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P25208

- NFYB_HUMAN

UniProt

P25208 - NFYB_HUMAN

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Protein
Nuclear transcription factor Y subunit beta
Gene
NFYB, HAP3
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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi59 – 657 By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. repressing transcription factor binding Source: UniProtKB
  4. sequence-specific DNA binding Source: InterPro
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. positive regulation of transcription, DNA-templated Source: Ensembl
  3. regulation of transcription, DNA-templated Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

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.
SignaLinkiP25208.

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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7805. NFYB.

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

PharmGKBiPA31610.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Nuclear transcription factor Y subunit beta
PRO_0000204609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki140 – 140Glycyl 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

MaxQBiP25208.
PaxDbiP25208.
PRIDEiP25208.

PTM databases

PhosphoSiteiP25208.

Expressioni

Gene expression databases

ArrayExpressiP25208.
BgeeiP25208.
CleanExiHS_NFYB.
GenevestigatoriP25208.

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
NFYAP235115EBI-389728,EBI-389739
NFYCQ139523EBI-389728,EBI-389755
TP53P046376EBI-389728,EBI-366083

Protein-protein interaction databases

BioGridi110867. 25 interactions.
IntActiP25208. 7 interactions.
MINTiMINT-146867.
STRINGi9606.ENSP00000240055.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi54 – 563
Helixi61 – 7010
Helixi80 – 10728
Beta strandi111 – 1133
Helixi115 – 12410
Helixi128 – 1303
Helixi131 – 14212

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N1JX-ray1.67A51-143[»]
4AWLX-ray3.08B51-143[»]
ProteinModelPortaliP25208.
SMRiP25208. Positions 57-143.

Miscellaneous databases

EvolutionaryTraceiP25208.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5252A domain
Add
BLAST
Regioni53 – 14290B domain
Add
BLAST
Regioni86 – 9712Subunit association domain (SAD) By similarity
Add
BLAST
Regioni143 – 20765C domain
Add
BLAST

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.

Phylogenomic databases

eggNOGiCOG2036.
HOGENOMiHOG000211832.
HOVERGENiHBG008864.
InParanoidiP25208.
KOiK08065.
OMAiIAGDYIG.
OrthoDBiEOG7RNK2W.
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

MTMDGDSSTT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE    50
SFREQDIYLP IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE 100
ASERCHQEKR KTINGEDILF AMSTLGFDSY VEPLKLYLQK FREAMKGEKG 150
IGGAVTATDG LSEELTEEAF TNQLPAGLIT TDGQQQNVMV YTTSYQQISG 200
VQQIQFS 207
Length:207
Mass (Da):22,831
Last modified:July 1, 1993 - v2
Checksum:i1ADFA0E45F3CF972
GO

Sequence cautioni

The sequence CAA42230.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291I → M in AAH07035. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. human.

Polymorphism databases

DMDMi399193.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9098.1.
PIRi S22817.
RefSeqi NP_006157.1. NM_006166.3.
UniGenei Hs.84928.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N1J X-ray 1.67 A 51-143 [» ]
4AWL X-ray 3.08 B 51-143 [» ]
ProteinModelPortali P25208.
SMRi P25208. Positions 57-143.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110867. 25 interactions.
IntActi P25208. 7 interactions.
MINTi MINT-146867.
STRINGi 9606.ENSP00000240055.

PTM databases

PhosphoSitei P25208.

Polymorphism databases

DMDMi 399193.

Proteomic databases

MaxQBi P25208.
PaxDbi P25208.
PRIDEi P25208.

Protocols and materials databases

DNASUi 4801.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000240055 ; ENSP00000240055 ; ENSG00000120837 .
ENST00000551727 ; ENSP00000447486 ; ENSG00000120837 .
GeneIDi 4801.
KEGGi hsa:4801.
UCSCi uc001tkl.1. human.

Organism-specific databases

CTDi 4801.
GeneCardsi GC12M104510.
HGNCi HGNC:7805. NFYB.
HPAi CAB004211.
MIMi 189904. gene.
neXtProti NX_P25208.
PharmGKBi PA31610.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2036.
HOGENOMi HOG000211832.
HOVERGENi HBG008864.
InParanoidi P25208.
KOi K08065.
OMAi IAGDYIG.
OrthoDBi EOG7RNK2W.
PhylomeDBi P25208.
TreeFami TF314521.

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 P25208.

Miscellaneous databases

ChiTaRSi NFYB. human.
EvolutionaryTracei P25208.
GeneWikii NFYB.
GenomeRNAii 4801.
NextBioi 18506.
PROi P25208.
SOURCEi Search...

Gene expression databases

ArrayExpressi P25208.
Bgeei P25208.
CleanExi HS_NFYB.
Genevestigatori P25208.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
IPR003956. Transcrpt_fac_NFYB/HAP3_CS.
[Graphical view ]
Pfami PF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00685. NFYB_HAP3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Intron-exon organization of the NF-Y genes. Tissue-specific splicing modifies an activation domain."
    Li X.-Y., Hooft van Huijsduijnen R., Mantovani R., Benoist C.O., Mathis D.
    J. Biol. Chem. 267:8984-8990(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of human NF-YB, a transcriptional regulatory protein of MHC class II genes."
    Badley Clarke J., Ting J.P.Y.
    Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Urinary bladder.
  7. "Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y, and inhibits CBF-mediated transcription activation in vitro."
    Chattopadhyay C., Hawke D., Kobayashi R., Maity S.N.
    Nucleic Acids Res. 32:3632-3641(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1QBP.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The NF-YB/NF-YC structure gives insight into DNA binding and transcription regulation by CCAAT factor NF-Y."
    Romier C., Cocchiarella F., Mantovani R., Moras D.
    J. Biol. Chem. 278:1336-1345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 51-143.
  10. "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 51-143 IN COMPLEX WITH NYFA; NYFC AND PROMOTER DNA, SUBUNIT, UBIQUITINATION AT LYS-140.

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: September 3, 2014
This is version 148 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

External Data

Dasty 3

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