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Protein

Nuclear transcription factor Y subunit beta

Gene

NFYB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi59 – 65By similarity7

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • repressing transcription factor binding Source: UniProtKB
  • sequence-specific DNA binding Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120837-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-380994. ATF4 activates genes.
R-HSA-381183. ATF6 (ATF6-alpha) activates chaperone genes.
SignaLinkiP25208.
SIGNORiP25208.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear transcription factor Y subunit beta
Alternative name(s):
CAAT box DNA-binding protein subunit B
Nuclear transcription factor Y subunit B
Short name:
NF-YB
Gene namesi
Name:NFYB
Synonyms:HAP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7805. NFYB.

Subcellular locationi

GO - Cellular componenti

  • CCAAT-binding factor complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein-DNA complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi4801.
OpenTargetsiENSG00000120837.
PharmGKBiPA31610.

Polymorphism and mutation databases

BioMutaiNFYB.
DMDMi399193.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002046091 – 207Nuclear transcription factor Y subunit betaAdd BLAST207

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Monoubiquitination at Lys-140 plays an important role in transcriptional activation by allowing the deposition of histone H3 methylations as well as histone H2B monoubiquitination at 'Lys-121'.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP25208.
MaxQBiP25208.
PaxDbiP25208.
PeptideAtlasiP25208.
PRIDEiP25208.

PTM databases

iPTMnetiP25208.
PhosphoSitePlusiP25208.

Expressioni

Gene expression databases

BgeeiENSG00000120837.
CleanExiHS_NFYB.
ExpressionAtlasiP25208. baseline and differential.
GenevisibleiP25208. HS.

Organism-specific databases

HPAiCAB004211.

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 C1QBP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-389728,EBI-741181
DRAP1Q149194EBI-389728,EBI-712941
NFYAP235118EBI-389728,EBI-389739
NFYAP23511-23EBI-389728,EBI-11061759
NFYCQ139524EBI-389728,EBI-389755
NFYCQ13952-24EBI-389728,EBI-11956831
POLE4Q9NR339EBI-389728,EBI-867034
TP53P046376EBI-389728,EBI-366083

GO - Molecular functioni

  • repressing transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110867. 31 interactors.
IntActiP25208. 10 interactors.
MINTiMINT-146867.
STRINGi9606.ENSP00000240055.

Structurei

Secondary structure

1207
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi54 – 56Combined sources3
Helixi61 – 70Combined sources10
Helixi80 – 107Combined sources28
Beta strandi111 – 113Combined sources3
Helixi115 – 124Combined sources10
Helixi128 – 130Combined sources3
Helixi131 – 142Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N1JX-ray1.67A51-143[»]
4AWLX-ray3.08B51-143[»]
4CSRX-ray1.50A51-143[»]
ProteinModelPortaliP25208.
SMRiP25208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25208.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 52A domainAdd BLAST52
Regioni53 – 142B domainAdd BLAST90
Regioni86 – 97Subunit association domain (SAD)By similarityAdd BLAST12
Regioni143 – 207C domainAdd BLAST65

Domaini

Can be divided into 3 domains: the weakly conserved A domain, the highly conserved B domain thought to be involved in subunit interaction and DNA binding, and the Glu-rich C domain.

Sequence similaritiesi

Belongs to the NFYB/HAP3 subunit family.Curated

Phylogenomic databases

eggNOGiKOG0869. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00550000074689.
HOGENOMiHOG000211832.
HOVERGENiHBG008864.
InParanoidiP25208.
KOiK08065.
OMAiIAGDYIG.
OrthoDBiEOG091G0Y4D.
PhylomeDBiP25208.
TreeFamiTF314521.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
IPR003956. Transcrpt_fac_NFYB/HAP3_CS.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00685. NFYB_HAP3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTMDGDSSTT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE
60 70 80 90 100
SFREQDIYLP IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE
110 120 130 140 150
ASERCHQEKR KTINGEDILF AMSTLGFDSY VEPLKLYLQK FREAMKGEKG
160 170 180 190 200
IGGAVTATDG LSEELTEEAF TNQLPAGLIT TDGQQQNVMV YTTSYQQISG

VQQIQFS
Length:207
Mass (Da):22,831
Last modified:July 1, 1993 - v2
Checksum:i1ADFA0E45F3CF972
GO

Sequence cautioni

The sequence CAA42230 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29I → M in AAH07035 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06145 mRNA. Translation: AAA59930.1.
X59710 mRNA. Translation: CAA42230.1. Different initiation.
AK291934 mRNA. Translation: BAF84623.1.
CH471054 Genomic DNA. Translation: EAW97740.1.
BC005316 mRNA. Translation: AAH05316.1.
BC005317 mRNA. Translation: AAH05317.1.
BC007035 mRNA. Translation: AAH07035.1.
CCDSiCCDS9098.1.
PIRiS22817.
RefSeqiNP_006157.1. NM_006166.3.
UniGeneiHs.84928.

Genome annotation databases

EnsembliENST00000240055; ENSP00000240055; ENSG00000120837.
ENST00000551727; ENSP00000447486; ENSG00000120837.
GeneIDi4801.
KEGGihsa:4801.
UCSCiuc001tkl.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06145 mRNA. Translation: AAA59930.1.
X59710 mRNA. Translation: CAA42230.1. Different initiation.
AK291934 mRNA. Translation: BAF84623.1.
CH471054 Genomic DNA. Translation: EAW97740.1.
BC005316 mRNA. Translation: AAH05316.1.
BC005317 mRNA. Translation: AAH05317.1.
BC007035 mRNA. Translation: AAH07035.1.
CCDSiCCDS9098.1.
PIRiS22817.
RefSeqiNP_006157.1. NM_006166.3.
UniGeneiHs.84928.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N1JX-ray1.67A51-143[»]
4AWLX-ray3.08B51-143[»]
4CSRX-ray1.50A51-143[»]
ProteinModelPortaliP25208.
SMRiP25208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110867. 31 interactors.
IntActiP25208. 10 interactors.
MINTiMINT-146867.
STRINGi9606.ENSP00000240055.

PTM databases

iPTMnetiP25208.
PhosphoSitePlusiP25208.

Polymorphism and mutation databases

BioMutaiNFYB.
DMDMi399193.

Proteomic databases

EPDiP25208.
MaxQBiP25208.
PaxDbiP25208.
PeptideAtlasiP25208.
PRIDEiP25208.

Protocols and materials databases

DNASUi4801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000240055; ENSP00000240055; ENSG00000120837.
ENST00000551727; ENSP00000447486; ENSG00000120837.
GeneIDi4801.
KEGGihsa:4801.
UCSCiuc001tkl.2. human.

Organism-specific databases

CTDi4801.
DisGeNETi4801.
GeneCardsiNFYB.
HGNCiHGNC:7805. NFYB.
HPAiCAB004211.
MIMi189904. gene.
neXtProtiNX_P25208.
OpenTargetsiENSG00000120837.
PharmGKBiPA31610.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0869. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00550000074689.
HOGENOMiHOG000211832.
HOVERGENiHBG008864.
InParanoidiP25208.
KOiK08065.
OMAiIAGDYIG.
OrthoDBiEOG091G0Y4D.
PhylomeDBiP25208.
TreeFamiTF314521.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000120837-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-380994. ATF4 activates genes.
R-HSA-381183. ATF6 (ATF6-alpha) activates chaperone genes.
SignaLinkiP25208.
SIGNORiP25208.

Miscellaneous databases

ChiTaRSiNFYB. human.
EvolutionaryTraceiP25208.
GeneWikiiNFYB.
GenomeRNAii4801.
PROiP25208.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120837.
CleanExiHS_NFYB.
ExpressionAtlasiP25208. baseline and differential.
GenevisibleiP25208. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
IPR003956. Transcrpt_fac_NFYB/HAP3_CS.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00685. NFYB_HAP3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNFYB_HUMAN
AccessioniPrimary (citable) accession number: P25208
Secondary accession number(s): A8K7B9, Q96IY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 171 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 12
    Human chromosome 12: 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

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.