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Protein

Protein NPAT

Gene

NPAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.14 Publications

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of gene expression Source: UniProtKB
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149308-MONOMER.
SIGNORiQ14207.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein NPAT
Alternative name(s):
Nuclear protein of the ataxia telangiectasia mutated locus
Short name:
Nuclear protein of the ATM locus
p220
Gene namesi
Name:NPAT
Synonyms:CAND3, E14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7896. NPAT.

Subcellular locationi

  • Nucleus
  • NucleusCajal body

  • Note: Concentrates in two Cajal bodies tethered to histone gene clusters at chromosome 6p21 during G1, S and G2 phases. Also concentrates in two additional Cajal bodies tethered to histone gene clusters at chromosome 1q21 specifically during S and G2 phases.

GO - Cellular componenti

  • Cajal body Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • Gemini of coiled bodies Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7V → A: Impairs activation of histone gene transcription; when associated with A-10; A-11; A-15 and A-18. 1 Publication1
Mutagenesisi10L → A: Impairs activation of histone gene transcription; when associated with A-7; A-11; A-15 and A-18. 1 Publication1
Mutagenesisi11V → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-15 and A-18. 1 Publication1
Mutagenesisi15L → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-18. 1 Publication1
Mutagenesisi18E → A: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-15. 1 Publication1
Mutagenesisi27F → A: Impairs activation of histone gene transcription; when associated with A-30. 1 Publication1
Mutagenesisi30E → A: Impairs activation of histone gene transcription; when associated with A-27. 1 Publication1
Mutagenesisi331 – 333LFD → AAA: Impairs activation of histone gene transcription. Impairs interaction with BZW1, RUVBL1, RUVBL2 and TRRAP. 1 Publication3
Mutagenesisi775S → A: Impairs activation of histone gene transcription; when associated with A-779; A-1100; A-1270 and A-1350. 4 Publications1
Mutagenesisi779S → A: Impairs activation of histone gene transcription; when associated with A-775; A-1100; A-1270 and A-1350. 4 Publications1
Mutagenesisi1100S → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1270 and A-1350. 4 Publications1
Mutagenesisi1270T → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1350. 4 Publications1
Mutagenesisi1350T → A: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1270. 4 Publications1

Organism-specific databases

DisGeNETi4863.
OpenTargetsiENSG00000149308.
PharmGKBiPA31697.

Polymorphism and mutation databases

BioMutaiNPAT.
DMDMi296439285.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003181631 – 1427Protein NPATAdd BLAST1427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei207PhosphoserineCombined sources1
Modified residuei554PhosphoserineCombined sources1
Modified residuei599PhosphoserineBy similarity1
Modified residuei775Phosphoserine; by CDK21 Publication1
Modified residuei779Phosphoserine; by CDK21 Publication1
Modified residuei1100Phosphoserine; by CDK21 Publication1
Modified residuei1151PhosphoserineCombined sources1
Modified residuei1200PhosphoserineCombined sources1
Modified residuei1228N6-acetyllysineCombined sources1
Modified residuei1254PhosphoserineBy similarity1
Modified residuei1270Phosphothreonine; by CDK21 Publication1
Modified residuei1350Phosphothreonine; by CDK2Combined sources1 Publication1

Post-translational modificationi

Phosphorylated at Ser-775, Ser-779, Ser-1100, Thr-1270 and Thr-1350 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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ14207.
MaxQBiQ14207.
PaxDbiQ14207.
PeptideAtlasiQ14207.
PRIDEiQ14207.

PTM databases

iPTMnetiQ14207.
PhosphoSitePlusiQ14207.

Expressioni

Tissue specificityi

Ubiquitously expressed.2 Publications

Developmental stagei

Expressed throughout the cell cycle. Expression peaks at the G1/S phase boundary and declines during S phase.2 Publications

Inductioni

By expression of E2F1, E2F2, E2F3 and E2F4. Expression is reduced in response to radiation-induced DNA damage.2 Publications

Gene expression databases

BgeeiENSG00000149308.
CleanExiHS_NPAT.
ExpressionAtlasiQ14207. baseline and differential.
GenevisibleiQ14207. HS.

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 STIP1.7 Publications

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110924. 29 interactors.
DIPiDIP-59961N.
IntActiQ14207. 8 interactors.
STRINGi9606.ENSP00000278612.

Structurei

3D structure databases

ProteinModelPortaliQ14207.
SMRiQ14207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 35LisHPROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 318Interaction with MIZF1 PublicationAdd BLAST318
Regioni5 – 25Required for activation of histone gene transcription and interaction with MIZF1 PublicationAdd BLAST21
Regioni121 – 145Required for activation of histone gene transcription and interaction with MIZF1 PublicationAdd BLAST25
Regioni262 – 338Mediates transcriptional activationAdd BLAST77
Regioni629 – 653Required for acceleration of G1 phaseAdd BLAST25
Regioni828 – 853Required for acceleration of G1 phaseAdd BLAST26
Regioni1039 – 1054Required for acceleration of G1 phaseAdd BLAST16
Regioni1228 – 1252Required for acceleration of G1 phaseAdd BLAST25
Regioni1325 – 1349Required for acceleration of G1 phaseAdd BLAST25

Domaini

The LisH domain is required for the activation of histone gene transcription.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IHIA. Eukaryota.
ENOG41112YA. LUCA.
GeneTreeiENSGT00390000012388.
HOVERGENiHBG108198.
InParanoidiQ14207.
OMAiKQMVIEN.
OrthoDBiEOG091G00OU.
PhylomeDBiQ14207.
TreeFamiTF332825.

Family and domain databases

InterProiIPR006594. LisH.
IPR031442. NPAT_C.
[Graphical view]
PfamiPF15712. NPAT_C. 1 hit.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLPSDVARL VLGYLQQENL ISTCQTFILE SSDLKEYAEH CTDEGFIPAC
60 70 80 90 100
LLSLFGKNLT TILNEYVAMK TKETSNNVPA IMSSLWKKLD HTLSQIRSMQ
110 120 130 140 150
SSPRFAGSQR ARTRTGIAEI KRQRKLASQT APASAELLTL PYLSGQFTTP
160 170 180 190 200
PSTGTQVTRP SGQISDPSRS YFVVVNHSQS QDTVTTGEAL NVIPGAQEKK
210 220 230 240 250
AHASLMSPGR RKSESQRKST TLSGPHSTIR NFQDPNAFAV EKQMVIENAR
260 270 280 290 300
EKILSNKSLQ EKLAENINKF LTSDNNIAQV PKQTDNNPTE PETSIDEFLG
310 320 330 340 350
LPSEIHMSEE AIQDILEQTE SDPAFQALFD LFDYGKTKNN KNISQSISSQ
360 370 380 390 400
PMESNPSIVL ADETNLAVKG SFETEESDGQ SGQPAFCTSY QNDDPLNALK
410 420 430 440 450
NSNNHDVLRQ EDQENFSQIS TSIQKKAFKT AVPTEQKCDI DITFESVPNL
460 470 480 490 500
NDFNQRGNSN AECNPHCAEL YTNQMSTETE MAIGIEKNSL SSNVPSESQL
510 520 530 540 550
QPDQPDIPIT SFVSLGCEAN NENLILSGKS SQLLSQDTSL TGKPSKKSQF
560 570 580 590 600
CENSNDTVKL KINFHGSKSS DSSEVHKSKI EINVLEPVMS QLSNCQDNSC
610 620 630 640 650
LQSEILPVSV ESSHLNVSGQ VEIHLGDSLS STKQPSNDSA SVELNHTENE
660 670 680 690 700
AQASKSENSQ EPSSSVKEEN TIFLSLGGNA NCEKVALTPP EGTPVENSHS
710 720 730 740 750
LPPESVCSSV GDSHPESQNT DDKPSSNNSA EIDASNIVSL KVIISDDPFV
760 770 780 790 800
SSDTELTSAV SSINGENLPT IILSSPTKSP TKNAELVKCL SSEETVGAVV
810 820 830 840 850
YAEVGDSASM EQSLLTFKSE DSAVNNTQNE DGIAFSANVT PCVSKDGGYI
860 870 880 890 900
QLMPATSTAF GNSNNILIAT CVTDPTALGT SVSQSNVVVL PGNSAPMTAQ
910 920 930 940 950
PLPPQLQTPP RSNSVFAVNQ AVSPNFSQGS AIIIASPVQP VLQGMVGMIP
960 970 980 990 1000
VSVVGQNGNN FSTPPRQVLH MPLTAPVCNR SIPQFPVPPK SQKAQGLRNK
1010 1020 1030 1040 1050
PCIGKQVNNL VDSSGHSVGC HAQKTEVSDK SIATDLGKKS EETTVPFPEE
1060 1070 1080 1090 1100
SIVPAAKPCH RRVLCFDSTT APVANTQGPN HKMVSQNKER NAVSFPNLDS
1110 1120 1130 1140 1150
PNVSSTLKPP SNNAIKREKE KPPLPKILSK SESAISRHTT IRETQSEKKV
1160 1170 1180 1190 1200
SPTEIVLESF HKATANKENE LCSDVERQKN PENSKLSIGQ QNGGLRSEKS
1210 1220 1230 1240 1250
IASLQEMTKK QGTSSNNKNV LSVGTAVKDL KQEQTKSASS LITTEMLQDI
1260 1270 1280 1290 1300
QRHSSVSRLA DSSDLPVPRT PGSGAGEKHK EEPIDIIKAP SSRRFSEDSS
1310 1320 1330 1340 1350
TSKVMVPPVT PDLPACSPAS ETGSENSVNM AAHTLMILSR AAISRTTSAT
1360 1370 1380 1390 1400
PLKDNTQQFR ASSRSTTKKR KIEELDERER NSRPSSKNLT NSSIPMKKKK
1410 1420
IKKKKLPSSF PAGMDVDKFL LSLHYDE
Length:1,427
Mass (Da):154,290
Last modified:May 18, 2010 - v3
Checksum:iD5C5E630A56227F9
GO

Sequence cautioni

The sequence AAB02735 differs from that shown. Chimeric cDNA. A chimeric cDNA originating from chromosomes 11 and 4.Curated
The sequence AAH40356 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH50561 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22S → Y in AAB02735 (PubMed:9060412).Curated1
Sequence conflicti101S → N in BAF84376 (PubMed:14702039).Curated1
Sequence conflicti329F → L in BAF84376 (PubMed:14702039).Curated1
Sequence conflicti471Y → N in CAA65824 (PubMed:8923007).Curated1
Sequence conflicti785E → G in BAF82709 (PubMed:14702039).Curated1
Sequence conflicti1145Q → R in BAF82709 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_038696295I → L.1 PublicationCorresponds to variant rs1131748dbSNPEnsembl.1
Natural variantiVAR_038697399L → M.1 PublicationCorresponds to variant rs1051521dbSNPEnsembl.1
Natural variantiVAR_038698447V → M.Corresponds to variant rs35504388dbSNPEnsembl.1
Natural variantiVAR_038699483I → L.Corresponds to variant rs968207dbSNPEnsembl.1
Natural variantiVAR_038700540L → F.1 PublicationCorresponds to variant rs4144901dbSNPEnsembl.1
Natural variantiVAR_038701575V → I.5 PublicationsCorresponds to variant rs2070661dbSNPEnsembl.1
Natural variantiVAR_038702608V → A.Corresponds to variant rs35095430dbSNPEnsembl.1
Natural variantiVAR_038703621V → I.1 PublicationCorresponds to variant rs1051522dbSNPEnsembl.1
Natural variantiVAR_038704967Q → E.1 PublicationCorresponds to variant rs1131750dbSNPEnsembl.1
Natural variantiVAR_038705973L → V.1 PublicationCorresponds to variant rs1131751dbSNPEnsembl.1
Natural variantiVAR_038706987V → A.1 PublicationCorresponds to variant rs1051524dbSNPEnsembl.1
Natural variantiVAR_038707999N → K.1 PublicationCorresponds to variant rs34052882dbSNPEnsembl.1
Natural variantiVAR_0387081191Q → R.1 PublicationCorresponds to variant rs1051525dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83243 mRNA. Translation: BAA11861.1.
X97186 mRNA. Translation: CAA65824.1.
D89854 Genomic DNA. Translation: BAA21367.1.
AK290020 mRNA. Translation: BAF82709.1.
AK291687 mRNA. Translation: BAF84376.1.
BC040356 mRNA. Translation: AAH40356.1. Sequence problems.
BC050561 mRNA. Translation: AAH50561.1. Sequence problems.
U58852 mRNA. Translation: AAB02735.1. Sequence problems.
CCDSiCCDS41710.1.
RefSeqiNP_002510.2. NM_002519.2.
UniGeneiHs.171061.

Genome annotation databases

EnsembliENST00000278612; ENSP00000278612; ENSG00000149308.
GeneIDi4863.
KEGGihsa:4863.
UCSCiuc001pjz.6. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83243 mRNA. Translation: BAA11861.1.
X97186 mRNA. Translation: CAA65824.1.
D89854 Genomic DNA. Translation: BAA21367.1.
AK290020 mRNA. Translation: BAF82709.1.
AK291687 mRNA. Translation: BAF84376.1.
BC040356 mRNA. Translation: AAH40356.1. Sequence problems.
BC050561 mRNA. Translation: AAH50561.1. Sequence problems.
U58852 mRNA. Translation: AAB02735.1. Sequence problems.
CCDSiCCDS41710.1.
RefSeqiNP_002510.2. NM_002519.2.
UniGeneiHs.171061.

3D structure databases

ProteinModelPortaliQ14207.
SMRiQ14207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110924. 29 interactors.
DIPiDIP-59961N.
IntActiQ14207. 8 interactors.
STRINGi9606.ENSP00000278612.

PTM databases

iPTMnetiQ14207.
PhosphoSitePlusiQ14207.

Polymorphism and mutation databases

BioMutaiNPAT.
DMDMi296439285.

Proteomic databases

EPDiQ14207.
MaxQBiQ14207.
PaxDbiQ14207.
PeptideAtlasiQ14207.
PRIDEiQ14207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278612; ENSP00000278612; ENSG00000149308.
GeneIDi4863.
KEGGihsa:4863.
UCSCiuc001pjz.6. human.

Organism-specific databases

CTDi4863.
DisGeNETi4863.
GeneCardsiNPAT.
H-InvDBHIX0035981.
HGNCiHGNC:7896. NPAT.
MIMi601448. gene.
neXtProtiNX_Q14207.
OpenTargetsiENSG00000149308.
PharmGKBiPA31697.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHIA. Eukaryota.
ENOG41112YA. LUCA.
GeneTreeiENSGT00390000012388.
HOVERGENiHBG108198.
InParanoidiQ14207.
OMAiKQMVIEN.
OrthoDBiEOG091G00OU.
PhylomeDBiQ14207.
TreeFamiTF332825.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149308-MONOMER.
SIGNORiQ14207.

Miscellaneous databases

GeneWikiiNPAT_(gene).
GenomeRNAii4863.
PROiQ14207.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149308.
CleanExiHS_NPAT.
ExpressionAtlasiQ14207. baseline and differential.
GenevisibleiQ14207. HS.

Family and domain databases

InterProiIPR006594. LisH.
IPR031442. NPAT_C.
[Graphical view]
PfamiPF15712. NPAT_C. 1 hit.
[Graphical view]
SMARTiSM00667. LisH. 1 hit.
[Graphical view]
PROSITEiPS50896. LISH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNPAT_HUMAN
AccessioniPrimary (citable) accession number: Q14207
Secondary accession number(s): A8K1V5
, A8K6M2, Q13632, Q14967, Q16580, Q86W55, Q8IWE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 18, 2010
Last modified: November 2, 2016
This is version 109 of the entry and version 3 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 11
    Human chromosome 11: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.