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Q8WYP5 (ELYS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein ELYS
Alternative name(s):
Embryonic large molecule derived from yolk sac
Protein MEL-28
Putative AT-hook-containing transcription factor 1
Gene names
Name:AHCTF1
Synonyms:ELYS, TMBS62
ORF Names:MSTP108
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2266 AA.
Sequence statusComplete.
Protein existenceEvidence 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.9 Ref.10

Subunit structure

Associates with the Nup107-160 subcomplex of the NPC.

Subcellular location

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. Ref.9 Ref.10

Domain

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 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.

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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
mRNA transport
Protein transport
Translocation
Transport
   Cellular componentCentromere
Chromosome
Cytoplasm
Kinetochore
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

nuclear pore complex assembly

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear pore

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 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
Isoform 3 (identifier: Q8WYP5-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22662266Protein ELYS
PRO_0000246319

Regions

DNA binding1971 – 198313A.T hook
Region1 – 981981Necessary for cytoplasmic localization By similarity
Region1 – 494494Seven-bladed beta propeller repeats By similarity
Region1019 – 22661248Disordered By similarity
Region1149 – 22661118Necessary for nuclear localization By similarity
Region1446 – 1698253Mediates transcriptional activity By similarity

Amino acid modifications

Modified residue5281Phosphoserine Ref.11 Ref.12 Ref.16
Modified residue10801Phosphoserine By similarity
Modified residue11421Phosphoserine Ref.13 Ref.17
Modified residue11501Phosphoserine Ref.13
Modified residue11551Phosphoserine Ref.13
Modified residue11601Phosphoserine Ref.13 Ref.16 Ref.17
Modified residue11751Phosphothreonine Ref.13
Modified residue12141Phosphoserine Ref.17
Modified residue12181Phosphoserine By similarity
Modified residue12221Phosphoserine Ref.11
Modified residue12321Phosphoserine Ref.7 Ref.16
Modified residue12501Phosphoserine Ref.13
Modified residue12831Phosphoserine Ref.7 Ref.12 Ref.15 Ref.16 Ref.17
Modified residue12971Phosphoserine Ref.16
Modified residue13691Phosphothreonine Ref.16
Modified residue13711Phosphoserine By similarity
Modified residue15131Phosphoserine Ref.16
Modified residue15171Phosphothreonine Ref.17
Modified residue15331Phosphoserine Ref.16 Ref.17
Modified residue15411Phosphoserine Ref.12 Ref.13 Ref.15 Ref.16 Ref.17
Modified residue17291Phosphoserine Ref.13
Modified residue18061Phosphoserine Ref.13
Modified residue18081Phosphothreonine Ref.13
Modified residue18781Phosphoserine Ref.12 Ref.13 Ref.16
Modified residue18841Phosphoserine Ref.13 Ref.15
Modified residue18981Phosphoserine Ref.13 Ref.16
Modified residue19441Phosphoserine Ref.16 Ref.17
Modified residue19461Phosphoserine Ref.16
Modified residue19961Phosphoserine Ref.7
Modified residue20431Phosphoserine Ref.16
Modified residue20441Phosphoserine Ref.16
Modified residue20601Phosphoserine Ref.13
Modified residue20891Phosphoserine Ref.13
Modified residue21201Phosphoserine Ref.12 Ref.13 Ref.16
Modified residue21231Phosphoserine Ref.13
Modified residue21541Phosphoserine Ref.13 Ref.16
Modified residue22121Phosphoserine Ref.13 Ref.16
Modified residue22221Phosphoserine Ref.8 Ref.12 Ref.15 Ref.16
Modified residue22261Phosphoserine Ref.8 Ref.12 Ref.15 Ref.16

Natural variations

Alternative sequence11M → MDSLAGLSPREAAGVLSLSC VGVCSTCAWAWPHGSM in isoform 2.
VSP_019844
Alternative sequence11M → MAAERRCGSM in isoform 3.
VSP_042691
Natural variant8741N → S.
Corresponds to variant rs2642990 [ dbSNP | Ensembl ].
VAR_027037
Natural variant21851L → V.
Corresponds to variant rs12410563 [ dbSNP | Ensembl ].
VAR_027038

Experimental info

Sequence conflict1681V → I in BAB78516. Ref.1
Sequence conflict2071Q → E in BAB78516. Ref.1
Sequence conflict2371V → A in BAB78516. Ref.1
Sequence conflict2791P → R in BAB78516. Ref.1
Sequence conflict4031D → G in AAN65622. Ref.2
Sequence conflict6461T → A in BAB78516. Ref.1
Sequence conflict7431D → G in AAN65622. Ref.2
Sequence conflict7531A → G in AAN65622. Ref.2
Sequence conflict11341F → S in AAN65622. Ref.2
Sequence conflict12071L → P in BAB78516. Ref.1
Sequence conflict12701L → P in BAB78516. Ref.1
Sequence conflict17371S → F in CAB45737. Ref.4
Sequence conflict17971S → F in BAB78516. Ref.1
Sequence conflict18301E → G in AAN65622. Ref.2
Sequence conflict21281K → E in AAN65622. Ref.2
Sequence conflict21871K → E in AAH12307. Ref.6
Sequence conflict22131P → L in BAB78516. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: 465452FD42ACCFAE

FASTA2,266252,498
        10         20         30         40         50         60 
MRDLRAQVTS GLLPFPEVTL QALGEDEITL ESVLRGKFAA GKNGLACLAC GPQLEVVNSI 

        70         80         90        100        110        120 
TGERLSAYRF SGVNEQPPVV LAVKEFSWQK RTGLLIGLEE TEGSVLCLYD LGISKVVKAV 

       130        140        150        160        170        180 
VLPGRVTAIE PIINHGGASA STQHLHPSLR WLFGVAAVVT DVGQILLVDL CLDDLSCNQN 

       190        200        210        220        230        240 
EVEASDLEVL TGIPAEVPHI RESVMRQGRH LCFQLVSPTG TAVSTLSYIS RTNQLAVGFS 

       250        260        270        280        290        300 
DGYLALWNMK SMKREYYIQL ESGQVPVYAV TFQEPENDPR NCCYLWAVQS TQDSEGDVLS 

       310        320        330        340        350        360 
LHLLQLAFGN RKCLASGQIL YEGLEYCEER YTLDLTGGMF PLRGQTSNTK LLGCQSIEKF 

       370        380        390        400        410        420 
RSHGDREEGV NEALSPDTSV SVFTWQVNIY GQGKPSVYLG LFDINRWYHA QMPDSLRSGE 

       430        440        450        460        470        480 
YLHNCSYFAL WSLESVVSRT SPHGILDILV HERSLNRGVP PSYPPPEQFF NPSTYNFDAT 

       490        500        510        520        530        540 
CLLNSGVVHL TCTGFQKETL TFLKKSGPSL NELIPDGYNR CLVAGLLSPR FVDVQPSSLS 

       550        560        570        580        590        600 
QEEQLEAILS AAIQTSSLGL LTGYIRRWIT EEQPNSATNL RFVLEWTWNK VVLTKEEFDR 

       610        620        630        640        650        660 
LCVPLFDGSC HFMDPQTIQS IQQCYLLLSN LNIVLSCFAS EAREITERGL IDLSNKFVVS 

       670        680        690        700        710        720 
HLICQYAQVV LWFSHSGLLP EGIDDSVQLS RLCYNYPVIQ NYYTSRRQKF ERLSRGKWNP 

       730        740        750        760        770        780 
DCLMIDGLVS QLGERIEKLW KRDEGGTGKY PPASLHAVLD MYLLDGVTEA AKHSITIYLL 

       790        800        810        820        830        840 
LDIMYSFPNK TDTPIESFPT VFAISWGQVK LIQGFWLIDH NDYESGLDLL FHPATAKPLS 

       850        860        870        880        890        900 
WQHSKIIQAF MSQGEHRQAL RYIQTMKPTV SSGNDVILHL TVLLFNRCMV EAWNFLRQHC 

       910        920        930        940        950        960 
NRLNIEELLK HMYEVCQEMG LMEDLLKLPF TDTEQECLVK FLQSSASVQN HEFLLVHHLQ 

       970        980        990       1000       1010       1020 
RANYVPALKL NQTLKINVMN DRDPRLRERS LARNSILDQY GKILPRVHRK LAIERAKPYH 

      1030       1040       1050       1060       1070       1080 
LSTSSVFRLV SRPKPLSAVP KQVVTGTVLT RSVFINNVLS KIGEVWASKE PINSTTPFNS 

      1090       1100       1110       1120       1130       1140 
SKIEEPSPIV YSLPAPELPE AFFGTPISKA SQKISRLLDL VVQPVPRPSQ CSEFIQQSSM 

      1150       1160       1170       1180       1190       1200 
KSPLYLVSRS LPSSSQLKGS PQAISRASEL HLLETPLVVK KAKSLAMSVT TSGFSEFTPQ 

      1210       1220       1230       1240       1250       1260 
SILRSTLRST PLASPSPSPG RSPQRLKETR ISFVEEDVHP KWIPGAADDS KLEVFTTPKK 

      1270       1280       1290       1300       1310       1320 
CAVPVETEWL KSKDRTTSFF LNSPEKEHQE MDEGSQSLEK LDVSKGNSSV SITSDETTLE 

      1330       1340       1350       1360       1370       1380 
YQDAPSPEDL EETVFTASKP KSSSTALTTN VTEQTEKDGD KDVFASEVTP SDLQKQMGNL 

      1390       1400       1410       1420       1430       1440 
EDAETKDLLV AAEAFSELNH LSPVQGTEAS LCAPSVYEGK IFTQKSKVPV LDEGLTSVET 

      1450       1460       1470       1480       1490       1500 
YTPAIRANDN KSMADVLGDG GNSSLTISEG PIVSERRLNQ EVALNLKEDH EVEVGVLKES 

      1510       1520       1530       1540       1550       1560 
VDLPEEKLPI SDSPPDTQEI HVIEQEKLEA QDSGEEARNL SFNELYPSGT LKLQYNFDTI 

      1570       1580       1590       1600       1610       1620 
DQQFCDLADN KDTAECDIAE VDGELFVAQS NFTLILEGEE GEVEPGDFAS SDVLPKAANT 

      1630       1640       1650       1660       1670       1680 
ATEEKLVCSG ENDNHGQIAN LPSAVTSDQK SQKVDTLPYV PEPIKVAIAE NLLDVIKDTR 

      1690       1700       1710       1720       1730       1740 
SKEITSDTME QSIHETIPLV SQNIMCPTKL VKSAFKTAQE TSTMTMNVSQ VDDVVSSKTR 

      1750       1760       1770       1780       1790       1800 
TRGQRIQNVN VKSAQQEASA DVATPKMPGQ SVRKKTRKAK EISEASENIY SDVRGLSQNQ 

      1810       1820       1830       1840       1850       1860 
QIPQNSVTPR RGRRKKEVNQ DILENTSSVE QELQITTGRE SKRLKSSQLL EPAVEETTKK 

      1870       1880       1890       1900       1910       1920 
EVKVSSVTKR TPRRIKRSVE NQESVEIIND LKVSTVTSPS RMIRKLRSTN LDASENTGNK 

      1930       1940       1950       1960       1970       1980 
QDDKSSDKQL RIKHVRRVRG REVSPSDVRE DSNLESSQLT VQAEFDMSAI PRKRGRPRKI 

      1990       2000       2010       2020       2030       2040 
NPSEDVGSKA VKEERSPKKK EAPSIRRRST RNTPAKSENV DVGKPALGKS ILVPNEELSM 

      2050       2060       2070       2080       2090       2100 
VMSSKKKLTK KTESQSQKRS LHSVSEERTD EMTHKETNEQ EERLLATASF TKSSRSSRTR 

      2110       2120       2130       2140       2150       2160 
SSKAILLPDL SEPNNEPLFS PASEVPRKAK AKKIEVPAQL KELVSDLSSQ FVISPPALRS 

      2170       2180       2190       2200       2210       2220 
RQKNTSNKNK LEDELKDDAQ SVETLGKPKA KRIRTSKTKQ ASKNTEKESA WSPPPIEIRL 

      2230       2240       2250       2260 
ISPLASPADG VKSKPRKTTE VTGTGLGRNR KKLSSYPKQI LRRKML 

« Hide

Isoform 2 [UniParc].

Checksum: 71D2E4A758E09BD3
Show »

FASTA2,301256,000
Isoform 3 [UniParc].

Checksum: 5C8BB4E793190599
Show »

FASTA2,275253,460

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] [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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1629.2. [Q8WYP5-3]
PIRT12528.
RefSeqNP_056261.4. NM_015446.4. [Q8WYP5-3]
XP_006711821.1. XM_006711758.1. [Q8WYP5-2]
XP_006711822.1. XM_006711759.1. [Q8WYP5-1]
UniGeneHs.300887.

3D structure databases

ProteinModelPortalQ8WYP5.
SMRQ8WYP5. Positions 3-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117414. 9 interactions.
IntActQ8WYP5. 24 interactions.
MINTMINT-3308913.
STRING9606.ENSP00000375705.

PTM databases

PhosphoSiteQ8WYP5.

Polymorphism databases

DMDM259016354.

Proteomic databases

MaxQBQ8WYP5.
PaxDbQ8WYP5.
PRIDEQ8WYP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326225; ENSP00000355465; ENSG00000153207. [Q8WYP5-3]
ENST00000366508; ENSP00000355464; ENSG00000153207. [Q8WYP5-2]
ENST00000391829; ENSP00000375705; ENSG00000153207. [Q8WYP5-1]
GeneID25909.
KEGGhsa:25909.
UCSCuc001ibv.2. human. [Q8WYP5-3]

Organism-specific databases

CTD25909.
GeneCardsGC01M247002.
HGNCHGNC:24618. AHCTF1.
HPAHPA031658.
MIM610853. gene.
neXtProtNX_Q8WYP5.
PharmGKBPA142672631.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70776.
OMAFTWQVNI.
OrthoDBEOG7P8P72.
PhylomeDBQ8WYP5.
TreeFamTF350425.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ8WYP5.
BgeeQ8WYP5.
CleanExHS_AHCTF1.
GenevestigatorQ8WYP5.

Family and domain databases

InterProIPR017956. AT_hook_DNA-bd_motif.
IPR025151. ELYS_dom.
IPR011047. Quinonprotein_ADH-like_supfam.
[Graphical view]
PfamPF13934. ELYS. 1 hit.
[Graphical view]
SMARTSM00384. AT_hook. 1 hit.
[Graphical view]
SUPFAMSSF50998. SSF50998. 2 hits.
ProtoNetSearch...

Other

ChiTaRSAHCTF1. human.
GeneWikiAHCTF1.
GenomeRNAi25909.
NextBio47390.
PMAP-CutDBQ8WYP5.
PROQ8WYP5.
SOURCESearch...

Entry information

Entry nameELYS_HUMAN
AccessionPrimary (citable) accession number: Q8WYP5
Secondary accession number(s): A6NGM0 expand/collapse secondary AC list , A8MSG9, A8MZ86, Q7Z4E3, Q8IZA4, Q96EH9, Q9Y4Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM