HUTH_MOUSE - dbPTM
HUTH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HUTH_MOUSE
UniProt AC P35492
Protein Name Histidine ammonia-lyase
Gene Name Hal
Organism Mus musculus (Mouse).
Sequence Length 657
Subcellular Localization
Protein Description
Protein Sequence MPRYTVHVRGEWLAVPCQDGKLTVGWLGREAVRRYMKNKPDNGGFTSVDEVQFLVHRCKGLGLLDNEDELEVALEDNEFVEVVIEGDVMSPDFIPSQPEGVFLYSKYREPEKYIALDGDSLSTEDLVNLGKGRYKIKLTSIAEKKVQQSREVIDSIIKERTVVYGITTGFGKFARTVIPANKLQELQVNLVRSHSSGVGKPLSPERCRMLLALRINVLAKGYSGISLETLKQVIEAFNASCLSYVPEKGTVGASGDLAPLSHLALGLIGEGKMWSPKSGWADAKYVLEAHGLKPIVLKPKEGLALINGTQMITSLGCEALERASAIARQADIVAALTLEVLKGTTKAFDTDIHAVRPHRGQIEVAFRFRSLLDSDHHPSEIAESHRFCDRVQDAYTLRCCPQVHGVVNDTIAFVKDIITTELNSATDNPMVFASRGETISGGNFHGEYPAKALDYLAIGVHELAAISERRIERLCNPSLSELPAFLVAEGGLNSGFMIAHCTAAALVSESKALCHPSSVDSLSTSAATEDHVSMGGWAARKALRVVEHVEQVLAIELLAACQGIEFLRPLKTTTPLEKVYDLVRSVVRPWIKDRFMAPDIEAAHRLLLDQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLESLRKNSATIPESDDL
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
37UbiquitinationEAVRRYMKNKPDNGG
HHHHHHHHCCCCCCC
53.54-
112AcetylationSKYREPEKYIALDGD
ECCCCCCCEEEECCC
53.3122733758
112UbiquitinationSKYREPEKYIALDGD
ECCCCCCCEEEECCC
53.31-
113PhosphorylationKYREPEKYIALDGDS
CCCCCCCEEEECCCC
6.9717242355
131UbiquitinationEDLVNLGKGRYKIKL
HHHHHCCCCCEEEEE
43.30-
131SuccinylationEDLVNLGKGRYKIKL
HHHHHCCCCCEEEEE
43.3023954790
137UbiquitinationGKGRYKIKLTSIAEK
CCCCEEEEEHHHHHH
41.37-
137MalonylationGKGRYKIKLTSIAEK
CCCCEEEEEHHHHHH
41.3726320211
140PhosphorylationRYKIKLTSIAEKKVQ
CEEEEEHHHHHHHHH
30.1823984901
144MalonylationKLTSIAEKKVQQSRE
EEHHHHHHHHHHHHH
49.5826320211
144SuccinylationKLTSIAEKKVQQSRE
EEHHHHHHHHHHHHH
49.5823954790
158MalonylationEVIDSIIKERTVVYG
HHHHHHHHHCEEEEE
39.2026320211
158UbiquitinationEVIDSIIKERTVVYG
HHHHHHHHHCEEEEE
39.20-
172AcetylationGITTGFGKFARTVIP
EEECCCHHHHCEEEE
33.3223954790
172UbiquitinationGITTGFGKFARTVIP
EEECCCHHHHCEEEE
33.32-
176PhosphorylationGFGKFARTVIPANKL
CCHHHHCEEEEHHHH
21.2521454597
182AcetylationRTVIPANKLQELQVN
CEEEEHHHHHHHHHH
54.3723954790
182UbiquitinationRTVIPANKLQELQVN
CEEEEHHHHHHHHHH
54.37-
200MalonylationSHSSGVGKPLSPERC
HCCCCCCCCCCHHHH
40.1430639696
200AcetylationSHSSGVGKPLSPERC
HCCCCCCCCCCHHHH
40.1423954790
200UbiquitinationSHSSGVGKPLSPERC
HCCCCCCCCCCHHHH
40.14-
203PhosphorylationSGVGKPLSPERCRML
CCCCCCCCHHHHHHH
32.9929472430
220UbiquitinationLRINVLAKGYSGISL
HHHHHHHCCCCCCCH
54.97-
254OtherEKGTVGASGDLAPLS
CCCCCCCCCCCHHHH
27.23-
254"2,3-didehydroalanine (Ser)"EKGTVGASGDLAPLS
CCCCCCCCCCCHHHH
27.23-
277UbiquitinationEGKMWSPKSGWADAK
CCCCCCCCCCCCCHH
56.96-
277SuccinylationEGKMWSPKSGWADAK
CCCCCCCCCCCCCHH
56.9623954790
284AcetylationKSGWADAKYVLEAHG
CCCCCCHHHHHHHCC
36.1223954790
293UbiquitinationVLEAHGLKPIVLKPK
HHHHCCCCCEEECCC
36.97-
298UbiquitinationGLKPIVLKPKEGLAL
CCCCEEECCCCCEEE
43.05-
300UbiquitinationKPIVLKPKEGLALIN
CCEEECCCCCEEEEC
63.93-
342UbiquitinationALTLEVLKGTTKAFD
HHHHHHHCCCCCCCC
60.43-
346UbiquitinationEVLKGTTKAFDTDIH
HHHCCCCCCCCCCEE
47.06-
396PhosphorylationDRVQDAYTLRCCPQV
CCCCCCHHHCCCCCC
14.9422817900
578UbiquitinationKTTTPLEKVYDLVRS
CCCCCHHHHHHHHHH
54.50-
578AcetylationKTTTPLEKVYDLVRS
CCCCCHHHHHHHHHH
54.5023954790
592MalonylationSVVRPWIKDRFMAPD
HHHHHHHHCCCCCCC
38.6926320211
592UbiquitinationSVVRPWIKDRFMAPD
HHHHHHHHCCCCCCC
38.69-
611UbiquitinationHRLLLDQKVWEVAAP
HHHHHCHHHHHHHHH
49.32-
611AcetylationHRLLLDQKVWEVAAP
HHHHHCHHHHHHHHH
49.3223954790
622UbiquitinationVAAPYIEKYRMEHIP
HHHHHHHHHCHHCCC
28.70-
622AcetylationVAAPYIEKYRMEHIP
HHHHHHHHHCHHCCC
28.7023954790
623PhosphorylationAAPYIEKYRMEHIPE
HHHHHHHHCHHCCCC
11.4723140645
625OxidationPYIEKYRMEHIPESR
HHHHHHCHHCCCCCC
3.8917242355
631PhosphorylationRMEHIPESRPLSPTA
CHHCCCCCCCCCCCC
33.5721082442
635PhosphorylationIPESRPLSPTAFSLE
CCCCCCCCCCCCCHH
23.9225521595
637PhosphorylationESRPLSPTAFSLESL
CCCCCCCCCCCHHHH
36.6425521595
640PhosphorylationPLSPTAFSLESLRKN
CCCCCCCCHHHHHHC
28.8523737553
643PhosphorylationPTAFSLESLRKNSAT
CCCCCHHHHHHCCCC
38.4721743459
648PhosphorylationLESLRKNSATIPESD
HHHHHHCCCCCCCCC
29.8025521595
650PhosphorylationSLRKNSATIPESDDL
HHHHCCCCCCCCCCC
36.5626487105
654PhosphorylationNSATIPESDDL----
CCCCCCCCCCC----
30.9428609623

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 HUTH_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HUTH_MOUSE !!

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 HUTH_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HUTH_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HUTH_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; SER-635 ANDSER-648, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND MASSSPECTROMETRY.

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