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Q96L91

- EP400_HUMAN

UniProt

Q96L91 - EP400_HUMAN

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Protein

E1A-binding protein p400

Gene

EP400

Organism
Homo sapiens (Human)
Status
Reviewed - 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. May regulate ZNF42 transcription activity. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1116 – 11238ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: InterPro
  3. DNA binding Source: UniProtKB-KW
  4. helicase activity Source: UniProtKB-KW

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. histone H2A acetylation Source: UniProtKB
  3. histone H4 acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
E1A-binding protein p400 (EC:3.6.4.-)
Alternative name(s):
CAG repeat protein 32
Domino homolog
Short name:
hDomino
Trinucleotide repeat-containing gene 12 protein
p400 kDa SWI2/SNF2-related protein
Gene namesi
Name:EP400
Synonyms:CAGH32, KIAA1498, KIAA1818, TNRC12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11958. EP400.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. NuA4 histone acetyltransferase complex Source: UniProtKB
  2. nuclear speck Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. Swr1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27808.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31593159E1A-binding protein p400PRO_0000074312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei736 – 7361Phosphoserine2 Publications
Modified residuei941 – 9411Phosphoserine1 Publication
Modified residuei945 – 9451Phosphothreonine1 Publication
Modified residuei1472 – 14721N6-acetyllysine1 Publication
Modified residuei1728 – 17281Phosphoserine1 Publication
Modified residuei1732 – 17321Phosphoserine1 Publication
Modified residuei2349 – 23491N6-acetyllysine1 Publication
Modified residuei2356 – 23561N6-acetyllysine1 Publication
Modified residuei2813 – 28131Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96L91.
PaxDbiQ96L91.
PRIDEiQ96L91.

PTM databases

PhosphoSiteiQ96L91.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ96L91.
CleanExiHS_EP400.
GenevestigatoriQ96L91.

Organism-specific databases

HPAiHPA016704.

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 and the adenovirus E1A protein. EP400 interacts with TRRAP, RUVBL1 and RUVBL2. Component of a SWR1-like complex. Interacts with ZNF42. Interacts with PHF5A (By similarity).By similarity

Protein-protein interaction databases

BioGridi121676. 30 interactions.
DIPiDIP-29915N.
IntActiQ96L91. 11 interactions.
MINTiMINT-1897496.
STRINGi9606.ENSP00000374213.

Structurei

3D structure databases

ProteinModelPortaliQ96L91.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini799 – 87173HSAPROSITE-ProRule annotationAdd
BLAST
Domaini1103 – 1268166Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1899 – 2056158Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2360 – 242970Myb-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni951 – 1365415Interactions with RUVBL1 and RUVBL2Add
BLAST
Regioni2524 – 2789266Interaction with ZNF42By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1219 – 12224DEAH box-like

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi278 – 2814Poly-Gln
Compositional biasi316 – 3194Poly-Pro
Compositional biasi426 – 43712Poly-GluAdd
BLAST
Compositional biasi1517 – 15226Poly-Ala
Compositional biasi2543 – 255412Poly-ProAdd
BLAST
Compositional biasi2557 – 25648Poly-Pro
Compositional biasi2756 – 278429Poly-GlnAdd
BLAST
Compositional biasi2828 – 28347Poly-Pro

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

eggNOGiCOG0553.
GeneTreeiENSGT00530000063427.
HOVERGENiHBG051488.
InParanoidiQ96L91.
KOiK11320.
OMAiAQVVHTQ.
OrthoDBiEOG7PVWPN.
PhylomeDBiQ96L91.
TreeFamiTF106424.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR013999. HAS_subgr.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR017877. Myb-like_dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00573. HSA. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 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. Align

Isoform 1 (identifier: Q96L91-1) [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
MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA
60 70 80 90 100
PQSPSYQIQQ LMNRSPATGQ NVNITLQSVG PVVGGNQQIT LAPLPLPSPT
110 120 130 140 150
SPGFQFSAQP RRFEHGSPSY IQVTSPLSQQ VQTQSPTQPS PGPGQALQNV
160 170 180 190 200
RAGAPGPGLG LCSSSPTGGF VDASVLVRQI SLSPSSGGHF VFQDGSGLTQ
210 220 230 240 250
IAQGAQVQLQ HPGTPITVRE RRPSQPHTQS GGTIHHLGPQ SPAAAGGAGL
260 270 280 290 300
QPLASPSHIT TANLPPQISS IIQGQLVQQQ QVLQGPPLPR PLGFERTPGV
310 320 330 340 350
LLPGAGGAAG FGMTSPPPPT SPSRTAVPPG LSSLPLTSVG NTGMKKVPKK
360 370 380 390 400
LEEIPPASPE MAQMRKQCLD YHYQEMQALK EVFKEYLIEL FFLQHFQGNM
410 420 430 440 450
MDFLAFKKKH YAPLQAYLRQ NDLDIEEEEE EEEEEEEKSE VINDEVKVVT
460 470 480 490 500
GKDGQTGTPV AIATQLPPKV SAAFSSQQQP FQQALAGSLV AGAGSTVETD
510 520 530 540 550
LFKRQQAMPS TGMAEQSKRP RLEVGHQGVV FQHPGADAGV PLQQLMPTAQ
560 570 580 590 600
GGMPPTPQAA QLAGQRQSQQ QYDPSTGPPV QNAASLHTPL PQLPGRLPPA
610 620 630 640 650
GVPTAALSSA LQFAQQPQVV EAQTQLQIPV KTQQPNVPIP APPSSQLPIP
660 670 680 690 700
PSQPAQLALH VPTPGKVQVQ ASQLSSLPQM VASTRLPVDP APPCPRPLPT
710 720 730 740 750
SSTSSLAPVS GSGPGPSPAR SSPVNRPSSA TNKALSPVTS RTPGVVASAP
760 770 780 790 800
TKPQSPAQNA TSSQDSSQDT LTEQITLENQ VHQRIAELRK AGLWSQRRLP
810 820 830 840 850
KLQEAPRPKS HWDYLLEEMQ WMATDFAQER RWKVAAAKKL VRTVVRHHEE
860 870 880 890 900
KQLREERGKK EEQSRLRRIA ASTAREIECF WSNIEQVVEI KLRVELEEKR
910 920 930 940 950
KKALNLQKVS RRGKELRPKG FDALQESSLD SGMSGRKRKA SISLTDDEVD
960 970 980 990 1000
DEEETIEEEE ANEGVVDHQT ELSNLAKEAE LPLLDLMKLY EGAFLPSSQW
1010 1020 1030 1040 1050
PRPKPDGEDT SGEEDADDCP GDRESRKDLV LIDSLFIMDQ FKAAERMNIG
1060 1070 1080 1090 1100
KPNAKDIADV TAVAEAILPK GSARVTTSVK FNAPSLLYGA LRDYQKIGLD
1110 1120 1130 1140 1150
WLAKLYRKNL NGILADEAGL GKTVQIIAFF AHLACNEGNW GPHLVVVRSC
1160 1170 1180 1190 1200
NILKWELELK RWCPGLKILS YIGSHRELKA KRQEWAEPNS FHVCITSYTQ
1210 1220 1230 1240 1250
FFRGLTAFTR VRWKCLVIDE MQRVKGMTER HWEAVFTLQS QQRLLLIDSP
1260 1270 1280 1290 1300
LHNTFLELWT MVHFLVPGIS RPYLSSPLRA PSEESQDYYH KVVIRLHRVT
1310 1320 1330 1340 1350
QPFILRRTKR DVEKQLTKKY EHVLKCRLSN RQKALYEDVI LQPGTQEALK
1360 1370 1380 1390 1400
SGHFVNVLSI LVRLQRICNH PGLVEPRHPG SSYVAGPLEY PSASLILKAL
1410 1420 1430 1440 1450
ERDFWKEADL SMFDLIGLEN KITRHEAELL SKKKIPRKLM EEISTSAAPA
1460 1470 1480 1490 1500
ARPAAAKLKA SRLFQPVQYG QKPEGRTVAF PSTHPPRTAA PTTASAAPQG
1510 1520 1530 1540 1550
PLRGRPPIAT FSANPEAKAA AAPFQTSQAS ASAPRHQPAS ASSTAASPAH
1560 1570 1580 1590 1600
PAKLRAQTTA QASTPGQPPP QPQAPSHAAG QSALPQRLVL PSQAQARLPS
1610 1620 1630 1640 1650
GEVVKIAQLA SITGPQSRVA QPETPVTLQF QGSKFTLSHS QLRQLTAGQP
1660 1670 1680 1690 1700
LQLQGSVLQI VSAPGQPYLR APGPVVMQTV SQAGAVHGAL GSKPPAGGPS
1710 1720 1730 1740 1750
PAPLTPQVGV PGRVAVNALA VGEPGTASKP ASPIGGPTQE EKTRLLKERL
1760 1770 1780 1790 1800
DQIYLVNERR CSQAPVYGRD LLRICALPSH GRVQWRGSLD GRRGKEAGPA
1810 1820 1830 1840 1850
HSYTSSSESP SELMLTLCRC GESLQDVIDR VAFVIPPVVA APPSLRVPRP
1860 1870 1880 1890 1900
PPLYSHRMRI LRQGLREHAA PYFQQLRQTT APRLLQFPEL RLVQFDSGKL
1910 1920 1930 1940 1950
EALAILLQKL KSEGRRVLIL SQMILMLDIL EMFLNFHYLT YVRIDENASS
1960 1970 1980 1990 2000
EQRQELMRSF NRDRRIFCAI LSTHSRTTGI NLVEADTVVF YDNDLNPVMD
2010 2020 2030 2040 2050
AKAQEWCDRI GRCKDIHIYR LVSGNSIEEK LLKNGTKDLI REVAAQGNDY
2060 2070 2080 2090 2100
SMAFLTQRTI QELFEVYSPM DDAGFPVKAE EFVVLSQEPS VTETIAPKIA
2110 2120 2130 2140 2150
RPFIEALKSI EYLEEDAQKS AQEGVLGPHT DALSSDSENM PCDEEPSQLE
2160 2170 2180 2190 2200
ELADFMEQLT PIEKYALNYL ELFHTSIEQE KERNSEDAVM TAVRAWEFWN
2210 2220 2230 2240 2250
LKTLQEREAR LRLEQEEAEL LTYTREDAYS MEYVYEDVDG QTEVMPLWTP
2260 2270 2280 2290 2300
PTPPQDDSDI YLDSVMCLMY EATPIPEAKL PPVYVRKERK RHKTDPSAAG
2310 2320 2330 2340 2350
RKKKQRHGEA VVPPRSLFDR ATPGLLKIRR EGKEQKKNIL LKQQVPFAKP
2360 2370 2380 2390 2400
LPTFAKPTAE PGQDNPEWLI SEDWALLQAV KQLLELPLNL TIVSPAHTPN
2410 2420 2430 2440 2450
WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA
2460 2470 2480 2490 2500
QDENATHTQL YTSHFDLMKM TAGKRSPPIK PLLGMNPFQK NPKHASVLAE
2510 2520 2530 2540 2550
SGINYDKPLP PIQVASLRAE RIAKEKKALA DQQKAQQPAV AQPPPPQPQP
2560 2570 2580 2590 2600
PPPPQQPPPP LPQPQAAGSQ PPAGPPAVQP QPQPQPQTQP QPVQAPAKAQ
2610 2620 2630 2640 2650
PAITTGGSAA VLAGTIKTSV TGTSMPTGAV SGNVIVNTIA GVPAATFQSI
2660 2670 2680 2690 2700
NKRLASPVAP GALTTPGGSA PAQVVHTQPP PRAVGSPATA TPDLVSMATT
2710 2720 2730 2740 2750
QGVRAVTSVT ASAVVTTNLT PVQTPARSLV PQVSQATGVQ LPGKTITPAH
2760 2770 2780 2790 2800
FQLLRQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQTTTTSQ VQVPQIQGQA
2810 2820 2830 2840 2850
QSPAQIKAVG KLTPEHLIKM QKQKLQMPPQ PPPPQAQSAP PQPTAQVQVQ
2860 2870 2880 2890 2900
TSQPPQQQSP QLTTVTAPRP GALLTGTTVA NLQVARLTRV PTSQLQAQGQ
2910 2920 2930 2940 2950
MQTQAPQPAQ VALAKPPVVS VPAAVVSSPG VTTLPMNVAG ISVAIGQPQK
2960 2970 2980 2990 3000
AAGQTVVAQP VHMQQLLKLK QQAVQQQKAI QPQAAQGPAA VQQKITAQQI
3010 3020 3030 3040 3050
TTPGAQQKVA YAAQPALKTQ FLTTPISQAQ KLAGAQQVQT QIQVAKLPQV
3060 3070 3080 3090 3100
VQQQTPVASI QQVASASQQA SPQTVALTQA TAAGQQVQMI PAVTATAQVV
3110 3120 3130 3140 3150
QQKLIQQQVV TTASAPLQTP GAPNPAQVPA SSDSPSQQPK LQMRVPAVRL

KTPTKPPCQ
Length:3,159
Mass (Da):343,489
Last modified:January 11, 2011 - v4
Checksum:i0E502CE1BE9CFAC1
GO
Isoform 2 (identifier: Q96L91-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-481: Missing.

Show »
Length:3,123
Mass (Da):339,823
Checksum:i846B71A59CE2B201
GO
Isoform 3 (identifier: Q96L91-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-481: Missing.
     482-482: Missing.
     515-550: Missing.

Note: No experimental confirmation available.

Show »
Length:3,086
Mass (Da):335,805
Checksum:i706B650493BC8580
GO
Isoform 4 (identifier: Q96L91-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-481: Missing.
     1519-1600: AAAAPFQTSQ...PSQAQARLPS → G

Note: No experimental confirmation available.

Show »
Length:3,042
Mass (Da):331,778
Checksum:i6D57F7F463C74FE1
GO
Isoform 5 (identifier: Q96L91-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     446-481: Missing.
     482-482: Missing.

Note: No experimental confirmation available.

Show »
Length:3,122
Mass (Da):339,695
Checksum:i0F04797ACF402088
GO

Sequence cautioni

The sequence AAH37208.1 differs from that shown. Reason: Intron retention.
The sequence AAH64554.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAB91441.1 differs from that shown. Reason: Frameshift at positions 2959 and 3020.
The sequence BAA96022.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti537 – 5371D → G in AAH37208. (PubMed:15489334)Curated
Sequence conflicti810 – 8101S → P in AAH37208. (PubMed:15489334)Curated
Sequence conflicti1563 – 15631S → F in AAK97789. (PubMed:11509179)Curated
Sequence conflicti1642 – 16421L → F in AAK97789. (PubMed:11509179)Curated
Sequence conflicti1645 – 16451L → F in AAK97789. (PubMed:11509179)Curated
Sequence conflicti2756 – 27561Q → QQ in AAK97789. (PubMed:11509179)Curated
Sequence conflicti2756 – 27561Q → QQ in BAB47447. (PubMed:11347906)Curated
Sequence conflicti2756 – 27561Q → QQ in AAB91441. (PubMed:9225980)Curated
Sequence conflicti2844 – 28441T → A in AAK97789. (PubMed:11509179)Curated
Sequence conflicti2844 – 28441T → A in AAB91441. (PubMed:9225980)Curated
Sequence conflicti2897 – 28971A → S in AAK97789. (PubMed:11509179)Curated
Sequence conflicti2897 – 28971A → S in AAB91441. (PubMed:9225980)Curated
Sequence conflicti2912 – 29143ALA → PLP in AAK97789. (PubMed:11509179)Curated
Sequence conflicti2912 – 29143ALA → PLP in AAB91441. (PubMed:9225980)Curated
Sequence conflicti2990 – 29901A → T in AAK97789. (PubMed:11509179)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1308 – 13081T → I.
Corresponds to variant rs13377636 [ dbSNP | Ensembl ].
VAR_046957

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei446 – 48136Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_011992Add
BLAST
Alternative sequencei482 – 4821Missing in isoform 3 and isoform 5. 2 PublicationsVSP_011993
Alternative sequencei515 – 55036Missing in isoform 3. 2 PublicationsVSP_011994Add
BLAST
Alternative sequencei1519 – 160082AAAAP…ARLPS → G in isoform 4. 1 PublicationVSP_011995Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY044869 mRNA. Translation: AAK97789.1.
AC137590 Genomic DNA. No translation available.
AC137632 Genomic DNA. No translation available.
AB040931 mRNA. Translation: BAA96022.1. Different initiation.
AK096311 mRNA. Translation: BAC04759.1.
BC037208 mRNA. Translation: AAH37208.1. Sequence problems.
BC064554 mRNA. Translation: AAH64554.1. Sequence problems.
AB058721 mRNA. Translation: BAB47447.1.
U80743 mRNA. Translation: AAB91441.1. Frameshift.
CCDSiCCDS31929.2. [Q96L91-2]
RefSeqiNP_056224.3. NM_015409.4. [Q96L91-2]
UniGeneiHs.723478.

Genome annotation databases

EnsembliENST00000389561; ENSP00000374212; ENSG00000183495. [Q96L91-2]
ENST00000389562; ENSP00000374213; ENSG00000183495. [Q96L91-2]
GeneIDi57634.
KEGGihsa:57634.
UCSCiuc001ujm.3. human. [Q96L91-4]
uc001ujn.3. human. [Q96L91-2]

Polymorphism databases

DMDMi317373565.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY044869 mRNA. Translation: AAK97789.1 .
AC137590 Genomic DNA. No translation available.
AC137632 Genomic DNA. No translation available.
AB040931 mRNA. Translation: BAA96022.1 . Different initiation.
AK096311 mRNA. Translation: BAC04759.1 .
BC037208 mRNA. Translation: AAH37208.1 . Sequence problems.
BC064554 mRNA. Translation: AAH64554.1 . Sequence problems.
AB058721 mRNA. Translation: BAB47447.1 .
U80743 mRNA. Translation: AAB91441.1 . Frameshift.
CCDSi CCDS31929.2. [Q96L91-2 ]
RefSeqi NP_056224.3. NM_015409.4. [Q96L91-2 ]
UniGenei Hs.723478.

3D structure databases

ProteinModelPortali Q96L91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121676. 30 interactions.
DIPi DIP-29915N.
IntActi Q96L91. 11 interactions.
MINTi MINT-1897496.
STRINGi 9606.ENSP00000374213.

PTM databases

PhosphoSitei Q96L91.

Polymorphism databases

DMDMi 317373565.

Proteomic databases

MaxQBi Q96L91.
PaxDbi Q96L91.
PRIDEi Q96L91.

Protocols and materials databases

DNASUi 57634.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389561 ; ENSP00000374212 ; ENSG00000183495 . [Q96L91-2 ]
ENST00000389562 ; ENSP00000374213 ; ENSG00000183495 . [Q96L91-2 ]
GeneIDi 57634.
KEGGi hsa:57634.
UCSCi uc001ujm.3. human. [Q96L91-4 ]
uc001ujn.3. human. [Q96L91-2 ]

Organism-specific databases

CTDi 57634.
GeneCardsi GC12P132434.
H-InvDB HIX0021564.
HGNCi HGNC:11958. EP400.
HPAi HPA016704.
MIMi 606265. gene.
neXtProti NX_Q96L91.
PharmGKBi PA27808.
HUGEi Search...
Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00530000063427.
HOVERGENi HBG051488.
InParanoidi Q96L91.
KOi K11320.
OMAi AQVVHTQ.
OrthoDBi EOG7PVWPN.
PhylomeDBi Q96L91.
TreeFami TF106424.

Enzyme and pathway databases

Reactomei REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi EP400. human.
GeneWikii EP400.
GenomeRNAii 57634.
NextBioi 64345.
PROi Q96L91.
SOURCEi Search...

Gene expression databases

Bgeei Q96L91.
CleanExi HS_EP400.
Genevestigatori Q96L91.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR013999. HAS_subgr.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR017877. Myb-like_dom.
IPR027417. P-loop_NTPase.
IPR001005. SANT/Myb.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00573. HSA. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 4 hits.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS50090. MYB_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY, ROLE OF EP400-CONTAINING COMPLEXES IN CELLULAR TRANSFORMATION BY ADENOVIRUS E1A PROTEIN, TISSUE SPECIFICITY, INTERACTION WITH TRRAP; RUVBL1 AND RUVBL2.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1847 (ISOFORM 4).
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-897 (ISOFORM 3).
  5. "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 1-978 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-895 (ISOFORM 3).
    Tissue: Lymph and Testis.
  6. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2004-3159.
    Tissue: Brain.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2463-3159.
    Tissue: Brain.
  8. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN NUA4 COMPLEX.
  9. "The highly conserved and multifunctional NuA4 HAT complex."
    Doyon Y., Cote J.
    Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON NUA4 COMPLEX.
  10. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN SRCAP-CONTAINING COMPLEX.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; THR-945; SER-1728 AND SER-1732, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1472; LYS-2349 AND LYS-2356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND THR-2813, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.

Entry informationi

Entry nameiEP400_HUMAN
AccessioniPrimary (citable) accession number: Q96L91
Secondary accession number(s): O15411
, Q6P2F5, Q8N8Q7, Q8NE05, Q96JK7, Q9P230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3