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Protein

E1A-binding protein p400

Gene

Ep400

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome (By similarity). Regulates transcriptional activity of ZNF42.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1115 – 11228ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
E1A-binding protein p400 (EC:3.6.4.-)
Alternative name(s):
Domino homolog
Short name:
mDomino
p400 kDa SWI2/SNF2-related protein
Gene namesi
Name:Ep400
Synonyms:Kiaa1498
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1276124. Ep400.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • Swr1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 30723072E1A-binding protein p400PRO_0000074313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei134 – 1341PhosphoserineCombined sources
Modified residuei315 – 3151PhosphoserineCombined sources
Modified residuei321 – 3211PhosphoserineCombined sources
Modified residuei735 – 7351PhosphoserineBy similarity
Modified residuei741 – 7411PhosphoserineCombined sources
Modified residuei754 – 7541PhosphoserineCombined sources
Modified residuei922 – 9221PhosphothreonineCombined sources
Modified residuei923 – 9231PhosphoserineCombined sources
Modified residuei927 – 9271PhosphoserineCombined sources
Modified residuei940 – 9401PhosphoserineCombined sources
Modified residuei944 – 9441PhosphothreonineCombined sources
Modified residuei1009 – 10091PhosphoserineCombined sources
Modified residuei1010 – 10101PhosphoserineCombined sources
Modified residuei1471 – 14711N6-acetyllysineBy similarity
Modified residuei1646 – 16461PhosphoserineBy similarity
Modified residuei1650 – 16501PhosphoserineBy similarity
Modified residuei2265 – 22651N6-acetyllysineBy similarity
Modified residuei2272 – 22721N6-acetyllysineBy similarity
Modified residuei2614 – 26141PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8CHI8.
MaxQBiQ8CHI8.
PaxDbiQ8CHI8.
PeptideAtlasiQ8CHI8.
PRIDEiQ8CHI8.

PTM databases

iPTMnetiQ8CHI8.
PhosphoSiteiQ8CHI8.

Expressioni

Tissue specificityi

Expressed in brain, thymus, lung, liver, spleen, kidney, colon and bone marrow.

Gene expression databases

BgeeiQ8CHI8.
CleanExiMM_EP400.
ExpressionAtlasiQ8CHI8. baseline and differential.
GenevisibleiQ8CHI8. MM.

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. May also participate in the formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit, but which include the SWI/SNF related protein SRCAP. The NuA4 complex interacts with MYC. EP400 interacts with TRRAP, RUVBL1 and RUVBL2. Component of a SWR1-like complex (By similarity). Interacts with ZNF42. Interacts with PHF5A.By similarity2 Publications

Protein-protein interaction databases

BioGridi217577. 16 interactions.
DIPiDIP-61766N.
IntActiQ8CHI8. 10 interactions.
MINTiMINT-4115994.
STRINGi10090.ENSMUSP00000049038.

Structurei

3D structure databases

ProteinModelPortaliQ8CHI8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini798 – 87073HSAPROSITE-ProRule annotationAdd
BLAST
Domaini1102 – 1267166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1815 – 1972158Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2276 – 234570Myb-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni950 – 1364415Interactions with RUVBL1 and RUVBL2By similarityAdd
BLAST
Regioni2440 – 2699260Interaction with ZNF42Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1218 – 12214DEAD box-like

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi277 – 2815Poly-Gln
Compositional biasi316 – 3194Poly-Pro
Compositional biasi426 – 43611Poly-GluAdd
BLAST
Compositional biasi699 – 7046Poly-Ser
Compositional biasi956 – 9594Poly-Glu
Compositional biasi2462 – 247918Poly-GlnAdd
BLAST
Compositional biasi2480 – 24845Poly-Pro
Compositional biasi2487 – 24948Poly-Pro
Compositional biasi2685 – 269814Poly-GlnAdd
BLAST
Compositional biasi2739 – 27457Poly-Pro
Compositional biasi2767 – 27704Poly-Gln

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 HSA domain.PROSITE-ProRule annotation
Contains 1 Myb-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0391. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00530000063427.
HOVERGENiHBG051488.
InParanoidiQ8CHI8.
KOiK11320.
OMAiAQVVHTQ.
OrthoDBiEOG7PVWPN.
TreeFamiTF106424.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031575. EP400_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014012. HSA_dom.
IPR017877. Myb-like_dom.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF15790. EP400_N. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CHI8-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MHHGSGPQNV QHQLQRSRSF TGSEEEQPAH PNLPPSPAAP FAPSASPSAP
60 70 80 90 100
QSPGYQIQQL MSRSPVAGQN VNITLQNVGP VVGGNQQITL APLPLPNPTS
110 120 130 140 150
PGFQFGAQQR RFEHGSPSYI QVTSPMSQQV QTQSPTQPSP GPGQTLQNVR
160 170 180 190 200
AGAPGPGLGI CSNSPTGGFV DASVLVRQIS LSPSSGGHFV FQEAPGLTQM
210 220 230 240 250
AQGAQVQLQH SGAPITVRER RLSQPHAQSG GTIHHLGPQS PAAAGGTGLQ
260 270 280 290 300
PLASPNHITT ASLPPQISSI IQGQLIQQQQ QVLQGQPMNR SLGFERTPGV
310 320 330 340 350
LLPGVGGPSA FGMTSPPPPT SPSRTTMPPG LSSVPLTSMG SSGMKKVPKK
360 370 380 390 400
LEEIPPASQE MAQMRKQCLD YHYKEMEALK EVFKEYLIEL FFLQHLQGNM
410 420 430 440 450
MDFLAFKKKH YAPLQAYLRQ NDLDIEEEEE EEEEEEGKSE VINDEVKVVT
460 470 480 490 500
GKDGQTGTPV AIATQLPPNV SAAFSSQQQP FQHQSLTGSL VVGPGSATEA
510 520 530 540 550
DPFKRQQVMP PTEQSKRPRL EVGHPGVVFQ HPGVNAGVPL QQLMPTVQGG
560 570 580 590 600
MPPTPQATQL TGQKQSQQQY DPSTGPPVQN AASLHTPPPQ LPARLPPASV
610 620 630 640 650
PATALPSTLQ FSQQSQMVEA STQLQIPVKT QQLNAPIPAP LPSQLPAPSS
660 670 680 690 700
QPAQPALHVP MPGKAQMQTS QLSSQTQTVA STRPPLDSAQ PCQRSLPTSS
710 720 730 740 750
SSSSLVPVSG SGPGPSPARS SPVNRPSSAT NKALSPITSR SPGVAVSAPP
760 770 780 790 800
KPQSPAQNAA SSQDGSQDKL AEQITLENQI HQRIADLRKE GLWSLRRLPK
810 820 830 840 850
LQEAPRPKSH WDYLLEEMQW MATDFAQERR WKLAAAKKLV RTVARHHEEK
860 870 880 890 900
KLREERGKKE EQSRLRRIAA TTAREIEYFW SNIEQVVEIK LQVELEEKRK
910 920 930 940 950
KALNLQKVSR RGKESRLKGF DTSPEHSLDL GISGRKRKAS TSLTDDEVED
960 970 980 990 1000
EEETIEEEEA HEGLVDHHTE LTNLAKEAEL PLIDLMKLYE GAFLPNFQWP
1010 1020 1030 1040 1050
QPEPDHEESS GEEDVEDCPS DRESRRDSVL IDSLFIMDQF KAAERMSIGK
1060 1070 1080 1090 1100
SNTKDITEVT AVAEAILPKG SARVTTAVKF SAPSLLYGAL RDYQKIGLDW
1110 1120 1130 1140 1150
LAKLYRKNLN GILADEAGLG KTVQIIAFFA HLACNEGNWG PHLVVMRSCN
1160 1170 1180 1190 1200
ILKWELELKR WCPGLKTLSY VGSHRELKAK RQEWTEPNNF HICITSYKQF
1210 1220 1230 1240 1250
FRGYTAFSRV HWKCLVVDEM QRVKGMTERH WEAIFKLQSQ QRLLLIDVPL
1260 1270 1280 1290 1300
HNTFLELWTM VHFLIPGISR PYLSFPLKAP NEENQDYYHK MVIRLHRVTQ
1310 1320 1330 1340 1350
PFILRRTKRD VEKQLTRKYE HVLKCRLSSR QKALYEDVIL QPRTQEALKS
1360 1370 1380 1390 1400
GHFVSVLSVL TRLQRICNHP GLVEPRVPGS SFAAGSLQYK SASLILRVLE
1410 1420 1430 1440 1450
REFWKETDLS IFDLIGLENK ITRHEAELLC KKKVTRKLME EVFASPPPSA
1460 1470 1480 1490 1500
RPAAVKLKAS RLFQPVQYGQ KPEGRTVAFP STHPPRMANT NTSTATPQGQ
1510 1520 1530 1540 1550
VRGRPPIATF SANPDTKGGE VVKIAQLASI AGPQSRVAQP ETPVTLQFQG
1560 1570 1580 1590 1600
NKFTLSHSQL RQLTAGQPLQ LQGSVLQIVS APGQPYLRAP GPVVMQTVSQ
1610 1620 1630 1640 1650
AGAVHSTLGS KPPTSGPSPA PLTPQVGVPG RVAVSAMAVG EPGLASKPAS
1660 1670 1680 1690 1700
PAAGPTQEEK SRLLKERLDQ IHFINERRCS QAPVYGRDLL RICSLPGRRK
1710 1720 1730 1740 1750
RPLCWSLDSN FGKGPKGVNY DMSLSKSEGD LILTLSQESL QDVLGRVACV
1760 1770 1780 1790 1800
IPPVVATPPS LWVARPPSLY SSRLRALRQC LREHTGPYHR QLQQLTALRS
1810 1820 1830 1840 1850
LQFPELRLVQ FDSGKLEALA ILLQKLKSEG RRVLILSQMV LMLDILEMFL
1860 1870 1880 1890 1900
NFHYLTYVRI DENANSEQRQ ELMRSFNRDR RIFCALLSTH SRATGINLVE
1910 1920 1930 1940 1950
ADTVVFYDND LNPVMDAKAQ EWCDRIGRCK DIHIYRLVSG NSIEEKLLKN
1960 1970 1980 1990 2000
GTKDLIREVA AQGNDYSMAF LTQRTIQELF EVYSPMDDTG FPVKAEEFVV
2010 2020 2030 2040 2050
LSQEPSVSET IAPKIARPFI EALKSIECLE EDAQRSTEEA VPGSSSVAVS
2060 2070 2080 2090 2100
SDSDGSRYDE EPSQLEELAD FMEQLTPIEK YALNYLELFH TTTEQEKERI
2110 2120 2130 2140 2150
SEDLVMASMK DWETRNARAL QEREARLQLE QEEAELLTYT REDAYTMEYV
2160 2170 2180 2190 2200
YEDADGQTEV MPLWTPPTPP QDDNDIYIDS VMCLMYETTP IPEAKLPPVY
2210 2220 2230 2240 2250
VRKERKRHKT DPSAAGRKKK QRHGEAVVPP RSLFDRATPG MLKIRREGKE
2260 2270 2280 2290 2300
QKKNLLLKQQ TPFAKPLPTY VKSSGEPAQD SPDWLIGEDW ALLQAVKQLL
2310 2320 2330 2340 2350
ELPLNLTIVS PAHTPNWDLV SDVVNSCSRI YRSSKQCRNR YENVIIPREE
2360 2370 2380 2390 2400
GKSKNNRPLR TSQIYAQDEN ATHTQLYTSH FELMKMTAGK RSPPIKPLLG
2410 2420 2430 2440 2450
MNPFQKNPKH ASVLAESGIN YDKPLPPIQV ASLRAERIAK EKKALADQQK
2460 2470 2480 2490 2500
AQQPPVTQPP PQQQQQQQQQ QQQQQQQQQP PPPPQQPPPP VPQPQAASSQ
2510 2520 2530 2540 2550
TPAGQPAVQP QPQPQVQTQP QPVQPQSKGQ PTMTTVGSAA VLAGTIKTSV
2560 2570 2580 2590 2600
TGTSIPTGTV SGNVIVNTIA GVPAATFQSI NKRLASPVAP GTLTTSGGSA
2610 2620 2630 2640 2650
PAQVVHTQQR AVGSPATATT DLVSMTTTQG VRAVTSVTAS AVVTTNLTPV
2660 2670 2680 2690 2700
QTPTRSLVTQ VSQATGVQLP GKTITPAAHF QLLRQQQQQQ QQQQQQQQTS
2710 2720 2730 2740 2750
QVQVPQLQSQ AQSPAQIKAV SKLGPEHIIK MQKQKMQLPP QPPPPQAQPG
2760 2770 2780 2790 2800
PPQQPAQVQV QTPQPPQQQQ SPQLTTVTAP RPGALLTGTT VTNLQVARLT
2810 2820 2830 2840 2850
RVPTSQLQAQ GQMQTQTPQP AQVALAKPPV VSVPAAVVSS PGVTTLPMNV
2860 2870 2880 2890 2900
AGISVAIGQP QKTAGQTVVA QPVNVQQLLK YKQQTAVQQQ KAIQPQVAQG
2910 2920 2930 2940 2950
QAAVQQKLTT QQITTQGPQQ KVAYAAQPAL KTQFLTTPIS QAQKLAGTQQ
2960 2970 2980 2990 3000
VQTQIQVAKL PQVVQQQTPV ASIQQVASAS QQASPQTVTL TQATAAGQQV
3010 3020 3030 3040 3050
QMIPTVTATA QLVQQKLIQQ QVVTTASASL QTPGGPSPAQ LPASSDSPSQ
3060 3070
QPKLQMRVPA VRLKTPTKPP CQ
Length:3,072
Mass (Da):337,180
Last modified:July 27, 2011 - v3
Checksum:i02990AAF5FAB7CEF
GO
Isoform 2 (identifier: Q8CHI8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-482: Missing.

Show »
Length:3,035
Mass (Da):333,399
Checksum:i523E218E21EF0D63
GO
Isoform 3 (identifier: Q8CHI8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-482: Missing.
     513-548: Missing.

Show »
Length:2,999
Mass (Da):329,486
Checksum:i8FA686677DA6A7F4
GO
Isoform 4 (identifier: Q8CHI8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2800-2806: Missing.

Note: No experimental confirmation available.
Show »
Length:3,065
Mass (Da):336,410
Checksum:iD27440C486EA5F2E
GO
Isoform 5 (identifier: Q8CHI8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1764-1919: Missing.
     2800-2806: Missing.

Note: No experimental confirmation available.
Show »
Length:2,909
Mass (Da):318,235
Checksum:i2783A7314508CE76
GO

Sequence cautioni

The sequence BAB24439.1 differs from that shown.Intron retention.Curated
The sequence BAC26781.1 differs from that shown.Intron retention.Curated
The sequence BAC32913.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021G → S in BAC26781 (PubMed:16141072).Curated
Sequence conflicti107 – 1071A → D in BAC29849 (PubMed:16141072).Curated
Sequence conflicti163 – 1631N → S in BAC45253 (PubMed:12653961).Curated
Sequence conflicti163 – 1631N → S in BAC45254 (PubMed:12653961).Curated
Sequence conflicti678 – 6869TVASTRPPL → VLCGHWLFY in BAB24439 (PubMed:16141072).Curated
Sequence conflicti678 – 6869TVASTRPPL → VLCGHWLFY in BAC26781 (PubMed:16141072).Curated
Sequence conflicti896 – 8961E → G in BAC29849 (PubMed:16141072).Curated
Sequence conflicti2249 – 22491K → N in BAC32913 (PubMed:16141072).Curated
Sequence conflicti2353 – 23597SKNNRPL → LICEANP in BAC32913 (PubMed:16141072).Curated
Sequence conflicti2518 – 25181T → A in BAC45253 (PubMed:12653961).Curated
Sequence conflicti2518 – 25181T → A in BAC45254 (PubMed:12653961).Curated
Sequence conflicti2518 – 25181T → A in AAH22153 (PubMed:15489334).Curated
Sequence conflicti2539 – 25391A → V in BAC45253 (PubMed:12653961).Curated
Sequence conflicti2539 – 25391A → V in BAC45254 (PubMed:12653961).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei446 – 48237Missing in isoform 2 and isoform 3. 2 PublicationsVSP_011996Add
BLAST
Alternative sequencei513 – 54836Missing in isoform 3. 2 PublicationsVSP_011997Add
BLAST
Alternative sequencei1764 – 1919156Missing in isoform 5. 1 PublicationVSP_017127Add
BLAST
Alternative sequencei2800 – 28067Missing in isoform 4 and isoform 5. 2 PublicationsVSP_011998

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB092694 mRNA. Translation: BAC45253.1.
AB092695 mRNA. Translation: BAC45254.1.
AC161348 Genomic DNA. No translation available.
AK006168 mRNA. Translation: BAB24439.1. Sequence problems.
AK030095 mRNA. Translation: BAC26781.1. Sequence problems.
AK037693 mRNA. Translation: BAC29849.2.
AK046892 mRNA. Translation: BAC32913.2. Different initiation.
AK163566 mRNA. Translation: BAE37399.1.
AK164049 mRNA. Translation: BAE37604.1.
AK122517 Transcribed RNA. Translation: BAC65799.2.
BC022153 mRNA. Translation: AAH22153.1.
BC085511 mRNA. Translation: AAH85511.1.
CCDSiCCDS19529.1. [Q8CHI8-2]
CCDS51612.1. [Q8CHI8-3]
RefSeqiNP_083613.2. NM_029337.2. [Q8CHI8-2]
NP_775089.1. NM_173066.1. [Q8CHI8-3]
XP_006535339.1. XM_006535276.2. [Q8CHI8-4]
UniGeneiMm.270487.

Genome annotation databases

EnsembliENSMUST00000041558; ENSMUSP00000049038; ENSMUSG00000029505. [Q8CHI8-2]
ENSMUST00000112435; ENSMUSP00000108054; ENSMUSG00000029505. [Q8CHI8-5]
ENSMUST00000112436; ENSMUSP00000108055; ENSMUSG00000029505. [Q8CHI8-3]
GeneIDi75560.
KEGGimmu:75560.
UCSCiuc008yrf.1. mouse. [Q8CHI8-4]
uc008yrg.1. mouse. [Q8CHI8-2]
uc008yrh.1. mouse. [Q8CHI8-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB092694 mRNA. Translation: BAC45253.1.
AB092695 mRNA. Translation: BAC45254.1.
AC161348 Genomic DNA. No translation available.
AK006168 mRNA. Translation: BAB24439.1. Sequence problems.
AK030095 mRNA. Translation: BAC26781.1. Sequence problems.
AK037693 mRNA. Translation: BAC29849.2.
AK046892 mRNA. Translation: BAC32913.2. Different initiation.
AK163566 mRNA. Translation: BAE37399.1.
AK164049 mRNA. Translation: BAE37604.1.
AK122517 Transcribed RNA. Translation: BAC65799.2.
BC022153 mRNA. Translation: AAH22153.1.
BC085511 mRNA. Translation: AAH85511.1.
CCDSiCCDS19529.1. [Q8CHI8-2]
CCDS51612.1. [Q8CHI8-3]
RefSeqiNP_083613.2. NM_029337.2. [Q8CHI8-2]
NP_775089.1. NM_173066.1. [Q8CHI8-3]
XP_006535339.1. XM_006535276.2. [Q8CHI8-4]
UniGeneiMm.270487.

3D structure databases

ProteinModelPortaliQ8CHI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi217577. 16 interactions.
DIPiDIP-61766N.
IntActiQ8CHI8. 10 interactions.
MINTiMINT-4115994.
STRINGi10090.ENSMUSP00000049038.

PTM databases

iPTMnetiQ8CHI8.
PhosphoSiteiQ8CHI8.

Proteomic databases

EPDiQ8CHI8.
MaxQBiQ8CHI8.
PaxDbiQ8CHI8.
PeptideAtlasiQ8CHI8.
PRIDEiQ8CHI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041558; ENSMUSP00000049038; ENSMUSG00000029505. [Q8CHI8-2]
ENSMUST00000112435; ENSMUSP00000108054; ENSMUSG00000029505. [Q8CHI8-5]
ENSMUST00000112436; ENSMUSP00000108055; ENSMUSG00000029505. [Q8CHI8-3]
GeneIDi75560.
KEGGimmu:75560.
UCSCiuc008yrf.1. mouse. [Q8CHI8-4]
uc008yrg.1. mouse. [Q8CHI8-2]
uc008yrh.1. mouse. [Q8CHI8-3]

Organism-specific databases

CTDi57634.
MGIiMGI:1276124. Ep400.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0391. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00530000063427.
HOVERGENiHBG051488.
InParanoidiQ8CHI8.
KOiK11320.
OMAiAQVVHTQ.
OrthoDBiEOG7PVWPN.
TreeFamiTF106424.

Enzyme and pathway databases

ReactomeiR-MMU-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
R-MMU-2559586. DNA Damage/Telomere Stress Induced Senescence.

Miscellaneous databases

ChiTaRSiEp400. mouse.
PROiQ8CHI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CHI8.
CleanExiMM_EP400.
ExpressionAtlasiQ8CHI8. baseline and differential.
GenevisibleiQ8CHI8. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031575. EP400_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014012. HSA_dom.
IPR017877. Myb-like_dom.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF15790. EP400_N. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00573. HSA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A SWI2/SNF2-type ATPase/helicase protein, mDomino, interacts with myeloid zinc finger protein 2A (MZF-2A) to regulate its transcriptional activity."
    Ogawa H., Ueda T., Aoyama T., Aronheim A., Nagata S., Fukunaga R.
    Genes Cells 8:325-339(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH ZNF42.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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 1-896 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-894 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-677 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 992-2359.
    Strain: C57BL/6J.
    Tissue: Cerebellum, Corpora quadrigemina, Embryo, Testis and Thymus.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1415-3072 (ISOFORM 5).
    Tissue: Brain.
  5. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  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 1881-3072 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2429-3072 (ISOFORMS 1/2/3).
    Strain: C57BL/6J and FVB/N-3.
    Tissue: Brain and Mammary gland.
  7. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2443-2450, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "PHF5A represents a bridge protein between splicing proteins and ATP-dependent helicases and is differentially expressed during mouse spermatogenesis."
    Rzymski T., Grzmil P., Meinhardt A., Wolf S., Burfeind P.
    Cytogenet. Genome Res. 121:232-244(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHF5A.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-134; SER-315; SER-321; SER-741; SER-754; THR-922; SER-923; SER-927; SER-940; THR-944; SER-1009 AND SER-1010, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiEP400_MOUSE
AccessioniPrimary (citable) accession number: Q8CHI8
Secondary accession number(s): E9QKV1
, Q3TPY1, Q5RKN8, Q80TC8, Q8BXI5, Q8BYW3, Q8C0P6, Q8CHI7, Q8VDF4, Q9DA54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.