P25208 (NFYB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NFYB
Synonyms:	HAP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	CCAAT-binding factor complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay Ref.7. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1PubMed 1774067. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NFYA	P23511	4	EBI-389728,EBI-389739
NFYC	Q13952	3	EBI-389728,EBI-389755

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 207

207

Nuclear transcription factor Y subunit beta

PRO_0000204609

Regions

DNA binding

59 – 65

7

By similarity

Region

1 – 52

52

A domain

Region

53 – 142

90

B domain

Region

86 – 97

12

Subunit association domain (SAD) By similarity

Region

143 – 207

65

C domain

Amino acid modifications

Cross-link

140

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

Experimental info

Sequence conflict

29

1

I → M in AAH07035. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

207

Helix Strand Turn

Details...

Helix

54 – 56

3

Helix

61 – 70

10

Helix

80 – 107

28

Beta strand

111 – 113

3

Helix

115 – 124

10

Helix

128 – 130

3

Helix

131 – 142

12

Sequences

	Sequence		Length	Mass (Da)
	P25208 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: 1ADFA0E45F3CF972	FASTA	207	22,831
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00013217.

PIR

S22817.

RefSeq

NP_006157.1. NM_006166.3.

UniGene

Hs.84928.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N1J	X-ray	1.67	A	51-143	[»]
4AWL	X-ray	3.08	B	51-143	[»]

ProteinModelPortal

P25208.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25208. 7 interactions.

MINT

MINT-146867.

STRING

9606.ENSP00000240055.

PTM databases

PhosphoSite

P25208.

Polymorphism databases

DMDM

399193.

Proteomic databases

PaxDb

P25208.

PRIDE

P25208.

Protocols and materials databases

DNASU

4801.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000240055; ENSP00000240055; ENSG00000120837.
ENST00000551727; ENSP00000447486; ENSG00000120837.

GeneID

4801.

KEGG

hsa:4801.

UCSC

uc001tkl.1. human.

Organism-specific databases

CTD

4801.

GeneCards

GC12M104510.

HGNC

HGNC:7805. NFYB.

HPA

CAB004211.

MIM

189904. gene.

neXtProt

NX_P25208.

PharmGKB

PA31610.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2036.

HOGENOM

HOG000211832.

HOVERGEN

HBG008864.

InParanoid

P25208.

KO

K08065.

OMA

KENFREQ.

OrthoDB

EOG4D52ZM.

PhylomeDB

P25208.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P25208.

Bgee

P25208.

CleanEx

HS_NFYB.

Genevestigator

P25208.

GermOnline

ENSG00000120837. Homo sapiens.

Family and domain databases

Gene3D

1.10.20.10. 1 hit.

InterPro

IPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
IPR003957. Transcrpt_fac_CBFA/NFYB_topo.
IPR003956. Transcrpt_fac_NFYB/HAP3_CS.
[Graphical view]

PANTHER

PTHR11064:SF9. PTHR11064:SF9. 1 hit.

Pfam

PF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]

PRINTS

PR00615. CCAATSUBUNTA.

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS00685. NFYB_HAP3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NFYB. human.

EvolutionaryTrace

P25208.

GenomeRNAi

4801.

NextBio

18506.

SOURCE

Search...

Entry information

Entry name

NFYB_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.