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UniProtKB - Q8TEQ6 (GEMI5_HUMAN)
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>sp|Q8TEQ6|GEMI5_HUMAN Gem-associated protein 5 OS=Homo sapiens OX=9606 GN=GEMIN5 PE=1 SV=3 MGQEPRTLPPSPNWYCARCSDAVPGGLFGFAARTSVFLVRVGPGAGESPGTPPFRVIGEL VGHTERVSGFTFSHHPGQYNLCATSSDDGTVKIWDVETKTVVTEHALHQHTISTLHWSPR VKDLIVSGDEKGVVFCYWFNRNDSQHLFIEPRTIFCLTCSPHHEDLVAIGYKDGIVVIID ISKKGEVIHRLRGHDDEIHSIAWCPLPGEDCLSINQEETSEEAEITNGNAVAQAPVTKGC YLATGSKDQTIRIWSCSRGRGVMILKLPFLKRRGGGIDPTVKERLWLTLHWPSNQPTQLV SSCFGGELLQWDLTQSWRRKYTLFSASSEGQNHSRIVFNLCPLQTEDDKQLLLSTSMDRD VKCWDIATLECSWTLPSLGGFAYSLAFSSVDIGSLAIGVGDGMIRVWNTLSIKNNYDVKN FWQGVKSKVTALCWHPTKEGCLAFGTDDGKVGLYDTYSNKPPQISSTYHKKTVYTLAWGP PVPPMSLGGEGDRPSLALYSCGGEGIVLQHNPWKLSGEAFDINKLIRDTNSIKYKLPVHT EISWKADGKIMALGNEDGSIEIFQIPNLKLICTIQQHHKLVNTISWHHEHGSQPELSYLM ASGSNNAVIYVHNLKTVIESSPESPVTITEPYRTLSGHTAKITSVAWSPHHDGRLVSASY DGTAQVWDALREEPLCNFRGHRGRLLCVAWSPLDPDCIYSGADDFCVHKWLTSMQDHSRP PQGKKSIELEKKRLSQPKAKPKKKKKPTLRTPVKLESIDGNEEESMKENSGPVENGVSDQ EGEEQAREPELPCGLAPAVSREPVICTPVSSGFEKSKVTINNKVILLKKEPPKEKPETLI KKRKARSLLPLSTSLDHRSKEELHQDCLVLATAKHSRELNEDVSADVEERFHLGLFTDRA TLYRMIDIEGKGHLENGHPELFHQLMLWKGDLKGVLQTAAERGELTDNLVAMAPAAGYHV WLWAVEAFAKQLCFQDQYVKAASHLLSIHKVYEAVELLKSNHFYREAIAIAKARLRPEDP VLKDLYLSWGTVLERDGHYAVAAKCYLGATCAYDAAKVLAKKGDAASLRTAAELAAIVGE DELSASLALRCAQELLLANNWVGAQEALQLHESLQGQRLVFCLLELLSRHLEEKQLSEGK SSSSYHTWNTGTEGPFVERVTAVWKSIFSLDTPEQYQEAFQKLQNIKYPSATNNTPAKQL LLHICHDLTLAVLSQQMASWDEAVQALLRAVVRSYDSGSFTIMQEVYSAFLPDGCDHLRD KLGDHQSPATPAFKSLEAFFLYGRLYEFWWSLSRPCPNSSVWVRAGHRTLSVEPSQQLDT ASTEETDPETSQPEPNRPSELDLRLTEEGERMLSTFKELFSEKHASLQNSQRTVAEVQET LAEMIRQHQKSQLCKSTANGPDKNEPEVEAEQPLCSSQSQCKEEKNEPLSLPELTKRLTE ANQRMAKFPESIKAWPFPDVLECCLVLLLIRSHFPGCLAQEMQQQAQELLQKYGNTKTYR RHCQTFCMCommunity curation ()Add a publicationFeedback
Protein
Gem-associated protein 5
Gene
GEMIN5
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:16857593, PubMed:18984161, PubMed:20513430, PubMed:33963192).
Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161).
To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161).
Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs) to the SMN complex (PubMed:11714716, PubMed:16857593, PubMed:19377484, PubMed:19750007, PubMed:20513430, PubMed:27834343, PubMed:27881600, PubMed:27881601, PubMed:16314521).
Binds to the 7-methylguanosine cap of RNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref. 27).
Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability (PubMed:25911097).
May play a role in the regulation of protein synthesis via its interaction with ribosomes (PubMed:27507887).
14 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682. - Ref.7"Specific sequence features, recognized by the SMN complex, identify snRNAs and determine their fate as snRNPs."
Golembe T.J., Yong J., Dreyfuss G.
Mol. Cell. Biol. 25:10989-11004(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX. - Ref.9"The Gemin5 protein of the SMN complex identifies snRNAs."
Battle D.J., Lau C.-K., Wan L., Deng H., Lotti F., Dreyfuss G.
Mol. Cell 23:273-279(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.11"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX. - Ref.14"Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains."
Lau C.K., Bachorik J.L., Dreyfuss G.
Nat. Struct. Mol. Biol. 16:486-491(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DOMAIN, RNA-BINDING REGION, SUBUNIT, MUTAGENESIS OF 271-LYS--ARG-273; TRP-286 AND HIS-290. - Ref.15"Identification of gemin5 as a novel 7-methylguanosine cap-binding protein."
Bradrick S.S., Gromeier M.
PLoS ONE 4:E7030-E7030(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX20 AND GEMIN4, MUTAGENESIS OF TRP-286. - Ref.16"Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis."
Yong J., Kasim M., Bachorik J.L., Wan L., Dreyfuss G.
Mol. Cell 38:551-562(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT. - Ref.21"Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression."
Workman E., Kalda C., Patel A., Battle D.J.
J. Biol. Chem. 290:15662-15669(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.22"The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation."
Francisco-Velilla R., Fernandez-Chamorro J., Ramajo J., Martinez-Salas E.
Nucleic Acids Res. 44:8335-8351(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIBOSOME SUBUNITS RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4, IDENTIFICATION IN THE SMN COMPLEX, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381. - Ref.24"Structural basis for specific recognition of pre-snRNA by Gemin5."
Tang X., Bharath S.R., Piao S., Tan V.Q., Bowler M.W., Song H.
Cell Res. 26:1353-1356(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-740 IN COMPLEXES WITH 7-METHYLGUANOSINE CAP AND SNRNA ANALOGS, FUNCTION, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15; PHE-381; TYR-474; LYS-641; TYR-660 AND ARG-684. - Ref.25"Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly."
Xu C., Ishikawa H., Izumikawa K., Li L., He H., Nobe Y., Yamauchi Y., Shahjee H.M., Wu X.H., Yu Y.T., Isobe T., Takahashi N., Min J.
Genes Dev. 30:2376-2390(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-739 IN COMPLEXES WITH SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15; GLU-197; PHE-381; TYR-474 AND LYS-641. - Ref.26"Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5."
Jin W., Wang Y., Liu C.P., Yang N., Jin M., Cong Y., Wang M., Xu R.M.
Genes Dev. 30:2391-2403(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-726 IN COMPLEXES WITH U4 SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, DOMAIN, FUNCTION, MUTAGENESIS OF TRP-14; TYR-15; ARG-33; ARG-335; ARG-359; PHE-381 AND TRP-422. - Ref.27"Crystal structure of Gemin5 WD40 repeats in complex with m7GpppG."
Chao X., Tempel W., Bian C., He H., Cerovina T., Bountra C., Arrowsmith C.H., Edwards A.M., Min J.
Submitted (SEP-2016) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-739 IN COMPLEX WITH 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN. - Ref.28"Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder."
Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S., Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J., Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K. , Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P., Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C., Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N., Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S., Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A., Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M., Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J., Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y., Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S., Senderek J., Pandey U.B.
Nat. Commun. 12:2558-2558(2021) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDCAM PRO-73; 94-TRP--MET-1508 DEL; ARG-105; ARG-162; TYR-210; 252-ARG--MET-1508 DEL; 534-TYR--MET-1508 DEL; MET-611; GLU-704; ARG-913; PRO-923; PHE-925; HIS-958; PHE-988; PRO-1000; THR-1007; GLU-1019; PRO-1068; SER-1119; HIS-1282; ASN-1286; CYS-1286; PRO-1364 AND PRO-1367, INVOLVEMENT IN NEDCAM, CHARACTERIZATION OF VARIANTS NEDCAM ARG-913 AND PRO-1068, FUNCTION, INTERACTION WITH DDX20 AND GEMIN4.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- mRNA 3'-UTR binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.21"Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression."
Workman E., Kalda C., Patel A., Battle D.J.
J. Biol. Chem. 290:15662-15669(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION.
- ribosome binding Source: UniProtKBInferred from direct assayi
- Ref.22"The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation."
Francisco-Velilla R., Fernandez-Chamorro J., Ramajo J., Martinez-Salas E.
Nucleic Acids Res. 44:8335-8351(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIBOSOME SUBUNITS RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4, IDENTIFICATION IN THE SMN COMPLEX, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381.
- RNA 7-methylguanosine cap binding Source: UniProtKBInferred from direct assayi
- Ref.15"Identification of gemin5 as a novel 7-methylguanosine cap-binding protein."
Bradrick S.S., Gromeier M.
PLoS ONE 4:E7030-E7030(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX20 AND GEMIN4, MUTAGENESIS OF TRP-286. - Ref.25"Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly."
Xu C., Ishikawa H., Izumikawa K., Li L., He H., Nobe Y., Yamauchi Y., Shahjee H.M., Wu X.H., Yu Y.T., Isobe T., Takahashi N., Min J.
Genes Dev. 30:2376-2390(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-739 IN COMPLEXES WITH SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15; GLU-197; PHE-381; TYR-474 AND LYS-641. - Ref.26"Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5."
Jin W., Wang Y., Liu C.P., Yang N., Jin M., Cong Y., Wang M., Xu R.M.
Genes Dev. 30:2391-2403(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-726 IN COMPLEXES WITH U4 SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, DOMAIN, FUNCTION, MUTAGENESIS OF TRP-14; TYR-15; ARG-33; ARG-335; ARG-359; PHE-381 AND TRP-422.
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- "Insights into RNA biology from an atlas of mammalian mRNA-binding proteins."
Castello A., Fischer B., Eichelbaum K., Horos R., Beckmann B.M., Strein C., Davey N.E., Humphreys D.T., Preiss T., Steinmetz L.M., Krijgsveld J., Hentze M.W.
Cell 149:1393-1406(2012) [PubMed] [Europe PMC] [Abstract]
- snRNA binding Source: UniProtKBInferred from direct assayi
- Ref.9"The Gemin5 protein of the SMN complex identifies snRNAs."
Battle D.J., Lau C.-K., Wan L., Deng H., Lotti F., Dreyfuss G.
Mol. Cell 23:273-279(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.
- U1 snRNA binding Source: UniProtKBInferred from direct assayi
- Ref.14"Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains."
Lau C.K., Bachorik J.L., Dreyfuss G.
Nat. Struct. Mol. Biol. 16:486-491(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DOMAIN, RNA-BINDING REGION, SUBUNIT, MUTAGENESIS OF 271-LYS--ARG-273; TRP-286 AND HIS-290. - Ref.15"Identification of gemin5 as a novel 7-methylguanosine cap-binding protein."
Bradrick S.S., Gromeier M.
PLoS ONE 4:E7030-E7030(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX20 AND GEMIN4, MUTAGENESIS OF TRP-286. - Ref.25"Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly."
Xu C., Ishikawa H., Izumikawa K., Li L., He H., Nobe Y., Yamauchi Y., Shahjee H.M., Wu X.H., Yu Y.T., Isobe T., Takahashi N., Min J.
Genes Dev. 30:2376-2390(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-739 IN COMPLEXES WITH SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15; GLU-197; PHE-381; TYR-474 AND LYS-641.
- U4atac snRNA binding Source: UniProtKBInferred from direct assayi
- Ref.16"Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis."
Yong J., Kasim M., Bachorik J.L., Wan L., Dreyfuss G.
Mol. Cell 38:551-562(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
- U4 snRNA binding Source: UniProtKBInferred from direct assayi
- Ref.14"Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains."
Lau C.K., Bachorik J.L., Dreyfuss G.
Nat. Struct. Mol. Biol. 16:486-491(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DOMAIN, RNA-BINDING REGION, SUBUNIT, MUTAGENESIS OF 271-LYS--ARG-273; TRP-286 AND HIS-290. - Ref.26"Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5."
Jin W., Wang Y., Liu C.P., Yang N., Jin M., Cong Y., Wang M., Xu R.M.
Genes Dev. 30:2391-2403(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-726 IN COMPLEXES WITH U4 SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, DOMAIN, FUNCTION, MUTAGENESIS OF TRP-14; TYR-15; ARG-33; ARG-335; ARG-359; PHE-381 AND TRP-422.
GO - Biological processi
- mRNA splicing, via spliceosome Source: UniProtKB
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
- protein-containing complex assembly Source: UniProtKBTraceable author statementi
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
- regulation of translation Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.21"Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression."
Workman E., Kalda C., Patel A., Battle D.J.
J. Biol. Chem. 290:15662-15669(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.22"The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation."
Francisco-Velilla R., Fernandez-Chamorro J., Ramajo J., Martinez-Salas E.
Nucleic Acids Res. 44:8335-8351(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIBOSOME SUBUNITS RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4, IDENTIFICATION IN THE SMN COMPLEX, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381.
- spliceosomal snRNP assembly Source: UniProtKBInferred from direct assayi
- Ref.11"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX.
- translation Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | RNA-binding |
| Biological process | mRNA processing, mRNA splicing, Protein biosynthesis, Translation regulation |
Enzyme and pathway databases
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | Q8TEQ6 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-191859, snRNP Assembly |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | Q8TEQ6 |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q8TEQ6 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Gem-associated protein 5Short name: Gemin5 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:GEMIN5 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:20043, GEMIN5 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 607005, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q8TEQ6 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000082516 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- nucleoplasm 1 Publication
Manual assertion based on experiment ini
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
- gem 1 Publication
Manual assertion based on experiment ini
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
- nucleoplasm 1 Publication
Cytoplasm and Cytosol
- Cytoplasm 5 Publications
Manual assertion based on experiment ini
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682. - Ref.15"Identification of gemin5 as a novel 7-methylguanosine cap-binding protein."
Bradrick S.S., Gromeier M.
PLoS ONE 4:E7030-E7030(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX20 AND GEMIN4, MUTAGENESIS OF TRP-286. - Ref.16"Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis."
Yong J., Kasim M., Bachorik J.L., Wan L., Dreyfuss G.
Mol. Cell 38:551-562(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT. - Ref.21"Gemin5 binds to the survival motor neuron mRNA to regulate SMN expression."
Workman E., Kalda C., Patel A., Battle D.J.
J. Biol. Chem. 290:15662-15669(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION. - Ref.22"The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation."
Francisco-Velilla R., Fernandez-Chamorro J., Ramajo J., Martinez-Salas E.
Nucleic Acids Res. 44:8335-8351(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIBOSOME SUBUNITS RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4, IDENTIFICATION IN THE SMN COMPLEX, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381.
Note: Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.1 Publication- Cytoplasm 5 Publications
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
Manual assertion based on experiment ini
Cytosol
- cytosol Source: UniProtKBInferred from direct assayi
- Ref.11"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX. - Ref.15"Identification of gemin5 as a novel 7-methylguanosine cap-binding protein."
Bradrick S.S., Gromeier M.
PLoS ONE 4:E7030-E7030(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX20 AND GEMIN4, MUTAGENESIS OF TRP-286. - Ref.16"Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis."
Yong J., Kasim M., Bachorik J.L., Wan L., Dreyfuss G.
Mol. Cell 38:551-562(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
- cytosol Source: UniProtKBInferred from direct assayi
Nucleus
- Gemini of coiled bodies Source: UniProtKB-SubCell
- nuclear body Source: UniProtKBInferred from direct assayi
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
- nucleoplasm Source: UniProtKBInferred from direct assayi
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
- SMN-Gemin2 complex Source: UniProtKBInferred from direct assayi
- Ref.14"Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains."
Lau C.K., Bachorik J.L., Dreyfuss G.
Nat. Struct. Mol. Biol. 16:486-491(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DOMAIN, RNA-BINDING REGION, SUBUNIT, MUTAGENESIS OF 271-LYS--ARG-273; TRP-286 AND HIS-290.
Other locations
- cytoplasm Source: UniProtKBInferred from direct assayi
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682.
- membrane Source: UniProtKBInferred from high throughput direct assayi
- "Defining the membrane proteome of NK cells."
Ghosh D., Lippert D., Krokhin O., Cortens J.P., Wilkins J.A.
J Mass Spectrom 45:1-25(2010) [PubMed] [Europe PMC] [Abstract]
- SMN complex Source: UniProtKBInferred from direct assayi
- Ref.10"A comprehensive interaction map of the human survival of motor neuron (SMN) complex."
Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.
J. Biol. Chem. 282:5825-5833(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE SMN COMPLEX, INTERACTION WITH GEMIN2. - Ref.11"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX. - Ref.16"Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis."
Yong J., Kasim M., Bachorik J.L., Wan L., Dreyfuss G.
Mol. Cell 38:551-562(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
- SMN-Sm protein complex Source: UniProtKBInferred from direct assayi
- Ref.11"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX.
- cytoplasm Source: UniProtKBInferred from direct assayi
Keywords - Cellular componenti
Cytoplasm, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Neurodevelopmental disorder with cerebellar atrophy and motor dysfunction (NEDCAM)1 PublicationManual assertion based on experiment ini
- Ref.28"Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder."
Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S., Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J., Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K. , Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P., Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C., Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N., Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S., Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A., Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M., Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J., Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y., Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S., Senderek J., Pandey U.B.
Nat. Commun. 12:2558-2558(2021) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDCAM PRO-73; 94-TRP--MET-1508 DEL; ARG-105; ARG-162; TYR-210; 252-ARG--MET-1508 DEL; 534-TYR--MET-1508 DEL; MET-611; GLU-704; ARG-913; PRO-923; PHE-925; HIS-958; PHE-988; PRO-1000; THR-1007; GLU-1019; PRO-1068; SER-1119; HIS-1282; ASN-1286; CYS-1286; PRO-1364 AND PRO-1367, INVOLVEMENT IN NEDCAM, CHARACTERIZATION OF VARIANTS NEDCAM ARG-913 AND PRO-1068, FUNCTION, INTERACTION WITH DDX20 AND GEMIN4.
Ref.28
"Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder."
Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S., Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J., Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K. , Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P., Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C., Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N., Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S., Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A., Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M., Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J., Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y., Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S., Senderek J., Pandey U.B.
Nat. Commun. 12:2558-2558(2021) [PubMed] [Europe PMC] [Abstract]
Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S., Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J., Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K. , Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P., Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C., Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N., Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S., Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A., Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M., Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J., Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y., Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S., Senderek J., Pandey U.B.
Nat. Commun. 12:2558-2558(2021) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NEDCAM PRO-73; 94-TRP--MET-1508 DEL; ARG-105; ARG-162; TYR-210; 252-ARG--MET-1508 DEL; 534-TYR--MET-1508 DEL; MET-611; GLU-704; ARG-913; PRO-923; PHE-925; HIS-958; PHE-988; PRO-1000; THR-1007; GLU-1019; PRO-1068; SER-1119; HIS-1282; ASN-1286; CYS-1286; PRO-1364 AND PRO-1367, INVOLVEMENT IN NEDCAM, CHARACTERIZATION OF VARIANTS NEDCAM ARG-913 AND PRO-1068, FUNCTION, INTERACTION WITH DDX20 AND GEMIN4.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by global developmental delay with predominantly motor abnormalities, axial hypotonia with decreased or absent reflexes, gait ataxia and appendicular spasticity. Affected individuals have cognitive impairment and speech delay. Brain imaging shows cerebellar atrophy.
Related information in OMIMMutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 14 | W → A: Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 15 | Y → A: Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 33 | R → A: Abolishes interaction with U4 snRNA. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 197 | E → A: Abolishes interaction with U4 snRNA. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 271 – 273 | KRR → AAA: No effect in interaction with U4 snRNA. No effect on interaction with SMN complex. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Mutagenesisi | 286 | W → A: Abolishes interaction with U4 snRNA. Abolishes interaction with the 7-methylguanosine cap of RNA molecules. No effect on interaction with SMN complex. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 290 | H → A: No effect in interaction with U4 snRNA. No effect on interaction with SMN complex. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 335 | R → E: Abolishes interaction with U4 snRNA. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 359 | R → A: Abolishes interaction with U4 snRNA. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 381 | F → A: Strongly decreases interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. Abolishes interaction with 80S ribosomes. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 381 | F → D: Abolishes interaction with U4 snRNA. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 422 | W → E: Abolishes interaction with U4 snRNA. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 474 | Y → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 641 | K → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 660 | Y → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 684 | R → A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNET More...DisGeNETi | 25929 |
| MIMi | 619333, phenotype |
Open Targets More...OpenTargetsi | ENSG00000082516 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134945791 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | Q8TEQ6, Tbio |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | GEMIN5 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 296439335 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000051004 | 1 – 1508 | Gem-associated protein 5Add BLAST | 1508 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 48 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 51 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 624 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 751 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 754 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| ||
| Modified residuei | 757 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 770 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 778 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 847 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q8TEQ6 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | Q8TEQ6 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | Q8TEQ6 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q8TEQ6 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q8TEQ6 |
PeptideAtlas More...PeptideAtlasi | Q8TEQ6 |
PRoteomics IDEntifications database More...PRIDEi | Q8TEQ6 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 74478 |
PTM databases
GlyGen: Computational and Informatics Resources for Glycoscience More...GlyGeni | Q8TEQ6, 2 sites, 1 O-linked glycan (2 sites) |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q8TEQ6 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q8TEQ6 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q8TEQ6 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000082516, Expressed in oocyte and 198 other tissues |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q8TEQ6, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000082516, Low tissue specificity |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:20513430, PubMed:27507887, PubMed:16314521, PubMed:19377484, PubMed:17178713). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:11714716, PubMed:20513430, PubMed:16314521).
Interacts with GEMIN2; the interaction is direct (PubMed:17178713).
Interacts with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE; the interaction is direct (PubMed:11714716).
Interacts with cytosolic DDX20/GEMIN3 and GEMIN4 (PubMed:19750007, PubMed:27507887, PubMed:33963192).
Interacts with SNRNP70 and HNRNPU (PubMed:27507887).
Identified in a complex with 80S ribosomes; binds to the 60S large ribosomal subunit (PubMed:27507887).
Interacts with the ribosomal subunits RPL3 and RPL4 (PubMed:27507887).
8 PublicationsManual assertion based on experiment ini
- Ref.1"Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins."
Gubitz A.K., Mourelatos Z., Abel L., Rappsilber J., Mann M., Dreyfuss G.
J. Biol. Chem. 277:5631-5636(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH SMN1; SNRPB; SNRPD1; SNRPD2; SNRPD3 AND SNRPE, SUBCELLULAR LOCATION, VARIANT GLN-682. - Ref.10"A comprehensive interaction map of the human survival of motor neuron (SMN) complex."
Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.
J. Biol. Chem. 282:5825-5833(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN THE SMN COMPLEX, INTERACTION WITH GEMIN2. - Ref.11"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN SMN-SM COMPLEX. - Ref.14"Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains."
Lau C.K., Bachorik J.L., Dreyfuss G.
Nat. Struct. Mol. Biol. 16:486-491(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DOMAIN, RNA-BINDING REGION, SUBUNIT, MUTAGENESIS OF 271-LYS--ARG-273; TRP-286 AND HIS-290. - Ref.15"Identification of gemin5 as a novel 7-methylguanosine cap-binding protein."
Bradrick S.S., Gromeier M.
PLoS ONE 4:E7030-E7030(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX20 AND GEMIN4, MUTAGENESIS OF TRP-286. - Ref.16"Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis."
Yong J., Kasim M., Bachorik J.L., Wan L., Dreyfuss G.
Mol. Cell 38:551-562(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT. - Ref.22"The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation."
Francisco-Velilla R., Fernandez-Chamorro J., Ramajo J., Martinez-Salas E.
Nucleic Acids Res. 44:8335-8351(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIBOSOME SUBUNITS RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4, IDENTIFICATION IN THE SMN COMPLEX, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381. - Ref.28"Loss of function mutations in GEMIN5 cause a neurodevelopmental disorder."
Kour S., Rajan D.S., Fortuna T.R., Anderson E.N., Ward C., Lee Y., Lee S., Shin Y.B., Chae J.H., Choi M., Siquier K., Cantagrel V., Amiel J., Stolerman E.S., Barnett S.S., Cousin M.A., Castro D., McDonald K. , Kirmse B., Nemeth A.H., Rajasundaram D., Innes A.M., Lynch D., Frosk P., Collins A., Gibbons M., Yang M., Desguerre I., Boddaert N., Gitiaux C., Rydning S.L., Selmer K.K., Urreizti R., Garcia-Oguiza A., Osorio A.N., Verdura E., Pujol A., McCurry H.R., Landers J.E., Agnihotri S., Andriescu E.C., Moody S.B., Phornphutkul C., Sacoto M.J.G., Begtrup A., Houlden H., Kirschner J., Schorling D., Rudnik-Schoeneborn S., Strom T.M., Leiz S., Juliette K., Richardson R., Yang Y., Zhang Y., Wang M., Wang J., Wang X., Platzer K., Donkervoort S., Boennemann C.G., Wagner M., Issa M.Y., Elbendary H.M., Stanley V., Maroofian R., Gleeson J.G., Zaki M.S., Senderek J., Pandey U.B.
Nat. Commun. 12:2558-2558(2021) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDCAM PRO-73; 94-TRP--MET-1508 DEL; ARG-105; ARG-162; TYR-210; 252-ARG--MET-1508 DEL; 534-TYR--MET-1508 DEL; MET-611; GLU-704; ARG-913; PRO-923; PHE-925; HIS-958; PHE-988; PRO-1000; THR-1007; GLU-1019; PRO-1068; SER-1119; HIS-1282; ASN-1286; CYS-1286; PRO-1364 AND PRO-1367, INVOLVEMENT IN NEDCAM, CHARACTERIZATION OF VARIANTS NEDCAM ARG-913 AND PRO-1068, FUNCTION, INTERACTION WITH DDX20 AND GEMIN4.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 33 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 284 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 335 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 359 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 381 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 422 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 426 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Sitei | 470 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Sitei | 474 | Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 556 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Sitei | 579 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Sitei | 641 | Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 660 | Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 684 | Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA moleculesCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 |
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Q8TEQ6
| With | #Exp. | IntAct |
|---|---|---|
| EIF4E [P06730] | 3 | EBI-443630,EBI-73440 |
| SMN2 [Q16637] | 7 | EBI-443630,EBI-395421 |
| SNRPE [P62304] | 3 | EBI-443630,EBI-348082 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 117429, 169 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-6031, SMN complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q8TEQ6 |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q8TEQ6 |
Protein interaction database and analysis system More...IntActi | Q8TEQ6, 68 interactors |
Molecular INTeraction database More...MINTi | Q8TEQ6 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000285873 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | Q8TEQ6, protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 6 – 8 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 19 – 23 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 24 – 26 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 27 – 32 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 35 – 42 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 43 – 45 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 49 – 51 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 53 – 60 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 67 – 72 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 81 – 86 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 87 – 89 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 91 – 95 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 96 – 99 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 100 – 105 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 112 – 117 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 119 – 121 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 124 – 129 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 132 – 138 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 139 – 141 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 143 – 148 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 154 – 159 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 166 – 171 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 176 – 180 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 181 – 183 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 187 – 191 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 198 – 203 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 205 – 207 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 208 – 212 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 241 – 246 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 249 – 255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 256 – 259 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 260 – 266 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 279 – 281 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 298 – 302 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 304 – 306 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 308 – 312 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 314 – 319 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 320 – 323 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 324 – 327 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 328 – 330 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 337 – 345 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 350 – 356 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 359 – 365 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Turni | 366 – 368 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 371 – 376 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 378 – 380 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 382 – 387 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 389 – 391 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 394 – 399 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 404 – 408 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 418 – 421 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 423 – 425 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 429 – 434 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 436 – 438 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 441 – 446 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 451 – 455 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 458 – 460 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 463 – 468 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 473 – 479 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 485 – 487 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 490 – 492 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 497 – 502 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 507 – 510 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 512 – 514 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 519 – 521 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 523 – 530 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 539 – 544 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 548 – 555 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 560 – 564 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 565 – 568 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 569 – 574 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 581 – 586 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 591 – 593 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 594 – 598 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 599 – 607 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 609 – 613 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 615 – 620 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 626 – 628 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 632 – 635 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 642 – 647 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 651 – 659 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 664 – 668 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 669 – 671 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 673 – 678 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 685 – 690 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 697 – 702 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 707 – 711 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 712 – 714 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 717 – 719 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 850 – 856 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 860 – 874 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
| Helixi | 885 – 889 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 891 – 895 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 899 – 916 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 18 | |
| Helixi | 919 – 929 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 932 – 942 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 947 – 952 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 953 – 956 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 958 – 974 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
| Helixi | 978 – 987 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 991 – 1000 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 1004 – 1014 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 1020 – 1035 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 16 | |
| Helixi | 1039 – 1048 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 1052 – 1060 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 1065 – 1078 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| Helixi | 1081 – 1095 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | Q8TEQ6 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8TEQ6 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 62 – 104 | WD 1Add BLAST | 43 | |
| Repeati | 107 – 148 | WD 2Add BLAST | 42 | |
| Repeati | 150 – 189 | WD 3Add BLAST | 40 | |
| Repeati | 193 – 264 | WD 4Add BLAST | 72 | |
| Repeati | 280 – 321 | WD 5Add BLAST | 42 | |
| Repeati | 333 – 374 | WD 6Add BLAST | 42 | |
| Repeati | 377 – 417 | WD 7Add BLAST | 41 | |
| Repeati | 424 – 464 | WD 8Add BLAST | 41 | |
| Repeati | 468 – 509 | WD 9Add BLAST | 42 | |
| Repeati | 533 – 573 | WD 10Add BLAST | 41 | |
| Repeati | 576 – 622 | WD 11Add BLAST | 47 | |
| Repeati | 637 – 677 | WD 12Add BLAST | 41 | |
| Repeati | 680 – 720 | WD 13Add BLAST | 41 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 124 | Important for interaction with U1 snRNA1 Publication Manual assertion based on experiment ini
| 124 | |
| Regioni | 13 – 15 | Interaction with U4 snRNACombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 3 | |
| Regioni | 715 – 790 | DisorderedSequence analysis <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More...</a></p> Automatic assertion according to sequence analysisi Add BLAST | 76 | |
| Regioni | 1313 – 1343 | DisorderedSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 31 | |
| Regioni | 1389 – 1428 | DisorderedSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 40 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 1362 – 1393 | Sequence analysisAdd BLAST | 32 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 721 – 735 | Basic and acidic residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 15 | |
| Compositional biasi | 750 – 769 | Basic and acidic residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 20 | |
| Compositional biasi | 1313 – 1337 | Polar residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 25 | |
| Compositional biasi | 1411 – 1425 | Polar residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 15 |
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
The WD repeat domain mediates binding to U1 snRNA and to U4 snRNA (PubMed:19377484, PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601). The WD repeat domain also mediates binding to the 7-methylguanosine cap that is found both on mRNA and snRNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref. 27). The regions that bind snRNA molecules and the isolated 7-methylguanosine cap overlap at least partially (PubMed:27834343, PubMed:27881600, PubMed:27881601). Besides, the WD repeat domain mediates interaction with the 60S large ribosomal subunit (PubMed:27507887).7 Publications
Manual assertion based on experiment ini
- Ref.14"Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains."
Lau C.K., Bachorik J.L., Dreyfuss G.
Nat. Struct. Mol. Biol. 16:486-491(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DOMAIN, RNA-BINDING REGION, SUBUNIT, MUTAGENESIS OF 271-LYS--ARG-273; TRP-286 AND HIS-290. - Ref.15"Identification of gemin5 as a novel 7-methylguanosine cap-binding protein."
Bradrick S.S., Gromeier M.
PLoS ONE 4:E7030-E7030(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX20 AND GEMIN4, MUTAGENESIS OF TRP-286. - Ref.22"The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation."
Francisco-Velilla R., Fernandez-Chamorro J., Ramajo J., Martinez-Salas E.
Nucleic Acids Res. 44:8335-8351(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH RIBOSOME SUBUNITS RPL3 AND RPL4; SNRNP70; HNRNPU; DDX20 AND GEMIN4, IDENTIFICATION IN THE SMN COMPLEX, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15 AND PHE-381. - Ref.24"Structural basis for specific recognition of pre-snRNA by Gemin5."
Tang X., Bharath S.R., Piao S., Tan V.Q., Bowler M.W., Song H.
Cell Res. 26:1353-1356(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-740 IN COMPLEXES WITH 7-METHYLGUANOSINE CAP AND SNRNA ANALOGS, FUNCTION, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15; PHE-381; TYR-474; LYS-641; TYR-660 AND ARG-684. - Ref.25"Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly."
Xu C., Ishikawa H., Izumikawa K., Li L., He H., Nobe Y., Yamauchi Y., Shahjee H.M., Wu X.H., Yu Y.T., Isobe T., Takahashi N., Min J.
Genes Dev. 30:2376-2390(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-739 IN COMPLEXES WITH SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN, MUTAGENESIS OF TRP-14; TYR-15; GLU-197; PHE-381; TYR-474 AND LYS-641. - Ref.26"Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5."
Jin W., Wang Y., Liu C.P., Yang N., Jin M., Cong Y., Wang M., Xu R.M.
Genes Dev. 30:2391-2403(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-726 IN COMPLEXES WITH U4 SNRNA FRAGMENT AND 7-METHYLGUANOSINE CAP, DOMAIN, FUNCTION, MUTAGENESIS OF TRP-14; TYR-15; ARG-33; ARG-335; ARG-359; PHE-381 AND TRP-422. - Ref.27"Crystal structure of Gemin5 WD40 repeats in complex with m7GpppG."
Chao X., Tempel W., Bian C., He H., Cerovina T., Bountra C., Arrowsmith C.H., Edwards A.M., Min J.
Submitted (SEP-2016) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-739 IN COMPLEX WITH 7-METHYLGUANOSINE CAP, FUNCTION, DOMAIN.
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the WD repeat gemin-5 family.Curated
Keywords - Domaini
Coiled coil, Repeat, WD repeatPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG502QPYZ, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00620000088064 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_004491_0_1_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q8TEQ6 |
Identification of Orthologs from Complete Genome Data More...OMAi | YWFNRND |
Database of Orthologous Groups More...OrthoDBi | 283127at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q8TEQ6 |
TreeFam database of animal gene trees More...TreeFami | TF328886 |
Family and domain databases
Database of protein disorder More...DisProti | DP03070 |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.130.10.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR024977, Apc4_WD40_dom IPR020472, G-protein_beta_WD-40_rep IPR011047, Quinoprotein_ADH-like_supfam IPR015943, WD40/YVTN_repeat-like_dom_sf IPR001680, WD40_repeat IPR019775, WD40_repeat_CS IPR036322, WD40_repeat_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF12894, ANAPC4_WD40, 2 hits PF00400, WD40, 3 hits |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00320, GPROTEINBRPT |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00320, WD40, 12 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50978, SSF50978, 1 hit SSF50998, SSF50998, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00678, WD_REPEATS_1, 3 hits PS50082, WD_REPEATS_2, 3 hits PS50294, WD_REPEATS_REGION, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
Q8TEQ6-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MGQEPRTLPP SPNWYCARCS DAVPGGLFGF AARTSVFLVR VGPGAGESPG
60 70 80 90 100
TPPFRVIGEL VGHTERVSGF TFSHHPGQYN LCATSSDDGT VKIWDVETKT
110 120 130 140 150
VVTEHALHQH TISTLHWSPR VKDLIVSGDE KGVVFCYWFN RNDSQHLFIE
160 170 180 190 200
PRTIFCLTCS PHHEDLVAIG YKDGIVVIID ISKKGEVIHR LRGHDDEIHS
210 220 230 240 250
IAWCPLPGED CLSINQEETS EEAEITNGNA VAQAPVTKGC YLATGSKDQT
260 270 280 290 300
IRIWSCSRGR GVMILKLPFL KRRGGGIDPT VKERLWLTLH WPSNQPTQLV
310 320 330 340 350
SSCFGGELLQ WDLTQSWRRK YTLFSASSEG QNHSRIVFNL CPLQTEDDKQ
360 370 380 390 400
LLLSTSMDRD VKCWDIATLE CSWTLPSLGG FAYSLAFSSV DIGSLAIGVG
410 420 430 440 450
DGMIRVWNTL SIKNNYDVKN FWQGVKSKVT ALCWHPTKEG CLAFGTDDGK
460 470 480 490 500
VGLYDTYSNK PPQISSTYHK KTVYTLAWGP PVPPMSLGGE GDRPSLALYS
510 520 530 540 550
CGGEGIVLQH NPWKLSGEAF DINKLIRDTN SIKYKLPVHT EISWKADGKI
560 570 580 590 600
MALGNEDGSI EIFQIPNLKL ICTIQQHHKL VNTISWHHEH GSQPELSYLM
610 620 630 640 650
ASGSNNAVIY VHNLKTVIES SPESPVTITE PYRTLSGHTA KITSVAWSPH
660 670 680 690 700
HDGRLVSASY DGTAQVWDAL REEPLCNFRG HRGRLLCVAW SPLDPDCIYS
710 720 730 740 750
GADDFCVHKW LTSMQDHSRP PQGKKSIELE KKRLSQPKAK PKKKKKPTLR
760 770 780 790 800
TPVKLESIDG NEEESMKENS GPVENGVSDQ EGEEQAREPE LPCGLAPAVS
810 820 830 840 850
REPVICTPVS SGFEKSKVTI NNKVILLKKE PPKEKPETLI KKRKARSLLP
860 870 880 890 900
LSTSLDHRSK EELHQDCLVL ATAKHSRELN EDVSADVEER FHLGLFTDRA
910 920 930 940 950
TLYRMIDIEG KGHLENGHPE LFHQLMLWKG DLKGVLQTAA ERGELTDNLV
960 970 980 990 1000
AMAPAAGYHV WLWAVEAFAK QLCFQDQYVK AASHLLSIHK VYEAVELLKS
1010 1020 1030 1040 1050
NHFYREAIAI AKARLRPEDP VLKDLYLSWG TVLERDGHYA VAAKCYLGAT
1060 1070 1080 1090 1100
CAYDAAKVLA KKGDAASLRT AAELAAIVGE DELSASLALR CAQELLLANN
1110 1120 1130 1140 1150
WVGAQEALQL HESLQGQRLV FCLLELLSRH LEEKQLSEGK SSSSYHTWNT
1160 1170 1180 1190 1200
GTEGPFVERV TAVWKSIFSL DTPEQYQEAF QKLQNIKYPS ATNNTPAKQL
1210 1220 1230 1240 1250
LLHICHDLTL AVLSQQMASW DEAVQALLRA VVRSYDSGSF TIMQEVYSAF
1260 1270 1280 1290 1300
LPDGCDHLRD KLGDHQSPAT PAFKSLEAFF LYGRLYEFWW SLSRPCPNSS
1310 1320 1330 1340 1350
VWVRAGHRTL SVEPSQQLDT ASTEETDPET SQPEPNRPSE LDLRLTEEGE
1360 1370 1380 1390 1400
RMLSTFKELF SEKHASLQNS QRTVAEVQET LAEMIRQHQK SQLCKSTANG
1410 1420 1430 1440 1450
PDKNEPEVEA EQPLCSSQSQ CKEEKNEPLS LPELTKRLTE ANQRMAKFPE
1460 1470 1480 1490 1500
SIKAWPFPDV LECCLVLLLI RSHFPGCLAQ EMQQQAQELL QKYGNTKTYR
RHCQTFCM
Length:1,508
Mass (Da):168,589
Last modified:May 18, 2010 - v3
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iEA5293F395BBF14E
<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence BAB84892 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 299 | L → P in BAB14222 (PubMed:14702039).Curated | 1 | |
| Sequence conflicti | 456 | T → A in BAB14222 (PubMed:14702039).Curated | 1 |