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Q13952 (NFYC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear transcription factor Y subunit gamma
Alternative name(s):
CAAT box DNA-binding protein subunit C
Nuclear transcription factor Y subunit C
Short name=NF-YC
Transactivator HSM-1/2
Gene names
Name:NFYC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length458 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. Ref.14

Subcellular location

Nucleus.

Sequence similarities

Belongs to the NFYC/HAP5 subunit family.

Sequence caution

The sequence BAD92212.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein folding

Traceable author statement Ref.4. Source: ProtInc

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.4. Source: ProtInc

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15243141. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCCAAT-binding factor complex

Inferred from direct assay PubMed 15243141. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 15243141. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15243141. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13PubMed 15243141PubMed 20936779PubMed 21988832Ref.14. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.4Ref.3. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.4. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q13952-1)

Also known as: DS2.8;

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 1 (identifier: Q13952-2)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     277-295: Missing.
     316-419: Missing.
Isoform 2 (identifier: Q13952-3)

The sequence of this isoform differs from the canonical sequence as follows:
     277-295: Missing.
Isoform 4 (identifier: Q13952-4)

The sequence of this isoform differs from the canonical sequence as follows:
     60-97: Missing.
     277-295: Missing.
     316-419: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q13952-5)

The sequence of this isoform differs from the canonical sequence as follows:
     316-419: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q13952-6)

The sequence of this isoform differs from the canonical sequence as follows:
     186-219: Missing.
     277-295: Missing.
     316-419: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q13952-7)

The sequence of this isoform differs from the canonical sequence as follows:
     277-295: Missing.
     315-315: Missing.
     316-419: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Nuclear transcription factor Y subunit gamma
PRO_0000218246

Natural variations

Alternative sequence60 – 9738Missing in isoform 4.
VSP_043348
Alternative sequence186 – 21934Missing in isoform 6.
VSP_043349
Alternative sequence277 – 29519Missing in isoform 1, isoform 2, isoform 4, isoform 6 and isoform 7.
VSP_000851
Alternative sequence3151Missing in isoform 7.
VSP_046350
Alternative sequence316 – 419104Missing in isoform 1, isoform 4, isoform 5, isoform 6 and isoform 7.
VSP_000852
Natural variant1651Q → H in a breast cancer sample; somatic mutation. Ref.15
VAR_035702
Natural variant2971T → I.
Corresponds to variant rs2230746 [ dbSNP | Ensembl ].
VAR_059460

Experimental info

Sequence conflict521M → I in CAA99055. Ref.3
Sequence conflict901D → N in BAA14051. Ref.4
Sequence conflict1551V → L in AAC50816. Ref.1
Sequence conflict1581Q → H in BAA14051. Ref.4
Sequence conflict1711T → N in BAA14051. Ref.4
Sequence conflict1751P → A in AAC50816. Ref.1
Sequence conflict1791I → F in BAA14051. Ref.4
Sequence conflict1981G → S in BAA12818. Ref.4
Sequence conflict1981G → S in BAA14051. Ref.4
Sequence conflict2021Q → K in BAA12818. Ref.4
Sequence conflict216 – 2172QS → HN in BAA14051. Ref.4
Sequence conflict2481L → V in AAC50816. Ref.1
Sequence conflict2711A → V in AAC50816. Ref.1
Sequence conflict4511Q → K in BAA14051. Ref.4

Secondary structure

.............. 458
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (DS2.8) [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: B17B2C7F622653B9

FASTA45850,302
        10         20         30         40         50         60 
MSTEGGFGGT SSSDAQQSLQ SFWPRVMEEI RNLTVKDFRV QELPLARIKK IMKLDEDVKM 

        70         80         90        100        110        120 
ISAEAPVLFA KAAQIFITEL TLRAWIHTED NKRRTLQRND IAMAITKFDQ FDFLIDIVPR 

       130        140        150        160        170        180 
DELKPPKRQE EVRQSVTPAE PVQYYFTLAQ QPTAVQVQGQ QQGQQTTSST TTIQPGQIII 

       190        200        210        220        230        240 
AQPQQGQTTP VTMQVGEGQQ VQIVQAQPQG QAQQAQSGTG QTMQVMQQII TNTGEIQQIP 

       250        260        270        280        290        300 
VQLNAGQLQY IRLAQPVSGT QVVQGQIQTL ATNAQQGQRN ASQGKPRRCL KETLQITQTE 

       310        320        330        340        350        360 
VQQGQQQFSQ FTDGQRNSVQ QARVSELTGE AEPREVKATG NSTPCTSSLP TTHPPSHRAG 

       370        380        390        400        410        420 
ASCVCCSQPQ QSSTSPPPSD ALQWVVVEVS GTPNQLETHR ELHAPLPGMT SLSPLHPSQQ 

       430        440        450 
LYQIQQVTMP AGQDLAQPMF IQSANQPSDG QAPQVTGD 

« Hide

Isoform 1 (Gamma) [UniParc].

Checksum: D83635C1773C3895
Show »

FASTA33537,194
Isoform 2 [UniParc].

Checksum: E3FED3512983A402
Show »

FASTA43948,150
Isoform 4 [UniParc].

Checksum: 6E5693FBF9D838ED
Show »

FASTA29732,828
Isoform 5 [UniParc].

Checksum: 80887376BB8125F3
Show »

FASTA35439,346
Isoform 6 [UniParc].

Checksum: 1BC4774E7E20894A
Show »

FASTA30133,702
Isoform 7 [UniParc].

Checksum: 685A01326BF0FFB1
Show »

FASTA33437,066

References

« Hide 'large scale' references
[1]"Subunit association and DNA binding activity of the heterotrimeric transcription factor NF-Y is regulated by cellular redox."
Nakshatri H., Bhat-Nakshatri P., Currie R.A.
J. Biol. Chem. 271:28784-28791(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning and expression of human NF-YC."
Bellorini M., Zemzoumi K., Farina A., Berthelsen J., Piaggio G., Mantovani R.
Gene 193:119-125(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Isolation and sequence analysis of the cDNA encoding subunit C of human CCAAT-binding transcription factor."
Dmitrenko V.V., Garifulin O.M., Kavsan V.M.
Gene 197:161-163(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Cell cycle-dependent switch of up- and down-regulation of human hsp70 gene expression by interaction between c-Myc and CBF/NF-Y."
Taira T., Sawai M., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.
J. Biol. Chem. 274:24270-24279(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"Cloning of a new variant of NFY-C."
Bringuier P.P., Schalken J.A., Yamasaki H., Giroldi L.A.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[6]"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] (ISOFORMS 2; 4; 5 AND 6).
Tissue: Synovium.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Brain.
[9]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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 1).
Tissue: Brain.
[12]"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].
[13]"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 27-120 IN COMPLEX WITH NF-YB.
[14]"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 27-120 IN COMPLEX WITH NYFA; NYFB AND PROMOTER DNA, SUBUNIT.
[15]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-165.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62296 mRNA. Translation: AAC50816.1.
U78774 mRNA. Translation: AAC51669.1.
Z74792 mRNA. Translation: CAA99055.1.
D85425 mRNA. Translation: BAA12818.1.
D89986 mRNA. Translation: BAA14051.1.
AF191744 mRNA. Translation: AAG28389.1.
AK000346 mRNA. Translation: BAA91100.1.
AK127677 mRNA. Translation: BAG54549.1.
AK300774 mRNA. Translation: BAG62438.1.
AK301385 mRNA. Translation: BAG62925.1.
BT020081 mRNA. Translation: AAV38884.1.
AB208975 mRNA. Translation: BAD92212.1. Different initiation.
AL031289 Genomic DNA. No translation available.
AL354914, AC119677 Genomic DNA. Translation: CAI16530.1.
AL354914, AC119677 Genomic DNA. Translation: CAI16531.1.
AL354914, AC119677 Genomic DNA. Translation: CAI16532.1.
AL354914, AC119677 Genomic DNA. Translation: CAI16533.1.
CH471059 Genomic DNA. Translation: EAX07198.1.
CH471059 Genomic DNA. Translation: EAX07201.1.
CH471059 Genomic DNA. Translation: EAX07202.1.
CH471059 Genomic DNA. Translation: EAX07203.1.
BC005003 mRNA. Translation: AAH05003.1.
CCDSCCDS44120.1. [Q13952-5]
CCDS44121.1. [Q13952-7]
CCDS44122.1. [Q13952-6]
CCDS44123.1. [Q13952-4]
CCDS455.1. [Q13952-2]
RefSeqNP_001136059.1. NM_001142587.1. [Q13952-7]
NP_001136060.1. NM_001142588.1. [Q13952-5]
NP_001136061.1. NM_001142589.1. [Q13952-4]
NP_001136062.1. NM_001142590.1. [Q13952-6]
NP_055038.2. NM_014223.4. [Q13952-2]
XP_005270950.1. XM_005270893.1. [Q13952-1]
XP_005270951.1. XM_005270894.1. [Q13952-1]
XP_005270953.1. XM_005270896.1. [Q13952-3]
XP_006710724.1. XM_006710661.1. [Q13952-3]
UniGeneHs.713051.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N1JX-ray1.67B27-120[»]
4AWLX-ray3.08C27-120[»]
ProteinModelPortalQ13952.
SMRQ13952. Positions 6-120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110868. 36 interactions.
IntActQ13952. 20 interactions.
MINTMINT-249381.

PTM databases

PhosphoSiteQ13952.

Polymorphism databases

DMDM20137773.

Proteomic databases

MaxQBQ13952.
PaxDbQ13952.
PRIDEQ13952.

Protocols and materials databases

DNASU4802.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308733; ENSP00000312617; ENSG00000066136. [Q13952-1]
ENST00000372651; ENSP00000361734; ENSG00000066136. [Q13952-2]
ENST00000372652; ENSP00000361736; ENSG00000066136. [Q13952-3]
ENST00000372653; ENSP00000361737; ENSG00000066136. [Q13952-6]
ENST00000372654; ENSP00000361738; ENSG00000066136. [Q13952-2]
ENST00000425457; ENSP00000396620; ENSG00000066136. [Q13952-5]
ENST00000427410; ENSP00000408315; ENSG00000066136. [Q13952-4]
ENST00000440226; ENSP00000414299; ENSG00000066136. [Q13952-2]
ENST00000447388; ENSP00000404427; ENSG00000066136. [Q13952-2]
ENST00000456393; ENSP00000408867; ENSG00000066136. [Q13952-7]
GeneID4802.
KEGGhsa:4802.
UCSCuc001cfx.4. human. [Q13952-5]
uc001cfy.4. human. [Q13952-2]
uc001cgb.3. human. [Q13952-3]
uc001cgc.3. human. [Q13952-6]
uc001cge.3. human. [Q13952-1]
uc010ojn.2. human. [Q13952-4]

Organism-specific databases

CTD4802.
GeneCardsGC01P041159.
HGNCHGNC:7806. NFYC.
HPAHPA055011.
MIM605344. gene.
neXtProtNX_Q13952.
PharmGKBPA31611.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5208.
HOGENOMHOG000231074.
HOVERGENHBG002885.
InParanoidQ13952.
KOK08066.
OMAATNAQQI.
OrthoDBEOG7BGHNS.
PhylomeDBQ13952.
TreeFamTF354207.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ13952.
BgeeQ13952.
GenevestigatorQ13952.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
IPR027170. NFYC/HAP5_su.
[Graphical view]
PANTHERPTHR10252:SF8. PTHR10252:SF8. 1 hit.
PfamPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNFYC. human.
EvolutionaryTraceQ13952.
GeneWikiNFYC.
GenomeRNAi4802.
NextBio18510.
PROQ13952.
SOURCESearch...

Entry information

Entry nameNFYC_HUMAN
AccessionPrimary (citable) accession number: Q13952
Secondary accession number(s): B4DUS6 expand/collapse secondary AC list , B4DW63, D3DPV9, F8VWM3, Q59GY4, Q5T6K8, Q5T6K9, Q5T6L1, Q5TZR6, Q92869, Q9HBX1, Q9NXB5, Q9UM67, Q9UML0, Q9UMT7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 149 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM