ACOC_RAT - dbPTM
ACOC_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACOC_RAT
UniProt AC Q63270
Protein Name Cytoplasmic aconitate hydratase
Gene Name Aco1
Organism Rattus norvegicus (Rat).
Sequence Length 889
Subcellular Localization Cytoplasm.
Protein Description Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding (By similarity).; Catalyzes the isomerization of citrate to isocitrate via cis-aconitate..
Protein Sequence MKNPFAHLAEPLDPAQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWSIMQHKSIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVHFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDDVSIAYLVQTGREEDKVKHIKRYLQAVGMFRDFSDSSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEIEKDFESCLGAKQGFKGFQVAPDHHNDHKTFIYNDSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLNVKPYVKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTVRIDFEKEPLGVNAQGQQVFLKDIWPTRDEIQEVERKYVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPRDFNSYGSRRGNDAIMARGTFANIRLLNKFLNKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERTHCSNLVGMGVIPLEYLPGETADSLGLTGRERYTIHIPEHLKPRMKVQIKLDTGKTFQAVMRFDTDVELTYFHNGGILNYMIRKMAQ
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
19AcetylationLDPAQPGKKFFNLNK
CCCCCCCCCCCCCCC
53.7622902405
20AcetylationDPAQPGKKFFNLNKL
CCCCCCCCCCCCCCC
62.1922902405
26AcetylationKKFFNLNKLEDSRYG
CCCCCCCCCCCCCCC
57.3222902405
30PhosphorylationNLNKLEDSRYGRLPF
CCCCCCCCCCCCCCH
20.3029779826
32PhosphorylationNKLEDSRYGRLPFSI
CCCCCCCCCCCCHHH
15.5622673903
79AcetylationKSIEVPFKPARVILQ
CCCCCCCCCCEEEEE
31.5322902405
138PhosphorylationHFNRRADSLQKNQDL
EEECCCHHHHHCCCC
31.548262977
141AcetylationRRADSLQKNQDLEFE
CCCHHHHHCCCCHHH
62.9722902405
184PhosphorylationIHQVNLEYLARVVFD
EEECCHHHHEEEEEC
14.61-
266AcetylationDIVLTITKHLRQVGV
HHHHHHHHHHHHHCC
36.4722902405
396AcetylationFESCLGAKQGFKGFQ
HHHHHCCCCCCCCEE
49.5122902405
464AcetylationVEAGLNVKPYVKTSL
HHCCCCCCCEEEEEE
29.5622902405
472PhosphorylationPYVKTSLSPGSGVVT
CEEEEEECCCCCEEE
27.2930181290
475PhosphorylationKTSLSPGSGVVTYYL
EEEECCCCCEEEEEE
31.6230181290
479PhosphorylationSPGSGVVTYYLRESG
CCCCCEEEEEECCCC
12.2130181290
480PhosphorylationPGSGVVTYYLRESGV
CCCCEEEEEECCCCC
6.7330181290
481PhosphorylationGSGVVTYYLRESGVM
CCCEEEEEECCCCCH
7.0130181290
572SuccinylationTVRIDFEKEPLGVNA
EEEEEECCCCCCCCC
65.7026843850
602SuccinylationEIQEVERKYVIPGMF
HHHHHHHHHCCCHHH
30.2926843850
610AcetylationYVIPGMFKEVYQKIE
HCCCHHHHHHHHHHH
37.0622902405
615AcetylationMFKEVYQKIETVNKS
HHHHHHHHHHHHHHH
25.4822902405
621UbiquitinationQKIETVNKSWNALAA
HHHHHHHHHHHHCCC
53.14-
621AcetylationQKIETVNKSWNALAA
HHHHHHHHHHHHCCC
53.1422902405
630PhosphorylationWNALAAPSEKLYAWN
HHHCCCCCCCEECCC
42.5123984901
632AcetylationALAAPSEKLYAWNPK
HCCCCCCCEECCCCC
51.6522902405
639AcetylationKLYAWNPKSTYIKSP
CEECCCCCCCCCCCC
52.8222902405
708PhosphorylationLTPRDFNSYGSRRGN
CCHHHCCCCCCCCCC
30.7530181290
711PhosphorylationRDFNSYGSRRGNDAI
HHCCCCCCCCCCCCC
15.578262977
736AcetylationLLNKFLNKQAPQTVH
HHHHHHCCCCCCEEE
50.4022902405
776PhosphorylationLAGKEYGSGSSRDWA
ECCCCCCCCCCCHHH
34.3023984901
778PhosphorylationGKEYGSGSSRDWAAK
CCCCCCCCCCHHHHC
24.7323984901
779PhosphorylationKEYGSGSSRDWAAKG
CCCCCCCCCHHHHCC
37.4723984901
848AcetylationEHLKPRMKVQIKLDT
CCCCCCCEEEEEECC
32.0672627359
852AcetylationPRMKVQIKLDTGKTF
CCCEEEEEECCCCEE
24.1822902405

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
138SPhosphorylationKinasePRKCAP04409
GPS
138SPhosphorylationKinasePKC-FAMILY-GPS
138SPhosphorylationKinasePKC_GROUP-PhosphoELM
711SPhosphorylationKinasePKC-FAMILY-GPS
711SPhosphorylationKinasePKC_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 ACOC_RAT !!

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

Oops, there are no PPI records of ACOC_RAT !!

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

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Related Literatures of Post-Translational Modification

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