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Q96L91

- EP400_HUMAN

UniProt

Q96L91 - EP400_HUMAN

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Protein
E1A-binding protein p400
Gene
EP400, CAGH32, KIAA1498, KIAA1818, TNRC12
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 – 11238ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. chromatin binding Source: InterPro
  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 By similarity

GO - Cellular componenti

  1. NuA4 histone acetyltransferase complex Source: UniProtKB
  2. Swr1 complex Source: UniProtKB
  3. nuclear speck Source: UniProtKB
  4. nucleoplasm Source: Reactome
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 p400
PRO_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

ArrayExpressiQ96L91.
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.4 Publications

Protein-protein interaction databases

BioGridi121676. 25 interactions.
DIPiDIP-29915N.
IntActiQ96L91. 11 interactions.
MINTiMINT-1897496.
STRINGi9606.ENSP00000374213.

Structurei

3D structure databases

ProteinModelPortaliQ96L91.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini799 – 87173HSA
Add
BLAST
Domaini1103 – 1268166Helicase ATP-binding
Add
BLAST
Domaini1899 – 2056158Helicase C-terminal
Add
BLAST
Domaini2360 – 242970Myb-like
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni951 – 1365415Interactions with RUVBL1 and RUVBL2
Add
BLAST
Regioni2524 – 2789266Interaction with ZNF42 By similarity
Add
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-Glu
Add
BLAST
Compositional biasi1517 – 15226Poly-Ala
Compositional biasi2543 – 255412Poly-Pro
Add
BLAST
Compositional biasi2557 – 25648Poly-Pro
Compositional biasi2756 – 278429Poly-Gln
Add
BLAST
Compositional biasi2828 – 28347Poly-Pro

Sequence similaritiesi

Contains 1 HSA domain.
Contains 1 Myb-like domain.

Phylogenomic databases

eggNOGiCOG0553.
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

MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA     50
PQSPSYQIQQ LMNRSPATGQ NVNITLQSVG PVVGGNQQIT LAPLPLPSPT 100
SPGFQFSAQP RRFEHGSPSY IQVTSPLSQQ VQTQSPTQPS PGPGQALQNV 150
RAGAPGPGLG LCSSSPTGGF VDASVLVRQI SLSPSSGGHF VFQDGSGLTQ 200
IAQGAQVQLQ HPGTPITVRE RRPSQPHTQS GGTIHHLGPQ SPAAAGGAGL 250
QPLASPSHIT TANLPPQISS IIQGQLVQQQ QVLQGPPLPR PLGFERTPGV 300
LLPGAGGAAG FGMTSPPPPT SPSRTAVPPG LSSLPLTSVG NTGMKKVPKK 350
LEEIPPASPE MAQMRKQCLD YHYQEMQALK EVFKEYLIEL FFLQHFQGNM 400
MDFLAFKKKH YAPLQAYLRQ NDLDIEEEEE EEEEEEEKSE VINDEVKVVT 450
GKDGQTGTPV AIATQLPPKV SAAFSSQQQP FQQALAGSLV AGAGSTVETD 500
LFKRQQAMPS TGMAEQSKRP RLEVGHQGVV FQHPGADAGV PLQQLMPTAQ 550
GGMPPTPQAA QLAGQRQSQQ QYDPSTGPPV QNAASLHTPL PQLPGRLPPA 600
GVPTAALSSA LQFAQQPQVV EAQTQLQIPV KTQQPNVPIP APPSSQLPIP 650
PSQPAQLALH VPTPGKVQVQ ASQLSSLPQM VASTRLPVDP APPCPRPLPT 700
SSTSSLAPVS GSGPGPSPAR SSPVNRPSSA TNKALSPVTS RTPGVVASAP 750
TKPQSPAQNA TSSQDSSQDT LTEQITLENQ VHQRIAELRK AGLWSQRRLP 800
KLQEAPRPKS HWDYLLEEMQ WMATDFAQER RWKVAAAKKL VRTVVRHHEE 850
KQLREERGKK EEQSRLRRIA ASTAREIECF WSNIEQVVEI KLRVELEEKR 900
KKALNLQKVS RRGKELRPKG FDALQESSLD SGMSGRKRKA SISLTDDEVD 950
DEEETIEEEE ANEGVVDHQT ELSNLAKEAE LPLLDLMKLY EGAFLPSSQW 1000
PRPKPDGEDT SGEEDADDCP GDRESRKDLV LIDSLFIMDQ FKAAERMNIG 1050
KPNAKDIADV TAVAEAILPK GSARVTTSVK FNAPSLLYGA LRDYQKIGLD 1100
WLAKLYRKNL NGILADEAGL GKTVQIIAFF AHLACNEGNW GPHLVVVRSC 1150
NILKWELELK RWCPGLKILS YIGSHRELKA KRQEWAEPNS FHVCITSYTQ 1200
FFRGLTAFTR VRWKCLVIDE MQRVKGMTER HWEAVFTLQS QQRLLLIDSP 1250
LHNTFLELWT MVHFLVPGIS RPYLSSPLRA PSEESQDYYH KVVIRLHRVT 1300
QPFILRRTKR DVEKQLTKKY EHVLKCRLSN RQKALYEDVI LQPGTQEALK 1350
SGHFVNVLSI LVRLQRICNH PGLVEPRHPG SSYVAGPLEY PSASLILKAL 1400
ERDFWKEADL SMFDLIGLEN KITRHEAELL SKKKIPRKLM EEISTSAAPA 1450
ARPAAAKLKA SRLFQPVQYG QKPEGRTVAF PSTHPPRTAA PTTASAAPQG 1500
PLRGRPPIAT FSANPEAKAA AAPFQTSQAS ASAPRHQPAS ASSTAASPAH 1550
PAKLRAQTTA QASTPGQPPP QPQAPSHAAG QSALPQRLVL PSQAQARLPS 1600
GEVVKIAQLA SITGPQSRVA QPETPVTLQF QGSKFTLSHS QLRQLTAGQP 1650
LQLQGSVLQI VSAPGQPYLR APGPVVMQTV SQAGAVHGAL GSKPPAGGPS 1700
PAPLTPQVGV PGRVAVNALA VGEPGTASKP ASPIGGPTQE EKTRLLKERL 1750
DQIYLVNERR CSQAPVYGRD LLRICALPSH GRVQWRGSLD GRRGKEAGPA 1800
HSYTSSSESP SELMLTLCRC GESLQDVIDR VAFVIPPVVA APPSLRVPRP 1850
PPLYSHRMRI LRQGLREHAA PYFQQLRQTT APRLLQFPEL RLVQFDSGKL 1900
EALAILLQKL KSEGRRVLIL SQMILMLDIL EMFLNFHYLT YVRIDENASS 1950
EQRQELMRSF NRDRRIFCAI LSTHSRTTGI NLVEADTVVF YDNDLNPVMD 2000
AKAQEWCDRI GRCKDIHIYR LVSGNSIEEK LLKNGTKDLI REVAAQGNDY 2050
SMAFLTQRTI QELFEVYSPM DDAGFPVKAE EFVVLSQEPS VTETIAPKIA 2100
RPFIEALKSI EYLEEDAQKS AQEGVLGPHT DALSSDSENM PCDEEPSQLE 2150
ELADFMEQLT PIEKYALNYL ELFHTSIEQE KERNSEDAVM TAVRAWEFWN 2200
LKTLQEREAR LRLEQEEAEL LTYTREDAYS MEYVYEDVDG QTEVMPLWTP 2250
PTPPQDDSDI YLDSVMCLMY EATPIPEAKL PPVYVRKERK RHKTDPSAAG 2300
RKKKQRHGEA VVPPRSLFDR ATPGLLKIRR EGKEQKKNIL LKQQVPFAKP 2350
LPTFAKPTAE PGQDNPEWLI SEDWALLQAV KQLLELPLNL TIVSPAHTPN 2400
WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA 2450
QDENATHTQL YTSHFDLMKM TAGKRSPPIK PLLGMNPFQK NPKHASVLAE 2500
SGINYDKPLP PIQVASLRAE RIAKEKKALA DQQKAQQPAV AQPPPPQPQP 2550
PPPPQQPPPP LPQPQAAGSQ PPAGPPAVQP QPQPQPQTQP QPVQAPAKAQ 2600
PAITTGGSAA VLAGTIKTSV TGTSMPTGAV SGNVIVNTIA GVPAATFQSI 2650
NKRLASPVAP GALTTPGGSA PAQVVHTQPP PRAVGSPATA TPDLVSMATT 2700
QGVRAVTSVT ASAVVTTNLT PVQTPARSLV PQVSQATGVQ LPGKTITPAH 2750
FQLLRQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQTTTTSQ VQVPQIQGQA 2800
QSPAQIKAVG KLTPEHLIKM QKQKLQMPPQ PPPPQAQSAP PQPTAQVQVQ 2850
TSQPPQQQSP QLTTVTAPRP GALLTGTTVA NLQVARLTRV PTSQLQAQGQ 2900
MQTQAPQPAQ VALAKPPVVS VPAAVVSSPG VTTLPMNVAG ISVAIGQPQK 2950
AAGQTVVAQP VHMQQLLKLK QQAVQQQKAI QPQAAQGPAA VQQKITAQQI 3000
TTPGAQQKVA YAAQPALKTQ FLTTPISQAQ KLAGAQQVQT QIQVAKLPQV 3050
VQQQTPVASI QQVASASQQA SPQTVALTQA TAAGQQVQMI PAVTATAQVV 3100
QQKLIQQQVV TTASAPLQTP GAPNPAQVPA SSDSPSQQPK LQMRVPAVRL 3150
KTPTKPPCQ 3159
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.

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.
VSP_011992Add
BLAST
Alternative sequencei482 – 4821Missing in isoform 3 and isoform 5.
VSP_011993
Alternative sequencei515 – 55036Missing in isoform 3.
VSP_011994Add
BLAST
Alternative sequencei1519 – 160082AAAAP…ARLPS → G in isoform 4.
VSP_011995Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti537 – 5371D → G in AAH37208. 1 Publication
Sequence conflicti810 – 8101S → P in AAH37208. 1 Publication
Sequence conflicti1563 – 15631S → F in AAK97789. 1 Publication
Sequence conflicti1642 – 16421L → F in AAK97789. 1 Publication
Sequence conflicti1645 – 16451L → F in AAK97789. 1 Publication
Sequence conflicti2756 – 27561Q → QQ in AAK97789. 1 Publication
Sequence conflicti2756 – 27561Q → QQ in BAB47447. 1 Publication
Sequence conflicti2756 – 27561Q → QQ in AAB91441. 1 Publication
Sequence conflicti2844 – 28441T → A in AAK97789. 1 Publication
Sequence conflicti2844 – 28441T → A in AAB91441. 1 Publication
Sequence conflicti2897 – 28971A → S in AAK97789. 1 Publication
Sequence conflicti2897 – 28971A → S in AAB91441. 1 Publication
Sequence conflicti2912 – 29143ALA → PLP in AAK97789. 1 Publication
Sequence conflicti2912 – 29143ALA → PLP in AAB91441. 1 Publication
Sequence conflicti2990 – 29901A → T in AAK97789. 1 Publication

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

EnsembliENST00000330386; ENSP00000330620; ENSG00000183495. [Q96L91-4]
ENST00000332482; ENSP00000331737; ENSG00000183495. [Q96L91-3]
ENST00000333577; ENSP00000333602; ENSG00000183495. [Q96L91-1]
ENST00000389561; ENSP00000374212; ENSG00000183495. [Q96L91-2]
ENST00000389562; ENSP00000374213; ENSG00000183495. [Q96L91-5]
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. 25 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 ENST00000330386 ; ENSP00000330620 ; ENSG00000183495 . [Q96L91-4 ]
ENST00000332482 ; ENSP00000331737 ; ENSG00000183495 . [Q96L91-3 ]
ENST00000333577 ; ENSP00000333602 ; ENSG00000183495 . [Q96L91-1 ]
ENST00000389561 ; ENSP00000374212 ; ENSG00000183495 . [Q96L91-2 ]
ENST00000389562 ; ENSP00000374213 ; ENSG00000183495 . [Q96L91-5 ]
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.
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

ArrayExpressi Q96L91.
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: September 3, 2014
This is version 132 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

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