Q14197 (ICT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-tRNA hydrolase ICT1, mitochondrial
EC=3.1.1.29

Alternative name(s):
Digestion substraction 1
Short name=DS-1
Immature colon carcinoma transcript 1 protein

Gene names

Name:	ICT1
Synonyms:	DS1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Catalytic activity	N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.
Subunit structure	Component of the mitochondrial 39S ribosomal subunit. Ref.8
Subcellular location	Mitochondrion Ref.8.
Tissue specificity	Down-regulated during the in vitro differentiation of HT29-D4 colon carcinoma cells. Ref.1
Sequence similarities	Belongs to the prokaryotic/mitochondrial release factor family. ICT1 subfamily.
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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mitochondrial translational termination Inferred from direct assay Ref.8. Source: UniProtKB
Cellular component	mitochondrial large ribosomal subunit Inferred from direct assay Ref.8. Source: UniProtKB
Molecular function	aminoacyl-tRNA hydrolase activity Inferred from direct assay Ref.8. Source: UniProtKB translation release factor activity, codon nonspecific Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 29	29	Mitochondrion Potential
	Chain	30 – 206	177	Peptidyl-tRNA hydrolase ICT1, mitochondrial		PRO_0000030339
Amino acid modifications
	Modified residue	169	1	Phosphothreonine Ref.7
Natural variations
	Natural variant	8	1	R → P. Corresponds to variant rs3744206 [ dbSNP | Ensembl ].		VAR_020045
	Natural variant	77	1	L → F. Corresponds to variant rs10512599 [ dbSNP | Ensembl ].		VAR_024604
	Natural variant	122	1	T → M. Corresponds to variant rs34496172 [ dbSNP | Ensembl ].		VAR_061767
Experimental info
	Mutagenesis	88	1	G → A: Strongly impairs peptide release activity. Ref.8
	Mutagenesis	89	1	G → S: Strongly impairs peptide release activity. Ref.8
	Sequence conflict	94	1	K → R in BAD96273. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q14197 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 663BF52443D41540	FASTA	206	23,630
	10 20 30 40 50 60 MAATRCLRWG LSRAGVWLLP PPARCPRRAL HKQKDGTEFK SIYSLDKLYP ESQGSDTAWR 70 80 90 100 110 120 VPNGAKQADS DIPLDRLTIS YCRSSGPGGQ NVNKVNSKAE VRFHLATAEW IAEPVRQKIA 130 140 150 160 170 180 ITHKNKINRL GELILTSESS RYQFRNLADC LQKIRDMITE ASQTPKEPTK EDVKLHRIRI 190 200 ENMNRERLRQ KRIHSAVKTS RRVDMD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8575443] [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: 14702039] [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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[7]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 20186120] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MITOCHONDRIAL 39S RIBOSOMAL SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-88 AND GLY-89.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00029114.
PIR	S63540.
RefSeq	NP_001536.1. NM_001545.1.
UniGene	Hs.407955.
3D structure databases
ProteinModelPortal	Q14197.
SMR	Q14197. Positions 65-205.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14197. 1 interaction.
STRING	Q14197.
Polymorphism databases
DMDM	6015033.
Proteomic databases
PRIDE	Q14197.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301585; ENSP00000301585; ENSG00000167862.
GeneID	3396.
KEGG	hsa:3396.
UCSC	uc002jmm.1. human.
Organism-specific databases
CTD	3396.
GeneCards	GC17P073008.
H-InvDB	HIX0202488.
HGNC	HGNC:5359. ICT1.
HPA	HPA003634.
MIM	603000. gene.
neXtProt	NX_Q14197.
PharmGKB	PA29607.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14936.
GeneTree	ENSGT00390000013268.
HOGENOM	HBG278364.
HOVERGEN	HBG006115.
InParanoid	Q14197.
OMA	RCLRWGL.
OrthoDB	EOG4ZCT5J.
PhylomeDB	Q14197.
Gene expression databases
ArrayExpress	Q14197.
Bgee	Q14197.
CleanEx	HS_ICT1.
Genevestigator	Q14197.
GermOnline	ENSG00000167862. Homo sapiens.
Family and domain databases
InterPro	IPR000352. Pep_chain_release_fac_I_II. [Graphical view]
KO	K15033.
Pfam	PF00472. RF-1. 1 hit. [Graphical view]
PROSITE	PS00745. RF_PROK_I. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	13418.
SOURCE	Search...

Entry information

Entry name

ICT1_HUMAN

Accession

Primary (citable) accession number: Q14197
Secondary accession number(s): B2RAD1, Q53HM7, Q53Y11

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.