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Protein

Peptidyl-tRNA hydrolase ICT1, mitochondrial

Gene

ICT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

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
Complete GO annotation...

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

BgeeiQ14197.
CleanExiHS_ICT1.
ExpressionAtlasiQ14197. baseline and differential.
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. 242 interactions.
IntActiQ14197. 217 interactions.
MINTiMINT-3029229.
STRINGi9606.ENSP00000301585.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40p1-206[»]
ProteinModelPortaliQ14197.
SMRiQ14197. Positions 38-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1186.
GeneTreeiENSGT00390000013268.
HOGENOMiHOG000231063.
HOVERGENiHBG006115.
InParanoidiQ14197.
KOiK15033.
OMAiNTKAEVR.
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

        10         20         30         40         50
MAATRCLRWG LSRAGVWLLP PPARCPRRAL HKQKDGTEFK SIYSLDKLYP
60 70 80 90 100
ESQGSDTAWR VPNGAKQADS DIPLDRLTIS YCRSSGPGGQ NVNKVNSKAE
110 120 130 140 150
VRFHLATAEW IAEPVRQKIA ITHKNKINRL GELILTSESS RYQFRNLADC
160 170 180 190 200
LQKIRDMITE ASQTPKEPTK EDVKLHRIRI ENMNRERLRQ KRIHSAVKTS

RRVDMD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40p1-206[»]
ProteinModelPortaliQ14197.
SMRiQ14197. Positions 38-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109622. 242 interactions.
IntActiQ14197. 217 interactions.
MINTiMINT-3029229.
STRINGi9606.ENSP00000301585.

PTM databases

PhosphoSiteiQ14197.

Proteomic databases

MaxQBiQ14197.
PaxDbiQ14197.
PRIDEiQ14197.

Protocols and materials databases

DNASUi3396.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3396.
GeneCardsiGC17P073008.
HGNCiHGNC:5359. ICT1.
HPAiHPA003634.
MIMi603000. gene.
neXtProtiNX_Q14197.
PharmGKBiPA29607.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1186.
GeneTreeiENSGT00390000013268.
HOGENOMiHOG000231063.
HOVERGENiHBG006115.
InParanoidiQ14197.
KOiK15033.
OMAiNTKAEVR.
PhylomeDBiQ14197.
TreeFamiTF315161.

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

Miscellaneous databases

GenomeRNAii3396.
NextBioi13418.
PROiQ14197.
SOURCEiSearch...

Gene expression databases

BgeeiQ14197.
CleanExiHS_ICT1.
ExpressionAtlasiQ14197. baseline and differential.
GenevestigatoriQ14197.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 123 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.