ID   AASD1_HUMAN             Reviewed;         412 AA.
AC   Q9BTE6; B4DI73;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   28-JAN-2026, entry version 184.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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., 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.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., 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 the
RT   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., 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.
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 project:
RT   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., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC       incorrectly charged tRNA(Ala). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- INTERACTION:
CC       Q9BTE6-2; Q4LE39-3: ARID4B; NbExp=3; IntAct=EBI-9357295, EBI-11957452;
CC       Q9BTE6-2; P63172: DYNLT1; NbExp=3; IntAct=EBI-9357295, EBI-1176455;
CC       Q9BTE6-2; Q0VG06-3: FAAP100; NbExp=3; IntAct=EBI-9357295, EBI-10226932;
CC       Q9BTE6-2; P58340: MLF1; NbExp=2; IntAct=EBI-9357295, EBI-721328;
CC       Q9BTE6-2; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-9357295, EBI-12037215;
CC       Q9BTE6-2; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-9357295, EBI-11993364;
CC       Q9BTE6-2; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-9357295, EBI-746595;
CC       Q9BTE6-2; O15231: ZNF185; NbExp=3; IntAct=EBI-9357295, EBI-6874731;
CC       Q9BTE6-2; Q96BE0; NbExp=2; IntAct=EBI-9357295, EBI-9356686;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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       Name=3;
CC         IsoId=Q9BTE6-3; Sequence=VSP_043142;
CC   -!- MISCELLANEOUS: [Isoform 2]: Based on a readthrough transcript which may
CC       produce a PTGES3L-AARSD1 fusion protein. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Based on a readthrough transcript which may
CC       produce a PTGES3L-AARSD1 fusion protein. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Alax-L subfamily. {ECO:0000305}.
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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   CCDS; CCDS58552.1; -. [Q9BTE6-1]
DR   RefSeq; NP_001129514.2; NM_001136042.2. [Q9BTE6-3]
DR   RefSeq; NP_001248363.1; NM_001261434.2. [Q9BTE6-1]
DR   RefSeq; NP_079543.1; NM_025267.3. [Q9BTE6-2]
DR   AlphaFoldDB; Q9BTE6; -.
DR   SMR; Q9BTE6; -.
DR   BioGRID; 123290; 146.
DR   BioGRID; 3190353; 22.
DR   FunCoup; Q9BTE6; 2205.
DR   IntAct; Q9BTE6; 191.
DR   MINT; Q9BTE6; -.
DR   STRING; 9606.ENSP00000400870; -.
DR   GlyGen; Q9BTE6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BTE6; -.
DR   PhosphoSitePlus; Q9BTE6; -.
DR   BioMuta; AARSD1; -.
DR   DMDM; 125987702; -.
DR   REPRODUCTION-2DPAGE; IPI00827636; -.
DR   jPOST; Q9BTE6; -.
DR   MassIVE; Q9BTE6; -.
DR   PaxDb; 9606-ENSP00000400870; -.
DR   PeptideAtlas; Q9BTE6; -.
DR   ProteomicsDB; 78985; -. [Q9BTE6-1]
DR   ProteomicsDB; 78986; -. [Q9BTE6-2]
DR   ProteomicsDB; 78987; -. [Q9BTE6-3]
DR   Pumba; Q9BTE6; -.
DR   Antibodypedia; 17173; 82 antibodies from 20 providers.
DR   Antibodypedia; 67174; 180 antibodies from 15 providers.
DR   DNASU; 80755; -.
DR   Ensembl; ENST00000360221.8; ENSP00000353355.4; ENSG00000108825.18. [Q9BTE6-2]
DR   Ensembl; ENST00000427569.7; ENSP00000400870.1; ENSG00000266967.8. [Q9BTE6-1]
DR   GeneID; 80755; -.
DR   KEGG; hsa:100885850; -.
DR   KEGG; hsa:80755; -.
DR   MANE-Select; ENST00000427569.7; ENSP00000400870.1; NM_001261434.2; NP_001248363.1.
DR   UCSC; uc002icd.3; human. [Q9BTE6-1]
DR   AGR; HGNC:28417; -.
DR   AGR; HGNC:43946; -.
DR   ClinPGx; PA142670464; -.
DR   CTD; 80755; -.
DR   GeneCards; AARSD1; -.
DR   GeneCards; PTGES3L-AARSD1; -.
DR   HGNC; HGNC:28417; AARSD1.
DR   HGNC; HGNC:43946; PTGES3L-AARSD1.
DR   HPA; ENSG00000108825; Tissue enhanced (skeletal muscle, tongue).
DR   HPA; ENSG00000266967; Low tissue specificity.
DR   MIM; 613212; gene.
DR   OpenTargets; ENSG00000108825; -.
DR   OpenTargets; ENSG00000266967; -.
DR   VEuPathDB; HostDB:ENSG00000108825; -.
DR   VEuPathDB; HostDB:ENSG00000266967; -.
DR   eggNOG; KOG2105; Eukaryota.
DR   GeneTree; ENSGT00940000156241; -.
DR   HOGENOM; CLU_004485_7_0_1; -.
DR   InParanoid; Q9BTE6; -.
DR   OMA; KYDTTSW; -.
DR   OrthoDB; 288942at2759; -.
DR   PAN-GO; Q9BTE6; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9BTE6; -.
DR   PathwayCommons; Q9BTE6; -.
DR   SignaLink; Q9BTE6; -.
DR   Agora; ENSG00000108825; -.
DR   Agora; ENSG00000266967; -.
DR   BioGRID-ORCS; 100885850; 23 hits in 1066 CRISPR screens.
DR   BioGRID-ORCS; 80755; 16 hits in 1113 CRISPR screens.
DR   Pharos; Q9BTE6; Tdark.
DR   PRO; PR:Q9BTE6; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9BTE6; protein.
DR   Bgee; ENSG00000108825; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 103 other cell types or tissues.
DR   ExpressionAtlas; Q9BTE6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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:0002196; F:Ser-tRNA(Ala) deacylase activity; IBA:GO_Central.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR   FunFam; 3.30.980.10:FF:000007; alanyl-tRNA editing protein Aarsd1; 1.
DR   FunFam; 2.40.30.130:FF:000012; Predicted gene, 27029; 1.
DR   Gene3D; 2.40.30.130; -; 1.
DR   Gene3D; 3.30.980.10; Threonyl-trna Synthetase, Chain A, domain 2; 1.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR051335; Alanyl-tRNA_Editing_Enzymes.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR   PANTHER; PTHR43462:SF1; ALANYL-TRNA EDITING PROTEIN AARSD1; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Metal-binding; Phosphoprotein;
KW   Protein biosynthesis; Proteomics identification; Reference proteome; Zinc.
FT   CHAIN           1..412
FT                   /note="Alanyl-tRNA editing protein Aarsd1"
FT                   /id="PRO_0000277465"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..13
FT                   /note="MAFWCQRDSYARE -> MEFCVEDSTDVHVLIEDHRIVFSCKNADGVELYNE
FT                   IEFYAKVNSKDSQDKRSSRSITCFVRKWKEKVAWPRLTKEDIKPVWLSVDFDNWRDWEG
FT                   DEEMELAHVEHYAELLKKVSTKRPPPAMDDLD (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023014"
FT   VAR_SEQ         1..13
FT                   /note="MAFWCQRDSYARE -> MFSLPLNCSPDHIRRGSCWGRPQDLKIAAPAWNSK
FT                   CHPGAGAAMARQHARTLWYDRPRYVFMEFCVEDSTDVHVLIEDHRIVFSCKNADGVELY
FT                   NEIEFYAKVNSKDSQDKRSSRSITCFVRKWKEKVAWPRLTKEDIKPVWLSVDFDNWRDW
FT                   EGDEEMELAHVEHYAELLKKVSTKRPPPAMDDLD (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="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
//