Reviewed,
UniProtKB/Swiss-Prot Q8WYP5 (ELYS_HUMAN)
Last modified
December 15, 2009.
Version 63.
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90%,
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Documents (5) |
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Names and origin
| Protein names | Recommended name: Protein ELYS Alternative name(s): Protein MEL-28 Putative AT-hook-containing transcription factor 1 Embryonic large molecule derived from yolk sac | ||||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete 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 | 2266 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. Ref.10 Ref.11 |
| Subunit structure | Associates with the Nup107-160 subcomplex of the NPC. |
| Subcellular location | Cytoplasm By similarity. Nucleus matrix By similarity. Kinetochore. Nucleus › nucleoplasm. Nucleus › nuclear pore complex. Note: Localizes to the nuclear pore complex (NPC) throughout interphase. Localizes to the kinetochore from prophase, and this appears to require the Nup107-160 subcomplex of the NPC. Localizes to the periphery of chromatin from late anaphase. |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 |
| Sequence similarities | Belongs to the ELYS family. Contains 1 A.T hook DNA-binding domain. |
| Sequence caution | The sequence AAN65622.1 differs from that shown. Reason: Frameshift at several positions. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8WYP5-1) 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: Q8WYP5-2) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MDSLAGLSPREAAGVLSLSCVGVCSTCAWAWPHGSM |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2266 | 2266 | Protein ELYS | PRO_0000246319 | |||||
Regions | |||||||||
| DNA binding | 1971 – 1983 | 13 | A.T hook | ||||||
| Region | 1 – 981 | 981 | Necessary for cytoplasmic localization By similarity | ||||||
| Region | 1149 – 2266 | 1118 | Necessary for nuclear localization By similarity | ||||||
| Region | 1446 – 1698 | 253 | Mediates transcriptional activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 528 | 1 | Phosphoserine Ref.9 Ref.14 Ref.15 | ||||||
| Modified residue | 1017 | 1 | N6-acetyllysine Ref.17 | ||||||
| Modified residue | 1087 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 1142 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1150 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1155 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1160 | 1 | Phosphoserine Ref.13 Ref.15 | ||||||
| Modified residue | 1175 | 1 | Phosphothreonine Ref.15 | ||||||
| Modified residue | 1216 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 1218 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 1222 | 1 | Phosphoserine Ref.14 | ||||||
| Modified residue | 1232 | 1 | Phosphoserine Ref.7 Ref.9 Ref.13 Ref.15 | ||||||
| Modified residue | 1250 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1257 | 1 | Phosphothreonine Ref.15 | ||||||
| Modified residue | 1283 | 1 | Phosphoserine Ref.7 Ref.9 Ref.12 Ref.15 | ||||||
| Modified residue | 1295 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1371 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1402 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1511 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1513 | 1 | Phosphoserine Ref.7 Ref.9 | ||||||
| Modified residue | 1541 | 1 | Phosphoserine Ref.7 Ref.9 Ref.15 | ||||||
| Modified residue | 1620 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 1692 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1729 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1737 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1764 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 1771 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1806 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1808 | 1 | Phosphothreonine Ref.14 Ref.15 | ||||||
| Modified residue | 1878 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1884 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 1898 | 1 | Phosphoserine Ref.13 Ref.15 | ||||||
| Modified residue | 1944 | 1 | Phosphoserine Ref.13 Ref.14 | ||||||
| Modified residue | 1952 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1996 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 2060 | 1 | Phosphoserine Ref.13 Ref.15 | ||||||
| Modified residue | 2063 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 2089 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 2120 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 2123 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 2154 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 2212 | 1 | Phosphoserine Ref.9 Ref.15 | ||||||
| Modified residue | 2222 | 1 | Phosphoserine Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 | ||||||
| Modified residue | 2226 | 1 | Phosphoserine Ref.7 Ref.8 Ref.13 Ref.15 | ||||||
| Modified residue | 2238 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 2242 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 2254 | 1 | Phosphoserine Ref.13 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 | 1 | M → MDSLAGLSPREAAGVLSLSC VGVCSTCAWAWPHGSM in isoform 2. | VSP_019844 | |||||
| Natural variant | 874 | 1 | N → S: dbSNP rs2642990. | VAR_027037 | |||||
| Natural variant | 2185 | 1 | L → V: dbSNP rs12410563. | VAR_027038 | |||||
Experimental info | |||||||||
| Sequence conflict | 168 | 1 | V → I in BAB78516. Ref.1 | ||||||
| Sequence conflict | 207 | 1 | Q → E in BAB78516. Ref.1 | ||||||
| Sequence conflict | 237 | 1 | V → A in BAB78516. Ref.1 | ||||||
| Sequence conflict | 279 | 1 | P → R in BAB78516. Ref.1 | ||||||
| Sequence conflict | 403 | 1 | D → G in AAN65622. Ref.2 | ||||||
| Sequence conflict | 646 | 1 | T → A in BAB78516. Ref.1 | ||||||
| Sequence conflict | 743 | 1 | D → G in AAN65622. Ref.2 | ||||||
| Sequence conflict | 753 | 1 | A → G in AAN65622. Ref.2 | ||||||
| Sequence conflict | 1134 | 1 | F → S in AAN65622. Ref.2 | ||||||
| Sequence conflict | 1207 | 1 | L → P in BAB78516. Ref.1 | ||||||
| Sequence conflict | 1270 | 1 | L → P in BAB78516. Ref.1 | ||||||
| Sequence conflict | 1737 | 1 | S → F in CAB45737. Ref.4 | ||||||
| Sequence conflict | 1797 | 1 | S → F in BAB78516. Ref.1 | ||||||
| Sequence conflict | 1830 | 1 | E → G in AAN65622. Ref.2 | ||||||
| Sequence conflict | 2128 | 1 | K → E in AAN65622. Ref.2 | ||||||
| Sequence conflict | 2187 | 1 | K → E in AAH12307. Ref.6 | ||||||
| Sequence conflict | 2213 | 1 | P → L in BAB78516. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Identification of a novel transcription factor, ELYS, expressed predominantly in mouse foetal haematopoietic tissues." Kimura N., Takizawa M., Okita K., Natori O., Igarashi K., Ueno M., Nakashima K., Nobuhisa I., Taga T. Genes Cells 7:435-446(2002) [PubMed: 11952839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fetal liver. |
| [2] | "Cloning of a cDNA that provides partial correction of mitomycin C sensitivity in Fanconi anemia FA-D1 cells." Lightfoot J., Alon N., Buchwald M. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Lymphoblast. |
| [3] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1522-2266 (ISOFORMS 1/2). Tissue: Testis. |
| [5] | Liu B., Zhao B., Wang X.Y., Liu Y.Q., Sheng H., Qin B.M., Zhang Q., Zheng W.Y., Xu H.S., Liu B.H., Lu H., Gong Q., Hui R.T. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1753-2266 (ISOFORMS 1/2). Tissue: Heart. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2037-2266 (ISOFORMS 1/2). Tissue: Retinoblastoma. |
| [7] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232; SER-1283; SER-1513; SER-1541; SER-1996; SER-2222 AND SER-2226, MASS SPECTROMETRY. Tissue: Epithelium. |
| [8] | "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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2222 AND SER-2226, MASS SPECTROMETRY. Tissue: Epithelium. |
| [9] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1087; SER-1232; SER-1283; SER-1513; SER-1541; SER-2212 AND SER-2222, MASS SPECTROMETRY. Tissue: Epithelium. |
| [10] | "ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division." Rasala B.A., Orjalo A.V., Shen Z., Briggs S., Forbes D.J. Proc. Natl. Acad. Sci. U.S.A. 103:17801-17806(2006) [PubMed: 17098863] [Abstract] Cited for: FUNCTION, ASSOCIATION WITH THE NUP107-160 COMPLEX, SUBCELLULAR LOCATION. |
| [11] | "MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly." Franz C., Walczak R., Yavuz S., Santarella R., Gentzel M., Askjaer P., Galy V., Hetzer M., Mattaj I.W., Antonin W. EMBO Rep. 8:165-172(2007) [PubMed: 17235358] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. |
| [12] | "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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283 AND SER-1295, MASS SPECTROMETRY. |
| [13] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160; SER-1232; SER-1402; SER-1511; THR-1620; SER-1692; SER-1737; THR-1764; SER-1771; SER-1898; SER-1944; SER-1952; SER-2060; SER-2063; SER-2222; SER-2226; THR-2238; THR-2242 AND SER-2254, MASS SPECTROMETRY. |
| [14] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1216; SER-1218; SER-1222; THR-1808 AND SER-1944, MASS SPECTROMETRY. |
| [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1142; SER-1150; SER-1155; SER-1160; THR-1175; SER-1232; SER-1250; THR-1257; SER-1283; SER-1541; SER-1729; SER-1806; THR-1808; SER-1878; SER-1884; SER-1898; SER-2060; SER-2089; SER-2120; SER-2123; SER-2154; SER-2212; SER-2222 AND SER-2226, MASS SPECTROMETRY. |
| [16] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283; SER-1541; SER-1878; SER-1884; SER-2222 AND SER-2226, MASS SPECTROMETRY. Tissue: T-cell. |
| [17] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1017, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AB059277 mRNA. Translation: BAB78516.1. AY157619 mRNA. Translation: AAN65622.1. Frameshift. AC113174 Genomic DNA. No translation available. AL080144 mRNA. Translation: CAB45737.1. AF173978 mRNA. Translation: AAQ13621.1. Different initiation. BC012307 mRNA. Translation: AAH12307.1. | |
| IPI | IPI00170594. IPI00878213. |
| PIR | T12528. |
| UniGene | Hs.300887 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8WYP5. |
PTM databases | |
| PhosphoSite | Q8WYP5. |
Proteomic databases | |
| PRIDE | Q8WYP5. |
Genome annotation databases | |
| Ensembl | ENST00000283201; ENSP00000283201; ENSG00000153207; Homo sapiens. [Genome view] ENST00000326225; ENSP00000355465; ENSG00000153207; Homo sapiens. [Genome view] ENST00000361182; ENSP00000354780; ENSG00000153207; Homo sapiens. [Genome view] ENST00000366508; ENSP00000355464; ENSG00000153207; Homo sapiens. [Genome view] ENST00000391829; ENSP00000375705; ENSG00000153207; Homo sapiens. [Genome view] ENST00000428671; ENSP00000394728; ENSG00000153207; Homo sapiens. [Genome view] |
| KEGG | hsa:25909. |
| UCSC | uc001ibv.1. human. |
Organism-specific databases | |
| CTD | 25909. |
| GeneCards | GC01M245069. |
| H-InvDB | HIX0002544. |
| HGNC | HGNC:24618. AHCTF1. |
| MIM | 610853. gene. |
| PharmGKB | PA142672631. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q8WYP5. |
| OrthoDB | EOG9R52N1. |
Enzyme and pathway databases | |
| Reactome | REACT_152. Cell Cycle, Mitotic. |
Gene expression databases | |
| ArrayExpress | Q8WYP5. |
| Bgee | Q8WYP5. |
| CleanEx | HS_AHCTF1. |
| Genevestigator | Q8WYP5. |
| GermOnline | ENSG00000153207. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR017956. AT_hook_DNA-bd_motif. [Graphical view] |
| Pfam | PF02178. AT_hook. 1 hit. [Graphical view] |
| SMART | SM00384. AT_hook. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 47390. |
| PMAP-CutDB | Q8WYP5. |
| SOURCE | Search... |
Entry information
| Entry name | ELYS_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8WYP5 Secondary accession number(s): A6NGM0 Q9Y4Q6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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 chromosome 1 Human chromosome 1: 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


