Q8WYP5 (ELYS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	AHCTF1
Synonyms:	ELYS, TMBS62
ORF Names:	MSTP108

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2266 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the assembly of a functional nuclear pore complex (NPC) on the surface of chromosomes as nuclei form at the end of mitosis. May initiate NPC assembly by binding to chromatin and recruiting the Nup107-160 subcomplex of the NPC. Also required for the localization of the Nup107-160 subcomplex of the NPC to the kinetochore during mitosis and for the completion of cytokinesis. Ref.10 Ref.11
Subunit structure	Associates with the Nup107-160 subcomplex of the NPC.
Subcellular location	Cytoplasm By similarity. Nucleus matrix By similarity. Chromosome › centromere › kinetochore. Nucleus › nucleoplasm. Nucleus › nuclear pore complex. Note: Localizes to the nuclear pore complex (NPC) throughout interphase. Localizes to the kinetochore from prophase, and this appears to require the Nup107-160 subcomplex of the NPC. Localizes to the periphery of chromatin from late anaphase. Ref.10 Ref.11
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 Ref.16
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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Protein transport Translocation Transport mRNA transport
Cellular component	Centromere Chromosome Cytoplasm Kinetochore Nuclear pore complex Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cytokinesis Inferred from mutant phenotype Ref.10. Source: UniProtKB mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW mitotic prometaphase Traceable author statement. Source: Reactome nuclear pore complex assembly Inferred from mutant phenotype Ref.10. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome 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
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WYP5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8WYP5-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2266	2266	Protein ELYS		PRO_0000246319
Regions
	DNA binding	1971 – 1983	13	A.T hook
	Region	1 – 981	981	Necessary for cytoplasmic localization By similarity
	Region	1149 – 2266	1118	Necessary for nuclear localization By similarity
	Region	1446 – 1698	253	Mediates transcriptional activity By similarity
Amino acid modifications
	Modified residue	528	1	Phosphoserine Ref.9 Ref.14 Ref.15
	Modified residue	1017	1	N6-acetyllysine Ref.17
	Modified residue	1087	1	Phosphoserine Ref.9
	Modified residue	1142	1	Phosphoserine Ref.15
	Modified residue	1150	1	Phosphoserine Ref.15
	Modified residue	1155	1	Phosphoserine Ref.15
	Modified residue	1160	1	Phosphoserine Ref.13 Ref.15
	Modified residue	1175	1	Phosphothreonine Ref.15
	Modified residue	1216	1	Phosphoserine Ref.14
	Modified residue	1218	1	Phosphoserine Ref.14
	Modified residue	1222	1	Phosphoserine Ref.14
	Modified residue	1232	1	Phosphoserine Ref.7 Ref.9 Ref.13 Ref.15
	Modified residue	1250	1	Phosphoserine Ref.15
	Modified residue	1257	1	Phosphothreonine Ref.15
	Modified residue	1283	1	Phosphoserine Ref.7 Ref.9 Ref.12 Ref.15 Ref.16
	Modified residue	1295	1	Phosphoserine Ref.12
	Modified residue	1371	1	Phosphoserine By similarity
	Modified residue	1402	1	Phosphoserine Ref.13
	Modified residue	1511	1	Phosphoserine Ref.13
	Modified residue	1513	1	Phosphoserine Ref.7 Ref.9
	Modified residue	1541	1	Phosphoserine Ref.7 Ref.9 Ref.15 Ref.16
	Modified residue	1620	1	Phosphothreonine Ref.13
	Modified residue	1692	1	Phosphoserine Ref.13
	Modified residue	1729	1	Phosphoserine Ref.15
	Modified residue	1737	1	Phosphoserine Ref.13
	Modified residue	1764	1	Phosphothreonine Ref.13
	Modified residue	1771	1	Phosphoserine Ref.13
	Modified residue	1806	1	Phosphoserine Ref.15
	Modified residue	1808	1	Phosphothreonine Ref.14 Ref.15
	Modified residue	1878	1	Phosphoserine Ref.15 Ref.16
	Modified residue	1884	1	Phosphoserine Ref.15 Ref.16
	Modified residue	1898	1	Phosphoserine Ref.13 Ref.15
	Modified residue	1944	1	Phosphoserine Ref.13 Ref.14
	Modified residue	1952	1	Phosphoserine Ref.13
	Modified residue	1996	1	Phosphoserine Ref.7
	Modified residue	2060	1	Phosphoserine Ref.13 Ref.15
	Modified residue	2063	1	Phosphoserine Ref.13
	Modified residue	2089	1	Phosphoserine Ref.15
	Modified residue	2120	1	Phosphoserine Ref.15
	Modified residue	2123	1	Phosphoserine Ref.15
	Modified residue	2154	1	Phosphoserine Ref.15
	Modified residue	2212	1	Phosphoserine Ref.9 Ref.15
	Modified residue	2222	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 Ref.16
	Modified residue	2226	1	Phosphoserine Ref.7 Ref.8 Ref.13 Ref.15 Ref.16
	Modified residue	2238	1	Phosphothreonine Ref.13
	Modified residue	2242	1	Phosphothreonine Ref.13
	Modified residue	2254	1	Phosphoserine Ref.13
Natural variations
	Alternative sequence	1	1	M → MDSLAGLSPREAAGVLSLSC VGVCSTCAWAWPHGSM in isoform 2.		VSP_019844
	Natural variant	874	1	N → S. Corresponds to variant rs2642990 [ dbSNP | Ensembl ].		VAR_027037
	Natural variant	2185	1	L → V. Corresponds to variant rs12410563 [ dbSNP | Ensembl ].		VAR_027038
Experimental info
	Sequence conflict	168	1	V → I in BAB78516. Ref.1
	Sequence conflict	207	1	Q → E in BAB78516. Ref.1
	Sequence conflict	237	1	V → A in BAB78516. Ref.1
	Sequence conflict	279	1	P → R in BAB78516. Ref.1
	Sequence conflict	403	1	D → G in AAN65622. Ref.2
	Sequence conflict	646	1	T → A in BAB78516. Ref.1
	Sequence conflict	743	1	D → G in AAN65622. Ref.2
	Sequence conflict	753	1	A → G in AAN65622. Ref.2
	Sequence conflict	1134	1	F → S in AAN65622. Ref.2
	Sequence conflict	1207	1	L → P in BAB78516. Ref.1
	Sequence conflict	1270	1	L → P in BAB78516. Ref.1
	Sequence conflict	1737	1	S → F in CAB45737. Ref.4
	Sequence conflict	1797	1	S → F in BAB78516. Ref.1
	Sequence conflict	1830	1	E → G in AAN65622. Ref.2
	Sequence conflict	2128	1	K → E in AAN65622. Ref.2
	Sequence conflict	2187	1	K → E in AAH12307. Ref.6
	Sequence conflict	2213	1	P → L in BAB78516. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 3. Checksum: 465452FD42ACCFAE	FASTA	2,266	252,498
	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
	Isoform 2 [UniParc]. Checksum: 71D2E4A758E09BD3	FASTA	2,301	256,000
	10 20 30 40 50 60 MDSLAGLSPR EAAGVLSLSC VGVCSTCAWA WPHGSMRDLR AQVTSGLLPF PEVTLQALGE 70 80 90 100 110 120 DEITLESVLR GKFAAGKNGL ACLACGPQLE VVNSITGERL SAYRFSGVNE QPPVVLAVKE 130 140 150 160 170 180 FSWQKRTGLL IGLEETEGSV LCLYDLGISK VVKAVVLPGR VTAIEPIINH GGASASTQHL 190 200 210 220 230 240 HPSLRWLFGV AAVVTDVGQI LLVDLCLDDL SCNQNEVEAS DLEVLTGIPA EVPHIRESVM 250 260 270 280 290 300 RQGRHLCFQL VSPTGTAVST LSYISRTNQL AVGFSDGYLA LWNMKSMKRE YYIQLESGQV 310 320 330 340 350 360 PVYAVTFQEP ENDPRNCCYL WAVQSTQDSE GDVLSLHLLQ LAFGNRKCLA SGQILYEGLE 370 380 390 400 410 420 YCEERYTLDL TGGMFPLRGQ TSNTKLLGCQ SIEKFRSHGD REEGVNEALS PDTSVSVFTW 430 440 450 460 470 480 QVNIYGQGKP SVYLGLFDIN RWYHAQMPDS LRSGEYLHNC SYFALWSLES VVSRTSPHGI 490 500 510 520 530 540 LDILVHERSL NRGVPPSYPP PEQFFNPSTY NFDATCLLNS GVVHLTCTGF QKETLTFLKK 550 560 570 580 590 600 SGPSLNELIP DGYNRCLVAG LLSPRFVDVQ PSSLSQEEQL EAILSAAIQT SSLGLLTGYI 610 620 630 640 650 660 RRWITEEQPN SATNLRFVLE WTWNKVVLTK EEFDRLCVPL FDGSCHFMDP QTIQSIQQCY 670 680 690 700 710 720 LLLSNLNIVL SCFASEAREI TERGLIDLSN KFVVSHLICQ YAQVVLWFSH SGLLPEGIDD 730 740 750 760 770 780 SVQLSRLCYN YPVIQNYYTS RRQKFERLSR GKWNPDCLMI DGLVSQLGER IEKLWKRDEG 790 800 810 820 830 840 GTGKYPPASL HAVLDMYLLD GVTEAAKHSI TIYLLLDIMY SFPNKTDTPI ESFPTVFAIS 850 860 870 880 890 900 WGQVKLIQGF WLIDHNDYES GLDLLFHPAT AKPLSWQHSK IIQAFMSQGE HRQALRYIQT 910 920 930 940 950 960 MKPTVSSGND VILHLTVLLF NRCMVEAWNF LRQHCNRLNI EELLKHMYEV CQEMGLMEDL 970 980 990 1000 1010 1020 LKLPFTDTEQ ECLVKFLQSS ASVQNHEFLL VHHLQRANYV PALKLNQTLK INVMNDRDPR 1030 1040 1050 1060 1070 1080 LRERSLARNS ILDQYGKILP RVHRKLAIER AKPYHLSTSS VFRLVSRPKP LSAVPKQVVT 1090 1100 1110 1120 1130 1140 GTVLTRSVFI NNVLSKIGEV WASKEPINST TPFNSSKIEE PSPIVYSLPA PELPEAFFGT 1150 1160 1170 1180 1190 1200 PISKASQKIS RLLDLVVQPV PRPSQCSEFI QQSSMKSPLY LVSRSLPSSS QLKGSPQAIS 1210 1220 1230 1240 1250 1260 RASELHLLET PLVVKKAKSL AMSVTTSGFS EFTPQSILRS TLRSTPLASP SPSPGRSPQR 1270 1280 1290 1300 1310 1320 LKETRISFVE EDVHPKWIPG AADDSKLEVF TTPKKCAVPV ETEWLKSKDR TTSFFLNSPE 1330 1340 1350 1360 1370 1380 KEHQEMDEGS QSLEKLDVSK GNSSVSITSD ETTLEYQDAP SPEDLEETVF TASKPKSSST 1390 1400 1410 1420 1430 1440 ALTTNVTEQT EKDGDKDVFA SEVTPSDLQK QMGNLEDAET KDLLVAAEAF SELNHLSPVQ 1450 1460 1470 1480 1490 1500 GTEASLCAPS VYEGKIFTQK SKVPVLDEGL TSVETYTPAI RANDNKSMAD VLGDGGNSSL 1510 1520 1530 1540 1550 1560 TISEGPIVSE RRLNQEVALN LKEDHEVEVG VLKESVDLPE EKLPISDSPP DTQEIHVIEQ 1570 1580 1590 1600 1610 1620 EKLEAQDSGE EARNLSFNEL YPSGTLKLQY NFDTIDQQFC DLADNKDTAE CDIAEVDGEL 1630 1640 1650 1660 1670 1680 FVAQSNFTLI LEGEEGEVEP GDFASSDVLP KAANTATEEK LVCSGENDNH GQIANLPSAV 1690 1700 1710 1720 1730 1740 TSDQKSQKVD TLPYVPEPIK VAIAENLLDV IKDTRSKEIT SDTMEQSIHE TIPLVSQNIM 1750 1760 1770 1780 1790 1800 CPTKLVKSAF KTAQETSTMT MNVSQVDDVV SSKTRTRGQR IQNVNVKSAQ QEASADVATP 1810 1820 1830 1840 1850 1860 KMPGQSVRKK TRKAKEISEA SENIYSDVRG LSQNQQIPQN SVTPRRGRRK KEVNQDILEN 1870 1880 1890 1900 1910 1920 TSSVEQELQI TTGRESKRLK SSQLLEPAVE ETTKKEVKVS SVTKRTPRRI KRSVENQESV 1930 1940 1950 1960 1970 1980 EIINDLKVST VTSPSRMIRK LRSTNLDASE NTGNKQDDKS SDKQLRIKHV RRVRGREVSP 1990 2000 2010 2020 2030 2040 SDVREDSNLE SSQLTVQAEF DMSAIPRKRG RPRKINPSED VGSKAVKEER SPKKKEAPSI 2050 2060 2070 2080 2090 2100 RRRSTRNTPA KSENVDVGKP ALGKSILVPN EELSMVMSSK KKLTKKTESQ SQKRSLHSVS 2110 2120 2130 2140 2150 2160 EERTDEMTHK ETNEQEERLL ATASFTKSSR SSRTRSSKAI LLPDLSEPNN EPLFSPASEV 2170 2180 2190 2200 2210 2220 PRKAKAKKIE VPAQLKELVS DLSSQFVISP PALRSRQKNT SNKNKLEDEL KDDAQSVETL 2230 2240 2250 2260 2270 2280 GKPKAKRIRT SKTKQASKNT EKESAWSPPP IEIRLISPLA SPADGVKSKP RKTTEVTGTG 2290 2300 LGRNRKKLSS YPKQILRRKM L

References

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[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. , 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: 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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2222 AND SER-2226, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: Cervix adenocarcinoma.
[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. Tissue: Embryonic kidney.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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: Leukemic 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
EMBL GenBank DDBJ	AB059277 mRNA. Translation: BAB78516.1. AY157619 mRNA. Translation: AAN65622.1. Frameshift. AC113174 Genomic DNA. No translation available. AL080144 mRNA. Translation: CAB45737.1. AF173978 mRNA. Translation: AAQ13621.1. Different initiation. BC012307 mRNA. Translation: AAH12307.1.
IPI	IPI00954159. IPI00979341.
PIR	T12528.
RefSeq	NP_056261.4. NM_015446.4.
UniGene	Hs.300887.
3D structure databases
ProteinModelPortal	Q8WYP5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WYP5. 5 interactions.
MINT	MINT-3308913.
STRING	Q8WYP5.
PTM databases
PhosphoSite	Q8WYP5.
Polymorphism databases
DMDM	259016354.
Proteomic databases
PRIDE	Q8WYP5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000283201; ENSP00000283201; ENSG00000153207. ENST00000326225; ENSP00000355465; ENSG00000153207. ENST00000361182; ENSP00000354780; ENSG00000153207. ENST00000366508; ENSP00000355464; ENSG00000153207. ENST00000391829; ENSP00000375705; ENSG00000153207. ENST00000428671; ENSP00000394728; ENSG00000153207.
GeneID	25909.
KEGG	hsa:25909.
UCSC	uc001ibv.1. human.
Organism-specific databases
CTD	25909.
GeneCards	GC01M247002.
H-InvDB	HIX0001764. HIX0002544.
HGNC	HGNC:24618. AHCTF1.
HPA	HPA031658.
MIM	610853. gene.
neXtProt	NX_Q8WYP5.
PharmGKB	PA142672631.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14521.
GeneTree	ENSGT00390000018900.
OrthoDB	EOG4FR0QQ.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	Q8WYP5.
Bgee	Q8WYP5.
CleanEx	HS_AHCTF1.
Genevestigator	Q8WYP5.
GermOnline	ENSG00000153207. Homo sapiens.
Family and domain databases
InterPro	IPR017956. AT_hook_DNA-bd_motif. [Graphical view]
SMART	SM00384. AT_hook. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	47390.
PMAP-CutDB	Q8WYP5.
SOURCE	Search...

Entry information

Entry name

ELYS_HUMAN

Accession

Primary (citable) accession number: Q8WYP5
Secondary accession number(s): A6NGM0 , A8MSG9, A8MZ86, Q7Z4E3, Q8IZA4, Q96EH9, Q9Y4Q6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	September 22, 2009
Last modified:	January 25, 2012
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.