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P25208 (NFYB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NFYB
Synonyms:HAP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters, for example in type 1 collagen, albumin and beta-actin genes.

Subunit structure

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. Ref.7 Ref.10

Subcellular location

Nucleus.

Domain

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.

Post-translational modification

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'.

Sequence similarities

Belongs to the NFYB/HAP3 subunit family.

Sequence caution

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

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Nuclear transcription factor Y subunit beta
PRO_0000204609

Regions

DNA binding59 – 657 By similarity
Region1 – 5252A domain
Region53 – 14290B domain
Region86 – 9712Subunit association domain (SAD) By similarity
Region143 – 20765C domain

Amino acid modifications

Cross-link140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10

Experimental info

Sequence conflict291I → M in AAH07035. Ref.6

Secondary structure

.............. 207
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25208 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 1ADFA0E45F3CF972

FASTA20722,831
        10         20         30         40         50         60 
MTMDGDSSTT DASQLGISAD YIGGSHYVIQ PHDDTEDSMN DHEDTNGSKE SFREQDIYLP 

        70         80         90        100        110        120 
IANVARIMKN AIPQTGKIAK DAKECVQECV SEFISFITSE ASERCHQEKR KTINGEDILF 

       130        140        150        160        170        180 
AMSTLGFDSY VEPLKLYLQK FREAMKGEKG IGGAVTATDG LSEELTEEAF TNQLPAGLIT 

       190        200 
TDGQQQNVMV YTTSYQQISG VQQIQFS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS22817.
RefSeqNP_006157.1. NM_006166.3.
UniGeneHs.84928.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N1JX-ray1.67A51-143[»]
4AWLX-ray3.08B51-143[»]
ProteinModelPortalP25208.
SMRP25208. Positions 57-143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110867. 25 interactions.
IntActP25208. 7 interactions.
MINTMINT-146867.
STRING9606.ENSP00000240055.

PTM databases

PhosphoSiteP25208.

Polymorphism databases

DMDM399193.

Proteomic databases

PaxDbP25208.
PRIDEP25208.

Protocols and materials databases

DNASU4801.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240055; ENSP00000240055; ENSG00000120837.
ENST00000551727; ENSP00000447486; ENSG00000120837.
GeneID4801.
KEGGhsa:4801.
UCSCuc001tkl.1. human.

Organism-specific databases

CTD4801.
GeneCardsGC12M104510.
HGNCHGNC:7805. NFYB.
HPACAB004211.
MIM189904. gene.
neXtProtNX_P25208.
PharmGKBPA31610.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2036.
HOGENOMHOG000211832.
HOVERGENHBG008864.
InParanoidP25208.
KOK08065.
OMATGEYMAS.
OrthoDBEOG7RNK2W.
PhylomeDBP25208.
TreeFamTF314521.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SignaLinkP25208.

Gene expression databases

ArrayExpressP25208.
BgeeP25208.
CleanExHS_NFYB.
GenevestigatorP25208.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
IPR003957. Transcrpt_fac_NFYB/HAP3.
IPR003956. Transcrpt_fac_NFYB/HAP3_CS.
[Graphical view]
PANTHERPTHR11064:SF9. PTHR11064:SF9. 1 hit.
PfamPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
PRINTSPR00615. CCAATSUBUNTA.
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00685. NFYB_HAP3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNFYB. human.
EvolutionaryTraceP25208.
GeneWikiNFYB.
GenomeRNAi4801.
NextBio18506.
PROP25208.
SOURCESearch...

Entry information

Entry nameNFYB_HUMAN
AccessionPrimary (citable) accession number: P25208
Secondary accession number(s): A8K7B9, Q96IY8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM