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Q9NP81

- SYSM_HUMAN

UniProt

Q9NP81 - SYSM_HUMAN

Protein

Serine--tRNA ligase, mitochondrial

Gene

SARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity.By similarity

    Catalytic activityi

    ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).
    ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei345 – 3451ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei352 – 3521SerineBy similarity
    Binding sitei453 – 4531SerineBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi330 – 3323ATPBy similarity
    Nucleotide bindingi418 – 4214ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. serine-tRNA ligase activity Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. selenocysteinyl-tRNA(Sec) biosynthetic process Source: UniProtKB-UniPathway
    3. seryl-tRNA aminoacylation Source: UniProtKB
    4. tRNA aminoacylation for protein translation Source: Reactome

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.11. 2681.
    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.
    UniPathwayiUPA00906; UER00895.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine--tRNA ligase, mitochondrial (EC:6.1.1.11)
    Alternative name(s):
    SerRSmt
    Seryl-tRNA synthetase
    Short name:
    SerRS
    Seryl-tRNA(Ser/Sec) synthetase
    Gene namesi
    Name:SARS2
    Synonyms:SARSM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:17697. SARS2.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Hyperuricemia pulmonary hypertension renal failure and alkalosis (HUPRA) [MIM:613845]: A multisystem disorder characterized by onset in infancy of progressive renal failure leading to electrolyte imbalances, metabolic alkalosis, pulmonary hypertension, hypotonia, and delayed development. Affected individuals are born prematurely.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti390 – 3901D → G in HUPRA. 1 Publication
    VAR_065820

    Organism-specific databases

    MIMi613845. phenotype.
    Orphaneti363694. Hyperuricemia-pulmonary hypertension-renal failure-alkalosis syndrome.
    PharmGKBiPA134899753.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434MitochondrionBy similarityAdd
    BLAST
    Chaini35 – 518484Serine--tRNA ligase, mitochondrialPRO_0000035822Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101N6-acetyllysineBy similarity
    Modified residuei195 – 1951N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NP81.
    PRIDEiQ9NP81.

    PTM databases

    PhosphoSiteiQ9NP81.

    Expressioni

    Gene expression databases

    BgeeiQ9NP81.
    CleanExiHS_SARS2.
    GenevestigatoriQ9NP81.

    Organism-specific databases

    HPAiHPA052730.
    HPA056957.

    Interactioni

    Subunit structurei

    Homodimer. The tRNA molecule binds across the dimer By similarity.By similarity

    Protein-protein interaction databases

    BioGridi120278. 19 interactions.
    IntActiQ9NP81. 7 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NP81.
    SMRiQ9NP81. Positions 39-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni299 – 3013Serine bindingBy similarity

    Domaini

    Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOGENOMiHOG000035937.
    HOVERGENiHBG023869.
    InParanoidiQ9NP81.
    KOiK01875.
    OMAiMGTDVIK.
    OrthoDBiEOG7WMCJ5.
    PhylomeDBiQ9NP81.

    Family and domain databases

    Gene3Di1.10.287.40. 1 hit.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR002317. Ser-tRNA-ligase_type_1.
    IPR015866. Ser-tRNA-synth_1_N.
    IPR010978. tRNA-bd_arm.
    [Graphical view]
    PANTHERiPTHR11778. PTHR11778. 1 hit.
    PfamiPF00587. tRNA-synt_2b. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
    PRINTSiPR00981. TRNASYNTHSER.
    SUPFAMiSSF46589. SSF46589. 1 hit.
    TIGRFAMsiTIGR00414. serS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NP81-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAASMARRLW PLLTRRGFRP RGGCISNDSP RRSFTTEKRN RNLLYEYARE    50
    GYSALPQLDI ERFCACPEEA AHALELRKGE LRSADLPAII STWQELRQLQ 100
    EQIRSLEEEK AAVTEAVRAL LANQDSGEVQ QDPKYQGLRA RGREIRKELV 150
    HLYPREAQLE EQFYLQALKL PNQTHPDVPV GDESQARVLH MVGDKPVFSF 200
    QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH GLVNFTFNKL 250
    LRRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPAR FKDLNLAGTA 300
    EVGLAGYFMD HTVAFRDLPV RMVCSSTCYR AETNTGQEPR GLYRVHHFTK 350
    VEMFGVTGPG LEQSSQLLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA 400
    YRKFDIEAWM PGRGRFGEVT SASNCTDFQS RRLHIMFQTE AGELQFAHTV 450
    NATACAVPRL LIALLESNQQ KDGSVLVPPA LQSYLGTDRI TAPTHVPLQY 500
    IGPNQPRKPG LPGQPAVS 518
    Length:518
    Mass (Da):58,283
    Last modified:October 1, 2000 - v1
    Checksum:iC6516A9527B34EB7
    GO
    Isoform 2 (identifier: Q9NP81-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         132-155: DPKYQGLRARGREIRKELVHLYPR → VRLDPGAGSIFGPTFLPFPGQLSLLV

    Note: No experimental confirmation available.

    Show »
    Length:520
    Mass (Da):58,030
    Checksum:i1CB28DA9FBFEED8D
    GO

    Sequence cautioni

    The sequence AAH01020.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351T → A.
    Corresponds to variant rs34264048 [ dbSNP | Ensembl ].
    VAR_052645
    Natural varianti83 – 831S → L.
    Corresponds to variant rs34050897 [ dbSNP | Ensembl ].
    VAR_052646
    Natural varianti390 – 3901D → G in HUPRA. 1 Publication
    VAR_065820

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei132 – 15524DPKYQ…HLYPR → VRLDPGAGSIFGPTFLPFPG QLSLLV in isoform 2. 1 PublicationVSP_043020Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029948 mRNA. Translation: BAA99557.1.
    AK000457 mRNA. Translation: BAA91176.1.
    AK293414 mRNA. Translation: BAG56921.1.
    AC011455 Genomic DNA. No translation available.
    BC001020 mRNA. Translation: AAH01020.2. Different initiation.
    BC042912 mRNA. Translation: AAH42912.1.
    CCDSiCCDS33017.1. [Q9NP81-1]
    CCDS54265.1. [Q9NP81-2]
    RefSeqiNP_001139373.1. NM_001145901.1. [Q9NP81-2]
    NP_060297.1. NM_017827.3. [Q9NP81-1]
    UniGeneiHs.709416.

    Genome annotation databases

    EnsembliENST00000221431; ENSP00000221431; ENSG00000104835. [Q9NP81-1]
    ENST00000600042; ENSP00000472847; ENSG00000104835. [Q9NP81-2]
    GeneIDi54938.
    KEGGihsa:54938.
    UCSCiuc002ojz.2. human. [Q9NP81-1]
    uc010xup.1. human. [Q9NP81-2]

    Polymorphism databases

    DMDMi23822219.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029948 mRNA. Translation: BAA99557.1 .
    AK000457 mRNA. Translation: BAA91176.1 .
    AK293414 mRNA. Translation: BAG56921.1 .
    AC011455 Genomic DNA. No translation available.
    BC001020 mRNA. Translation: AAH01020.2 . Different initiation.
    BC042912 mRNA. Translation: AAH42912.1 .
    CCDSi CCDS33017.1. [Q9NP81-1 ]
    CCDS54265.1. [Q9NP81-2 ]
    RefSeqi NP_001139373.1. NM_001145901.1. [Q9NP81-2 ]
    NP_060297.1. NM_017827.3. [Q9NP81-1 ]
    UniGenei Hs.709416.

    3D structure databases

    ProteinModelPortali Q9NP81.
    SMRi Q9NP81. Positions 39-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120278. 19 interactions.
    IntActi Q9NP81. 7 interactions.

    PTM databases

    PhosphoSitei Q9NP81.

    Polymorphism databases

    DMDMi 23822219.

    Proteomic databases

    MaxQBi Q9NP81.
    PRIDEi Q9NP81.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221431 ; ENSP00000221431 ; ENSG00000104835 . [Q9NP81-1 ]
    ENST00000600042 ; ENSP00000472847 ; ENSG00000104835 . [Q9NP81-2 ]
    GeneIDi 54938.
    KEGGi hsa:54938.
    UCSCi uc002ojz.2. human. [Q9NP81-1 ]
    uc010xup.1. human. [Q9NP81-2 ]

    Organism-specific databases

    CTDi 54938.
    GeneCardsi GC19M039405.
    HGNCi HGNC:17697. SARS2.
    HPAi HPA052730.
    HPA056957.
    MIMi 612804. gene.
    613845. phenotype.
    neXtProti NX_Q9NP81.
    Orphaneti 363694. Hyperuricemia-pulmonary hypertension-renal failure-alkalosis syndrome.
    PharmGKBi PA134899753.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000035937.
    HOVERGENi HBG023869.
    InParanoidi Q9NP81.
    KOi K01875.
    OMAi MGTDVIK.
    OrthoDBi EOG7WMCJ5.
    PhylomeDBi Q9NP81.

    Enzyme and pathway databases

    UniPathwayi UPA00906 ; UER00895 .
    BRENDAi 6.1.1.11. 2681.
    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi SARS2. human.
    GeneWikii SARS2.
    GenomeRNAii 54938.
    NextBioi 58062.
    PROi Q9NP81.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NP81.
    CleanExi HS_SARS2.
    Genevestigatori Q9NP81.

    Family and domain databases

    Gene3Di 1.10.287.40. 1 hit.
    InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR002317. Ser-tRNA-ligase_type_1.
    IPR015866. Ser-tRNA-synth_1_N.
    IPR010978. tRNA-bd_arm.
    [Graphical view ]
    PANTHERi PTHR11778. PTHR11778. 1 hit.
    Pfami PF00587. tRNA-synt_2b. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
    PRINTSi PR00981. TRNASYNTHSER.
    SUPFAMi SSF46589. SSF46589. 1 hit.
    TIGRFAMsi TIGR00414. serS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase."
      Yokogawa T., Shimada N., Takeuchi N., Benkowski L., Suzuki T., Omori A., Ueda T., Nishikawa K., Spremulli L.L., Watanabe K.
      J. Biol. Chem. 275:19913-19920(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain and Eye.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Mutations in the mitochondrial seryl-tRNA synthetase cause hyperuricemia, pulmonary hypertension, renal failure in infancy and alkalosis, HUPRA syndrome."
      Belostotsky R., Ben-Shalom E., Rinat C., Becker-Cohen R., Feinstein S., Zeligson S., Segel R., Elpeleg O., Nassar S., Frishberg Y.
      Am. J. Hum. Genet. 88:193-200(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HUPRA GLY-390.

    Entry informationi

    Entry nameiSYSM_HUMAN
    AccessioniPrimary (citable) accession number: Q9NP81
    Secondary accession number(s): A6NHW7, B4DE10, Q9BVP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3