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Protein

Nuclear transcription factor Y subunit alpha

Gene

Nfya

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi290 – 31526NFYA/HAP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-2426168. Activation of gene expression by SREBF (SREBP).

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear transcription factor Y subunit alpha
Alternative name(s):
CAAT box DNA-binding protein subunit A
CCAAT-binding transcription factor subunit A
Short name:
CBF-A
Nuclear transcription factor Y subunit A
Short name:
NF-YA
Gene namesi
Name:Nfya
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi70976. Nfya.

Subcellular locationi

GO - Cellular componenti

  • CCAAT-binding factor complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Nuclear transcription factor Y subunit alphaPRO_0000198770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei320 – 3201PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18576.
PRIDEiP18576.

PTM databases

iPTMnetiP18576.

Expressioni

Gene expression databases

ExpressionAtlasiP18576. baseline and differential.
GenevisibleiP18576. RN.

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 (By similarity). Interacts with SP1; the interaction is inhibited by glycosylation of SP1. Interacts (via N-terminus) with ZHX2 (via homeobox domain). Interacts with ZFX3. Interacts with ZHX1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Sp1Q017142EBI-862695,EBI-862787

GO - Molecular functioni

  • transcription cofactor binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi248146. 1 interaction.
IntActiP18576. 2 interactions.
STRINGi10116.ENSRNOP00000017157.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi260 – 28324Subunit association domain (SAD)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi14 – 161148Gln-richAdd
BLAST
Compositional biasi200 – 21617Thr-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1561. Eukaryota.
COG5224. LUCA.
GeneTreeiENSGT00390000015714.
HOGENOMiHOG000247016.
HOVERGENiHBG005253.
InParanoidiP18576.
KOiK08064.
OMAiTQMIRVS.
OrthoDBiEOG7MD4RM.
PhylomeDBiP18576.

Family and domain databases

InterProiIPR018362. CCAAT-binding_factor_CS.
IPR001289. NFYA.
[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]

Sequencei

Sequence statusi: Complete.

P18576-1 [UniParc]FASTAAdd to basket

« 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 QQGMITIPAA SLAGAQIVQT
210 220 230 240 250
GANTNTTSSG QGTVTVTLPV AGNVVNSGGM VMMVPGAGSV PAIQRIPLPG
260 270 280 290 300
AEMLEEEPLY VNAKQYHRIL KRRQARAKLE AEGKIPKERR KYLHESRHRH
310 320 330 340
AMARKRGEGG RFFSPKEKDS PHMQDPNQAD EEAMTQIIRV S
Length:341
Mass (Da):36,294
Last modified:November 1, 1990 - v1
Checksum:i3332DB595D67B3A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34238 mRNA. Translation: AAA40889.1.
PIRiA35777.
RefSeqiNP_036997.1. NM_012865.1.
UniGeneiRn.10747.

Genome annotation databases

EnsembliENSRNOT00000017157; ENSRNOP00000017157; ENSRNOG00000012702.
GeneIDi29508.
KEGGirno:29508.
UCSCiRGD:70976. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34238 mRNA. Translation: AAA40889.1.
PIRiA35777.
RefSeqiNP_036997.1. NM_012865.1.
UniGeneiRn.10747.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248146. 1 interaction.
IntActiP18576. 2 interactions.
STRINGi10116.ENSRNOP00000017157.

PTM databases

iPTMnetiP18576.

Proteomic databases

PaxDbiP18576.
PRIDEiP18576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017157; ENSRNOP00000017157; ENSRNOG00000012702.
GeneIDi29508.
KEGGirno:29508.
UCSCiRGD:70976. rat.

Organism-specific databases

CTDi4800.
RGDi70976. Nfya.

Phylogenomic databases

eggNOGiKOG1561. Eukaryota.
COG5224. LUCA.
GeneTreeiENSGT00390000015714.
HOGENOMiHOG000247016.
HOVERGENiHBG005253.
InParanoidiP18576.
KOiK08064.
OMAiTQMIRVS.
OrthoDBiEOG7MD4RM.
PhylomeDBiP18576.

Enzyme and pathway databases

ReactomeiR-RNO-2426168. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

PROiP18576.

Gene expression databases

ExpressionAtlasiP18576. baseline and differential.
GenevisibleiP18576. RN.

Family and domain databases

InterProiIPR018362. CCAAT-binding_factor_CS.
IPR001289. NFYA.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The B subunit of a rat heteromeric CCAAT-binding transcription factor shows a striking sequence identity with the yeast Hap2 transcription factor."
    Maity S.N., Vuorio T., de Crombrugghe B.
    Proc. Natl. Acad. Sci. U.S.A. 87:5378-5382(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Sprague-Dawley.
  2. "Biochemical analysis of the B subunit of the heteromeric CCAAT-binding factor. A DNA-binding domain and a subunit interaction domain are specified by two separate segments."
    Maity S.N., de Crombrugghe B.
    J. Biol. Chem. 267:8286-8292(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNFYA_RAT
AccessioniPrimary (citable) accession number: P18576
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.