHHHHHHHCCCHH
23.6828152594
233PhosphorylationEQVEKSAYEFSETES
HHHHHHHHCCCHHHH
25.2928152594
236PhosphorylationEKSAYEFSETESMLK
HHHHHCCCHHHHHHH
31.50-
238PhosphorylationSAYEFSETESMLKIA
HHHCCCHHHHHHHHH
31.9628348404
240PhosphorylationYEFSETESMLKIAED
HCCCHHHHHHHHHHH
36.5128348404
313AcetylationLVTNKTWDHFWLNEG
EEECCCEEEEEECCC
32.1319608861
313UbiquitinationLVTNKTWDHFWLNEG
EEECCCEEEEEECCC
32.1319608861
337AcetylationCGRLFGEKFRHFNAL
HHHHHHHHCCCCCCC
48.3419608861
337UbiquitinationCGRLFGEKFRHFNAL
HHHHHHHHCCCCCCC
48.3419608861
3372-HydroxyisobutyrylationCGRLFGEKFRHFNAL
HHHHHHHHCCCCCCC
48.34-
337MalonylationCGRLFGEKFRHFNAL
HHHHHHHHCCCCCCC
48.3432601280
355UbiquitinationGELQNSVKTFGETHP
HHHHHHHCCCCCCCC
37.65-
355 (in isoform 2)Ubiquitination-37.65-
355AcetylationGELQNSVKTFGETHP
HHHHHHHCCCCCCCC
37.6526051181
365UbiquitinationGETHPFTKLVVDLTD
CCCCCCCEEEEECCC
39.40-
379PhosphorylationDIDPDVAYSSVPYEK
CCCCCCCCCCCCHHH
11.0025147952
390UbiquitinationPYEKGFALLFYLEQL
CHHHHHHHHHHHHHH
2.9521890473
390AcetylationPYEKGFALLFYLEQL
CHHHHHHHHHHHHHH
2.9519608861
390UbiquitinationPYEKGFALLFYLEQL
CHHHHHHHHHHHHHH
2.9519608861
394UbiquitinationGFALLFYLEQLLGGP
HHHHHHHHHHHHCCH
2.3721890473
414AcetylationFLKAYVEKFSYKSIT
HHHHHHHHCCCCCCC
29.5719608861
414UbiquitinationFLKAYVEKFSYKSIT
HHHHHHHHCCCCCCC
29.5721890473
4142-HydroxyisobutyrylationFLKAYVEKFSYKSIT
HHHHHHHHCCCCCCC
29.57-
414 (in isoform 1)Ubiquitination-29.5721890473
414 (in isoform 2)Ubiquitination-29.5721890473
416PhosphorylationKAYVEKFSYKSITTD
HHHHHHCCCCCCCCC
42.6029496963
417PhosphorylationAYVEKFSYKSITTDD
HHHHHCCCCCCCCCH
16.3422817900
418AcetylationYVEKFSYKSITTDDW
HHHHCCCCCCCCCHH
33.9023236377
418UbiquitinationYVEKFSYKSITTDDW
HHHHCCCCCCCCCHH
33.9021890473
418 (in isoform 2)Ubiquitination-33.9021890473
4182-HydroxyisobutyrylationYVEKFSYKSITTDDW
HHHHCCCCCCCCCHH
33.90-
418 (in isoform 1)Ubiquitination-33.9021890473
430PhosphorylationDDWKDFLYSYFKDKV
CHHHHHHHHHHCCHH
11.00-
434AcetylationDFLYSYFKDKVDVLN
HHHHHHHCCHHCCHH
48.7023954790
434UbiquitinationDFLYSYFKDKVDVLN
HHHHHHHCCHHCCHH
48.70-
434SuccinylationDFLYSYFKDKVDVLN
HHHHHHHCCHHCCHH
48.7023954790
456UbiquitinationLYSPGLPPIKPNYDM
HCCCCCCCCCCCCCC
52.8821890473
480AcetylationSQRWITAKEDDLNSF
HHHCHHCCHHHHHCC
53.6923954790
480UbiquitinationSQRWITAKEDDLNSF
HHHCHHCCHHHHHCC
53.6921890473
480 (in isoform 2)Ubiquitination-53.6921890473
480 (in isoform 1)Ubiquitination-53.6921890473
486PhosphorylationAKEDDLNSFNATDLK
CCHHHHHCCCCCCHH
27.4629514088
490PhosphorylationDLNSFNATDLKDLSS
HHHCCCCCCHHHCCH
42.8622985185
493UbiquitinationSFNATDLKDLSSHQL
CCCCCCHHHCCHHHH
60.47-
496PhosphorylationATDLKDLSSHQLNEF
CCCHHHCCHHHHHHH
35.5920873877
497PhosphorylationTDLKDLSSHQLNEFL
CCHHHCCHHHHHHHH
23.6620873877
507PhosphorylationLNEFLAQTLQRAPLP
HHHHHHHHHHHCCCC
21.1720873877
519UbiquitinationPLPLGHIKRMQEVYN
CCCHHHHHHHHHHHC
35.82-
519AcetylationPLPLGHIKRMQEVYN
CCCHHHHHHHHHHHC
35.8225953088
521SulfoxidationPLGHIKRMQEVYNFN
CHHHHHHHHHHHCCC
3.1930846556
549AcetylationLCIQSKWEDAIPLAL
HHHHHCHHHHHHHHH
41.1019608861
549UbiquitinationLCIQSKWEDAIPLAL
HHHHHCHHHHHHHHH
41.1019608861
557UbiquitinationDAIPLALKMATEQGR
HHHHHHHHHHHHCCC
22.38-
566UbiquitinationATEQGRMKFTRPLFK
HHHCCCCCCCHHHHH
42.07-
573AcetylationKFTRPLFKDLAAFDK
CCCHHHHHHHHHHCC
60.5619608861
573UbiquitinationKFTRPLFKDLAAFDK
CCCHHHHHHHHHHCC
60.5621890473
573SuccinylationKFTRPLFKDLAAFDK
CCCHHHHHHHHHHCC
60.5623954790
573 (in isoform 1)Ubiquitination-60.5621890473
580UbiquitinationKDLAAFDKSHDQAVR
HHHHHHCCCHHHHHH
43.14-
5802-HydroxyisobutyrylationKDLAAFDKSHDQAVR
HHHHHHCCCHHHHHH
43.14-
580AcetylationKDLAAFDKSHDQAVR
HHHHHHCCCHHHHHH
43.1425953088
589PhosphorylationHDQAVRTYQEHKASM
HHHHHHHHHHHHHCC
11.0118767875
593UbiquitinationVRTYQEHKASMHPVT
HHHHHHHHHCCCCCH
41.2121890473
593 (in isoform 1)Ubiquitination-41.2121890473
595PhosphorylationTYQEHKASMHPVTAM
HHHHHHHCCCCCHHH
23.5618767875
600PhosphorylationKASMHPVTAMLVGKD
HHCCCCCHHHHHCCC
15.7118767875
606UbiquitinationVTAMLVGKDLKVD--
CHHHHHCCCCCCC--
53.02-
606AcetylationVTAMLVGKDLKVD--
CHHHHHCCCCCCC--
53.0225953088

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 LKHA4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
416SPhosphorylation

9395533

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 LKHA4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMM62_HUMANTMEM62physical
16169070
SIR1_HUMANSIRT1physical
22939629
ZN593_HUMANZNF593physical
22939629
PNCB_HUMANNAPRTphysical
26344197
TAGL2_HUMANTAGLN2physical
26344197

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
DB01197Captopril
Regulatory Network of LKHA4_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-73; LYS-337; LYS-414 ANDLYS-573, AND MASS SPECTROMETRY.

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