HACL1_HUMAN - dbPTM
HACL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HACL1_HUMAN
UniProt AC Q9UJ83
Protein Name 2-hydroxyacyl-CoA lyase 1
Gene Name HACL1
Organism Homo sapiens (Human).
Sequence Length 578
Subcellular Localization Peroxisome.
Protein Description Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde..
Protein Sequence MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM
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
4Phosphorylation----MPDSNFAERSE
----CCCCCCHHCCH
28.1629255136
10PhosphorylationDSNFAERSEEQVSGA
CCCCHHCCHHHHCHH
36.6723312004
15PhosphorylationERSEEQVSGAKVIAQ
HCCHHHHCHHHHHHH
32.5023312004
18UbiquitinationEEQVSGAKVIAQALK
HHHHCHHHHHHHHHH
37.3921890473
18UbiquitinationEEQVSGAKVIAQALK
HHHHCHHHHHHHHHH
37.3921890473
18UbiquitinationEEQVSGAKVIAQALK
HHHHCHHHHHHHHHH
37.3921906983
18UbiquitinationEEQVSGAKVIAQALK
HHHHCHHHHHHHHHH
37.3921906983
109UbiquitinationCWPLLVIGGSSERNQ
CEEEEEECCCCCCCH
23.58-
119SulfoxidationSERNQETMGAFQEFP
CCCCHHHHHHHHHCH
3.4221406390
126UbiquitinationMGAFQEFPQVEACRL
HHHHHHCHHHHHHHH
36.23-
135PhosphorylationVEACRLYTKFSARPS
HHHHHHHHCCCCCCC
30.15-
136UbiquitinationEACRLYTKFSARPSS
HHHHHHHCCCCCCCC
24.62-
138PhosphorylationCRLYTKFSARPSSIE
HHHHHCCCCCCCCCC
25.56-
142PhosphorylationTKFSARPSSIEAIPF
HCCCCCCCCCCCCCH
38.09-
153UbiquitinationAIPFVIEKAVRSSIY
CCCHHHHHHHHHHCC
40.8517370265
187UbiquitinationNVNSIKYMERCMSPP
EHHHHHHHHHHCCCC
1.91-
192PhosphorylationKYMERCMSPPISMAE
HHHHHHCCCCCCHHH
31.0225850435
196PhosphorylationRCMSPPISMAETSAV
HHCCCCCCHHHHHHH
20.0829449344
200PhosphorylationPPISMAETSAVCTAA
CCCCHHHHHHHHHHH
16.6725850435
201PhosphorylationPISMAETSAVCTAAS
CCCHHHHHHHHHHHH
15.3725850435
214AcetylationASVIRNAKQPLLIIG
HHHHHHCCCCEEEEE
56.8723954790
214UbiquitinationASVIRNAKQPLLIIG
HHHHHHCCCCEEEEE
56.87-
214UbiquitinationASVIRNAKQPLLIIG
HHHHHHCCCCEEEEE
56.87-
224UbiquitinationLLIIGKGAAYAHAEE
EEEEECCHHHHHHHH
10.77-
234AcetylationAHAEESIKKLVEQYK
HHHHHHHHHHHHHCC
49.7025953088
234UbiquitinationAHAEESIKKLVEQYK
HHHHHHHHHHHHHCC
49.70-
235UbiquitinationHAEESIKKLVEQYKL
HHHHHHHHHHHHCCC
56.97-
241UbiquitinationKKLVEQYKLPFLPTP
HHHHHHCCCCCCCCC
49.75-
241AcetylationKKLVEQYKLPFLPTP
HHHHHHCCCCCCCCC
49.7526051181
247PhosphorylationYKLPFLPTPMGKGVV
CCCCCCCCCCCCCCC
28.2321406692
251UbiquitinationFLPTPMGKGVVPDNH
CCCCCCCCCCCCCCC
42.13-
251AcetylationFLPTPMGKGVVPDNH
CCCCCCCCCCCCCCC
42.1326051181
260PhosphorylationVVPDNHPYCVGAARS
CCCCCCCCCHHHHHH
7.69-
283UbiquitinationIVLFGARLNWILHFG
HHHHHHCHHHHHHCC
6.5421890473
348AcetylationWQYPPESKWWKTLRE
CCCCCCCHHHHHHHH
56.2526051181
351AcetylationPPESKWWKTLREKMK
CCCCHHHHHHHHHHH
36.2426051181
351SuccinylationPPESKWWKTLREKMK
CCCCHHHHHHHHHHH
36.24-
351SuccinylationPPESKWWKTLREKMK
CCCCHHHHHHHHHHH
36.24-
358SuccinylationKTLREKMKSNEAASK
HHHHHHHHCCHHHHH
62.29-
358SuccinylationKTLREKMKSNEAASK
HHHHHHHHCCHHHHH
62.29-
359O-linked_GlycosylationTLREKMKSNEAASKE
HHHHHHHCCHHHHHH
36.0830379171
365UbiquitinationKSNEAASKELASKKS
HCCHHHHHHHHHCCC
52.61-
365AcetylationKSNEAASKELASKKS
HCCHHHHHHHHHCCC
52.6126051181
365SuccinylationKSNEAASKELASKKS
HCCHHHHHHHHHCCC
52.6121890473
365SuccinylationKSNEAASKELASKKS
HCCHHHHHHHHHCCC
52.61-
377PhosphorylationKKSLPMNYYTVFYHV
CCCCCCCHHHHHHHH
8.34-
382PhosphorylationMNYYTVFYHVQEQLP
CCHHHHHHHHHHHCC
9.20-
407PhosphorylationNTMDIGRTVLQNYLP
CCCHHCHHHHHHCCC
21.9824114839
412PhosphorylationGRTVLQNYLPRHRLD
CHHHHHHCCCHHCCC
12.72-
422PhosphorylationRHRLDAGTFGTMGVG
HHCCCCCCCCCCHHH
22.17-
425PhosphorylationLDAGTFGTMGVGLGF
CCCCCCCCCHHHHHH
13.42-
458UbiquitinationCVEGDSAFGFSGMEV
EEECCCCCCCCCCCH
13.5421890473
486PhosphorylationVVNNNGIYQGFDTDT
EECCCCCCCCCCHHH
12.18-
513UbiquitinationVVPPMCLLPNSHYEQ
ECCCEECCCCCHHHH
3.0021890473
540UbiquitinationQTPEELQKSLRQSLA
CCHHHHHHHHHHHHC
65.1721890473
540AcetylationQTPEELQKSLRQSLA
CCHHHHHHHHHHHHC
65.1723954790
541PhosphorylationTPEELQKSLRQSLAD
CHHHHHHHHHHHHCC
18.8024719451
545PhosphorylationLQKSLRQSLADTTKP
HHHHHHHHHCCCCCC
21.0621406692
549PhosphorylationLRQSLADTTKPSLIN
HHHHHCCCCCCHHEE
30.9821406692
550PhosphorylationRQSLADTTKPSLINI
HHHHCCCCCCHHEEE
41.3221406692
551AcetylationQSLADTTKPSLINIM
HHHCCCCCCHHEEEE
34.4026051181
551UbiquitinationQSLADTTKPSLINIM
HHHCCCCCCHHEEEE
34.40-
553PhosphorylationLADTTKPSLINIMIE
HCCCCCCHHEEEEEC
43.3621406692
564PhosphorylationIMIEPQATRKAQDFH
EEECCCCCCCHHHCH
27.7021406692
566UbiquitinationIEPQATRKAQDFHWL
ECCCCCCCHHHCHHH
46.15-
574PhosphorylationAQDFHWLTRSNM---
HHHCHHHHCCCC---
27.1924719451

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 HACL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HACL1_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 HACL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZMY19_HUMANZMYND19physical
16189514
HACL1_HUMANHACL1physical
16189514
HACL1_HUMANHACL1physical
25416956
ZMY19_HUMANZMYND19physical
25416956
MAGB6_HUMANMAGEB6physical
25416956
PTPRF_HUMANPTPRFphysical
26344197
WDFY1_HUMANWDFY1physical
26344197
ASPC1_HUMANASPSCR1physical
28514442
PXDC2_HUMANPLXDC2physical
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 HACL1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.

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