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Q96L91 (EP400_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EP400
Synonyms:CAGH32, KIAA1498, KIAA1818, TNRC12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3159 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.19

Subunit structure

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. Ref.1 Ref.8 Ref.10 Ref.19

Subcellular location

Nucleus By similarity.

Tissue specificity

Ubiquitously expressed. Ref.1

Sequence similarities

Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 HSA domain.

Contains 1 Myb-like domain.

Sequence caution

The sequence AAB91441.1 differs from that shown. Reason: Frameshift at positions 2959 and 3020.

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 BAA96022.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96L91-1)

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.
Isoform 2 (identifier: Q96L91-2)

The sequence of this isoform differs from the canonical sequence as follows:
     446-481: Missing.
Isoform 3 (identifier: Q96L91-3)

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.
Isoform 4 (identifier: Q96L91-4)

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.
Isoform 5 (identifier: Q96L91-5)

The sequence of this isoform differs from the canonical sequence as follows:
     446-481: Missing.
     482-482: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31593159E1A-binding protein p400
PRO_0000074312

Regions

Domain799 – 87173HSA
Domain1103 – 1268166Helicase ATP-binding
Domain1899 – 2056158Helicase C-terminal
Domain2360 – 242970Myb-like
Nucleotide binding1116 – 11238ATP Potential
Region951 – 1365415Interactions with RUVBL1 and RUVBL2
Region2524 – 2789266Interaction with ZNF42 By similarity
Motif1219 – 12224DEAH box-like
Compositional bias278 – 2814Poly-Gln
Compositional bias316 – 3194Poly-Pro
Compositional bias426 – 43712Poly-Glu
Compositional bias1517 – 15226Poly-Ala
Compositional bias2543 – 255412Poly-Pro
Compositional bias2557 – 25648Poly-Pro
Compositional bias2756 – 278429Poly-Gln
Compositional bias2828 – 28347Poly-Pro

Amino acid modifications

Modified residue7361Phosphoserine Ref.16 Ref.18
Modified residue9411Phosphoserine Ref.12
Modified residue9451Phosphothreonine Ref.12
Modified residue14721N6-acetyllysine Ref.15
Modified residue17281Phosphoserine Ref.12
Modified residue17321Phosphoserine Ref.12
Modified residue23491N6-acetyllysine Ref.15
Modified residue23561N6-acetyllysine Ref.15
Modified residue28131Phosphothreonine Ref.16

Natural variations

Alternative sequence446 – 48136Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_011992
Alternative sequence4821Missing in isoform 3 and isoform 5.
VSP_011993
Alternative sequence515 – 55036Missing in isoform 3.
VSP_011994
Alternative sequence1519 – 160082AAAAP…ARLPS → G in isoform 4.
VSP_011995
Natural variant13081T → I.
Corresponds to variant rs13377636 [ dbSNP | Ensembl ].
VAR_046957

Experimental info

Sequence conflict5371D → G in AAH37208. Ref.5
Sequence conflict8101S → P in AAH37208. Ref.5
Sequence conflict15631S → F in AAK97789. Ref.1
Sequence conflict16421L → F in AAK97789. Ref.1
Sequence conflict16451L → F in AAK97789. Ref.1
Sequence conflict27561Q → QQ in AAK97789. Ref.1
Sequence conflict27561Q → QQ in BAB47447. Ref.6
Sequence conflict27561Q → QQ in AAB91441. Ref.7
Sequence conflict28441T → A in AAK97789. Ref.1
Sequence conflict28441T → A in AAB91441. Ref.7
Sequence conflict28971A → S in AAK97789. Ref.1
Sequence conflict28971A → S in AAB91441. Ref.7
Sequence conflict2912 – 29143ALA → PLP in AAK97789. Ref.1
Sequence conflict2912 – 29143ALA → PLP in AAB91441. Ref.7
Sequence conflict29901A → T in AAK97789. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 0E502CE1BE9CFAC1

FASTA3,159343,489
        10         20         30         40         50         60 
MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ 

        70         80         90        100        110        120 
LMNRSPATGQ NVNITLQSVG PVVGGNQQIT LAPLPLPSPT SPGFQFSAQP RRFEHGSPSY 

       130        140        150        160        170        180 
IQVTSPLSQQ VQTQSPTQPS PGPGQALQNV RAGAPGPGLG LCSSSPTGGF VDASVLVRQI 

       190        200        210        220        230        240 
SLSPSSGGHF VFQDGSGLTQ IAQGAQVQLQ HPGTPITVRE RRPSQPHTQS GGTIHHLGPQ 

       250        260        270        280        290        300 
SPAAAGGAGL QPLASPSHIT TANLPPQISS IIQGQLVQQQ QVLQGPPLPR PLGFERTPGV 

       310        320        330        340        350        360 
LLPGAGGAAG FGMTSPPPPT SPSRTAVPPG LSSLPLTSVG NTGMKKVPKK LEEIPPASPE 

       370        380        390        400        410        420 
MAQMRKQCLD YHYQEMQALK EVFKEYLIEL FFLQHFQGNM MDFLAFKKKH YAPLQAYLRQ 

       430        440        450        460        470        480 
NDLDIEEEEE EEEEEEEKSE VINDEVKVVT GKDGQTGTPV AIATQLPPKV SAAFSSQQQP 

       490        500        510        520        530        540 
FQQALAGSLV AGAGSTVETD LFKRQQAMPS TGMAEQSKRP RLEVGHQGVV FQHPGADAGV 

       550        560        570        580        590        600 
PLQQLMPTAQ GGMPPTPQAA QLAGQRQSQQ QYDPSTGPPV QNAASLHTPL PQLPGRLPPA 

       610        620        630        640        650        660 
GVPTAALSSA LQFAQQPQVV EAQTQLQIPV KTQQPNVPIP APPSSQLPIP PSQPAQLALH 

       670        680        690        700        710        720 
VPTPGKVQVQ ASQLSSLPQM VASTRLPVDP APPCPRPLPT SSTSSLAPVS GSGPGPSPAR 

       730        740        750        760        770        780 
SSPVNRPSSA TNKALSPVTS RTPGVVASAP TKPQSPAQNA TSSQDSSQDT LTEQITLENQ 

       790        800        810        820        830        840 
VHQRIAELRK AGLWSQRRLP KLQEAPRPKS HWDYLLEEMQ WMATDFAQER RWKVAAAKKL 

       850        860        870        880        890        900 
VRTVVRHHEE KQLREERGKK EEQSRLRRIA ASTAREIECF WSNIEQVVEI KLRVELEEKR 

       910        920        930        940        950        960 
KKALNLQKVS RRGKELRPKG FDALQESSLD SGMSGRKRKA SISLTDDEVD DEEETIEEEE 

       970        980        990       1000       1010       1020 
ANEGVVDHQT ELSNLAKEAE LPLLDLMKLY EGAFLPSSQW PRPKPDGEDT SGEEDADDCP 

      1030       1040       1050       1060       1070       1080 
GDRESRKDLV LIDSLFIMDQ FKAAERMNIG KPNAKDIADV TAVAEAILPK GSARVTTSVK 

      1090       1100       1110       1120       1130       1140 
FNAPSLLYGA LRDYQKIGLD WLAKLYRKNL NGILADEAGL GKTVQIIAFF AHLACNEGNW 

      1150       1160       1170       1180       1190       1200 
GPHLVVVRSC NILKWELELK RWCPGLKILS YIGSHRELKA KRQEWAEPNS FHVCITSYTQ 

      1210       1220       1230       1240       1250       1260 
FFRGLTAFTR VRWKCLVIDE MQRVKGMTER HWEAVFTLQS QQRLLLIDSP LHNTFLELWT 

      1270       1280       1290       1300       1310       1320 
MVHFLVPGIS RPYLSSPLRA PSEESQDYYH KVVIRLHRVT QPFILRRTKR DVEKQLTKKY 

      1330       1340       1350       1360       1370       1380 
EHVLKCRLSN RQKALYEDVI LQPGTQEALK SGHFVNVLSI LVRLQRICNH PGLVEPRHPG 

      1390       1400       1410       1420       1430       1440 
SSYVAGPLEY PSASLILKAL ERDFWKEADL SMFDLIGLEN KITRHEAELL SKKKIPRKLM 

      1450       1460       1470       1480       1490       1500 
EEISTSAAPA ARPAAAKLKA SRLFQPVQYG QKPEGRTVAF PSTHPPRTAA PTTASAAPQG 

      1510       1520       1530       1540       1550       1560 
PLRGRPPIAT FSANPEAKAA AAPFQTSQAS ASAPRHQPAS ASSTAASPAH PAKLRAQTTA 

      1570       1580       1590       1600       1610       1620 
QASTPGQPPP QPQAPSHAAG QSALPQRLVL PSQAQARLPS GEVVKIAQLA SITGPQSRVA 

      1630       1640       1650       1660       1670       1680 
QPETPVTLQF QGSKFTLSHS QLRQLTAGQP LQLQGSVLQI VSAPGQPYLR APGPVVMQTV 

      1690       1700       1710       1720       1730       1740 
SQAGAVHGAL GSKPPAGGPS PAPLTPQVGV PGRVAVNALA VGEPGTASKP ASPIGGPTQE 

      1750       1760       1770       1780       1790       1800 
EKTRLLKERL DQIYLVNERR CSQAPVYGRD LLRICALPSH GRVQWRGSLD GRRGKEAGPA 

      1810       1820       1830       1840       1850       1860 
HSYTSSSESP SELMLTLCRC GESLQDVIDR VAFVIPPVVA APPSLRVPRP PPLYSHRMRI 

      1870       1880       1890       1900       1910       1920 
LRQGLREHAA PYFQQLRQTT APRLLQFPEL RLVQFDSGKL EALAILLQKL KSEGRRVLIL 

      1930       1940       1950       1960       1970       1980 
SQMILMLDIL EMFLNFHYLT YVRIDENASS EQRQELMRSF NRDRRIFCAI LSTHSRTTGI 

      1990       2000       2010       2020       2030       2040 
NLVEADTVVF YDNDLNPVMD AKAQEWCDRI GRCKDIHIYR LVSGNSIEEK LLKNGTKDLI 

      2050       2060       2070       2080       2090       2100 
REVAAQGNDY SMAFLTQRTI QELFEVYSPM DDAGFPVKAE EFVVLSQEPS VTETIAPKIA 

      2110       2120       2130       2140       2150       2160 
RPFIEALKSI EYLEEDAQKS AQEGVLGPHT DALSSDSENM PCDEEPSQLE ELADFMEQLT 

      2170       2180       2190       2200       2210       2220 
PIEKYALNYL ELFHTSIEQE KERNSEDAVM TAVRAWEFWN LKTLQEREAR LRLEQEEAEL 

      2230       2240       2250       2260       2270       2280 
LTYTREDAYS MEYVYEDVDG QTEVMPLWTP PTPPQDDSDI YLDSVMCLMY EATPIPEAKL 

      2290       2300       2310       2320       2330       2340 
PPVYVRKERK RHKTDPSAAG RKKKQRHGEA VVPPRSLFDR ATPGLLKIRR EGKEQKKNIL 

      2350       2360       2370       2380       2390       2400 
LKQQVPFAKP LPTFAKPTAE PGQDNPEWLI SEDWALLQAV KQLLELPLNL TIVSPAHTPN 

      2410       2420       2430       2440       2450       2460 
WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA QDENATHTQL 

      2470       2480       2490       2500       2510       2520 
YTSHFDLMKM TAGKRSPPIK PLLGMNPFQK NPKHASVLAE SGINYDKPLP PIQVASLRAE 

      2530       2540       2550       2560       2570       2580 
RIAKEKKALA DQQKAQQPAV AQPPPPQPQP PPPPQQPPPP LPQPQAAGSQ PPAGPPAVQP 

      2590       2600       2610       2620       2630       2640 
QPQPQPQTQP QPVQAPAKAQ PAITTGGSAA VLAGTIKTSV TGTSMPTGAV SGNVIVNTIA 

      2650       2660       2670       2680       2690       2700 
GVPAATFQSI NKRLASPVAP GALTTPGGSA PAQVVHTQPP PRAVGSPATA TPDLVSMATT 

      2710       2720       2730       2740       2750       2760 
QGVRAVTSVT ASAVVTTNLT PVQTPARSLV PQVSQATGVQ LPGKTITPAH FQLLRQQQQQ 

      2770       2780       2790       2800       2810       2820 
QQQQQQQQQQ QQQQQQQQQQ QQQQTTTTSQ VQVPQIQGQA QSPAQIKAVG KLTPEHLIKM 

      2830       2840       2850       2860       2870       2880 
QKQKLQMPPQ PPPPQAQSAP PQPTAQVQVQ TSQPPQQQSP QLTTVTAPRP GALLTGTTVA 

      2890       2900       2910       2920       2930       2940 
NLQVARLTRV PTSQLQAQGQ MQTQAPQPAQ VALAKPPVVS VPAAVVSSPG VTTLPMNVAG 

      2950       2960       2970       2980       2990       3000 
ISVAIGQPQK AAGQTVVAQP VHMQQLLKLK QQAVQQQKAI QPQAAQGPAA VQQKITAQQI 

      3010       3020       3030       3040       3050       3060 
TTPGAQQKVA YAAQPALKTQ FLTTPISQAQ KLAGAQQVQT QIQVAKLPQV VQQQTPVASI 

      3070       3080       3090       3100       3110       3120 
QQVASASQQA SPQTVALTQA TAAGQQVQMI PAVTATAQVV QQKLIQQQVV TTASAPLQTP 

      3130       3140       3150 
GAPNPAQVPA SSDSPSQQPK LQMRVPAVRL KTPTKPPCQ 

« Hide

Isoform 2 [UniParc].

Checksum: 846B71A59CE2B201
Show »

FASTA3,123339,823
Isoform 3 [UniParc].

Checksum: 706B650493BC8580
Show »

FASTA3,086335,805
Isoform 4 [UniParc].

Checksum: 6D57F7F463C74FE1
Show »

FASTA3,042331,778
Isoform 5 [UniParc].

Checksum: 0F04797ACF402088
Show »

FASTA3,122339,695

References

« Hide 'large scale' references
[1]"The p400 complex is an essential E1A transformation target."
Fuchs M., Gerber J., Drapkin R., Sif S., Ikura T., Ogryzko V., Lane W.S., Nakatani Y., Livingston D.M.
Cell 106:297-307(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"cDNAs with long CAG trinucleotide repeats from human brain."
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.
Hum. Genet. 100:114-122(1997) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"ANP32E is a histone chaperone that removes H2A.Z from chromatin."
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., Hamiche A.
Nature 505:648-653(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_056224.3. NM_015409.4.
UniGeneHs.723478.

3D structure databases

ProteinModelPortalQ96L91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121676. 24 interactions.
DIPDIP-29915N.
IntActQ96L91. 11 interactions.
MINTMINT-1897496.
STRING9606.ENSP00000374213.

PTM databases

PhosphoSiteQ96L91.

Polymorphism databases

DMDM317373565.

Proteomic databases

PaxDbQ96L91.
PRIDEQ96L91.

Protocols and materials databases

DNASU57634.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330386; ENSP00000330620; ENSG00000183495. [Q96L91-4]
ENST00000332482; ENSP00000331737; ENSG00000183495. [Q96L91-3]
ENST00000333577; ENSP00000333602; ENSG00000183495. [Q96L91-1]
ENST00000389561; ENSP00000374212; ENSG00000183495. [Q96L91-2]
ENST00000389562; ENSP00000374213; ENSG00000183495. [Q96L91-5]
GeneID57634.
KEGGhsa:57634.
UCSCuc001ujm.3. human. [Q96L91-4]
uc001ujn.3. human. [Q96L91-2]

Organism-specific databases

CTD57634.
GeneCardsGC12P132434.
H-InvDBHIX0021564.
HGNCHGNC:11958. EP400.
HPAHPA016704.
MIM606265. gene.
neXtProtNX_Q96L91.
PharmGKBPA27808.
HUGESearch...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOVERGENHBG051488.
InParanoidQ96L91.
KOK11320.
OMAAQVVHTQ.
OrthoDBEOG7PVWPN.
PhylomeDBQ96L91.
TreeFamTF106424.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressQ96L91.
BgeeQ96L91.
CleanExHS_EP400.
GenevestigatorQ96L91.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR013999. 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]
PfamPF00271. Helicase_C. 1 hit.
PF07529. HSA. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00573. HSA. 1 hit.
SM00717. SANT. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEP400. human.
GeneWikiEP400.
GenomeRNAi57634.
NextBio64345.
PROQ96L91.
SOURCESearch...

Entry information

Entry nameEP400_HUMAN
AccessionPrimary (citable) accession number: Q96L91
Secondary accession number(s): O15411 expand/collapse secondary AC list , Q6P2F5, Q8N8Q7, Q8NE05, Q96JK7, Q9P230
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM