CPLM-001584

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-001584

UniProt Accession

SYFM_HUMAN; O95363; B2R664; Q53F66; Q5TCS3; Q6FG29; Q9NPY7; Q9P062

Genbank Protein ID

AF097441; AK312454; CR542279; AK223423; AL133473; AL022097; AL590868; AL121978; AL392184; AL022097; AL121978; AL392184; AL590868; AL133473; AL392184; AL121978; AL590868; AL133473; AL022097; AL121978; AL133473; AL022097; AL392184; AL590868; AL590868; AL392184; AL133473; AL121978; AL022097; BC020239; BC021112; AF161438

Genbank Nucleotide ID

AAC83802.1; BAG35361.1; CAG47075.1; BAD97143.1; CAI19901.1; CAI19901.1; CAI19901.1; CAI19901.1; CAI19901.1; CAI19950.1; CAI19950.1; CAI19950.1; CAI19950.1; CAI19950.1; CAI20375.1; CAI20375.1; CAI20375.1; CAI20375.1; CAI20375.1; CAI21657.1; CAI21657.1; CAI21657.1; CAI21657.1; CAI21657.1; CAI39442.1; CAI39442.1; CAI39442.1; CAI39442.1; CAI39442.1; AAH20239.1; AAH21112.1; AAF28998.1

Protein Name

Phenylalanine--tRNA ligase, mitochondrial

Protein Synonyms/Alias

Phenylalanyl-tRNA synthetase; PheRS

Gene Name

FARS2

Gene Synonyms/Alias

FARS1; HSPC320

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
202	EAVRLFSKHELFAGI	acetylation	[1]

Reference

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]

Functional 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.

Sequence Annotation

DOMAIN 358 450 FDX-ACB.
REGION 157 160 Substrate binding.
REGION 186 188 Substrate binding.
REGION 193 195 Substrate binding.
BINDING 179 179 Substrate.
BINDING 287 287 Substrate; via carbonyl oxygen.
BINDING 312 312 Substrate; via carbonyl oxygen.
MOD_RES 202 202 N6-acetyllysine.

Keyword

3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Disease mutation; Ligase; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

451 AA

Protein Sequence

MVGSALRRGA HAYVYLVSKA SHISRGHQHQ AWGSRPPAAE CATQRAPGSV VELLGKSYPQ 60
DDHSNLTRKV LTRVGRNLHN QQHHPLWLIK ERVKEHFYKQ YVGRFGTPLF SVYDNLSPVV 120
TTWQNFDSLL IPADHPSRKK GDNYYLNRTH MLRAHTSAHQ WDLLHAGLDA FLVVGDVYRR 180
DQIDSQHYPI FHQLEAVRLF SKHELFAGIK DGESLQLFEQ SSRSAHKQET HTMEAVKLVE 240
FDLKQTLTRL MAHLFGDELE IRWVDCYFPF THPSFEMEIN FHGEWLEVLG CGVMEQQLVN 300
SAGAQDRIGW AFGLGLERLA MILYDIPDIR LFWCEDERFL KQFCVSNINQ KVKFQPLSKY 360
PAVINDISFW LPSENYAEND FYDLVRTIGG DLVEKVDLID KFVHPKTHKT SHCYRITYRH 420
MERTLSQREV RHIHQALQEA AVQLLGVEGR F 451

Gene Ontology

GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO:0004826; F:phenylalanine-tRNA ligase activity; IDA:UniProtKB.
GO:0000049; F:tRNA binding; IDA:UniProtKB.
GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:UniProtKB.
GO:0008033; P:tRNA processing; IDA:UniProtKB.

Interpro

IPR006195; aa-tRNA-synth_II.
IPR004530; Phe-tRNA-synth_IIc_mito.
IPR002319; Phenylalanyl-tRNA_Synthase.
IPR005121; PheS_beta_Fdx_antiC-bd.

Pfam

PF03147; FDX-ACB
PF01409; tRNA-synt_2d

SMART

SM00896; FDX-ACB

PROSITE

PS50862; AA_TRNA_LIGASE_II
PS51447; FDX_ACB

PRINTS