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Protein

Protein ELYS

Gene

Ahctf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity). Has also been proposed to function as a transcription factor which may play a specific role in hematopoietic tissues (PubMed:11952839).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1955 – 196713A.T hookAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • transcription factor activity, sequence-specific DNA binding Source: MGI

GO - Biological processi

  • cytokinesis Source: UniProtKB
  • hemopoiesis Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • mRNA transport Source: UniProtKB-KW
  • nuclear pore complex assembly Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of transcription, DNA-templated Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

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

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1915033. Ahctf1.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: Ensembl
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • nuclear matrix Source: MGI
  • nuclear membrane Source: MGI
  • nuclear pore outer ring Source: Ensembl
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality before E7.5. Impaired proliferation of the inner cells of the blastocyst due at least in part to increased apoptosis.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi272 – 2809FQEPENDPR → GSGSGSGSG: Abolishes nuclear pore localization; when associated with S-284. 1 Publication
Mutagenesisi284 – 2841Y → S: Abolishes nuclear pore localization; when associated with 272-GSGSGSGSG-280. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22432243Protein ELYSPRO_0000246320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei528 – 5281PhosphoserineCombined sources
Modified residuei1080 – 10801PhosphoserineCombined sources
Modified residuei1083 – 10831PhosphothreonineCombined sources
Modified residuei1138 – 11381PhosphoserineCombined sources
Modified residuei1142 – 11421PhosphoserineBy similarity
Modified residuei1150 – 11501PhosphoserineBy similarity
Modified residuei1155 – 11551PhosphoserineBy similarity
Modified residuei1175 – 11751PhosphothreonineBy similarity
Modified residuei1214 – 12141PhosphoserineCombined sources
Modified residuei1218 – 12181PhosphoserineCombined sources
Modified residuei1222 – 12221PhosphoserineBy similarity
Modified residuei1235 – 12351PhosphoserineBy similarity
Modified residuei1381 – 13811PhosphoserineCombined sources
Modified residuei1517 – 15171PhosphothreonineBy similarity
Modified residuei1533 – 15331PhosphoserineBy similarity
Modified residuei1541 – 15411PhosphoserineCombined sources
Modified residuei1725 – 17251PhosphoserineBy similarity
Modified residuei1864 – 18641PhosphoserineBy similarity
Modified residuei1870 – 18701PhosphoserineBy similarity
Modified residuei1884 – 18841PhosphoserineBy similarity
Modified residuei1928 – 19281PhosphoserineCombined sources
Modified residuei1930 – 19301PhosphoserineBy similarity
Modified residuei1980 – 19801PhosphoserineBy similarity
Modified residuei2021 – 20211PhosphoserineBy similarity
Modified residuei2099 – 20991PhosphoserineBy similarity
Modified residuei2132 – 21321PhosphoserineBy similarity
Modified residuei2188 – 21881PhosphoserineCombined sources
Modified residuei2198 – 21981PhosphoserineCombined sources
Modified residuei2202 – 22021PhosphoserineBy similarity
Modified residuei2221 – 22211N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CJF7.
MaxQBiQ8CJF7.
PaxDbiQ8CJF7.
PRIDEiQ8CJF7.

PTM databases

iPTMnetiQ8CJF7.
PhosphoSiteiQ8CJF7.

Expressioni

Tissue specificityi

Widely expressed with higher expression in testis, lung and kidney. Expressed in T-cells, B-cells and granulocytes in bone marrow.1 Publication

Developmental stagei

Expressed throughout the embryo at E3.5 and E6.5. Higher expression is detected at 10.5 dpc nad then progressively decreases. Highly expressed in fetal hematopoietic tissues including liver, spleen and thymus. Expressed in the endothelium lining the dorsal aorta of 11.5 dpc embryos (at protein level).2 Publications

Gene expression databases

BgeeiQ8CJF7.
CleanExiMM_AHCTF1.
ExpressionAtlasiQ8CJF7. baseline and differential.
GenevisibleiQ8CJF7. MM.

Interactioni

Subunit structurei

Associates with the Nup107-160 subcomplex of the NPC.By similarity

Protein-protein interaction databases

BioGridi230549. 3 interactions.
IntActiQ8CJF7. 2 interactions.
MINTiMINT-4119775.
STRINGi10090.ENSMUSP00000027768.

Structurei

Secondary structure

1
2243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 248Combined sources
Beta strandi27 – 293Combined sources
Beta strandi35 – 384Combined sources
Beta strandi40 – 434Combined sources
Beta strandi45 – 506Combined sources
Beta strandi53 – 586Combined sources
Turni59 – 613Combined sources
Beta strandi64 – 696Combined sources
Beta strandi79 – 8810Combined sources
Beta strandi91 – 999Combined sources
Beta strandi101 – 11010Combined sources
Turni111 – 1144Combined sources
Beta strandi115 – 12410Combined sources
Beta strandi126 – 1349Combined sources
Helixi140 – 1423Combined sources
Helixi147 – 1504Combined sources
Beta strandi152 – 1609Combined sources
Beta strandi165 – 1695Combined sources
Helixi181 – 1833Combined sources
Beta strandi187 – 1926Combined sources
Helixi197 – 20610Combined sources
Beta strandi210 – 2145Combined sources
Beta strandi223 – 2297Combined sources
Turni230 – 2334Combined sources
Beta strandi234 – 2396Combined sources
Beta strandi242 – 2487Combined sources
Turni249 – 2513Combined sources
Beta strandi254 – 2596Combined sources
Beta strandi267 – 2737Combined sources
Beta strandi282 – 2909Combined sources
Turni292 – 2954Combined sources
Beta strandi299 – 31315Combined sources
Beta strandi319 – 33618Combined sources
Beta strandi347 – 35913Combined sources
Beta strandi377 – 38913Combined sources
Beta strandi396 – 4038Combined sources
Helixi404 – 4096Combined sources
Helixi422 – 4243Combined sources
Beta strandi428 – 4325Combined sources
Helixi434 – 4407Combined sources
Beta strandi445 – 4506Combined sources
Helixi452 – 4543Combined sources
Helixi467 – 4704Combined sources
Helixi472 – 4743Combined sources
Beta strandi476 – 4838Combined sources
Beta strandi486 – 4927Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I0OX-ray1.90A1-494[»]
ProteinModelPortaliQ8CJF7.
SMRiQ8CJF7. Positions 3-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 981981Necessary for cytoplasmic localizationAdd
BLAST
Regioni1 – 494494Seven-bladed beta propeller repeatsAdd
BLAST
Regioni1019 – 22431225DisorderedAdd
BLAST
Regioni1149 – 22431095Necessary for nuclear localizationAdd
BLAST
Regioni1447 – 1694248Mediates transcriptional activityAdd
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 (PubMed:23499022).1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IG0H. Eukaryota.
ENOG410XQV6. LUCA.
GeneTreeiENSGT00390000018900.
HOGENOMiHOG000293244.
InParanoidiQ8CJF7.
OMAiFTWQVNI.
OrthoDBiEOG7P8P72.
PhylomeDBiQ8CJF7.
TreeFamiTF350425.

Family and domain databases

InterProiIPR032040. ELYS-bb.
IPR025151. ELYS_dom.
[Graphical view]
PfamiPF13934. ELYS. 1 hit.
PF16687. ELYS-bb. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CJF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDLTAQVTS DLLHFPEVTI EALGEDEITL ESVLRGKFAA GKNGLACLAC
60 70 80 90 100
GPQLEVVNSL TGERLSAYRF SGVNEQPPVV LAVKEFSWHK RTGLLIGLEE
110 120 130 140 150
ADGSVLCLYD LGISRVVKAV VLPGRVTAIE PIINHGGASA STQHLHPSLR
160 170 180 190 200
WLFGVAAVVT DVGQILLIDL CLDDLSCSQN EVEASDLEVI TGIPAEVPHI
210 220 230 240 250
RERVMREGRH LCFQLVSPLG VAISTLSYIN RTNQLAVGFS DGYLALWNMK
260 270 280 290 300
SMKREYYTQL EGGRVPVHAV AFQEPENDPR NCCYLWAVQS TQDSEGDVLS
310 320 330 340 350
LHLLQLAFGD RKCLASGQIL YEGLEYCEER YTLDLAGGTF PLRGQTSNTK
360 370 380 390 400
LLGCQSIERF PSHGDREESM REALSPDTSV SVFTWQVNIY GQGKPSVYLG
410 420 430 440 450
LFDINRWYHA QMPDSLRSGE SLHNCSYFAL WSLDSVVSRT SPHHILDILV
460 470 480 490 500
HERSLNRGVP PSYPPPEQFF NPSTFNFDAT CLLDSGVIHV TCAGFQKETL
510 520 530 540 550
TFLKKSGPTL NEVIPDSYNR CLVAGLLSPR LIDIQPSSLS QEEQLEAILS
560 570 580 590 600
AAIQTSSLGL LTGYIRTWII EEQPNSAANL RFVLEWTWNK VVLTKEEFDR
610 620 630 640 650
LCVPLFDGSC RFIDPQTIQS IQQCHLLLSN LSTVLSCFAM EAQGITERGL
660 670 680 690 700
VDLSNKHMVT QLLCQYAHMV LWFCHSGLLP EGLDDALQLS RLRYNYPVIQ
710 720 730 740 750
NYYTSRRQKS ERSPRGKWNH DCLMIDGLVS QLGDEVEKLW KRDEGGTGRY
760 770 780 790 800
PPASIHALLD IYLLDNITEA SKHAITIYLL LDIMYSFPNK TDTPIESFPT
810 820 830 840 850
AFAISWGQVK LVQGFWLLDH NDYENGLDLL FHPVTAKPAS WQHSKIIEAF
860 870 880 890 900
MSQGEHKQAL RYLQTMKPTV SSSNEVILHL TVLLFNRCMV EAWNLLRQNS
910 920 930 940 950
NRVNIEELLK HAYEVCQEMG LMEDLLKLPF TNTEQECLVK FLQSSTSVEN
960 970 980 990 1000
HEFLLVHHLQ RANYISALKL NQILKNNLMS DRDPRLRERS VTRNSILDQY
1010 1020 1030 1040 1050
GKILPRVQRK LAVERAKPYH LSTSSVFHEV SRPKPLSAFP KKAITGTVLT
1060 1070 1080 1090 1100
RSTFISNVLS KIGEVWASHE PRNGVSLFNS PKTEQPSPVV HSFPHPELPE
1110 1120 1130 1140 1150
AFVGTPISNT SQRISRLLDL VVHPVPQPSQ CLEFIQQSPT RSPLCLLSSS
1160 1170 1180 1190 1200
LPLSSQFKRP HQNTSRPSEL LLLETPLIVK KAKSLALSAT SSGFAEFTPP
1210 1220 1230 1240 1250
SILRSGFRTT PLASPSLSPG RSLTPPFRVK ETRISFMEEG MNTHWTDRAT
1260 1270 1280 1290 1300
DDRNTKAFVS TSFHKCGLPA ETEWMKTSDK NTYFPLDVPA KGPQKVVAES
1310 1320 1330 1340 1350
LATHSGRLEK LDVSKEDSTA STRSDQTSLE YHDAPSPEDL EGAVFVSPKP
1360 1370 1380 1390 1400
ASSSTELTTN STLQTERDND KDAFKSEGAP SPVKKQIGTG DAAVEAFSEL
1410 1420 1430 1440 1450
SRLDPVERAE ASFAVSSVCE GETSTSNSKT SVLDGIVPIE SRTSILTADH
1460 1470 1480 1490 1500
KESVANTVAD VESSGSTSSK CPVTSERSLG QKLTLNLKED EIEAHVPKEN
1510 1520 1530 1540 1550
VGLPEESPRI SAAPSDTHEI HLIGCENLEV QNSEEEAKNL SFDELYPLGA
1560 1570 1580 1590 1600
EKLEYNLSTI EQQFCDLPDD KDSAECDAAE VDGELFVAQS NFTLILEGEE
1610 1620 1630 1640 1650
GEAEASDSAA PNMLPKATKE KPVCHREPHN QERVTDLPSA VTADQESHKV
1660 1670 1680 1690 1700
ETLPYVPEPV KVAIAENLLD VIKDTRSKEA TPVAAGEAGD EDGAVIVSKA
1710 1720 1730 1740 1750
AHSSRLTNST PKTVKEPHAE TVNTSQNDDM VSSRTLTRRQ HALSLNVTSE
1760 1770 1780 1790 1800
QEPSAVATPK KRTRKIKETP ESSERTCSDL KVAPENQLTA QSPPAPRRGK
1810 1820 1830 1840 1850
KKDVSQGTLP SSGAVEPEPE PQGTPGRLRL RTQPPEPAAE ETPSRTKVRL
1860 1870 1880 1890 1900
SSVRKGTPRR LKKSVENGQS TEILDDLKGS EAASHDGTVT ELRNANLEDT
1910 1920 1930 1940 1950
QNMEYKQDEH SDQQLPLKRK RVREREVSVS SVTEEPKLDS SQLPLQTGLD
1960 1970 1980 1990 2000
VPATPRKRGR PRKVVPLEAD GGTTGKEQTS PQKKDVPVVR RSTRNTPARN
2010 2020 2030 2040 2050
VSTLEKSVLV PNKEAALVVT SKRRPTKKSA EESSKDPSAA VSDLAGGAAH
2060 2070 2080 2090 2100
TESADRRDGL LAAAALTPSA QGTRTRSRRT MLLTDISEPK TEPLFPPPSV
2110 2120 2130 2140 2150
KVPKKKSKAE NMEAAAQLKE LVSDLSSQFV VSPPALRTRQ KSISNTSKLL
2160 2170 2180 2190 2200
GELESDPKPL EIIEQKPKRS RTVKTRASRN TGKGSSWSPP PVEIKLVSPL
2210 2220 2230 2240
ASPVDEIKTG KPRKTAEIAG KTLGRGRKKP SSFPKQILRR KML
Length:2,243
Mass (Da):247,646
Last modified:March 1, 2003 - v1
Checksum:iEEEA09B70F2B5691
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1207 – 12071F → L in BAB78517 (PubMed:11952839).Curated
Sequence conflicti1379 – 13791A → T in BAB78517 (PubMed:11952839).Curated
Sequence conflicti1414 – 14141A → G in BAB78517 (PubMed:11952839).Curated
Sequence conflicti1718 – 17181H → R in BAB78517 (PubMed:11952839).Curated
Sequence conflicti2084 – 20841T → A in BAC37101 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059278 mRNA. Translation: BAB78517.1.
AB081498 Genomic DNA. Translation: BAC22610.1.
BC138343 mRNA. Translation: AAI38344.1.
BC138344 mRNA. Translation: AAI38345.1.
AK078022 mRNA. Translation: BAC37101.2. Sequence problems.
CCDSiCCDS15564.1.
RefSeqiNP_080651.2. NM_026375.2.
UniGeneiMm.128165.

Genome annotation databases

EnsembliENSMUST00000027768; ENSMUSP00000027768; ENSMUSG00000026491.
GeneIDi226747.
KEGGimmu:226747.
UCSCiuc011wxn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059278 mRNA. Translation: BAB78517.1.
AB081498 Genomic DNA. Translation: BAC22610.1.
BC138343 mRNA. Translation: AAI38344.1.
BC138344 mRNA. Translation: AAI38345.1.
AK078022 mRNA. Translation: BAC37101.2. Sequence problems.
CCDSiCCDS15564.1.
RefSeqiNP_080651.2. NM_026375.2.
UniGeneiMm.128165.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I0OX-ray1.90A1-494[»]
ProteinModelPortaliQ8CJF7.
SMRiQ8CJF7. Positions 3-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230549. 3 interactions.
IntActiQ8CJF7. 2 interactions.
MINTiMINT-4119775.
STRINGi10090.ENSMUSP00000027768.

PTM databases

iPTMnetiQ8CJF7.
PhosphoSiteiQ8CJF7.

Proteomic databases

EPDiQ8CJF7.
MaxQBiQ8CJF7.
PaxDbiQ8CJF7.
PRIDEiQ8CJF7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027768; ENSMUSP00000027768; ENSMUSG00000026491.
GeneIDi226747.
KEGGimmu:226747.
UCSCiuc011wxn.1. mouse.

Organism-specific databases

CTDi25909.
MGIiMGI:1915033. Ahctf1.

Phylogenomic databases

eggNOGiENOG410IG0H. Eukaryota.
ENOG410XQV6. LUCA.
GeneTreeiENSGT00390000018900.
HOGENOMiHOG000293244.
InParanoidiQ8CJF7.
OMAiFTWQVNI.
OrthoDBiEOG7P8P72.
PhylomeDBiQ8CJF7.
TreeFamiTF350425.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

NextBioi378313.
PROiQ8CJF7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CJF7.
CleanExiMM_AHCTF1.
ExpressionAtlasiQ8CJF7. baseline and differential.
GenevisibleiQ8CJF7. MM.

Family and domain databases

InterProiIPR032040. ELYS-bb.
IPR025151. ELYS_dom.
[Graphical view]
PfamiPF13934. ELYS. 1 hit.
PF16687. ELYS-bb. 1 hit.
[Graphical view]
ProtoNetiSearch...

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], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
    Tissue: Yolk sac.
  2. "Genomic organization and characterization of the mouse ELYS gene."
    Okita K., Takizawa M., Ueno M., Kimura N., Nobuhisa I., Taga T.
    Biochem. Biophys. Res. Commun. 305:327-332(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. "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].
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2082-2243.
    Strain: C57BL/6J.
    Tissue: Fetal head.
  5. "Targeted disruption of the mouse ELYS gene results in embryonic death at peri-implantation development."
    Okita K., Kiyonari H., Nobuhisa I., Kimura N., Aizawa S., Taga T.
    Genes Cells 9:1083-1091(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080 AND SER-1218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528; THR-1083; SER-1138; SER-1214; SER-1218; SER-1381; SER-1541; SER-1928; SER-2188 AND SER-2198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Structural and functional studies of the 252 kDa nucleoporin ELYS reveal distinct roles for its three tethered domains."
    Bilokapic S., Schwartz T.U.
    Structure 21:572-580(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-494, REPEATS, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-284 AND 272-PHE--ARG-280.

Entry informationi

Entry nameiELYS_MOUSE
AccessioniPrimary (citable) accession number: Q8CJF7
Secondary accession number(s): B2RRC8, Q8BVJ5, Q8VD55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.