FAKD1_HUMAN - dbPTM
FAKD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAKD1_HUMAN
UniProt AC Q53R41
Protein Name FAST kinase domain-containing protein 1, mitochondrial
Gene Name FASTKD1
Organism Homo sapiens (Human).
Sequence Length 847
Subcellular Localization Mitochondrion . Preferentially localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly (PubMed:28335001).
Protein Description Regulates the stability of mitochondrial MT-ND3 mRNA. [PubMed: 28335001]
Protein Sequence MKKTPVFLESLVTNMLRLRAICPFSWRVFQFRPISCEPLIIQMNKCTDEEQMFGFIERNKAILSEKQVGCAFDMLWKLQKQKTSLLKNAEYVRDHPQFLTLHNLATNKFKLMNDDTLVNVLYVTQQFAGEAHDPLVEALVTEAWRRLERFDIKLLSEFSSCLADQHLYFSPLMGKIADIVHRNLETTQDLSSLSVLMVNISSLISRHFQQQLVNKTELLFDTIDSSEVNVAKSIAKFLRNVRYRYQPLLERCNNVFLSNVDHLDLDSISKILSVYKFLQFNSFEFIIMAKKKLTEMIPLCNHPASFVKLFVALGPIAGPEEKKQLKSTMLLMSEDLTGEQALAVLGAMGDMESRNSCLIKRVTSVLHKHLDGYKPLELLKITQELTFLHFQRKEFFAKLRELLLSYLKNSFIPTEVSVLVRAISLLPSPHLDEVGISRIEAVLPQCDLNNLSSFATSVLRWIQHDHMYLDNMTAKQLKLLQKLDHYGRQRLQHSNSLDLLRKELKSLKGNTFPESLLEEMIATLQHFMDDINYINVGEIASFISSTDYLSTLLLDRIASVAVQQIEKIHPFTIPAIIRPFSVLNYDPPQRDEFLGTCVQHLNSYLGILDPFILVFLGFSLATLEYFPEDLLKAIFNIKFLARLDSQLEILSPSRSARVQFHLMELNRSVCLECPEFQIPWFHDRFCQQYNKGIGGMDGTQQQIFKMLAEVLGGINCVKASVLTPYYHKVDFECILDKRKKPLPYGSHNIALGQLPEMPWESNIEIVGSRLPPGAERIALEFLDSKALCRNIPHMKGKSAMKKRHLEILGYRVIQISQFEWNSMALSTKDARMDYLRECIFGEVKSCL
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
60UbiquitinationFGFIERNKAILSEKQ
HHHHHHHHHHHCHHH		42.92-
64PhosphorylationERNKAILSEKQVGCA
HHHHHHHCHHHHHHH		36.3124719451
83PhosphorylationWKLQKQKTSLLKNAE
HHHHHHHCHHHHCCH		23.32-
84PhosphorylationKLQKQKTSLLKNAEY
HHHHHHCHHHHCCHH		38.4524719451
87UbiquitinationKQKTSLLKNAEYVRD
HHHCHHHHCCHHHHC		60.45-
116PhosphorylationFKLMNDDTLVNVLYV
EECCCCCCHHHHHHH		35.1527174698
122PhosphorylationDTLVNVLYVTQQFAG
CCHHHHHHHHHHHCC		9.3627174698
124PhosphorylationLVNVLYVTQQFAGEA
HHHHHHHHHHHCCCC		11.7727174698
159PhosphorylationIKLLSEFSSCLADQH
HHHHHHHHHHHCCCH		18.9824114839
168PhosphorylationCLADQHLYFSPLMGK
HHCCCHHHCCHHHHH		10.41-
170PhosphorylationADQHLYFSPLMGKIA
CCCHHHCCHHHHHHH		11.99-
194PhosphorylationTQDLSSLSVLMVNIS
CCCHHHHHHHHHCHH		18.36-
202PhosphorylationVLMVNISSLISRHFQ
HHHHCHHHHHHHHHH		26.4024719451
205PhosphorylationVNISSLISRHFQQQL
HCHHHHHHHHHHHHH		25.6224719451
236MalonylationNVAKSIAKFLRNVRY
HHHHHHHHHHHHHHH		43.1726320211
236AcetylationNVAKSIAKFLRNVRY
HHHHHHHHHHHHHHH		43.1725953088
305PhosphorylationPLCNHPASFVKLFVA
HHCCCCHHHHHHHHH		34.72-
322UbiquitinationPIAGPEEKKQLKSTM
CCCCHHHHHHHHHHH		44.13-
323UbiquitinationIAGPEEKKQLKSTML
CCCHHHHHHHHHHHH		65.23-
327PhosphorylationEEKKQLKSTMLLMSE
HHHHHHHHHHHHHCC		27.8622210691
328PhosphorylationEKKQLKSTMLLMSED
HHHHHHHHHHHHCCC		15.3922210691
333PhosphorylationKSTMLLMSEDLTGEQ
HHHHHHHCCCCCHHH		28.1124719451
337PhosphorylationLLMSEDLTGEQALAV
HHHCCCCCHHHHHHH		51.5024719451
353PhosphorylationGAMGDMESRNSCLIK
HHHCCHHHHHHHHHH		30.0822210691
360SuccinylationSRNSCLIKRVTSVLH
HHHHHHHHHHHHHHH		28.0627452117
360AcetylationSRNSCLIKRVTSVLH
HHHHHHHHHHHHHHH		28.0619608861
374UbiquitinationHKHLDGYKPLELLKI
HHHHCCCCCHHHHHH		48.97-
405PhosphorylationKLRELLLSYLKNSFI
HHHHHHHHHHHHCCC		28.5224719451
406PhosphorylationLRELLLSYLKNSFIP
HHHHHHHHHHHCCCC		22.9724719451
478UbiquitinationNMTAKQLKLLQKLDH
CCCHHHHHHHHHCCH		44.66-
478AcetylationNMTAKQLKLLQKLDH
CCCHHHHHHHHHCCH		44.6625953088
482UbiquitinationKQLKLLQKLDHYGRQ
HHHHHHHHCCHHHHH		56.71-
482AcetylationKQLKLLQKLDHYGRQ
HHHHHHHHCCHHHHH		56.7123236377
482SuccinylationKQLKLLQKLDHYGRQ
HHHHHHHHCCHHHHH		56.7123954790
486PhosphorylationLLQKLDHYGRQRLQH
HHHHCCHHHHHHHHC		17.42-
496PhosphorylationQRLQHSNSLDLLRKE
HHHHCCCHHHHHHHH		26.6923186163
546PhosphorylationIASFISSTDYLSTLL
HHHHHHCHHHHHHHH		23.13-
551PhosphorylationSSTDYLSTLLLDRIA
HCHHHHHHHHHHHHH		20.87-
649 (in isoform 2)Phosphorylation-6.6627050516
691UbiquitinationRFCQQYNKGIGGMDG
HHHHHHHCCCCCCCH		47.15-
726PhosphorylationASVLTPYYHKVDFEC
HHHCCCCCCCCCHHH		9.07-
728UbiquitinationVLTPYYHKVDFECIL
HCCCCCCCCCHHHHH		27.64-
737UbiquitinationDFECILDKRKKPLPY
CHHHHHCCCCCCCCC		63.77-
785UbiquitinationALEFLDSKALCRNIP
HHHHHCHHHHHHCCC		45.07-
785AcetylationALEFLDSKALCRNIP
HHHHHCHHHHHHCCC		45.0725953088
795UbiquitinationCRNIPHMKGKSAMKK
HHCCCHHCCCHHHHH		61.22-
797UbiquitinationNIPHMKGKSAMKKRH
CCCHHCCCHHHHHHH		29.53-
801UbiquitinationMKGKSAMKKRHLEIL
HCCCHHHHHHHHHHH		46.50-
810PhosphorylationRHLEILGYRVIQISQ
HHHHHHCEEEEEEEE		9.77-
844UbiquitinationECIFGEVKSCL----
HHHHHHHHHCC----		31.02-
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 FAKD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAKD1_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 FAKD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FAKD1_HUMAN !!
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 FAKD1_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-360, AND MASS SPECTROMETRY.

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