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Q14197

- ICT1_HUMAN

UniProt

Q14197 - ICT1_HUMAN

Protein

Peptidyl-tRNA hydrolase ICT1, mitochondrial

Gene

ICT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit. Acts as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion, possibly in case of abortive elongation. May be involved in the hydrolysis of peptidyl-tRNAs that have been prematurely terminated and thus in the recycling of stalled mitochondrial ribosomes.1 Publication

    Catalytic activityi

    N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.

    GO - Molecular functioni

    1. aminoacyl-tRNA hydrolase activity Source: UniProtKB
    2. translation release factor activity, codon nonspecific Source: UniProtKB

    GO - Biological processi

    1. mitochondrial translational termination Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Protein biosynthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-tRNA hydrolase ICT1, mitochondrial (EC:3.1.1.29)
    Alternative name(s):
    39S ribosomal protein L58, mitochondrial
    Short name:
    MRP-L58
    Digestion substraction 1
    Short name:
    DS-1
    Immature colon carcinoma transcript 1 protein
    Gene namesi
    Name:ICT1
    Synonyms:DS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:5359. ICT1.

    Subcellular locationi

    Mitochondrion 2 Publications

    GO - Cellular componenti

    1. mitochondrial large ribosomal subunit Source: UniProtKB
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi88 – 881G → A: Strongly impairs peptide release activity. 1 Publication
    Mutagenesisi89 – 891G → S: Strongly impairs peptide release activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29607.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionSequence AnalysisAdd
    BLAST
    Chaini30 – 206177Peptidyl-tRNA hydrolase ICT1, mitochondrialPRO_0000030339Add
    BLAST

    Proteomic databases

    MaxQBiQ14197.
    PaxDbiQ14197.
    PRIDEiQ14197.

    PTM databases

    PhosphoSiteiQ14197.

    Expressioni

    Tissue specificityi

    Down-regulated during the in vitro differentiation of HT29-D4 colon carcinoma cells.1 Publication

    Gene expression databases

    ArrayExpressiQ14197.
    BgeeiQ14197.
    CleanExiHS_ICT1.
    GenevestigatoriQ14197.

    Organism-specific databases

    HPAiHPA003634.

    Interactioni

    Subunit structurei

    Component of the mitochondrial ribosome large subunit (39S) which comprises a 16S rRNA and about 50 distinct proteins.2 Publications

    Protein-protein interaction databases

    BioGridi109622. 237 interactions.
    IntActiQ14197. 217 interactions.
    MINTiMINT-3029229.
    STRINGi9606.ENSP00000301585.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14197.
    SMRiQ14197. Positions 65-162.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1186.
    HOGENOMiHOG000231063.
    HOVERGENiHBG006115.
    InParanoidiQ14197.
    KOiK15033.
    OMAiLYPESRG.
    PhylomeDBiQ14197.
    TreeFamiTF315161.

    Family and domain databases

    InterProiIPR000352. Pep_chain_release_fac_I_II.
    [Graphical view]
    PfamiPF00472. RF-1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q14197-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAATRCLRWG LSRAGVWLLP PPARCPRRAL HKQKDGTEFK SIYSLDKLYP    50
    ESQGSDTAWR VPNGAKQADS DIPLDRLTIS YCRSSGPGGQ NVNKVNSKAE 100
    VRFHLATAEW IAEPVRQKIA ITHKNKINRL GELILTSESS RYQFRNLADC 150
    LQKIRDMITE ASQTPKEPTK EDVKLHRIRI ENMNRERLRQ KRIHSAVKTS 200
    RRVDMD 206
    Length:206
    Mass (Da):23,630
    Last modified:November 1, 1996 - v1
    Checksum:i663BF52443D41540
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941K → R in BAD96273. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81R → P.
    Corresponds to variant rs3744206 [ dbSNP | Ensembl ].
    VAR_020045
    Natural varianti77 – 771L → F.
    Corresponds to variant rs10512599 [ dbSNP | Ensembl ].
    VAR_024604
    Natural varianti122 – 1221T → M.
    Corresponds to variant rs34496172 [ dbSNP | Ensembl ].
    VAR_061767

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81788 mRNA. Translation: CAA57387.1.
    BT007111 mRNA. Translation: AAP35775.1.
    AK222553 mRNA. Translation: BAD96273.1.
    AK314138 mRNA. Translation: BAG36828.1.
    CH471099 Genomic DNA. Translation: EAW89227.1.
    BC015335 mRNA. Translation: AAH15335.1.
    CCDSiCCDS11711.1.
    PIRiS63540.
    RefSeqiNP_001536.1. NM_001545.1.
    UniGeneiHs.407955.

    Genome annotation databases

    EnsembliENST00000301585; ENSP00000301585; ENSG00000167862.
    GeneIDi3396.
    KEGGihsa:3396.
    UCSCiuc002jmm.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81788 mRNA. Translation: CAA57387.1 .
    BT007111 mRNA. Translation: AAP35775.1 .
    AK222553 mRNA. Translation: BAD96273.1 .
    AK314138 mRNA. Translation: BAG36828.1 .
    CH471099 Genomic DNA. Translation: EAW89227.1 .
    BC015335 mRNA. Translation: AAH15335.1 .
    CCDSi CCDS11711.1.
    PIRi S63540.
    RefSeqi NP_001536.1. NM_001545.1.
    UniGenei Hs.407955.

    3D structure databases

    ProteinModelPortali Q14197.
    SMRi Q14197. Positions 65-162.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109622. 237 interactions.
    IntActi Q14197. 217 interactions.
    MINTi MINT-3029229.
    STRINGi 9606.ENSP00000301585.

    PTM databases

    PhosphoSitei Q14197.

    Proteomic databases

    MaxQBi Q14197.
    PaxDbi Q14197.
    PRIDEi Q14197.

    Protocols and materials databases

    DNASUi 3396.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301585 ; ENSP00000301585 ; ENSG00000167862 .
    GeneIDi 3396.
    KEGGi hsa:3396.
    UCSCi uc002jmm.3. human.

    Organism-specific databases

    CTDi 3396.
    GeneCardsi GC17P073008.
    HGNCi HGNC:5359. ICT1.
    HPAi HPA003634.
    MIMi 603000. gene.
    neXtProti NX_Q14197.
    PharmGKBi PA29607.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1186.
    HOGENOMi HOG000231063.
    HOVERGENi HBG006115.
    InParanoidi Q14197.
    KOi K15033.
    OMAi LYPESRG.
    PhylomeDBi Q14197.
    TreeFami TF315161.

    Miscellaneous databases

    GenomeRNAii 3396.
    NextBioi 13418.
    PROi Q14197.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14197.
    Bgeei Q14197.
    CleanExi HS_ICT1.
    Genevestigatori Q14197.

    Family and domain databases

    InterProi IPR000352. Pep_chain_release_fac_I_II.
    [Graphical view ]
    Pfami PF00472. RF-1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of mRNAs that show modulated expression during colon carcinoma cell differentiation."
      van Belzen N., Diesveld M.P.G., van der Made A.C.J., Nozawa Y., Dinjens W.N.M., Vlietstra R., Trapman J., Bosman F.T.
      Eur. J. Biochem. 234:843-848(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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].
      Tissue: Tongue.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adipose tissue.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Lymph.
    7. "A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome."
      Richter R., Rorbach J., Pajak A., Smith P.M., Wessels H.J., Huynen M.A., Smeitink J.A., Lightowlers R.N., Chrzanowska-Lightowlers Z.M.
      EMBO J. 29:1116-1125(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL 39S RIBOSOMAL SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-88 AND GLY-89.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as new members of the mammalian mitochondrial ribosome."
      Koc E.C., Cimen H., Kumcuoglu B., Abu N., Akpinar G., Haque M.E., Spremulli L.L., Koc H.
      Front. Physiol. 4:183-183(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiICT1_HUMAN
    AccessioniPrimary (citable) accession number: Q14197
    Secondary accession number(s): B2RAD1, Q53HM7, Q53Y11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 119 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

    Caution

    In contrast to other members of the family, lacks the regions that come into close contact with the mRNA in the ribosomal A-site and determine the STOP codon specificity, explaining the loss of codon specificity for translation release factor activity.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3