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Q8WYP5

- ELYS_HUMAN

UniProt

Q8WYP5 - ELYS_HUMAN

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Protein

Protein ELYS

Gene
AHCTF1, ELYS, TMBS62, MSTP108
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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.2 Publications

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
Complete GO annotation...

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 – 10801Phosphoserine By 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 – 12181Phosphoserine By 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 – 13711Phosphoserine By 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 981981Necessary for cytoplasmic localization By similarityAdd
BLAST
Regioni1 – 494494Seven-bladed beta propeller repeats By similarityAdd
BLAST
Regioni1019 – 22661248Disordered By similarityAdd
BLAST
Regioni1149 – 22661118Necessary for nuclear localization By similarityAdd
BLAST
Regioni1446 – 1698253Mediates transcriptional activity By 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.

Sequence similaritiesi

Belongs to the ELYS family.

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.

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. VSP_019844
Alternative sequencei1 – 11M → MAAERRCGSM in isoform 3. VSP_042691

Sequence conflict

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

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]
ENST00000391829; ENSP00000375705; ENSG00000153207. [Q8WYP5-1]
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 ]
ENST00000391829 ; ENSP00000375705 ; ENSG00000153207 . [Q8WYP5-1 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 105 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

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