UniProt ID | ICT1_HUMAN | |
---|---|---|
UniProt AC | Q14197 | |
Protein Name | Peptidyl-tRNA hydrolase ICT1, mitochondrial | |
Gene Name | MRPL58 {ECO:0000312|HGNC:HGNC:5359} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 206 | |
Subcellular Localization | Mitochondrion . | |
Protein Description | 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.. | |
Protein Sequence | MAATRCLRWGLSRAGVWLLPPPARCPRRALHKQKDGTEFKSIYSLDKLYPESQGSDTAWRVPNGAKQADSDIPLDRLTISYCRSSGPGGQNVNKVNSKAEVRFHLATAEWIAEPVRQKIAITHKNKINRLGELILTSESSRYQFRNLADCLQKIRDMITEASQTPKEPTKEDVKLHRIRIENMNRERLRQKRIHSAVKTSRRVDMD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
38 | Ubiquitination | HKQKDGTEFKSIYSL HCCCCCCCCCEEEEH | 57.52 | 24816145 | |
43 | Phosphorylation | GTEFKSIYSLDKLYP CCCCCEEEEHHHHCC | 15.40 | - | |
44 | Phosphorylation | TEFKSIYSLDKLYPE CCCCEEEEHHHHCCC | 28.55 | - | |
47 | Ubiquitination | KSIYSLDKLYPESQG CEEEEHHHHCCCCCC | 56.04 | 21890473 | |
47 | Ubiquitination | KSIYSLDKLYPESQG CEEEEHHHHCCCCCC | 56.04 | 21890473 | |
49 | Phosphorylation | IYSLDKLYPESQGSD EEEHHHHCCCCCCCC | 15.64 | 28152594 | |
66 | Ubiquitination | WRVPNGAKQADSDIP EECCCCCCCCCCCCC | 47.63 | 21890473 | |
66 | Ubiquitination | WRVPNGAKQADSDIP EECCCCCCCCCCCCC | 47.63 | 21890473 | |
70 | Phosphorylation | NGAKQADSDIPLDRL CCCCCCCCCCCHHHE | 40.22 | - | |
76 | Methylation | DSDIPLDRLTISYCR CCCCCHHHEEEEHHH | 41.22 | 115480125 | |
84 | Phosphorylation | LTISYCRSSGPGGQN EEEEHHHCCCCCCCC | 35.76 | - | |
85 | Phosphorylation | TISYCRSSGPGGQNV EEEHHHCCCCCCCCC | 29.65 | - | |
93 | Ubiquitination | GPGGQNVNKVNSKAE CCCCCCCCCCCCCCE | 50.54 | 24816145 | |
94 | Acetylation | PGGQNVNKVNSKAEV CCCCCCCCCCCCCEE | 38.21 | 25953088 | |
97 | Phosphorylation | QNVNKVNSKAEVRFH CCCCCCCCCCEEEEE | 35.91 | - | |
98 | Acetylation | NVNKVNSKAEVRFHL CCCCCCCCCEEEEEE | 43.28 | 25953088 | |
98 | Succinylation | NVNKVNSKAEVRFHL CCCCCCCCCEEEEEE | 43.28 | 23954790 | |
98 | Ubiquitination | NVNKVNSKAEVRFHL CCCCCCCCCEEEEEE | 43.28 | 24816145 | |
110 | Ubiquitination | FHLATAEWIAEPVRQ EEEHHHHHHHHHHHH | 7.82 | 24816145 | |
153 | Ubiquitination | NLADCLQKIRDMITE CHHHHHHHHHHHHHH | 27.10 | 24816145 | |
159 | Phosphorylation | QKIRDMITEASQTPK HHHHHHHHHHHCCCC | 20.89 | 21406692 | |
162 | Phosphorylation | RDMITEASQTPKEPT HHHHHHHHCCCCCCC | 28.49 | 21406692 | |
164 | Phosphorylation | MITEASQTPKEPTKE HHHHHHCCCCCCCHH | 33.56 | 21406692 | |
169 | Phosphorylation | SQTPKEPTKEDVKLH HCCCCCCCHHHHHHH | 48.43 | 21406692 | |
170 | Ubiquitination | QTPKEPTKEDVKLHR CCCCCCCHHHHHHHH | 63.73 | 24816145 | |
195 | Phosphorylation | LRQKRIHSAVKTSRR HHHHHHHHHHHHHCC | 32.17 | 28509920 | |
199 | Phosphorylation | RIHSAVKTSRRVDMD HHHHHHHHHCCCCCC | 22.37 | 28509920 | |
200 | Phosphorylation | IHSAVKTSRRVDMD- HHHHHHHHCCCCCC- | 16.63 | 28509920 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ICT1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ICT1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ICT1_HUMAN !! |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, AND MASSSPECTROMETRY. |