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Q14197

- ICT1_HUMAN

UniProt

Q14197 - ICT1_HUMAN

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Protein

Peptidyl-tRNA hydrolase ICT1, mitochondrial

Gene
ICT1, DS1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

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 – 2929Mitochondrion Reviewed predictionAdd
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.

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

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 conflict

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

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

« 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: September 3, 2014
This is version 118 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.

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

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