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Q8WYP5

- ELYS_HUMAN

UniProt

Q8WYP5 - ELYS_HUMAN

Protein

Protein ELYS

Gene

AHCTF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (22 Sep 2009)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi1971 – 198313A.T hookAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. sequence-specific DNA binding transcription factor activity Source: Ensembl

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. mitotic cell cycle Source: Reactome
    3. mRNA transport Source: UniProtKB-KW
    4. nuclear pore complex assembly Source: UniProtKB
    5. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, mRNA transport, Protein transport, Translocation, Transport

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein ELYS
    Alternative name(s):
    Embryonic large molecule derived from yolk sac
    Protein MEL-28
    Putative AT-hook-containing transcription factor 1
    Gene namesi
    Name:AHCTF1
    Synonyms:ELYS, TMBS62
    ORF Names:MSTP108
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24618. AHCTF1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus matrix By similarity. Chromosomecentromerekinetochore. Nucleusnucleoplasm. Nucleusnuclear 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.

    GO - Cellular componenti

    1. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nuclear matrix Source: UniProtKB-SubCell
    5. nuclear membrane Source: HPA
    6. nuclear pore Source: UniProtKB-SubCell
    7. nucleoplasm Source: UniProtKB-SubCell
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Kinetochore, Nuclear pore complex, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672631.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22662266Protein ELYSPRO_0000246319Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei528 – 5281Phosphoserine3 Publications
    Modified residuei1080 – 10801PhosphoserineBy similarity
    Modified residuei1142 – 11421Phosphoserine2 Publications
    Modified residuei1150 – 11501Phosphoserine1 Publication
    Modified residuei1155 – 11551Phosphoserine1 Publication
    Modified residuei1160 – 11601Phosphoserine3 Publications
    Modified residuei1175 – 11751Phosphothreonine1 Publication
    Modified residuei1214 – 12141Phosphoserine1 Publication
    Modified residuei1218 – 12181PhosphoserineBy similarity
    Modified residuei1222 – 12221Phosphoserine1 Publication
    Modified residuei1232 – 12321Phosphoserine2 Publications
    Modified residuei1250 – 12501Phosphoserine1 Publication
    Modified residuei1283 – 12831Phosphoserine5 Publications
    Modified residuei1297 – 12971Phosphoserine1 Publication
    Modified residuei1369 – 13691Phosphothreonine1 Publication
    Modified residuei1371 – 13711PhosphoserineBy similarity
    Modified residuei1513 – 15131Phosphoserine1 Publication
    Modified residuei1517 – 15171Phosphothreonine1 Publication
    Modified residuei1533 – 15331Phosphoserine2 Publications
    Modified residuei1541 – 15411Phosphoserine5 Publications
    Modified residuei1729 – 17291Phosphoserine1 Publication
    Modified residuei1806 – 18061Phosphoserine1 Publication
    Modified residuei1808 – 18081Phosphothreonine1 Publication
    Modified residuei1878 – 18781Phosphoserine3 Publications
    Modified residuei1884 – 18841Phosphoserine2 Publications
    Modified residuei1898 – 18981Phosphoserine2 Publications
    Modified residuei1944 – 19441Phosphoserine2 Publications
    Modified residuei1946 – 19461Phosphoserine1 Publication
    Modified residuei1996 – 19961Phosphoserine1 Publication
    Modified residuei2043 – 20431Phosphoserine1 Publication
    Modified residuei2044 – 20441Phosphoserine1 Publication
    Modified residuei2060 – 20601Phosphoserine1 Publication
    Modified residuei2089 – 20891Phosphoserine1 Publication
    Modified residuei2120 – 21201Phosphoserine3 Publications
    Modified residuei2123 – 21231Phosphoserine1 Publication
    Modified residuei2154 – 21541Phosphoserine2 Publications
    Modified residuei2212 – 22121Phosphoserine2 Publications
    Modified residuei2222 – 22221Phosphoserine4 Publications
    Modified residuei2226 – 22261Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8WYP5.
    PaxDbiQ8WYP5.
    PRIDEiQ8WYP5.

    PTM databases

    PhosphoSiteiQ8WYP5.

    Miscellaneous databases

    PMAP-CutDBQ8WYP5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8WYP5.
    BgeeiQ8WYP5.
    CleanExiHS_AHCTF1.
    GenevestigatoriQ8WYP5.

    Organism-specific databases

    HPAiHPA031658.

    Interactioni

    Subunit structurei

    Associates with the Nup107-160 subcomplex of the NPC.

    Protein-protein interaction databases

    BioGridi117414. 9 interactions.
    IntActiQ8WYP5. 24 interactions.
    MINTiMINT-3308913.
    STRINGi9606.ENSP00000375705.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WYP5.
    SMRiQ8WYP5. Positions 3-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 981981Necessary for cytoplasmic localizationBy similarityAdd
    BLAST
    Regioni1 – 494494Seven-bladed beta propeller repeatsBy similarityAdd
    BLAST
    Regioni1019 – 22661248DisorderedBy similarityAdd
    BLAST
    Regioni1149 – 22661118Necessary for nuclear localizationBy similarityAdd
    BLAST
    Regioni1446 – 1698253Mediates transcriptional activityBy similarityAdd
    BLAST

    Domaini

    The N-terminus forms a highly conserved seven-bladed beta propeller decorated with long loops and mediates anchorage to the Nup107-160 subcomplex of the nuclear pore, synergistically with the central alpha domain. The disordered C-terminus is responsible for the interactions with chromatin By similarity.By similarity

    Sequence similaritiesi

    Belongs to the ELYS family.Curated
    Contains 1 A.T hook DNA-binding domain.Curated

    Phylogenomic databases

    eggNOGiNOG70776.
    OMAiFTWQVNI.
    OrthoDBiEOG7P8P72.
    PhylomeDBiQ8WYP5.
    TreeFamiTF350425.

    Family and domain databases

    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR025151. ELYS_dom.
    IPR011047. Quinonprotein_ADH-like_supfam.
    [Graphical view]
    PfamiPF13934. ELYS. 1 hit.
    [Graphical view]
    SMARTiSM00384. AT_hook. 1 hit.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WYP5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRDLRAQVTS GLLPFPEVTL QALGEDEITL ESVLRGKFAA GKNGLACLAC     50
    GPQLEVVNSI TGERLSAYRF SGVNEQPPVV LAVKEFSWQK RTGLLIGLEE 100
    TEGSVLCLYD LGISKVVKAV VLPGRVTAIE PIINHGGASA STQHLHPSLR 150
    WLFGVAAVVT DVGQILLVDL CLDDLSCNQN EVEASDLEVL TGIPAEVPHI 200
    RESVMRQGRH LCFQLVSPTG TAVSTLSYIS RTNQLAVGFS DGYLALWNMK 250
    SMKREYYIQL ESGQVPVYAV TFQEPENDPR NCCYLWAVQS TQDSEGDVLS 300
    LHLLQLAFGN RKCLASGQIL YEGLEYCEER YTLDLTGGMF PLRGQTSNTK 350
    LLGCQSIEKF RSHGDREEGV NEALSPDTSV SVFTWQVNIY GQGKPSVYLG 400
    LFDINRWYHA QMPDSLRSGE YLHNCSYFAL WSLESVVSRT SPHGILDILV 450
    HERSLNRGVP PSYPPPEQFF NPSTYNFDAT CLLNSGVVHL TCTGFQKETL 500
    TFLKKSGPSL NELIPDGYNR CLVAGLLSPR FVDVQPSSLS QEEQLEAILS 550
    AAIQTSSLGL LTGYIRRWIT EEQPNSATNL RFVLEWTWNK VVLTKEEFDR 600
    LCVPLFDGSC HFMDPQTIQS IQQCYLLLSN LNIVLSCFAS EAREITERGL 650
    IDLSNKFVVS HLICQYAQVV LWFSHSGLLP EGIDDSVQLS RLCYNYPVIQ 700
    NYYTSRRQKF ERLSRGKWNP DCLMIDGLVS QLGERIEKLW KRDEGGTGKY 750
    PPASLHAVLD MYLLDGVTEA AKHSITIYLL LDIMYSFPNK TDTPIESFPT 800
    VFAISWGQVK LIQGFWLIDH NDYESGLDLL FHPATAKPLS WQHSKIIQAF 850
    MSQGEHRQAL RYIQTMKPTV SSGNDVILHL TVLLFNRCMV EAWNFLRQHC 900
    NRLNIEELLK HMYEVCQEMG LMEDLLKLPF TDTEQECLVK FLQSSASVQN 950
    HEFLLVHHLQ RANYVPALKL NQTLKINVMN DRDPRLRERS LARNSILDQY 1000
    GKILPRVHRK LAIERAKPYH LSTSSVFRLV SRPKPLSAVP KQVVTGTVLT 1050
    RSVFINNVLS KIGEVWASKE PINSTTPFNS SKIEEPSPIV YSLPAPELPE 1100
    AFFGTPISKA SQKISRLLDL VVQPVPRPSQ CSEFIQQSSM KSPLYLVSRS 1150
    LPSSSQLKGS PQAISRASEL HLLETPLVVK KAKSLAMSVT TSGFSEFTPQ 1200
    SILRSTLRST PLASPSPSPG RSPQRLKETR ISFVEEDVHP KWIPGAADDS 1250
    KLEVFTTPKK CAVPVETEWL KSKDRTTSFF LNSPEKEHQE MDEGSQSLEK 1300
    LDVSKGNSSV SITSDETTLE YQDAPSPEDL EETVFTASKP KSSSTALTTN 1350
    VTEQTEKDGD KDVFASEVTP SDLQKQMGNL EDAETKDLLV AAEAFSELNH 1400
    LSPVQGTEAS LCAPSVYEGK IFTQKSKVPV LDEGLTSVET YTPAIRANDN 1450
    KSMADVLGDG GNSSLTISEG PIVSERRLNQ EVALNLKEDH EVEVGVLKES 1500
    VDLPEEKLPI SDSPPDTQEI HVIEQEKLEA QDSGEEARNL SFNELYPSGT 1550
    LKLQYNFDTI DQQFCDLADN KDTAECDIAE VDGELFVAQS NFTLILEGEE 1600
    GEVEPGDFAS SDVLPKAANT ATEEKLVCSG ENDNHGQIAN LPSAVTSDQK 1650
    SQKVDTLPYV PEPIKVAIAE NLLDVIKDTR SKEITSDTME QSIHETIPLV 1700
    SQNIMCPTKL VKSAFKTAQE TSTMTMNVSQ VDDVVSSKTR TRGQRIQNVN 1750
    VKSAQQEASA DVATPKMPGQ SVRKKTRKAK EISEASENIY SDVRGLSQNQ 1800
    QIPQNSVTPR RGRRKKEVNQ DILENTSSVE QELQITTGRE SKRLKSSQLL 1850
    EPAVEETTKK EVKVSSVTKR TPRRIKRSVE NQESVEIIND LKVSTVTSPS 1900
    RMIRKLRSTN LDASENTGNK QDDKSSDKQL RIKHVRRVRG REVSPSDVRE 1950
    DSNLESSQLT VQAEFDMSAI PRKRGRPRKI NPSEDVGSKA VKEERSPKKK 2000
    EAPSIRRRST RNTPAKSENV DVGKPALGKS ILVPNEELSM VMSSKKKLTK 2050
    KTESQSQKRS LHSVSEERTD EMTHKETNEQ EERLLATASF TKSSRSSRTR 2100
    SSKAILLPDL SEPNNEPLFS PASEVPRKAK AKKIEVPAQL KELVSDLSSQ 2150
    FVISPPALRS RQKNTSNKNK LEDELKDDAQ SVETLGKPKA KRIRTSKTKQ 2200
    ASKNTEKESA WSPPPIEIRL ISPLASPADG VKSKPRKTTE VTGTGLGRNR 2250
    KKLSSYPKQI LRRKML 2266
    Length:2,266
    Mass (Da):252,498
    Last modified:September 22, 2009 - v3
    Checksum:i465452FD42ACCFAE
    GO
    Isoform 2 (identifier: Q8WYP5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MDSLAGLSPREAAGVLSLSCVGVCSTCAWAWPHGSM

    Show »
    Length:2,301
    Mass (Da):256,000
    Checksum:i71D2E4A758E09BD3
    GO
    Isoform 3 (identifier: Q8WYP5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAAERRCGSM

    Show »
    Length:2,275
    Mass (Da):253,460
    Checksum:i5C8BB4E793190599
    GO

    Sequence cautioni

    The sequence AAN65622.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAQ13621.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB78516.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti168 – 1681V → I in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti207 – 2071Q → E in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti237 – 2371V → A in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti279 – 2791P → R in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti403 – 4031D → G in AAN65622. 1 PublicationCurated
    Sequence conflicti646 – 6461T → A in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti743 – 7431D → G in AAN65622. 1 PublicationCurated
    Sequence conflicti753 – 7531A → G in AAN65622. 1 PublicationCurated
    Sequence conflicti1134 – 11341F → S in AAN65622. 1 PublicationCurated
    Sequence conflicti1207 – 12071L → P in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti1270 – 12701L → P in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti1737 – 17371S → F in CAB45737. (PubMed:17974005)Curated
    Sequence conflicti1797 – 17971S → F in BAB78516. (PubMed:11952839)Curated
    Sequence conflicti1830 – 18301E → G in AAN65622. 1 PublicationCurated
    Sequence conflicti2128 – 21281K → E in AAN65622. 1 PublicationCurated
    Sequence conflicti2187 – 21871K → E in AAH12307. (PubMed:15489334)Curated
    Sequence conflicti2213 – 22131P → L in BAB78516. (PubMed:11952839)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti874 – 8741N → S.
    Corresponds to variant rs2642990 [ dbSNP | Ensembl ].
    VAR_027037
    Natural varianti2185 – 21851L → V.
    Corresponds to variant rs12410563 [ dbSNP | Ensembl ].
    VAR_027038

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MDSLAGLSPREAAGVLSLSC VGVCSTCAWAWPHGSM in isoform 2. 1 PublicationVSP_019844
    Alternative sequencei1 – 11M → MAAERRCGSM in isoform 3. 1 PublicationVSP_042691

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB059277 mRNA. Translation: BAB78516.1. Different initiation.
    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.
    CCDSiCCDS1629.2. [Q8WYP5-3]
    PIRiT12528.
    RefSeqiNP_056261.4. NM_015446.4. [Q8WYP5-3]
    XP_006711821.1. XM_006711758.1. [Q8WYP5-2]
    XP_006711822.1. XM_006711759.1. [Q8WYP5-1]
    UniGeneiHs.300887.

    Genome annotation databases

    EnsembliENST00000326225; ENSP00000355465; ENSG00000153207. [Q8WYP5-3]
    ENST00000366508; ENSP00000355464; ENSG00000153207. [Q8WYP5-2]
    GeneIDi25909.
    KEGGihsa:25909.
    UCSCiuc001ibv.2. human. [Q8WYP5-3]

    Polymorphism databases

    DMDMi259016354.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB059277 mRNA. Translation: BAB78516.1 . Different initiation.
    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 .
    CCDSi CCDS1629.2. [Q8WYP5-3 ]
    PIRi T12528.
    RefSeqi NP_056261.4. NM_015446.4. [Q8WYP5-3 ]
    XP_006711821.1. XM_006711758.1. [Q8WYP5-2 ]
    XP_006711822.1. XM_006711759.1. [Q8WYP5-1 ]
    UniGenei Hs.300887.

    3D structure databases

    ProteinModelPortali Q8WYP5.
    SMRi Q8WYP5. Positions 3-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117414. 9 interactions.
    IntActi Q8WYP5. 24 interactions.
    MINTi MINT-3308913.
    STRINGi 9606.ENSP00000375705.

    PTM databases

    PhosphoSitei Q8WYP5.

    Polymorphism databases

    DMDMi 259016354.

    Proteomic databases

    MaxQBi Q8WYP5.
    PaxDbi Q8WYP5.
    PRIDEi Q8WYP5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326225 ; ENSP00000355465 ; ENSG00000153207 . [Q8WYP5-3 ]
    ENST00000366508 ; ENSP00000355464 ; ENSG00000153207 . [Q8WYP5-2 ]
    GeneIDi 25909.
    KEGGi hsa:25909.
    UCSCi uc001ibv.2. human. [Q8WYP5-3 ]

    Organism-specific databases

    CTDi 25909.
    GeneCardsi GC01M247002.
    HGNCi HGNC:24618. AHCTF1.
    HPAi HPA031658.
    MIMi 610853. gene.
    neXtProti NX_Q8WYP5.
    PharmGKBi PA142672631.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70776.
    OMAi FTWQVNI.
    OrthoDBi EOG7P8P72.
    PhylomeDBi Q8WYP5.
    TreeFami TF350425.

    Enzyme and pathway databases

    Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_682. Mitotic Prometaphase.

    Miscellaneous databases

    ChiTaRSi AHCTF1. human.
    GeneWikii AHCTF1.
    GenomeRNAii 25909.
    NextBioi 47390.
    PMAP-CutDB Q8WYP5.
    PROi Q8WYP5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WYP5.
    Bgeei Q8WYP5.
    CleanExi HS_AHCTF1.
    Genevestigatori Q8WYP5.

    Family and domain databases

    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR025151. ELYS_dom.
    IPR011047. Quinonprotein_ADH-like_supfam.
    [Graphical view ]
    Pfami PF13934. ELYS. 1 hit.
    [Graphical view ]
    SMARTi SM00384. AT_hook. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      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.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1522-2266 (ISOFORMS 1/2/3).
      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 1/2/3).
      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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2037-2266 (ISOFORMS 1/2/3).
      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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1232; SER-1283 AND SER-1996, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2222 AND SER-2226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE NUP107-160 COMPLEX, SUBCELLULAR LOCATION.
    10. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-1222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1283; SER-1541; SER-1878; SER-2120; SER-2222 AND SER-2226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142; SER-1150; SER-1155; SER-1160; THR-1175; SER-1250; SER-1541; SER-1729; SER-1806; THR-1808; SER-1878; SER-1884; SER-1898; SER-2060; SER-2089; SER-2120; SER-2123; SER-2154 AND SER-2212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283; SER-1541; SER-1884; SER-2222 AND SER-2226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; SER-1160; SER-1232; SER-1283; SER-1297; THR-1369; SER-1513; SER-1533; SER-1541; SER-1878; SER-1898; SER-1944; SER-1946; SER-2043; SER-2044; SER-2120; SER-2154; SER-2212; SER-2222 AND SER-2226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1142; SER-1160; SER-1214; SER-1283; THR-1517; SER-1533; SER-1541 AND SER-1944, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiELYS_HUMAN
    AccessioniPrimary (citable) accession number: Q8WYP5
    Secondary accession number(s): A6NGM0
    , A8MSG9, A8MZ86, Q7Z4E3, Q8IZA4, Q96EH9, Q9Y4Q6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3