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Reviewed, UniProtKB/Swiss-Prot Q8WYP5 (ELYS_HUMAN)

Last modified December 15, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Name: AHCTF1
Synonyms: ELYS, TMBS62
ORF Names: MSTP108
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2266 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.10 Ref.11

Subunit structure

Associates with the Nup107-160 subcomplex of the NPC.

Subcellular location

Cytoplasm By similarity. Nucleus matrix By similarity. Kinetochore. 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.

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.

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 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
Region1149 – 22661118Necessary for nuclear localization By similarity
Region1446 – 1698253Mediates transcriptional activity By similarity

Amino acid modifications

Modified residue5281Phosphoserine Ref.9 Ref.14 Ref.15
Modified residue10171N6-acetyllysine Ref.17
Modified residue10871Phosphoserine Ref.9
Modified residue11421Phosphoserine Ref.15
Modified residue11501Phosphoserine Ref.15
Modified residue11551Phosphoserine Ref.15
Modified residue11601Phosphoserine Ref.13 Ref.15
Modified residue11751Phosphothreonine Ref.15
Modified residue12161Phosphoserine Ref.14
Modified residue12181Phosphoserine Ref.14
Modified residue12221Phosphoserine Ref.14
Modified residue12321Phosphoserine Ref.7 Ref.9 Ref.13 Ref.15
Modified residue12501Phosphoserine Ref.15
Modified residue12571Phosphothreonine Ref.15
Modified residue12831Phosphoserine Ref.7 Ref.9 Ref.12 Ref.15
Modified residue12951Phosphoserine Ref.12
Modified residue13711Phosphoserine By similarity
Modified residue14021Phosphoserine Ref.13
Modified residue15111Phosphoserine Ref.13
Modified residue15131Phosphoserine Ref.7 Ref.9
Modified residue15411Phosphoserine Ref.7 Ref.9 Ref.15
Modified residue16201Phosphothreonine Ref.13
Modified residue16921Phosphoserine Ref.13
Modified residue17291Phosphoserine Ref.15
Modified residue17371Phosphoserine Ref.13
Modified residue17641Phosphothreonine Ref.13
Modified residue17711Phosphoserine Ref.13
Modified residue18061Phosphoserine Ref.15
Modified residue18081Phosphothreonine Ref.14 Ref.15
Modified residue18781Phosphoserine Ref.15
Modified residue18841Phosphoserine Ref.15
Modified residue18981Phosphoserine Ref.13 Ref.15
Modified residue19441Phosphoserine Ref.13 Ref.14
Modified residue19521Phosphoserine Ref.13
Modified residue19961Phosphoserine Ref.7
Modified residue20601Phosphoserine Ref.13 Ref.15
Modified residue20631Phosphoserine Ref.13
Modified residue20891Phosphoserine Ref.15
Modified residue21201Phosphoserine Ref.15
Modified residue21231Phosphoserine Ref.15
Modified residue21541Phosphoserine Ref.15
Modified residue22121Phosphoserine Ref.9 Ref.15
Modified residue22221Phosphoserine Ref.7 Ref.8 Ref.9 Ref.13 Ref.15
Modified residue22261Phosphoserine Ref.7 Ref.8 Ref.13 Ref.15
Modified residue22381Phosphothreonine Ref.13
Modified residue22421Phosphothreonine Ref.13
Modified residue22541Phosphoserine Ref.13

Natural variations

Alternative sequence11M → MDSLAGLSPREAAGVLSLSC VGVCSTCAWAWPHGSM in isoform 2.
VSP_019844
Natural variant8741N → S: dbSNP rs2642990.
VAR_027037
Natural variant21851L → V: dbSNP rs12410563.
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.

Checksum: 71D2E4A758E09BD3
Show »

FASTA2,301256,000

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. 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: 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.
IPIIPI00170594.
IPI00878213.
PIRT12528.
UniGeneHs.300887

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8WYP5.

PTM databases

PhosphoSiteQ8WYP5.

Proteomic databases

PRIDEQ8WYP5.

Genome annotation databases

EnsemblENST00000283201; 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]
KEGGhsa:25909.
UCSCuc001ibv.1. human.

Organism-specific databases

CTD25909.
GeneCardsGC01M245069.
H-InvDBHIX0002544.
HGNCHGNC:24618. AHCTF1.
MIM610853. gene.
PharmGKBPA142672631.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8WYP5.
OrthoDBEOG9R52N1.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressQ8WYP5.
BgeeQ8WYP5.
CleanExHS_AHCTF1.
GenevestigatorQ8WYP5.
GermOnlineENSG00000153207. Homo sapiens.

Family and domain databases

InterProIPR017956. AT_hook_DNA-bd_motif.
[Graphical view]
PfamPF02178. AT_hook. 1 hit.
[Graphical view]
SMARTSM00384. AT_hook. 1 hit.
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NextBio47390.
PMAP-CutDBQ8WYP5.
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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: December 15, 2009
This is version 63 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents