Insufficient scRNA-seq data for expression of NTAQ1 at single-cell level.
Insufficient scRNA-seq data for expression of NTAQ1 at tissue level.
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
esophagus | 100% | 398.30 | 1444 / 1445 | 100% | 9.08 | 183 / 183 |
breast | 100% | 498.32 | 459 / 459 | 100% | 12.96 | 1117 / 1118 |
brain | 100% | 556.24 | 2639 / 2642 | 100% | 9.25 | 705 / 705 |
prostate | 100% | 551.24 | 245 / 245 | 100% | 10.24 | 501 / 502 |
uterus | 100% | 487.48 | 170 / 170 | 100% | 10.38 | 458 / 459 |
ovary | 100% | 730.23 | 180 / 180 | 100% | 10.86 | 429 / 430 |
lung | 100% | 440.84 | 576 / 578 | 100% | 10.31 | 1154 / 1155 |
stomach | 100% | 429.49 | 359 / 359 | 99% | 7.93 | 284 / 286 |
intestine | 100% | 422.47 | 966 / 966 | 99% | 8.35 | 522 / 527 |
pancreas | 100% | 358.69 | 328 / 328 | 99% | 7.74 | 176 / 178 |
thymus | 100% | 443.15 | 653 / 653 | 99% | 6.72 | 598 / 605 |
bladder | 100% | 525.90 | 21 / 21 | 99% | 8.99 | 498 / 504 |
skin | 100% | 451.87 | 1809 / 1809 | 98% | 9.03 | 463 / 472 |
kidney | 100% | 525.43 | 89 / 89 | 96% | 5.28 | 863 / 901 |
adrenal gland | 100% | 591.11 | 258 / 258 | 94% | 6.89 | 216 / 230 |
liver | 99% | 243.56 | 223 / 226 | 92% | 5.93 | 372 / 406 |
blood vessel | 100% | 507.73 | 1335 / 1335 | 0% | 0 | 0 / 0 |
lymph node | 0% | 0 | 0 / 0 | 100% | 8.44 | 29 / 29 |
muscle | 100% | 605.27 | 803 / 803 | 0% | 0 | 0 / 0 |
spleen | 100% | 330.38 | 241 / 241 | 0% | 0 | 0 / 0 |
tonsil | 0% | 0 | 0 / 0 | 100% | 8.74 | 45 / 45 |
ureter | 0% | 0 | 0 / 0 | 100% | 8.42 | 1 / 1 |
adipose | 100% | 465.67 | 1203 / 1204 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 99% | 9.80 | 79 / 80 |
heart | 98% | 561.85 | 846 / 861 | 0% | 0 | 0 / 0 |
peripheral blood | 55% | 237.81 | 514 / 929 | 0% | 0 | 0 / 0 |
abdomen | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
bone marrow | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
diaphragm | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
gingiva | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasal cavity | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasopharynx | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nose | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
placenta | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
spinal column | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
GO_0036211 | Biological process | protein modification process |
GO_0005829 | Cellular component | cytosol |
GO_0005634 | Cellular component | nucleus |
GO_0008418 | Molecular function | protein-N-terminal asparagine amidohydrolase activity |
GO_0070773 | Molecular function | protein-N-terminal glutamine amidohydrolase activity |
GO_0005515 | Molecular function | protein binding |
Gene name | NTAQ1 |
Protein name | N-terminal glutamine amidase 1 Protein N-terminal glutamine amidohydrolase (EC 3.5.1.122) (Protein NH2-terminal glutamine deamidase) Protein N-terminal glutamine amidohydrolase (EC 3.5.1.122) (Protein NH2-terminal glutamine deamidase) (N-terminal Gln amidase) (Nt(Q)-amidase) (WDYHV motif-containing protein 1) |
Synonyms | C8orf32 WDYHV1 |
Description | FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine. . FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine. . FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine. . FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine. . FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine. . |
Accessions | ENST00000287387.7 [Q96HA8-1] ENST00000524254.5 [Q96HA8-2] A0A3B3ITI2 A0A3B3ITD7 ENST00000523984.5 [Q96HA8-2] ENST00000650311.1 E5RHC2 ENST00000523356.1 Q96HA8 ENST00000523551.1 E5RIY9 ENST00000518125.1 ENST00000519199.5 A0A3B3IS49 H0YBV4 ENST00000517609.5 |