dbPTM

FAKD5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FAKD5_HUMAN
UniProt AC	Q7L8L6
Protein Name	FAST kinase domain-containing protein 5, mitochondrial
Gene Name	FASTKD5
Organism	Homo sapiens (Human).
Sequence Length	764
Subcellular Localization	Mitochondrion matrix, mitochondrion nucleoid . Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids.
Protein Description	Plays an important role in the processing of non-canonical mitochondrial mRNA precursors. [PubMed: 25683715]
Protein Sequence	MAATLKSLKLVRYRAFCSPSAFGAVRSVSYWNVSSTQHGGQDPPEHISLCHSAKKVKNICSTFSSRRILTTSSAHPGLEFSKTSSSKASTLQLGSPRATGVDEEDVEVFDSFENMRVFLQLRPEYRVHSYNASETSQLLSVSEGELILHKVRVNQNNLQAQVIVDYLCKLSSLPAEQHPVLLGSTSFALLCQLSVKKIQLFDTQDLINVLKAFVILGIPHSHSMLDVYETKCCHQVWEMNMDQLLLVADLWRYLGRKVPRFLNIFSSYLNLHWKDLSLSQLVHLIYVIGENRQVSQDLMQKLESLILKYIDLINLEEVGTICLGFFKSSTNLSEFVMRKIGDLACANIQHLSSRSLVNIVKMFRFTHVDHINFMKQIGEIAPQRIPSLGVQGVMHLTLYCSALRFLNEGVMNAVAASLPPRVAHCRSKDVAKILWSFGTLNYKPPNAEEFYSSLISEIHRKMPEFNQYPEHLPTCLLGLAFLEYFPVELIDFALSPGFVRLAQERTKFDLLKELYTLDGTVGIECPDYRGNRLSTHLQQEGSELLWYLAEKDMNSKPEFLETVFLLETMLGGPQYVKHHMILPHTRSSDLEVQLDVNLKPLPFNREATPAENVAKLRLEHVGVSLTDDLMNKLLKGKARGHFQGKTESEPGQQPMELENKAAVPLGGFLCNVADKSGAMEMAGLCPAACMQTPRMKLAVQFTNRNQYCYGSRDLLGLHNMKRRQLARLGYRVVELSYWEWLPLLKRTRLEKLAFLHEKVFTSAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAATLKSLKLV ----CCCHHHHHHHE	25.77	24719451
7	Phosphorylation	-MAATLKSLKLVRYR -CCCHHHHHHHEEEE	33.57	25159151
61	Phosphorylation	KKVKNICSTFSSRRI HHHHHHHHHCCCCEE	28.79	29083192
62	Phosphorylation	KVKNICSTFSSRRIL HHHHHHHHCCCCEEE	24.11	29083192
64	Phosphorylation	KNICSTFSSRRILTT HHHHHHCCCCEEEEC	24.03	29083192
65	Phosphorylation	NICSTFSSRRILTTS HHHHHCCCCEEEECC	22.76	29083192
73	Phosphorylation	RRILTTSSAHPGLEF CEEEECCCCCCCCCC	28.62	-
81	Phosphorylation	AHPGLEFSKTSSSKA CCCCCCCCCCCCCCC	26.16	-
82	Ubiquitination	HPGLEFSKTSSSKAS CCCCCCCCCCCCCCC	58.72	22817900
83	Phosphorylation	PGLEFSKTSSSKAST CCCCCCCCCCCCCCE	32.42	-
87	Ubiquitination	FSKTSSSKASTLQLG CCCCCCCCCCEEECC	48.59	21906983
89	Phosphorylation	KTSSSKASTLQLGSP CCCCCCCCEEECCCC	33.13	23186163
90	Phosphorylation	TSSSKASTLQLGSPR CCCCCCCEEECCCCC	24.31	29396449
95	Phosphorylation	ASTLQLGSPRATGVD CCEEECCCCCCCCCC	21.58	30266825
99	Phosphorylation	QLGSPRATGVDEEDV ECCCCCCCCCCHHHC	38.73	18452278
166	Phosphorylation	QAQVIVDYLCKLSSL CHHHHHHHHHHHHCC	11.78	-
171	Phosphorylation	VDYLCKLSSLPAEQH HHHHHHHHCCCHHHC	18.47	28387310
361	Succinylation	RSLVNIVKMFRFTHV CHHHHHHHHHHCCCC	28.64	23954790
361	Ubiquitination	RSLVNIVKMFRFTHV CHHHHHHHHHHCCCC	28.64	-
417	Phosphorylation	VMNAVAASLPPRVAH HHHHHHHHCCCCCCC	31.50	24719451
436	Phosphorylation	DVAKILWSFGTLNYK HHHHHHHHHCCCCCC	15.45	29449344
439	Phosphorylation	KILWSFGTLNYKPPN HHHHHHCCCCCCCCC	15.15	29449344
442	Phosphorylation	WSFGTLNYKPPNAEE HHHCCCCCCCCCHHH	28.16	29449344
451	Phosphorylation	PPNAEEFYSSLISEI CCCHHHHHHHHHHHH	10.71	-
507	Acetylation	RLAQERTKFDLLKEL HHHHHHHHHHHHHHH	43.00	19608861
507	Malonylation	RLAQERTKFDLLKEL HHHHHHHHHHHHHHH	43.00	26320211
507	Succinylation	RLAQERTKFDLLKEL HHHHHHHHHHHHHHH	43.00	23954790
608	Phosphorylation	LPFNREATPAENVAK CCCCCCCCCHHHHHH	20.48	-
615	Ubiquitination	TPAENVAKLRLEHVG CCHHHHHHHHHHHHC	29.83	24816145
646	Phosphorylation	RGHFQGKTESEPGQQ CCCCCCCCCCCCCCC	52.12	27732954
648	Phosphorylation	HFQGKTESEPGQQPM CCCCCCCCCCCCCCC	55.08	27732954
670	S-nitrosylation	VPLGGFLCNVADKSG CCCCCCHHHCCCCCC	3.43	19483679
670	S-nitrosocysteine	VPLGGFLCNVADKSG CCCCCCHHHCCCCCC	3.43	-
676	Phosphorylation	LCNVADKSGAMEMAG HHHCCCCCCCHHHCC	32.12	-
692	Phosphorylation	CPAACMQTPRMKLAV CHHHHHCCCCCEEEE	5.98	27732954
704	Methylation	LAVQFTNRNQYCYGS EEEEECCCCCCEECC	28.68	-
721	2-Hydroxyisobutyrylation	LLGLHNMKRRQLARL HCCCCCCCHHHHHHH	50.15	-
730	Phosphorylation	RQLARLGYRVVELSY HHHHHHCCEEEEHHH	12.58	-
761	Phosphorylation	FLHEKVFTSAL---- HHHHHHHHHCC----	18.97	-
762	Phosphorylation	LHEKVFTSAL----- HHHHHHHHCC-----	18.99	-

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 FAKD5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of FAKD5_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 FAKD5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of FAKD5_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 FAKD5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-507, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.	16964243 [Abstract]