P23511 (NFYA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear transcription factor Y subunit alpha

Alternative name(s):
CAAT box DNA-binding protein subunit A
Nuclear transcription factor Y subunit A
Short name=NF-YA

Gene names

Name:

NFYA

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	347 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. Ref.8
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 SP1; the interaction is inhibited by glycosylation of SP1. Interacts with ZHX1. Interacts (via N-terminus) with ZHX2 (via homeobox domain). Interacts with ZFX3. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Subcellular location	Nucleus.
Sequence similarities	Belongs to the NFYA/HAP2 subunit family. Contains 1 NFYA/HAP2-type DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.4. Source: ProtInc
Cellular_component	CCAAT-binding factor complex Inferred from direct assay PubMed 15243141. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay PubMed 15243141. Source: UniProtKB sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 1774067Ref.4. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APPBP2	Q92624	3	EBI-389739,EBI-743771
NFYB	P25208	4	EBI-389739,EBI-389728
NFYC	Q13952	3	EBI-389739,EBI-389755
SRSF1	Q07955	5	EBI-389739,EBI-398920
TP53	P04637	11	EBI-389739,EBI-366083

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P23511-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P23511-2)

The sequence of this isoform differs from the canonical sequence as follows:
     26-54: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 347

347

Nuclear transcription factor Y subunit alpha

PRO_0000198768

Regions

DNA binding

296 – 321

26

NFYA/HAP2-type

Motif

266 – 289

24

Subunit association domain (SAD)

Compositional bias

14 – 161

148

Gln-rich

Amino acid modifications

Modified residue

326

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

26 – 54

29

Missing in isoform Short.

VSP_000849

Experimental info

Sequence conflict

273

1

H → N in AAH39244. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

347

Helix Strand Turn

Details...

Beta strand

264 – 267

4

Turn

269 – 271

3

Helix

272 – 287

16

Helix

301 – 309

9

Helix

314 – 316

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified May 1, 1992. Version 2. Checksum: D00BE17041EB1A9E	FASTA	347	36,877
	10 20 30 40 50 60 MEQYTANSNS STEQIVVQAG QIQQQQQGGV TAVQLQTEAQ VASASGQQVQ TLQVVQGQPL 70 80 90 100 110 120 MVQVSGGQLI TSTGQPIMVQ AVPGGQGQTI MQVPVSGTQG LQQIQLVPPG QIQIQGGQAV 130 140 150 160 170 180 QVQGQQGQTQ QIIIQQPQTA VTAGQTQTQQ QIAVQGQQVA QTAEGQTIVY QPVNADGTIL 190 200 210 220 230 240 QQVTVPVSGM ITIPAASLAG AQIVQTGANT NTTSSGQGTV TVTLPVAGNV VNSGGMVMMV 250 260 270 280 290 300 PGAGSVPAIQ RIPLPGAEML EEEPLYVNAK QYHRILKRRQ ARAKLEAEGK IPKERRKYLH 310 320 330 340 ESRHRHAMAR KRGEGGRFFS PKEKDSPHMQ DPNQADEEAM TQIIRVS
	Isoform Short [UniParc]. Checksum: 9BF57D6031D83D8C	FASTA	318	33,939
	10 20 30 40 50 60 MEQYTANSNS STEQIVVQAG QIQQQVQGQP LMVQVSGGQL ITSTGQPIMV QAVPGGQGQT 70 80 90 100 110 120 IMQVPVSGTQ GLQQIQLVPP GQIQIQGGQA VQVQGQQGQT QQIIIQQPQT AVTAGQTQTQ 130 140 150 160 170 180 QQIAVQGQQV AQTAEGQTIV YQPVNADGTI LQQVTVPVSG MITIPAASLA GAQIVQTGAN 190 200 210 220 230 240 TNTTSSGQGT VTVTLPVAGN VVNSGGMVMM VPGAGSVPAI QRIPLPGAEM LEEEPLYVNA 250 260 270 280 290 300 KQYHRILKRR QARAKLEAEG KIPKERRKYL HESRHRHAMA RKRGEGGRFF SPKEKDSPHM 310 QDPNQADEEA MTQIIRVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORM SHORT). Tissue: Testis.
[4]	"A cDNA encoding a human CCAAT-binding protein cloned by functional complementation in yeast." Becker D.M., Fikes J.D., Guarente L. Proc. Natl. Acad. Sci. U.S.A. 88:1968-1972(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-347.
[5]	"Human ZHX1: cloning, chromosomal location, and interaction with transcription factor NF-Y." Yamada K., Printz R.L., Osawa H., Granner D.K. Biochem. Biophys. Res. Commun. 261:614-621(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZHX1.
[6]	"Identification of proteins that interact with NF-YA." Yamada K., Osawa H., Granner D.K. FEBS Lett. 460:41-45(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZHX1.
[7]	"Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins: molecular cloning and characterization of a member of the ZHX family, ZHX3." Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T., Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K. Biochem. J. 373:167-178(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZFX3. Tissue: Testis.
[8]	"Zinc-fingers and homeoboxes (ZHX) 2, a novel member of the ZHX family, functions as a transcriptional repressor." Kawata H., Yamada K., Shou Z., Mizutani T., Yazawa T., Yoshino M., Sekiguchi T., Kajitani T., Miyamoto K. Biochem. J. 373:747-757(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ZHX2. Tissue: Testis.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y." Lim K., Chang H.I. Biochem. Biophys. Res. Commun. 382:593-597(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SP1.
[11]	"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 262-332 IN COMPLEX WITH NYFB; NYFC AND PROMOTER DNA, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59711 mRNA. Translation: CAA42231.1.
AL031778 Genomic DNA. Translation: CAB44743.1.
AL031778 Genomic DNA. Translation: CAI20286.1.
BC039244 mRNA. Translation: AAH39244.1.
M59079 mRNA. Translation: AAA35950.1.

IPI

IPI00218470.
IPI00333568.

PIR

A39123. S22816.

RefSeq

NP_002496.1. NM_002505.4.
NP_068351.1. NM_021705.3.

UniGene

Hs.10441.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AWL	X-ray	3.08	A	262-332	[»]

ProteinModelPortal

P23511.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23511. 8 interactions.

MINT

MINT-98352.

STRING

9606.ENSP00000345702.

PTM databases

PhosphoSite

P23511.

Polymorphism databases

DMDM

115844.

Proteomic databases

PaxDb

P23511.

PRIDE

P23511.

Protocols and materials databases

DNASU

4800.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341376; ENSP00000345702; ENSG00000001167.
ENST00000353205; ENSP00000229418; ENSG00000001167.

GeneID

4800.

KEGG

hsa:4800.

UCSC

uc003opo.3. human.
uc003opp.3. human.

Organism-specific databases

CTD

4800.

GeneCards

GC06P041040.

HGNC

HGNC:7804. NFYA.

HPA

CAB009250.
HPA050779.

MIM

189903. gene.

neXtProt

NX_P23511.

PharmGKB

PA31609.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5224.

HOGENOM

HOG000247016.

HOVERGEN

HBG005253.

InParanoid

P23511.

KO

K08064.

OMA

QGMITIP.

OrthoDB

EOG451DS2.

PhylomeDB

P23511.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

P23511.

CleanEx

HS_NFYA.

Genevestigator

P23511.

GermOnline

ENSG00000001167. Homo sapiens.

Family and domain databases

InterPro

IPR018362. CCAAT-binding_factor_CS.
IPR001289. TF_CBFB.
[Graphical view]

PANTHER

PTHR12632. PTHR12632. 1 hit.

Pfam

PF02045. CBFB_NFYA. 1 hit.
[Graphical view]

PRINTS

PR00616. CCAATSUBUNTB.

SMART

SM00521. CBF. 1 hit.
[Graphical view]

PROSITE

PS00686. NFYA_HAP2_1. 1 hit.
PS51152. NFYA_HAP2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NFYA. human.

GenomeRNAi

4800.

NextBio

18500.

SOURCE

Search...

Entry information

Entry name

NFYA_HUMAN

Accession

Primary (citable) accession number: P23511
Secondary accession number(s): Q8IXU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 125 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.