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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)DescriptionActionsGraphical viewLength
DNA bindingi1955 – 1967A.T hookAdd BLAST13

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)DescriptionActionsGraphical viewLength
Mutagenesisi272 – 280FQEPENDPR → GSGSGSGSG: Abolishes nuclear pore localization; when associated with S-284. 1 Publication9
Mutagenesisi284Y → S: Abolishes nuclear pore localization; when associated with 272-GSGSGSGSG-280. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002463201 – 2243Protein ELYSAdd BLAST2243

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei528PhosphoserineCombined sources1
Modified residuei1080PhosphoserineCombined sources1
Modified residuei1083PhosphothreonineCombined sources1
Modified residuei1138PhosphoserineCombined sources1
Modified residuei1142PhosphoserineBy similarity1
Modified residuei1150PhosphoserineBy similarity1
Modified residuei1155PhosphoserineBy similarity1
Modified residuei1175PhosphothreonineBy similarity1
Modified residuei1214PhosphoserineCombined sources1
Modified residuei1218PhosphoserineCombined sources1
Modified residuei1222PhosphoserineBy similarity1
Modified residuei1235PhosphoserineBy similarity1
Modified residuei1381PhosphoserineCombined sources1
Modified residuei1517PhosphothreonineBy similarity1
Modified residuei1533PhosphoserineBy similarity1
Modified residuei1541PhosphoserineCombined sources1
Modified residuei1725PhosphoserineBy similarity1
Modified residuei1864PhosphoserineBy similarity1
Modified residuei1870PhosphoserineBy similarity1
Modified residuei1884PhosphoserineBy similarity1
Modified residuei1928PhosphoserineCombined sources1
Modified residuei1930PhosphoserineBy similarity1
Modified residuei1980PhosphoserineBy similarity1
Modified residuei2021PhosphoserineBy similarity1
Modified residuei2099PhosphoserineBy similarity1
Modified residuei2132PhosphoserineBy similarity1
Modified residuei2188PhosphoserineCombined sources1
Modified residuei2198PhosphoserineCombined sources1
Modified residuei2202PhosphoserineBy similarity1
Modified residuei2221N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CJF7.
MaxQBiQ8CJF7.
PaxDbiQ8CJF7.
PeptideAtlasiQ8CJF7.
PRIDEiQ8CJF7.

PTM databases

iPTMnetiQ8CJF7.
PhosphoSitePlusiQ8CJF7.

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

BgeeiENSMUSG00000026491.
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 interactors.
IntActiQ8CJF7. 2 interactors.
MINTiMINT-4119775.
STRINGi10090.ENSMUSP00000027768.

Structurei

Secondary structure

12243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 24Combined sources8
Beta strandi27 – 29Combined sources3
Beta strandi35 – 38Combined sources4
Beta strandi40 – 43Combined sources4
Beta strandi45 – 50Combined sources6
Beta strandi53 – 58Combined sources6
Turni59 – 61Combined sources3
Beta strandi64 – 69Combined sources6
Beta strandi79 – 88Combined sources10
Beta strandi91 – 99Combined sources9
Beta strandi101 – 110Combined sources10
Turni111 – 114Combined sources4
Beta strandi115 – 124Combined sources10
Beta strandi126 – 134Combined sources9
Helixi140 – 142Combined sources3
Helixi147 – 150Combined sources4
Beta strandi152 – 160Combined sources9
Beta strandi165 – 169Combined sources5
Helixi181 – 183Combined sources3
Beta strandi187 – 192Combined sources6
Helixi197 – 206Combined sources10
Beta strandi210 – 214Combined sources5
Beta strandi223 – 229Combined sources7
Turni230 – 233Combined sources4
Beta strandi234 – 239Combined sources6
Beta strandi242 – 248Combined sources7
Turni249 – 251Combined sources3
Beta strandi254 – 259Combined sources6
Beta strandi267 – 273Combined sources7
Beta strandi282 – 290Combined sources9
Turni292 – 295Combined sources4
Beta strandi299 – 313Combined sources15
Beta strandi319 – 336Combined sources18
Beta strandi347 – 359Combined sources13
Beta strandi377 – 389Combined sources13
Beta strandi396 – 403Combined sources8
Helixi404 – 409Combined sources6
Helixi422 – 424Combined sources3
Beta strandi428 – 432Combined sources5
Helixi434 – 440Combined sources7
Beta strandi445 – 450Combined sources6
Helixi452 – 454Combined sources3
Helixi467 – 470Combined sources4
Helixi472 – 474Combined sources3
Beta strandi476 – 483Combined sources8
Beta strandi486 – 492Combined sources7

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 981Necessary for cytoplasmic localizationAdd BLAST981
Regioni1 – 494Seven-bladed beta propeller repeatsAdd BLAST494
Regioni1019 – 2243DisorderedAdd BLAST1225
Regioni1149 – 2243Necessary for nuclear localizationAdd BLAST1095
Regioni1447 – 1694Mediates transcriptional activityAdd BLAST248

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.
OrthoDBiEOG091G006H.
PhylomeDBiQ8CJF7.
TreeFamiTF350425.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR032040. ELYS-bb.
IPR025151. ELYS_dom.
IPR015943. WD40/YVTN_repeat-like_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)DescriptionActionsGraphical viewLength
Sequence conflicti1207F → L in BAB78517 (PubMed:11952839).Curated1
Sequence conflicti1379A → T in BAB78517 (PubMed:11952839).Curated1
Sequence conflicti1414A → G in BAB78517 (PubMed:11952839).Curated1
Sequence conflicti1718H → R in BAB78517 (PubMed:11952839).Curated1
Sequence conflicti2084T → A in BAC37101 (PubMed:16141072).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4I0OX-ray1.90A1-494[»]
ProteinModelPortaliQ8CJF7.
SMRiQ8CJF7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ8CJF7.
PhosphoSitePlusiQ8CJF7.

Proteomic databases

EPDiQ8CJF7.
MaxQBiQ8CJF7.
PaxDbiQ8CJF7.
PeptideAtlasiQ8CJF7.
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.
OrthoDBiEOG091G006H.
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

PROiQ8CJF7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026491.
CleanExiMM_AHCTF1.
ExpressionAtlasiQ8CJF7. baseline and differential.
GenevisibleiQ8CJF7. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR032040. ELYS-bb.
IPR025151. ELYS_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF13934. ELYS. 1 hit.
PF16687. ELYS-bb. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 116 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.