ID Q6IBR2_HUMAN Unreviewed; 508 AA. AC Q6IBR2; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 02-SEP-2026, entry version 160. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|ARBA:ARBA00015409}; DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814}; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|ARBA:ARBA00030612}; GN Name=FARSLA {ECO:0000313|EMBL:CAG33021.1}; GN ORFNames=hCG_172485 {ECO:0000313|EMBL:EAW84329.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CAG33021.1}; RN [1] {ECO:0000313|EMBL:EAW84329.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:BAG52481.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., RA Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., RA Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., RA Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., RA Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., RA Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., RA Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., RA Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., RA Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., RA Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., RA Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., RA Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., RA Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., RA Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., RA Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] {ECO:0000313|EMBL:CAG33021.1} RP NUCLEOTIDE SEQUENCE. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:EAW84329.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Phe) + L-phenylalanine + ATP = L-phenylalanyl-tRNA(Phe) + CC AMP + diphosphate + H(+); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; CC Evidence={ECO:0000256|ARBA:ARBA00052760}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19414; CC Evidence={ECO:0000256|ARBA:ARBA00052760}; CC -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and CC FARSB. {ECO:0000256|ARBA:ARBA00066021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Phe-tRNA synthetase alpha subunit type 2 subfamily. CC {ECO:0000256|ARBA:ARBA00006703}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK092093; BAG52481.1; -; mRNA. DR EMBL; CR456740; CAG33021.1; -; mRNA. DR EMBL; CH471106; EAW84329.1; -; Genomic_DNA. DR RefSeq; NP_004452.1; NM_004461.3. DR AlphaFoldDB; Q6IBR2; -. DR SMR; Q6IBR2; -. DR IntAct; Q6IBR2; 2. DR Antibodypedia; 1072; 139 antibodies from 26 providers. DR DNASU; 2193; -. DR GeneID; 2193; -. DR KEGG; hsa:2193; -. DR ClinPGx; PA28005; -. DR CTD; 2193; -. DR DisGeNET; 2193; -. DR VEuPathDB; HostDB:ENSG00000179115; -. DR OMA; QIEGWVM; -. DR OrthoDB; 238316at2759; -. DR BioGRID-ORCS; 2193; 818 hits in 1167 CRISPR screens. DR ChiTaRS; FARSA; human. DR ExpressionAtlas; Q6IBR2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro. DR CDD; cd00496; PheRS_alpha_core; 1. DR FunFam; 1.10.10.2320:FF:000001; phenylalanine--tRNA ligase alpha subunit; 1. DR FunFam; 1.10.10.2330:FF:000001; phenylalanine--tRNA ligase alpha subunit; 1. DR FunFam; 3.30.1370.240:FF:000002; phenylalanine--tRNA ligase alpha subunit; 1. DR FunFam; 3.30.930.10:FF:000036; phenylalanine--tRNA ligase alpha subunit; 1. DR Gene3D; 1.10.10.2320; -; 1. DR Gene3D; 1.10.10.2330; -; 1. DR Gene3D; 3.30.1370.240; -; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR InterPro; IPR040724; PheRS_DBD1. DR InterPro; IPR040586; PheRS_DBD2. DR InterPro; IPR040725; PheRS_DBD3. DR InterPro; IPR036390; WH_DNA-bd_sf. DR NCBIfam; TIGR00468; pheS; 1. DR NCBIfam; NF003210; PRK04172.1; 1. DR PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1. DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1. DR Pfam; PF18552; PheRS_DBD1; 1. DR Pfam; PF18554; PheRS_DBD2; 1. DR Pfam; PF18553; PheRS_DBD3; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 2: Evidence at transcript level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000313|EMBL:BAG52481.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}. FT DOMAIN 229..502 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" SQ SEQUENCE 508 AA; 57564 MW; 99BC12E1F3C5FCFD CRC64; MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV IEAELRSTKH WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG KVGFSKAMSN KWIRVDKSAA DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK LGEKERSELR KRKLLAEVTL KTYWVSKGSA FSTSISKQET ELSPEMISSG SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY FSIDRVFRNE TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH KVNLQMVYDS PLCRLDAEPR PPPTQEAA //