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Q8BMA5

- NPAT_MOUSE

UniProt

Q8BMA5 - NPAT_MOUSE

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Protein

Protein NPAT

Gene

Npat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters (By similarity). Required for early embryonic development.By similarity1 Publication

GO - Molecular functioni

  1. sequence-specific DNA binding transcription factor activity Source: Ensembl
  2. transcription coactivator activity Source: UniProtKB
  3. transcription corepressor activity Source: Ensembl

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: Ensembl
  2. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Ensembl
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein NPAT
Gene namesi
Name:Npat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:107605. Npat.

Subcellular locationi

Nucleus 1 Publication
Note: Concentrates in Cajal bodies tethered to histone gene clusters.By similarity

GO - Cellular componenti

  1. Cajal body Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. Gemini of coiled bodies Source: UniProtKB
  4. nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14201420Protein NPATPRO_0000318164Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei771 – 7711Phosphoserine; by CDK2By similarity
Modified residuei773 – 7731Phosphoserine; by CDK2By similarity
Modified residuei1096 – 10961Phosphoserine; by CDK2By similarity
Modified residuei1223 – 12231N6-acetyllysineBy similarity
Modified residuei1264 – 12641Phosphothreonine; by CDK2By similarity
Modified residuei1343 – 13431Phosphothreonine; by CDK2By similarity

Post-translational modificationi

Phosphorylated at Ser-771, Ser-773, Ser-1096, Thr-1264 and Thr-1343 by CCNE1/CDK2 at G1-S transition and until prophase, which promotes association with histone gene clusters and stimulates activation of histone transcription. Also phosphorylated by CCNA1/CDK2 in vitro (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BMA5.
PRIDEiQ8BMA5.

PTM databases

PhosphoSiteiQ8BMA5.

Expressioni

Developmental stagei

Expression peaks at the G1/S phase boundary.1 Publication

Gene expression databases

BgeeiQ8BMA5.
CleanExiMM_NPAT.
GenevestigatoriQ8BMA5.

Interactioni

Subunit structurei

Interacts with the cylin/CDK complexes CCNE1/CDK2 and CCNA1/CDK2. Interacts with BZW1, CASP8AP2, CREBBP, MIZF and YY1. Interacts with the RUVBL1, RUVBL2 and TRRAP subunits of the NuA4 complex. May also interact with GAPDH, NME1, NME2 and STIP1 (By similarity).By similarity

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 3533LisHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 319319Interaction with MIZFBy similarityAdd
BLAST
Regioni5 – 2521Required for activation of histone gene transcription and interaction with MIZFBy similarityAdd
BLAST
Regioni121 – 14525Required for activation of histone gene transcription and interaction with MIZFBy similarityAdd
BLAST
Regioni263 – 33977Mediates transcriptional activationBy similarityAdd
BLAST
Regioni628 – 65225Required for acceleration of G1 phaseBy similarityAdd
BLAST
Regioni822 – 84726Required for acceleration of G1 phaseBy similarityAdd
BLAST
Regioni1033 – 104816Required for acceleration of G1 phaseBy similarityAdd
BLAST
Regioni1223 – 124725Required for acceleration of G1 phaseBy similarityAdd
BLAST
Regioni1319 – 134224Required for acceleration of G1 phaseBy similarityAdd
BLAST

Domaini

The LisH domain is required for the activation of histone gene transcription.By similarity

Sequence similaritiesi

Belongs to the NPAT family.Curated
Contains 1 LisH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG29266.
GeneTreeiENSGT00390000012388.
HOGENOMiHOG000113840.
HOVERGENiHBG108198.
InParanoidiQ8BMA5.
OMAiFDLFDYG.
OrthoDBiEOG7JDQX0.
PhylomeDBiQ8BMA5.
TreeFamiTF332825.

Family and domain databases

InterProiIPR006594. LisH_dimerisation.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BMA5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLPSDVARL VLGYLQQENL TSTCQTFILE SSNLKEYAEH CTDEGFIPAC
60 70 80 90 100
LLSLFGKNLT TILNEYVAMK AKETSNDVPT IMSSLWKKLD HTLSQIRSMH
110 120 130 140 150
SSPGFAAHQR ARTRNGIAEI KRQRWLASQA APVSSELLVL PYASGQFTTS
160 170 180 190 200
PLVATQAVKP TGPISTPVRS NIVVVNQSQP QSTVTNTAGE SLNIIPGPQE
210 220 230 240 250
RKTQTSLMSP GRRKSESQKK SLTSSGPHSS RNFQDPNAFA VEKQMVIENA
260 270 280 290 300
REKILSNKSL QEKLAENINK FLTSDSSVAQ VPKQTDSNPT EPETSIDELL
310 320 330 340 350
GLPSEIHMSE EAIQDILEQT ESDPAFQALF DLFDYGKTKN NKNMPQISSQ
360 370 380 390 400
PMETNSNIVL PEETNLTIKS SFETEESDGQ SGQPPFCTSY QNEDVLLNDL
410 420 430 440 450
KSGNSHDVLP QESQENFSQI SSNIQKKTFK TAIPAEQKCA LDITLESVSN
460 470 480 490 500
LSDFNQRGSS AECNEHCSEL FASQIPTEAE VAVGEKNSLS ADILSQSQYQ
510 520 530 540 550
PDQPSVPVTS FVSLGGETND KNLVLSGKNS QLLSQSTPLT TKPSKSQLCE
560 570 580 590 600
NSNNIIKVKT NPQASESADS SETANRKTET NTVSPAAAQP QADCQDNSPL
610 620 630 640 650
QSKPPPGIGE SLGVNVTEKI EIHLEEPAPS DKQLSNDAAS VDLNPTESKT
660 670 680 690 700
EPLQSASAQE PEPPSVKDGD TIFLSLSEHN SCEEVALVLG EGNPVKNNNS
710 720 730 740 750
LSSESGGSVG VSPETQNTDG KTSNSTEVDA SSIVSLKIII SDDPFVSSDA
760 770 780 790 800
ELNSAVSSIS GENLPTIILS SKSPAKNAEF VTCLSSEETA SAVVSVEVGD
810 820 830 840 850
SGSMEQNLLV LKPEEPMVNN TQNEDGIAFS ANVAPCVPKD GGYIQLMPTT
860 870 880 890 900
STAFGNSSNI LIATCMTDST ALGPTVSQSN VVVLPGSSAP MTAQPPQQQL
910 920 930 940 950
QTPPKSNSAF AVSQAVSPNF SQGSAIIIAS PVQPVLQGMV GMIPVSVVGQ
960 970 980 990 1000
NGNTFSTPPQ QVLHMPLAAP VCNRSIAQLP IPQKSQKAQG LRNKLITGKQ
1010 1020 1030 1040 1050
VNNLTNLSSL SEACHTQRTE ASDKNIATEL GKKMEDTTIS LSGERVAPPS
1060 1070 1080 1090 1100
KPFESHRRVL CFDSTVSSVA NTQGSLYKMT SENKEKKEAS FSHLDSPILS
1110 1120 1130 1140 1150
STLKPPPNNA IKREREKTVP KILSKSETAS SRHTTVKEVQ SEKKVSPTEV
1160 1170 1180 1190 1200
ALESLHKATA NKENELCGDG ERPKNADTSK LPGGQQNGSL RNEKAIASLQ
1210 1220 1230 1240 1250
ELTKKQATPS NNKNATSVGG TVKDQKQEQS KPASSLIGAE ILQDVPIHSP
1260 1270 1280 1290 1300
ANRSADTDLP VPRTPGSGAG EKHKEEPSDS MKAPASRRCG EEGSMPRVMI
1310 1320 1330 1340 1350
PPVTADLPAC SPASETGSEN SVSMAAHTLM ILSRAAIART TATPLKDNTQ
1360 1370 1380 1390 1400
QFRTSSRSTT KKRKIEELDE CERNSRTSGK NLANSSVPMK KKKIKKKKLP
1410 1420
SSFPAGMDVD KFLLSLHYDE
Length:1,420
Mass (Da):152,176
Last modified:February 5, 2008 - v2
Checksum:i1035459489343314
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1141 – 11411S → P in BAC35255. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033012 mRNA. Translation: BAC28125.1.
AK042624 mRNA. Translation: BAC31308.1.
AK053074 mRNA. Translation: BAC35255.1.
AC156640 Genomic DNA. No translation available.
CCDSiCCDS40637.1.
RefSeqiNP_001074621.1. NM_001081152.1.
UniGeneiMm.116713.

Genome annotation databases

EnsembliENSMUST00000035850; ENSMUSP00000048709; ENSMUSG00000033054.
GeneIDi244879.
KEGGimmu:244879.
UCSCiuc009pmf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033012 mRNA. Translation: BAC28125.1 .
AK042624 mRNA. Translation: BAC31308.1 .
AK053074 mRNA. Translation: BAC35255.1 .
AC156640 Genomic DNA. No translation available.
CCDSi CCDS40637.1.
RefSeqi NP_001074621.1. NM_001081152.1.
UniGenei Mm.116713.

3D structure databases

ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BMA5.

Proteomic databases

MaxQBi Q8BMA5.
PRIDEi Q8BMA5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035850 ; ENSMUSP00000048709 ; ENSMUSG00000033054 .
GeneIDi 244879.
KEGGi mmu:244879.
UCSCi uc009pmf.1. mouse.

Organism-specific databases

CTDi 4863.
MGIi MGI:107605. Npat.

Phylogenomic databases

eggNOGi NOG29266.
GeneTreei ENSGT00390000012388.
HOGENOMi HOG000113840.
HOVERGENi HBG108198.
InParanoidi Q8BMA5.
OMAi FDLFDYG.
OrthoDBi EOG7JDQX0.
PhylomeDBi Q8BMA5.
TreeFami TF332825.

Miscellaneous databases

NextBioi 386460.
PROi Q8BMA5.
SOURCEi Search...

Gene expression databases

Bgeei Q8BMA5.
CleanExi MM_NPAT.
Genevestigatori Q8BMA5.

Family and domain databases

InterProi IPR006594. LisH_dimerisation.
[Graphical view ]
SMARTi SM00667. LisH. 1 hit.
[Graphical view ]
PROSITEi PS50896. LISH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Head and Muellerian duct.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Proviral inactivation of the Npat gene of Mpv 20 mice results in early embryonic arrest."
    Di Fruscio M., Weiher H., Vanderhyden B.C., Imai T., Shiomi T., Hori T., Jaenisch R., Gray D.A.
    Mol. Cell. Biol. 17:4080-4086(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "NPAT expression is regulated by E2F and is essential for cell cycle progression."
    Gao G., Bracken A.P., Burkard K., Pasini D., Classon M., Attwooll C., Sagara M., Imai T., Helin K., Zhao J.
    Mol. Cell. Biol. 23:2821-2833(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  5. Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNPAT_MOUSE
AccessioniPrimary (citable) accession number: Q8BMA5
Secondary accession number(s): Q8BWA9, Q8BY06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: October 29, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3