Q96Q15 (SMG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 101.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Serine/threonine-protein kinase SMG1 Short name=SMG-1 Short name=hSMG-1 EC=2.7.11.1 Alternative name(s): 61E3.4 Lambda/iota protein kinase C-interacting protein Short name=Lambda-interacting protein | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 3661 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. Ref.2 Ref.3 Ref.4 Ref.12 |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. Ref.16 |
| Cofactor | Manganese. Ref.3 |
| Enzyme regulation | Inhibited by caffeine, LY294002 and wortmannin. Ref.2 Ref.3 Ref.4 |
| Subunit structure | Component of the SMG1C complex composed of SMG1, SMG8 and SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large conformational change in the SMG1 C-terminal head domain containing the catalytic domain. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with PRKCI. Interacts with TELO2 and TTI1. Interacts with RUVBL1 and RUVBL2. Interacts with UPF2. Ref.2 Ref.8 Ref.10 Ref.11 Ref.12 Ref.16 Ref.19 Ref.20 Ref.21 Ref.24 |
| Subcellular location | |
| Tissue specificity | Widely expressed, with highest level in heart and skeletal muscle. Expressed in placenta, brain, lung and spleen, but not in liver. Ref.4 Ref.8 |
| Post-translational modification | |
| Miscellaneous | This gene is located in a region of chromosome 16 that contains 2 segmental duplications. Other genes that are highly related to this exist, but they probably represent pseudogenes. |
| Sequence similarities | Belongs to the PI3/PI4-kinase family. Contains 1 FAT domain. Contains 1 FATC domain. Contains 1 HEAT repeat. Contains 1 PI3K/PI4K domain. |
| Sequence caution | The sequence AAA86535.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| PABPC1 | P11940 | 2 | EBI-1049832,EBI-81531 | |
| UPF2 | Q9HAU5 | 6 | EBI-1049832,EBI-372073 |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q96Q15-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q96Q15-2) The sequence of this isoform differs from the canonical sequence as follows: 1-140: Missing. | ||||||
| Isoform 3 (identifier: Q96Q15-3) The sequence of this isoform differs from the canonical sequence as follows: 1-630: Missing. | ||||||
| Isoform 4 (identifier: Q96Q15-4) Also known as: BLIP; The sequence of this isoform differs from the canonical sequence as follows: 1-1269: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3661 | 3661 | Serine/threonine-protein kinase SMG1 | PRO_0000229791 | |||||
Regions | |||||||||
| Domain | 1131 – 1866 | 736 | FAT | ||||||
| Repeat | 1817 – 1852 | 36 | HEAT | ||||||
| Domain | 2150 – 2478 | 329 | PI3K/PI4K | ||||||
| Domain | 3629 – 3661 | 33 | FATC | ||||||
| Region | 1 – 1977 | 1977 | Interaction with SMG8 and SMG9 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 173 | 1 | N6-acetyllysine Ref.18 | ||||||
| Modified residue | 3550 | 1 | Phosphothreonine Ref.14 | ||||||
| Modified residue | 3556 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 3570 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 3573 | 1 | Phosphothreonine Ref.22 | ||||||
| Modified residue | 3577 | 1 | Phosphothreonine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 1269 | 1269 | Missing in isoform 4. | VSP_017746 | |||||
| Alternative sequence | 1 – 630 | 630 | Missing in isoform 3. | VSP_017747 | |||||
| Alternative sequence | 1 – 140 | 140 | Missing in isoform 2. | VSP_017748 | |||||
| Natural variant | 35 | 1 | A → T. Ref.26 | VAR_041623 | |||||
| Natural variant | 126 | 1 | R → C. Ref.26 | VAR_041624 | |||||
| Natural variant | 144 | 1 | S → C. Ref.4 Ref.26 | VAR_041625 | |||||
| Natural variant | 151 | 1 | N → Y. Ref.26 | VAR_041626 | |||||
| Natural variant | 160 | 1 | D → N. Ref.26 | VAR_041627 | |||||
| Natural variant | 167 | 1 | A → V. Ref.26 | VAR_041628 | |||||
| Natural variant | 320 | 1 | D → G. Ref.26 | VAR_041629 | |||||
| Natural variant | 465 | 1 | G → S. Ref.26 | VAR_041630 | |||||
| Natural variant | 546 | 1 | H → R. Ref.26 | VAR_041631 | |||||
| Natural variant | 588 | 1 | A → S. Ref.26 | VAR_041632 | |||||
| Natural variant | 612 | 1 | I → K. Ref.4 Ref.26 | VAR_041633 | |||||
| Natural variant | 753 | 1 | S → C. Ref.26 | VAR_041634 | |||||
| Natural variant | 809 | 1 | S → C. Ref.26 | VAR_041635 | |||||
| Natural variant | 812 | 1 | R → C. Ref.26 | VAR_041636 | |||||
| Natural variant | 829 | 1 | V → I. Ref.26 | VAR_041637 | |||||
| Natural variant | 832 | 1 | N → D. Ref.26 | VAR_041638 | |||||
| Natural variant | 952 | 1 | A → G. Ref.26 | VAR_041639 | |||||
| Natural variant | 969 | 1 | N → S. Ref.26 | VAR_041640 | |||||
| Natural variant | 1016 | 1 | F → L. Ref.26 | VAR_041641 | |||||
| Natural variant | 1029 | 1 | R → Q. Ref.26 | VAR_041642 | |||||
| Natural variant | 1072 | 1 | T → S. Ref.26 | VAR_041643 | |||||
| Natural variant | 1103 | 1 | N → H. Ref.26 | VAR_041644 | |||||
| Natural variant | 1275 | 1 | P → R. Ref.26 | VAR_041645 | |||||
| Natural variant | 1292 | 1 | Q → P. Ref.26 | VAR_041646 | |||||
| Natural variant | 1332 | 1 | I → V. Ref.26 | VAR_041647 | |||||
| Natural variant | 1358 | 1 | S → P. Ref.26 | VAR_041648 | |||||
| Natural variant | 1418 | 1 | R → T. Ref.26 | VAR_041649 | |||||
| Natural variant | 2171 | 1 | S → C in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.26 | VAR_041650 | |||||
| Natural variant | 2258 | 1 | G → S. Ref.26 | VAR_041651 | |||||
| Natural variant | 2345 | 1 | M → K. Ref.26 | VAR_041652 | |||||
| Natural variant | 2730 | 1 | Q → E. Ref.26 | VAR_041653 | |||||
| Natural variant | 2889 | 1 | G → S. Ref.26 | VAR_041654 | |||||
| Natural variant | 2899 | 1 | P → A. Ref.26 | VAR_041655 | |||||
| Natural variant | 3239 | 1 | I → T in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.26 | VAR_041656 | |||||
| Natural variant | 3583 | 1 | K → Q in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.26 | VAR_041657 | |||||
Experimental info | |||||||||
| Mutagenesis | 2335 | 1 | D → A: Loss of function. Ref.2 Ref.3 Ref.4 | ||||||
| Sequence conflict | 14 | 1 | G → GGGGG in BAB70696. Ref.2 | ||||||
| Sequence conflict | 20 | 1 | K → N in BAB70696. Ref.2 | ||||||
| Sequence conflict | 22 | 1 | P → S in BAB70696. Ref.2 | ||||||
| Sequence conflict | 40 | 1 | D → G in BAB70696. Ref.2 | ||||||
| Sequence conflict | 686 | 1 | S → A in BAB70696. Ref.2 | ||||||
| Sequence conflict | 743 | 1 | K → R in BAB70696. Ref.2 | ||||||
| Sequence conflict | 1193 | 1 | C → F in BAB70696. Ref.2 | ||||||
| Sequence conflict | 2009 | 1 | K → R in BAB70696. Ref.2 | ||||||
| Sequence conflict | 2077 | 1 | S → N in AAK58892. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62." Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T. Mol. Cell. Biol. 18:3069-3080(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). |
| [2] | "Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay." Yamashita A., Ohnishi T., Kashima I., Taya Y., Ohno S. Genes Dev. 15:2215-2228(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION OF RENT1, ALTERNATIVE SPLICING, ENZYME REGULATION, PHOSPHORYLATION, INTERACTION WITH RENT1; UPF2 AND UPF3, MUTAGENESIS OF ASP-2335. |
| [3] | "Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein." Denning G., Jamieson L., Maquat L.E., Thompson E.A., Fields A.P. J. Biol. Chem. 276:22709-22714(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, PHOSPHORYLATION OF RENT1, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF ASP-2335. |
| [4] | "The mRNA surveillance protein hSMG-1 functions in genotoxic stress response pathways in mammalian cells." Brumbaugh K.M., Otterness D.M., Geisen C., Oliveira V., Brognard J., Li X., Lejeune F., Tibbetts R.S., Maquat L.E., Abraham R.T. Mol. Cell 14:585-598(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION OF TP53, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF ASP-2335, VARIANTS CYS-144 AND LYS-612. |
| [5] | "The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. Pennacchio L.A.Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro." Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1674-3661. Tissue: Brain. |
| [7] | "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION. |
| [8] | "Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo." Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J. Mol. Cell. Biol. 16:105-114(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2878-3661, TISSUE SPECIFICITY, INTERACTION WITH PRKCI. |
| [9] | "Divergent origins and concerted expansion of two segmental duplications on chromosome 16." Eichler E.E., Johnson M.E., Alkan C., Tuzun E., Sahinalp C., Misceo D., Archidiacono N., Rocchi M. J. Hered. 92:462-468(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DUPLICATION. |
| [10] | "Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7." Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A., Hachiya T., Hentze M.W., Anderson P., Ohno S. Mol. Cell 12:1187-1200(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SMG5. |
| [11] | "Characterization of human Smg5/7a: a protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1." Chiu S.-Y., Serin G., Ohara O., Maquat L.E. RNA 9:77-87(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RENT1; UPF2; EST1A AND UPF3B. |
| [12] | "Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA decay." Kashima I., Yamashita A., Izumi N., Kataoka N., Morishita R., Hoshino S., Ohno M., Dreyfuss G., Ohno S. Genes Dev. 20:355-367(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH UPF2, IDENTIFICATION IN THE SURF COMPLEX. |
| [13] | "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma. |
| [14] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3550 AND SER-3556, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [15] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3570, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [16] | "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay." Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S. Genes Dev. 23:1091-1105(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, IDENTIFICATION IN THE SMG1C COMPLEX. |
| [17] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell. |
| [18] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, MASS SPECTROMETRY. |
| [19] | "Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly." Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N. J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TELO2 AND TTI1. |
| [20] | "A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability." Hurov K.E., Cotta-Ramusino C., Elledge S.J. Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TTI1. |
| [21] | "AAA+ proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in nonsense-mediated mRNA decay." Izumi N., Yamashita A., Iwamatsu A., Kurata R., Nakamura H., Saari B., Hirano H., Anderson P., Ohno S. Sci. Signal. 3:RA27-RA27(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RUVBL1 AND RUVBL2. |
| [22] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3573, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [23] | "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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [24] | "The nonsense-mediated mRNA decay SMG-1 kinase is regulated by large-scale conformational changes controlled by SMG-8." Arias-Palomo E., Yamashita A., Fernandez I.S., Nunez-Ramirez R., Bamba Y., Izumi N., Ohno S., Llorca O. Genes Dev. 25:153-164(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SMG8 AND SMG9, ELECTRON MICROSCOPY OF THE SMG1C COMPLEX. |
| [25] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [26] | "Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. Stratton M.R.Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-35; CYS-126; CYS-144; TYR-151; ASN-160; VAL-167; GLY-320; SER-465; ARG-546; SER-588; LYS-612; CYS-753; CYS-809; CYS-812; ILE-829; ASP-832; GLY-952; SER-969; LEU-1016; GLN-1029; SER-1072; HIS-1103; ARG-1275; PRO-1292; VAL-1332; PRO-1358; THR-1418; CYS-2171; SER-2258; LYS-2345; GLU-2730; SER-2889; ALA-2899; THR-3239 AND GLN-3583. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF186377 mRNA. Translation: AAK58892.1. AB061371 mRNA. Translation: BAB70696.1. AY014957 mRNA. Translation: AAK00511.1. AF395444 mRNA. Translation: AAM73708.1. AC092287 Genomic DNA. No translation available. AB007881 mRNA. Translation: BAA24851.2. U32581 mRNA. Translation: AAA86535.2. Different initiation. |
| IPI | IPI00183368. IPI00639874. IPI00640955. IPI00939320. |
| PIR | JC6084. |
| RefSeq | NP_055907.3. NM_015092.4. |
| UniGene | Hs.460179. |
3D structure databases | |
| ProteinModelPortal | Q96Q15. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q96Q15. 30 interactions. |
| MINT | MINT-1513197. |
| STRING | 9606.ENSP00000402515. |
PTM databases | |
| PhosphoSite | Q96Q15. |
Polymorphism databases | |
| DMDM | 91208166. |
Proteomic databases | |
| PaxDb | Q96Q15. |
| PRIDE | Q96Q15. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000446231; ENSP00000402515; ENSG00000157106. |
| GeneID | 23049. |
| KEGG | hsa:23049. |
| UCSC | uc002dfm.3. human. |
Organism-specific databases | |
| CTD | 23049. |
| GeneCards | GC16M018816. |
| H-InvDB | HIX0012849. HIX0038625. HIX0202313. |
| HGNC | HGNC:30045. SMG1. |
| HPA | HPA006870. |
| MIM | 607032. gene. |
| neXtProt | NX_Q96Q15. |
| PharmGKB | PA164725852. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | COG5032. |
| HOGENOM | HOG000168703. |
| HOVERGEN | HBG093965. |
| InParanoid | Q96Q15. |
| KO | K08873. |
| OrthoDB | EOG4320X5. |
Enzyme and pathway databases | |
| Reactome | REACT_21257. Metabolism of RNA. REACT_71. Gene Expression. |
Gene expression databases | |
| ArrayExpress | Q96Q15. |
| Bgee | Q96Q15. |
| Genevestigator | Q96Q15. |
| GermOnline | ENSG00000157106. Homo sapiens. |
Family and domain databases | |
| Gene3D | 1.10.1070.11. 2 hits. |
| InterPro | IPR016024. ARM-type_fold. IPR003152. FATC. IPR011009. Kinase-like_dom. IPR000403. PI3/4_kinase_cat_dom. IPR018936. PI3/4_kinase_CS. IPR014009. PIK_FAT. [Graphical view] |
| Pfam | PF02260. FATC. 1 hit. PF00454. PI3_PI4_kinase. 1 hit. [Graphical view] |
| SMART | SM00146. PI3Kc. 1 hit. [Graphical view] |
| SUPFAM | SSF48371. ARM-type_fold. 1 hit. SSF56112. Kinase_like. 1 hit. |
| PROSITE | PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS50077. HEAT_REPEAT. False negative. PS00915. PI3_4_KINASE_1. False negative. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChEMBL | CHEMBL1795195. |
| ChiTaRS | SMG1. human. |
| GenomeRNAi | 23049. |
| NextBio | 44092. |
| SOURCE | Search... |
Entry information
| Entry name | SMG1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96Q15 Secondary accession number(s): O43305 Q96RW3 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| Human chromosome 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
