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P23511

- NFYA_HUMAN

UniProt

P23511 - NFYA_HUMAN

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Protein

Nuclear transcription factor Y subunit alpha

Gene

NFYA

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

Functioni

Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-YA positively regulates the transcription of the core clock component ARNTL/BMAL1.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi296 – 32126NFYA/HAP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. core promoter sequence-specific DNA binding Source: UniProtKB
  2. DNA binding Source: UniProtKB
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. positive regulation of stem cell proliferation Source: Ensembl
  3. positive regulation of transcription, DNA-templated Source: UniProtKB
  4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. regulation of stem cell maintenance Source: Ensembl
  6. regulation of transcription, DNA-templated Source: UniProtKB
  7. rhythmic process Source: UniProtKB-KW
  8. small molecule metabolic process Source: Reactome
  9. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_18355. ATF4 activates genes.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinkiP23511.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear transcription factor Y subunit alpha
Alternative name(s):
CAAT box DNA-binding protein subunit A
Nuclear transcription factor Y subunit A
Short name:
NF-YA
Gene namesi
Name:NFYA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:7804. NFYA.

Subcellular locationi

GO - Cellular componenti

  1. CCAAT-binding factor complex Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31609.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Nuclear transcription factor Y subunit alphaPRO_0000198768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei326 – 3261Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP23511.
PaxDbiP23511.
PRIDEiP23511.

PTM databases

PhosphoSiteiP23511.

Expressioni

Gene expression databases

BgeeiP23511.
CleanExiHS_NFYA.
ExpressionAtlasiP23511. baseline and differential.
GenevestigatoriP23511.

Organism-specific databases

HPAiCAB009250.
HPA050779.

Interactioni

Subunit structurei

Heterotrimeric transcription factor composed of three components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and dimerize for NF-YA association and DNA binding. Interacts with SP1; the interaction is inhibited by glycosylation of SP1. Interacts with ZHX1. Interacts (via N-terminus) with ZHX2 (via homeobox domain). Interacts with ZFX3.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-389739,EBI-743771
NFYBP252085EBI-389739,EBI-389728
NFYCQ139524EBI-389739,EBI-389755
SRSF1Q079555EBI-389739,EBI-398920
TP53P0463711EBI-389739,EBI-366083

Protein-protein interaction databases

BioGridi110866. 38 interactions.
IntActiP23511. 9 interactions.
MINTiMINT-98352.
STRINGi9606.ENSP00000345702.

Structurei

Secondary structure

1
347
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi264 – 2674
Turni269 – 2713
Helixi272 – 28716
Helixi301 – 3099
Helixi314 – 3163

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AWLX-ray3.08A262-332[»]
ProteinModelPortaliP23511.
SMRiP23511. Positions 262-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi266 – 28924Subunit association domain (SAD)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 161148Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the NFYA/HAP2 subunit family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5224.
GeneTreeiENSGT00390000015714.
HOGENOMiHOG000247016.
HOVERGENiHBG005253.
InParanoidiP23511.
KOiK08064.
OMAiQGMITIP.
OrthoDBiEOG7MD4RM.
PhylomeDBiP23511.
TreeFamiTF323257.

Family and domain databases

InterProiIPR018362. CCAAT-binding_factor_CS.
IPR001289. TF_CBFB.
[Graphical view]
PANTHERiPTHR12632. PTHR12632. 1 hit.
PfamiPF02045. CBFB_NFYA. 1 hit.
[Graphical view]
PRINTSiPR00616. CCAATSUBUNTB.
SMARTiSM00521. CBF. 1 hit.
[Graphical view]
PROSITEiPS00686. NFYA_HAP2_1. 1 hit.
PS51152. NFYA_HAP2_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P23511-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEQYTANSNS STEQIVVQAG QIQQQQQGGV TAVQLQTEAQ VASASGQQVQ
60 70 80 90 100
TLQVVQGQPL MVQVSGGQLI TSTGQPIMVQ AVPGGQGQTI MQVPVSGTQG
110 120 130 140 150
LQQIQLVPPG QIQIQGGQAV QVQGQQGQTQ QIIIQQPQTA VTAGQTQTQQ
160 170 180 190 200
QIAVQGQQVA QTAEGQTIVY QPVNADGTIL QQVTVPVSGM ITIPAASLAG
210 220 230 240 250
AQIVQTGANT NTTSSGQGTV TVTLPVAGNV VNSGGMVMMV PGAGSVPAIQ
260 270 280 290 300
RIPLPGAEML EEEPLYVNAK QYHRILKRRQ ARAKLEAEGK IPKERRKYLH
310 320 330 340
ESRHRHAMAR KRGEGGRFFS PKEKDSPHMQ DPNQADEEAM TQIIRVS
Length:347
Mass (Da):36,877
Last modified:May 1, 1992 - v2
Checksum:iD00BE17041EB1A9E
GO
Isoform Short (identifier: P23511-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-54: Missing.

Show »
Length:318
Mass (Da):33,939
Checksum:i9BF57D6031D83D8C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731H → N in AAH39244. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 5429Missing in isoform Short. 1 PublicationVSP_000849Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59711 mRNA. Translation: CAA42231.1.
AL031778 Genomic DNA. Translation: CAB44743.1.
AL031778 Genomic DNA. Translation: CAI20286.1.
BC039244 mRNA. Translation: AAH39244.1.
M59079 mRNA. Translation: AAA35950.1.
CCDSiCCDS4849.1. [P23511-1]
CCDS4850.1. [P23511-2]
PIRiS22816. A39123.
RefSeqiNP_002496.1. NM_002505.4. [P23511-1]
NP_068351.1. NM_021705.3. [P23511-2]
UniGeneiHs.10441.

Genome annotation databases

EnsembliENST00000341376; ENSP00000345702; ENSG00000001167. [P23511-1]
ENST00000353205; ENSP00000229418; ENSG00000001167. [P23511-2]
GeneIDi4800.
KEGGihsa:4800.
UCSCiuc003opo.3. human. [P23511-1]
uc003opp.3. human. [P23511-2]

Polymorphism databases

DMDMi115844.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59711 mRNA. Translation: CAA42231.1 .
AL031778 Genomic DNA. Translation: CAB44743.1 .
AL031778 Genomic DNA. Translation: CAI20286.1 .
BC039244 mRNA. Translation: AAH39244.1 .
M59079 mRNA. Translation: AAA35950.1 .
CCDSi CCDS4849.1. [P23511-1 ]
CCDS4850.1. [P23511-2 ]
PIRi S22816. A39123.
RefSeqi NP_002496.1. NM_002505.4. [P23511-1 ]
NP_068351.1. NM_021705.3. [P23511-2 ]
UniGenei Hs.10441.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AWL X-ray 3.08 A 262-332 [» ]
ProteinModelPortali P23511.
SMRi P23511. Positions 262-322.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110866. 38 interactions.
IntActi P23511. 9 interactions.
MINTi MINT-98352.
STRINGi 9606.ENSP00000345702.

PTM databases

PhosphoSitei P23511.

Polymorphism databases

DMDMi 115844.

Proteomic databases

MaxQBi P23511.
PaxDbi P23511.
PRIDEi P23511.

Protocols and materials databases

DNASUi 4800.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341376 ; ENSP00000345702 ; ENSG00000001167 . [P23511-1 ]
ENST00000353205 ; ENSP00000229418 ; ENSG00000001167 . [P23511-2 ]
GeneIDi 4800.
KEGGi hsa:4800.
UCSCi uc003opo.3. human. [P23511-1 ]
uc003opp.3. human. [P23511-2 ]

Organism-specific databases

CTDi 4800.
GeneCardsi GC06P041040.
HGNCi HGNC:7804. NFYA.
HPAi CAB009250.
HPA050779.
MIMi 189903. gene.
neXtProti NX_P23511.
PharmGKBi PA31609.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5224.
GeneTreei ENSGT00390000015714.
HOGENOMi HOG000247016.
HOVERGENi HBG005253.
InParanoidi P23511.
KOi K08064.
OMAi QGMITIP.
OrthoDBi EOG7MD4RM.
PhylomeDBi P23511.
TreeFami TF323257.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_18355. ATF4 activates genes.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinki P23511.

Miscellaneous databases

ChiTaRSi NFYA. human.
GeneWikii NFYA.
GenomeRNAii 4800.
NextBioi 18500.
PROi P23511.
SOURCEi Search...

Gene expression databases

Bgeei P23511.
CleanExi HS_NFYA.
ExpressionAtlasi P23511. baseline and differential.
Genevestigatori P23511.

Family and domain databases

InterProi IPR018362. CCAAT-binding_factor_CS.
IPR001289. TF_CBFB.
[Graphical view ]
PANTHERi PTHR12632. PTHR12632. 1 hit.
Pfami PF02045. CBFB_NFYA. 1 hit.
[Graphical view ]
PRINTSi PR00616. CCAATSUBUNTB.
SMARTi SM00521. CBF. 1 hit.
[Graphical view ]
PROSITEi PS00686. NFYA_HAP2_1. 1 hit.
PS51152. NFYA_HAP2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Evolutionary variation of the CCAAT-binding transcription factor NF-Y."
    Li X.-Y., Mantovani R., Hooft van Huijsduijnen R., Andre I., Benoist C., Mathis D.
    Nucleic Acids Res. 20:1087-1091(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM SHORT).
    Tissue: Testis.
  4. "A cDNA encoding a human CCAAT-binding protein cloned by functional complementation in yeast."
    Becker D.M., Fikes J.D., Guarente L.
    Proc. Natl. Acad. Sci. U.S.A. 88:1968-1972(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-347.
  5. "Human ZHX1: cloning, chromosomal location, and interaction with transcription factor NF-Y."
    Yamada K., Printz R.L., Osawa H., Granner D.K.
    Biochem. Biophys. Res. Commun. 261:614-621(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZHX1.
  6. "Identification of proteins that interact with NF-YA."
    Yamada K., Osawa H., Granner D.K.
    FEBS Lett. 460:41-45(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZHX1.
  7. "Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins: molecular cloning and characterization of a member of the ZHX family, ZHX3."
    Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T., Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K.
    Biochem. J. 373:167-178(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZFX3.
    Tissue: Testis.
  8. "Zinc-fingers and homeoboxes (ZHX) 2, a novel member of the ZHX family, functions as a transcriptional repressor."
    Kawata H., Yamada K., Shou Z., Mizutani T., Yazawa T., Yoshino M., Sekiguchi T., Kajitani T., Miyamoto K.
    Biochem. J. 373:747-757(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZHX2.
    Tissue: Testis.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y."
    Lim K., Chang H.I.
    Biochem. Biophys. Res. Commun. 382:593-597(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP1.
  11. "Sequence-specific transcription factor NF-Y displays histone-like DNA binding and H2B-like ubiquitination."
    Nardini M., Gnesutta N., Donati G., Gatta R., Forni C., Fossati A., Vonrhein C., Moras D., Romier C., Bolognesi M., Mantovani R.
    Cell 152:132-143(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 262-332 IN COMPLEX WITH NYFB; NYFC AND PROMOTER DNA, SUBUNIT.

Entry informationi

Entry nameiNFYA_HUMAN
AccessioniPrimary (citable) accession number: P23511
Secondary accession number(s): Q8IXU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 1, 1992
Last modified: October 29, 2014
This is version 140 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3