Full text data of AARSD1
AARSD1
[Confidence: low (only semi-automatic identification from reviews)]
Alanyl-tRNA editing protein Aarsd1 (Alanyl-tRNA synthetase domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Alanyl-tRNA editing protein Aarsd1 (Alanyl-tRNA synthetase domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BTE6
ID AASD1_HUMAN Reviewed; 412 AA.
AC Q9BTE6; B4DI73;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Alanyl-tRNA editing protein Aarsd1;
DE AltName: Full=Alanyl-tRNA synthetase domain-containing protein 1;
GN Name=AARSD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC incorrectly charged tRNA(Ala) (By similarity).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BTE6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTE6-2; Sequence=VSP_023014;
CC Note=Based on a readthrough transcript which may produce a
CC PTGES3L-AARSD1 fusion protein. No experimental confirmation
CC available;
CC Name=3;
CC IsoId=Q9BTE6-3; Sequence=VSP_043142;
CC Note=Based on a readthrough transcript which may produce a
CC PTGES3L-AARSD1 fusion protein. No experimental confirmation
CC available;
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Alax-L subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK295447; BAG58385.1; -; mRNA.
DR EMBL; CR608238; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC055866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60903.1; -; Genomic_DNA.
DR EMBL; BC004172; AAH04172.1; -; mRNA.
DR EMBL; BC019324; AAH19324.1; -; mRNA.
DR RefSeq; NP_001129514.2; NM_001136042.2.
DR RefSeq; NP_001248363.1; NM_001261434.1.
DR RefSeq; NP_079543.1; NM_025267.3.
DR UniGene; Hs.317403; -.
DR ProteinModelPortal; Q9BTE6; -.
DR SMR; Q9BTE6; 8-247.
DR IntAct; Q9BTE6; 4.
DR STRING; 9606.ENSP00000386621; -.
DR DMDM; 125987702; -.
DR REPRODUCTION-2DPAGE; IPI00827636; -.
DR PaxDb; Q9BTE6; -.
DR PRIDE; Q9BTE6; -.
DR DNASU; 80755; -.
DR Ensembl; ENST00000360221; ENSP00000353355; ENSG00000108825.
DR Ensembl; ENST00000409399; ENSP00000386621; ENSG00000108825.
DR Ensembl; ENST00000421990; ENSP00000409924; ENSG00000108825.
DR Ensembl; ENST00000427569; ENSP00000400870; ENSG00000266967.
DR GeneID; 100885850; -.
DR GeneID; 80755; -.
DR KEGG; hsa:100885850; -.
DR KEGG; hsa:80755; -.
DR UCSC; uc010cyu.2; human.
DR CTD; 100885850; -.
DR CTD; 80755; -.
DR GeneCards; GC17M041102; -.
DR GeneCards; GC17M041103; -.
DR HGNC; HGNC:28417; AARSD1.
DR HGNC; HGNC:43946; PTGES3L-AARSD1.
DR HPA; HPA021408; -.
DR HPA; HPA022869; -.
DR HPA; HPA023714; -.
DR MIM; 613212; gene.
DR neXtProt; NX_Q9BTE6; -.
DR PharmGKB; PA142670464; -.
DR eggNOG; COG2872; -.
DR HOGENOM; HOG000230967; -.
DR HOVERGEN; HBG080017; -.
DR InParanoid; Q9BTE6; -.
DR KO; K07050; -.
DR OMA; GDNEFMN; -.
DR OrthoDB; EOG71RXJT; -.
DR NextBio; 71103; -.
DR PRO; PR:Q9BTE6; -.
DR ArrayExpress; Q9BTE6; -.
DR Bgee; Q9BTE6; -.
DR CleanEx; HS_AARSD1; -.
DR Genevestigator; Q9BTE6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Metal-binding;
KW Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1 412 Alanyl-tRNA editing protein Aarsd1.
FT /FTId=PRO_0000277465.
FT METAL 109 109 Zinc (Potential).
FT METAL 113 113 Zinc (Potential).
FT METAL 209 209 Zinc (Potential).
FT METAL 213 213 Zinc (Potential).
FT VAR_SEQ 1 13 MAFWCQRDSYARE -> MEFCVEDSTDVHVLIEDHRIVFSC
FT KNADGVELYNEIEFYAKVNSKDSQDKRSSRSITCFVRKWKE
FT KVAWPRLTKEDIKPVWLSVDFDNWRDWEGDEEMELAHVEHY
FT AELLKKVSTKRPPPAMDDLD (in isoform 2).
FT /FTId=VSP_023014.
FT VAR_SEQ 1 13 MAFWCQRDSYARE -> MFSLPLNCSPDHIRRGSCWGRPQD
FT LKIAAPAWNSKCHPGAGAAMARQHARTLWYDRPRYVFMEFC
FT VEDSTDVHVLIEDHRIVFSCKNADGVELYNEIEFYAKVNSK
FT DSQDKRSSRSITCFVRKWKEKVAWPRLTKEDIKPVWLSVDF
FT DNWRDWEGDEEMELAHVEHYAELLKKVSTKRPPPAMDDLD
FT (in isoform 3).
FT /FTId=VSP_043142.
SQ SEQUENCE 412 AA; 45480 MW; 2E14B6274C6EF897 CRC64;
MAFWCQRDSY AREFTTTVVS CCPAELQTEG SNGKKEVLSG FQVVLEDTVL FPEGGGQPDD
RGTINDISVL RVTRRGEQAD HFTQTPLDPG SQVLVRVDWE RRFDHMQQHS GQHLITAVAD
HLFKLKTTSW ELGRFRSAIE LDTPSMTAEQ VAAIEQSVNE KIRDRLPVNV RELSLDDPEV
EQVSGRGLPD DHAGPIRVVN IEGVDSNMCC GTHVSNLSDL QVIKILGTEK GKKNRTNLIF
LSGNRVLKWM ERSHGTEKAL TALLKCGAED HVEAVKKLQN STKILQKNNL NLLRDLAVHI
AHSLRNSPDW GGVVILHRKE GDSEFMNIIA NEIGSEETLL FLTVGDEKGG GLFLLAGPPA
SVETLGPRVA EVLEGKGAGK KGRFQGKATK MSRRMEAQAL LQDYISTQSA KE
//
ID AASD1_HUMAN Reviewed; 412 AA.
AC Q9BTE6; B4DI73;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-FEB-2007, sequence version 2.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Alanyl-tRNA editing protein Aarsd1;
DE AltName: Full=Alanyl-tRNA synthetase domain-containing protein 1;
GN Name=AARSD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hippocampus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC incorrectly charged tRNA(Ala) (By similarity).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BTE6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTE6-2; Sequence=VSP_023014;
CC Note=Based on a readthrough transcript which may produce a
CC PTGES3L-AARSD1 fusion protein. No experimental confirmation
CC available;
CC Name=3;
CC IsoId=Q9BTE6-3; Sequence=VSP_043142;
CC Note=Based on a readthrough transcript which may produce a
CC PTGES3L-AARSD1 fusion protein. No experimental confirmation
CC available;
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Alax-L subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK295447; BAG58385.1; -; mRNA.
DR EMBL; CR608238; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC055866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60903.1; -; Genomic_DNA.
DR EMBL; BC004172; AAH04172.1; -; mRNA.
DR EMBL; BC019324; AAH19324.1; -; mRNA.
DR RefSeq; NP_001129514.2; NM_001136042.2.
DR RefSeq; NP_001248363.1; NM_001261434.1.
DR RefSeq; NP_079543.1; NM_025267.3.
DR UniGene; Hs.317403; -.
DR ProteinModelPortal; Q9BTE6; -.
DR SMR; Q9BTE6; 8-247.
DR IntAct; Q9BTE6; 4.
DR STRING; 9606.ENSP00000386621; -.
DR DMDM; 125987702; -.
DR REPRODUCTION-2DPAGE; IPI00827636; -.
DR PaxDb; Q9BTE6; -.
DR PRIDE; Q9BTE6; -.
DR DNASU; 80755; -.
DR Ensembl; ENST00000360221; ENSP00000353355; ENSG00000108825.
DR Ensembl; ENST00000409399; ENSP00000386621; ENSG00000108825.
DR Ensembl; ENST00000421990; ENSP00000409924; ENSG00000108825.
DR Ensembl; ENST00000427569; ENSP00000400870; ENSG00000266967.
DR GeneID; 100885850; -.
DR GeneID; 80755; -.
DR KEGG; hsa:100885850; -.
DR KEGG; hsa:80755; -.
DR UCSC; uc010cyu.2; human.
DR CTD; 100885850; -.
DR CTD; 80755; -.
DR GeneCards; GC17M041102; -.
DR GeneCards; GC17M041103; -.
DR HGNC; HGNC:28417; AARSD1.
DR HGNC; HGNC:43946; PTGES3L-AARSD1.
DR HPA; HPA021408; -.
DR HPA; HPA022869; -.
DR HPA; HPA023714; -.
DR MIM; 613212; gene.
DR neXtProt; NX_Q9BTE6; -.
DR PharmGKB; PA142670464; -.
DR eggNOG; COG2872; -.
DR HOGENOM; HOG000230967; -.
DR HOVERGEN; HBG080017; -.
DR InParanoid; Q9BTE6; -.
DR KO; K07050; -.
DR OMA; GDNEFMN; -.
DR OrthoDB; EOG71RXJT; -.
DR NextBio; 71103; -.
DR PRO; PR:Q9BTE6; -.
DR ArrayExpress; Q9BTE6; -.
DR Bgee; Q9BTE6; -.
DR CleanEx; HS_AARSD1; -.
DR Genevestigator; Q9BTE6; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Metal-binding;
KW Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1 412 Alanyl-tRNA editing protein Aarsd1.
FT /FTId=PRO_0000277465.
FT METAL 109 109 Zinc (Potential).
FT METAL 113 113 Zinc (Potential).
FT METAL 209 209 Zinc (Potential).
FT METAL 213 213 Zinc (Potential).
FT VAR_SEQ 1 13 MAFWCQRDSYARE -> MEFCVEDSTDVHVLIEDHRIVFSC
FT KNADGVELYNEIEFYAKVNSKDSQDKRSSRSITCFVRKWKE
FT KVAWPRLTKEDIKPVWLSVDFDNWRDWEGDEEMELAHVEHY
FT AELLKKVSTKRPPPAMDDLD (in isoform 2).
FT /FTId=VSP_023014.
FT VAR_SEQ 1 13 MAFWCQRDSYARE -> MFSLPLNCSPDHIRRGSCWGRPQD
FT LKIAAPAWNSKCHPGAGAAMARQHARTLWYDRPRYVFMEFC
FT VEDSTDVHVLIEDHRIVFSCKNADGVELYNEIEFYAKVNSK
FT DSQDKRSSRSITCFVRKWKEKVAWPRLTKEDIKPVWLSVDF
FT DNWRDWEGDEEMELAHVEHYAELLKKVSTKRPPPAMDDLD
FT (in isoform 3).
FT /FTId=VSP_043142.
SQ SEQUENCE 412 AA; 45480 MW; 2E14B6274C6EF897 CRC64;
MAFWCQRDSY AREFTTTVVS CCPAELQTEG SNGKKEVLSG FQVVLEDTVL FPEGGGQPDD
RGTINDISVL RVTRRGEQAD HFTQTPLDPG SQVLVRVDWE RRFDHMQQHS GQHLITAVAD
HLFKLKTTSW ELGRFRSAIE LDTPSMTAEQ VAAIEQSVNE KIRDRLPVNV RELSLDDPEV
EQVSGRGLPD DHAGPIRVVN IEGVDSNMCC GTHVSNLSDL QVIKILGTEK GKKNRTNLIF
LSGNRVLKWM ERSHGTEKAL TALLKCGAED HVEAVKKLQN STKILQKNNL NLLRDLAVHI
AHSLRNSPDW GGVVILHRKE GDSEFMNIIA NEIGSEETLL FLTVGDEKGG GLFLLAGPPA
SVETLGPRVA EVLEGKGAGK KGRFQGKATK MSRRMEAQAL LQDYISTQSA KE
//
MIM
613212
*RECORD*
*FIELD* NO
613212
*FIELD* TI
*613212 ALANYL-tRNA SYNTHETASE DOMAIN-CONTAINING 1; AARSD1
*FIELD* TX
GENE FUNCTION
read more
Mistranslation arising from confusion of serine for alanine by
alanyl-tRNA synthetases (AlaRSs; see 601065 and 612035) has profound
functional consequences. Throughout evolution, 2 editing checkpoints
prevent disease-causing mistranslation from confusing glycine or serine
for alanine at the active site of AlaRS. In both bacteria and mice,
serine poses a bigger challenge than glycine. One checkpoint is the
AlaRS editing center. The other is from widely distributed AlaXps
(Aarsd1), free-standing, genome-encoded editing proteins that clear
Ser-tRNA(Ala) (Beebe et al., 2008). The paradox of misincorporating both
a smaller (glycine) and a larger (serine) amino acid suggests a deep
conflict for nature-designed AlaRS. Guo et al. (2009) showed the
chemical basis for this conflict. Nine crystal structures, together with
kinetic and mutational analysis, provided snapshots of adenylate
formation for each amino acid. An inherent dilemma is posed by
constraints of a structural design that pins down the alpha-amino group
of the bound amino acid by using an acidic residue. This design, dating
back more than 3 billion years, creates a serendipitous interaction with
the serine hydroxide that is difficult to avoid. Apparently because no
better architecture for the recognition of alanine could be found, the
serine misactivation problem was solved through free-standing AlaXps,
which appeared contemporaneously with early AlaRSs.
MAPPING
Hartz (2010) mapped the AARSD1 gene to chromosome 17q21.31 based on an
alignment of the AARSD1 sequence (GenBank GENBANK BC019324) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Beebe, K.; Mock, M.; Merriman, E.; Schimmel, P.: Distinct domains
of tRNA synthetase recognize the same base pair. Nature 451: 90-93,
2008.
2. Guo, M.; Chong, Y. E.; Shapiro, R.; Beebe, K.; Yang, X.-L.; Schimmel,
P.: Paradox of mistranslation of serine for alanine caused by AlaRS
recognition dilemma. Nature 462: 808-812, 2009.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/19/2010.
*FIELD* CN
Patricia A. Hartz - updated: 2/19/2010
*FIELD* CD
Ada Hamosh: 1/11/2010
*FIELD* ED
mgross: 02/24/2010
terry: 2/19/2010
alopez: 1/11/2010
*RECORD*
*FIELD* NO
613212
*FIELD* TI
*613212 ALANYL-tRNA SYNTHETASE DOMAIN-CONTAINING 1; AARSD1
*FIELD* TX
GENE FUNCTION
read more
Mistranslation arising from confusion of serine for alanine by
alanyl-tRNA synthetases (AlaRSs; see 601065 and 612035) has profound
functional consequences. Throughout evolution, 2 editing checkpoints
prevent disease-causing mistranslation from confusing glycine or serine
for alanine at the active site of AlaRS. In both bacteria and mice,
serine poses a bigger challenge than glycine. One checkpoint is the
AlaRS editing center. The other is from widely distributed AlaXps
(Aarsd1), free-standing, genome-encoded editing proteins that clear
Ser-tRNA(Ala) (Beebe et al., 2008). The paradox of misincorporating both
a smaller (glycine) and a larger (serine) amino acid suggests a deep
conflict for nature-designed AlaRS. Guo et al. (2009) showed the
chemical basis for this conflict. Nine crystal structures, together with
kinetic and mutational analysis, provided snapshots of adenylate
formation for each amino acid. An inherent dilemma is posed by
constraints of a structural design that pins down the alpha-amino group
of the bound amino acid by using an acidic residue. This design, dating
back more than 3 billion years, creates a serendipitous interaction with
the serine hydroxide that is difficult to avoid. Apparently because no
better architecture for the recognition of alanine could be found, the
serine misactivation problem was solved through free-standing AlaXps,
which appeared contemporaneously with early AlaRSs.
MAPPING
Hartz (2010) mapped the AARSD1 gene to chromosome 17q21.31 based on an
alignment of the AARSD1 sequence (GenBank GENBANK BC019324) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Beebe, K.; Mock, M.; Merriman, E.; Schimmel, P.: Distinct domains
of tRNA synthetase recognize the same base pair. Nature 451: 90-93,
2008.
2. Guo, M.; Chong, Y. E.; Shapiro, R.; Beebe, K.; Yang, X.-L.; Schimmel,
P.: Paradox of mistranslation of serine for alanine caused by AlaRS
recognition dilemma. Nature 462: 808-812, 2009.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 2/19/2010.
*FIELD* CN
Patricia A. Hartz - updated: 2/19/2010
*FIELD* CD
Ada Hamosh: 1/11/2010
*FIELD* ED
mgross: 02/24/2010
terry: 2/19/2010
alopez: 1/11/2010