PFKAM_RAT - dbPTM
PFKAM_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PFKAM_RAT
UniProt AC P47858
Protein Name ATP-dependent 6-phosphofructokinase, muscle type {ECO:0000255|HAMAP-Rule:MF_03184}
Gene Name Pfkm
Organism Rattus norvegicus (Rat).
Sequence Length 780
Subcellular Localization Cytoplasm .
Protein Description Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis..
Protein Sequence MTHEEHHEAKTLGIGKAIAVLTSGGDAQGMNATVRAVVRVGIFTGLRVFFVHEGYQGLVDGGEHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLNDLQKDGKITAEERTKSSYLNIVFLVGSIDNDFCGTDMTIGTDSALHRIVEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNTAVRLPLMECVQVTKDVTKAMDEKRFDEAIKLRGRSFMNNWEVYKLLAHVRPPVSKGGLHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKNLEQISANITKYNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSIGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQVNVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGNPTPFDRNFATKMGAKATNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHISRKRSGEAAV
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
2Acetylation------MTHEEHHEA
------CCHHHHHHH
-
10AcetylationHEEHHEAKTLGIGKA
HHHHHHHHHCCCCCE
22902405
107AcetylationRAAHNLVKRGITNLC
HHHHHHHHCCCCEEE
22902405
133PhosphorylationDTFRSEWSDLLNDLQ
HHHHHHHHHHHHHHH
22673903
141AcetylationDLLNDLQKDGKITAE
HHHHHHHHCCCCCHH
22902405
285AcetylationDIKNLVVKRLGYDTR
HHHHHHHHHCCCCCE
22902405
304PhosphorylationGHVQRGGTPSAFDRI
EEHHHCCCHHHHHHH
25403869
306PhosphorylationVQRGGTPSAFDRILG
HHHCCCHHHHHHHHH
22673903
360AcetylationQVTKDVTKAMDEKRF
HHCHHHHHHHHHHHH
22902405
372AcetylationKRFDEAIKLRGRSFM
HHHHHHHHHHCCHHH
22902405
377PhosphorylationAIKLRGRSFMNNWEV
HHHHHCCHHHCCHHH
22673903
386AcetylationMNNWEVYKLLAHVRP
HCCHHHHHHHHCCCC
22902405
530O-linked_GlycosylationVVIPATVSNNVPGSD
EEEEEECCCCCCCCC
-
557OtherCTTCDRIKQSAAGTK
HHHHHHHHHCCCCCC
-
615AcetylationNVEHLVQKMKTTVKR
CHHHHHHHHHHHHHH
22902405
656AcetylationKGIFDSRKNVLGHMQ
CCCCCCCCHHHHCHH
22902405
678AcetylationFDRNFATKMGAKATN
CCHHHHHHHCCHHHH
22902405
692AcetylationNWMSGKIKESYRNGR
HCCCCCHHHHHHCCC
22902405
727AcetylationFQPVTELKDQTDFEH
EEEECCCCCCCCCCC
22902405
738AcetylationDFEHRIPKEQWWLKL
CCCCCCCHHHHHHHH
22902405
744AcetylationPKEQWWLKLRPILKI
CHHHHHHHHHHHHHH
22902405
754AcetylationPILKILAKYEIDLDT
HHHHHHHHCCCCCCC
22902405
775PhosphorylationEHISRKRSGEAAV--
HHHHHCCCCCCCC--
25403869

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 PFKAM_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PFKAM_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 PFKAM_RAT !!

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

Oops, there are no PPI records of PFKAM_RAT !!

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

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Related Literatures of Post-Translational Modification

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