SYFM_HUMAN - dbPTM
SYFM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYFM_HUMAN
UniProt AC O95363
Protein Name Phenylalanine--tRNA ligase, mitochondrial
Gene Name FARS2
Organism Homo sapiens (Human).
Sequence Length 451
Subcellular Localization Mitochondrion matrix . Mitochondrion .
Protein Description Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins..
Protein Sequence MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLGVEGRF
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----MVGSALRRGAH
----CCCHHHHCCCE		16.8423663014
13PhosphorylationLRRGAHAYVYLVSKA
HHCCCEEEEEEEECC		4.6323663014
15PhosphorylationRGAHAYVYLVSKASH
CCCEEEEEEEECCHH		6.6825072903
18PhosphorylationHAYVYLVSKASHISR
EEEEEEEECCHHCCC		21.6523663014
21PhosphorylationVYLVSKASHISRGHQ
EEEEECCHHCCCCCC		25.7025072903
24PhosphorylationVSKASHISRGHQHQA
EECCHHCCCCCCCCC		27.1325072903
56UbiquitinationSVVELLGKSYPQDDH
CHHHHCCCCCCCCCC		46.9529967540
57PhosphorylationVVELLGKSYPQDDHS
HHHHCCCCCCCCCCC		40.00-
99SuccinylationRVKEHFYKQYVGRFG
HHHHHHHHHHHHCCC		33.9223954790
201PhosphorylationLEAVRLFSKHELFAG
HHHHHHHCCCCCEEC		37.3824719451
202AcetylationEAVRLFSKHELFAGI
HHHHHHCCCCCEECC		33.4919608861
221PhosphorylationSLQLFEQSSRSAHKQ
HHHHHHHHCCHHHHC		22.1129083192
222PhosphorylationLQLFEQSSRSAHKQE
HHHHHHHCCHHHHCC		29.9229083192
2442-HydroxyisobutyrylationKLVEFDLKQTLTRLM
HHHHCCHHHHHHHHH		42.98-
246PhosphorylationVEFDLKQTLTRLMAH
HHCCHHHHHHHHHHH		28.63-
351UbiquitinationCVSNINQKVKFQPLS
HHCCCCCCEEECCHH		42.7929967540
387PhosphorylationDFYDLVRTIGGDLVE
CHHHHHHHHCCCHHH		19.25-
3952-HydroxyisobutyrylationIGGDLVEKVDLIDKF
HCCCHHHHHEEEHHH		33.30-
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 SYFM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYFM_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 SYFM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRIM1_HUMANMID2physical
25416956
IKZF3_HUMANIKZF3physical
25416956
DP13A_HUMANAPPL1physical
25416956
ATL4_HUMANADAMTSL4physical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
TRI54_HUMANTRIM54physical
25416956
HMBX1_HUMANHMBOX1physical
25416956
CKLF5_HUMANCMTM5physical
25416956
K1C40_HUMANKRT40physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614946Combined oxidative phosphorylation deficiency 14 (COXPD14)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00120L-Phenylalanine
Regulatory Network of SYFM_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-202, AND MASS SPECTROMETRY.

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