NFYC_HUMAN
ID NFYC_HUMAN Reviewed; 458 AA.
AC Q13952; B4DUS6; B4DW63; D3DPV9; F8VWM3; Q59GY4; Q5T6K8; Q5T6K9; Q5T6L1;
AC Q5TZR6; Q92869; Q9HBX1; Q9NXB5; Q9UM67; Q9UML0; Q9UMT7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Nuclear transcription factor Y subunit gamma;
DE AltName: Full=CAAT box DNA-binding protein subunit C;
DE AltName: Full=Nuclear transcription factor Y subunit C;
DE Short=NF-YC;
DE AltName: Full=Transactivator HSM-1/2;
GN Name=NFYC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8910521; DOI=10.1074/jbc.271.46.28784;
RA Nakshatri H., Bhat-Nakshatri P., Currie R.A.;
RT "Subunit association and DNA binding activity of the heterotrimeric
RT transcription factor NF-Y is regulated by cellular redox.";
RL J. Biol. Chem. 271:28784-28791(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9249075; DOI=10.1016/s0378-1119(97)00109-1;
RA Bellorini M., Zemzoumi K., Farina A., Berthelsen J., Piaggio G.,
RA Mantovani R.;
RT "Cloning and expression of human NF-YC.";
RL Gene 193:119-125(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9332362; DOI=10.1016/s0378-1119(97)00255-2;
RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.;
RT "Isolation and sequence analysis of the cDNA encoding subunit C of human
RT CCAAT-binding transcription factor.";
RL Gene 197:161-163(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10446203; DOI=10.1074/jbc.274.34.24270;
RA Taira T., Sawai M., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.;
RT "Cell cycle-dependent switch of up- and down-regulation of human hsp70 gene
RT expression by interaction between c-Myc and CBF/NF-Y.";
RL J. Biol. Chem. 274:24270-24279(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Bringuier P.P., Schalken J.A., Yamasaki H., Giroldi L.A.;
RT "Cloning of a new variant of NFY-C.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 5 AND 6).
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 27-120 IN COMPLEX WITH NF-YB.
RX PubMed=12401788; DOI=10.1074/jbc.m209635200;
RA Romier C., Cocchiarella F., Mantovani R., Moras D.;
RT "The NF-YB/NF-YC structure gives insight into DNA binding and transcription
RT regulation by CCAAT factor NF-Y.";
RL J. Biol. Chem. 278:1336-1345(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 27-120 IN COMPLEX WITH NYFA; NYFB
RP AND PROMOTER DNA, AND SUBUNIT.
RX PubMed=23332751; DOI=10.1016/j.cell.2012.11.047;
RA Nardini M., Gnesutta N., Donati G., Gatta R., Forni C., Fossati A.,
RA Vonrhein C., Moras D., Romier C., Bolognesi M., Mantovani R.;
RT "Sequence-specific transcription factor NF-Y displays histone-like DNA
RT binding and H2B-like ubiquitination.";
RL Cell 152:132-143(2013).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-165.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of the sequence-specific heterotrimeric
CC transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3'
CC box motif found in the promoters of its target genes. NF-Y can function
CC as both an activator and a repressor, depending on its interacting
CC cofactors.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and
CC dimerize for NF-YA association and DNA binding.
CC {ECO:0000269|PubMed:12401788, ECO:0000269|PubMed:23332751}.
CC -!- INTERACTION:
CC Q13952; P23511: NFYA; NbExp=6; IntAct=EBI-389755, EBI-389739;
CC Q13952; P25208: NFYB; NbExp=6; IntAct=EBI-389755, EBI-389728;
CC Q13952-2; Q8IZF2: ADGRF5; NbExp=3; IntAct=EBI-11956831, EBI-7600130;
CC Q13952-2; Q9BRG6: APOL4; NbExp=3; IntAct=EBI-11956831, EBI-10296818;
CC Q13952-2; Q9BUT1: BDH2; NbExp=3; IntAct=EBI-11956831, EBI-6137689;
CC Q13952-2; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11956831, EBI-742887;
CC Q13952-2; Q8N365: CIART; NbExp=3; IntAct=EBI-11956831, EBI-10265133;
CC Q13952-2; O43186: CRX; NbExp=3; IntAct=EBI-11956831, EBI-748171;
CC Q13952-2; Q8TB03: CXorf38; NbExp=3; IntAct=EBI-11956831, EBI-12024320;
CC Q13952-2; Q01658: DR1; NbExp=3; IntAct=EBI-11956831, EBI-750300;
CC Q13952-2; P32519: ELF1; NbExp=3; IntAct=EBI-11956831, EBI-765526;
CC Q13952-2; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-11956831, EBI-11978259;
CC Q13952-2; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-11956831, EBI-10220102;
CC Q13952-2; O14964: HGS; NbExp=3; IntAct=EBI-11956831, EBI-740220;
CC Q13952-2; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-11956831, EBI-3957665;
CC Q13952-2; O14901: KLF11; NbExp=3; IntAct=EBI-11956831, EBI-948266;
CC Q13952-2; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-11956831, EBI-2796400;
CC Q13952-2; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-11956831, EBI-9478422;
CC Q13952-2; Q6MZP7: LIN54; NbExp=3; IntAct=EBI-11956831, EBI-1389411;
CC Q13952-2; P61968: LMO4; NbExp=3; IntAct=EBI-11956831, EBI-2798728;
CC Q13952-2; P23511-2: NFYA; NbExp=4; IntAct=EBI-11956831, EBI-11061759;
CC Q13952-2; P25208: NFYB; NbExp=6; IntAct=EBI-11956831, EBI-389728;
CC Q13952-2; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-11956831, EBI-10240813;
CC Q13952-2; Q02548: PAX5; NbExp=3; IntAct=EBI-11956831, EBI-296331;
CC Q13952-2; P26367: PAX6; NbExp=3; IntAct=EBI-11956831, EBI-747278;
CC Q13952-2; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-11956831, EBI-1389308;
CC Q13952-2; Q14863: POU6F1; NbExp=3; IntAct=EBI-11956831, EBI-18138148;
CC Q13952-2; P78424: POU6F2; NbExp=3; IntAct=EBI-11956831, EBI-12029004;
CC Q13952-2; P86480: PRR20D; NbExp=3; IntAct=EBI-11956831, EBI-12754095;
CC Q13952-2; P43351: RAD52; NbExp=3; IntAct=EBI-11956831, EBI-706448;
CC Q13952-2; Q9UBE0: SAE1; NbExp=3; IntAct=EBI-11956831, EBI-743154;
CC Q13952-2; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-11956831, EBI-12061577;
CC Q13952-2; Q02086-2: SP2; NbExp=3; IntAct=EBI-11956831, EBI-9088579;
CC Q13952-2; Q02446: SP4; NbExp=3; IntAct=EBI-11956831, EBI-10198587;
CC Q13952-2; Q12772: SREBF2; NbExp=3; IntAct=EBI-11956831, EBI-465059;
CC Q13952-2; Q6ZVD7: STOX1; NbExp=3; IntAct=EBI-11956831, EBI-3923644;
CC Q13952-2; O94888: UBXN7; NbExp=3; IntAct=EBI-11956831, EBI-1993627;
CC Q13952-2; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-11956831, EBI-12949277;
CC Q13952-2; Q8NBB4-2: ZSCAN1; NbExp=3; IntAct=EBI-11956831, EBI-12021938;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=3; Synonyms=DS2.8;
CC IsoId=Q13952-1; Sequence=Displayed;
CC Name=1; Synonyms=Gamma;
CC IsoId=Q13952-2; Sequence=VSP_000851, VSP_000852;
CC Name=2;
CC IsoId=Q13952-3; Sequence=VSP_000851;
CC Name=4;
CC IsoId=Q13952-4; Sequence=VSP_043348, VSP_000851, VSP_000852;
CC Name=5;
CC IsoId=Q13952-5; Sequence=VSP_000852;
CC Name=6;
CC IsoId=Q13952-6; Sequence=VSP_043349, VSP_000851, VSP_000852;
CC Name=7;
CC IsoId=Q13952-7; Sequence=VSP_000851, VSP_046350, VSP_000852;
CC -!- SIMILARITY: Belongs to the NFYC/HAP5 subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92212.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U62296; AAC50816.1; -; mRNA.
DR EMBL; U78774; AAC51669.1; -; mRNA.
DR EMBL; Z74792; CAA99055.1; -; mRNA.
DR EMBL; D85425; BAA12818.1; -; mRNA.
DR EMBL; D89986; BAA14051.1; -; mRNA.
DR EMBL; AF191744; AAG28389.1; -; mRNA.
DR EMBL; AK000346; BAA91100.1; -; mRNA.
DR EMBL; AK127677; BAG54549.1; -; mRNA.
DR EMBL; AK300774; BAG62438.1; -; mRNA.
DR EMBL; AK301385; BAG62925.1; -; mRNA.
DR EMBL; BT020081; AAV38884.1; -; mRNA.
DR EMBL; AB208975; BAD92212.1; ALT_INIT; mRNA.
DR EMBL; AL031289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07198.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07201.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07202.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07203.1; -; Genomic_DNA.
DR EMBL; BC005003; AAH05003.1; -; mRNA.
DR CCDS; CCDS44120.1; -. [Q13952-5]
DR CCDS; CCDS44121.1; -. [Q13952-7]
DR CCDS; CCDS44122.1; -. [Q13952-6]
DR CCDS; CCDS44123.1; -. [Q13952-4]
DR CCDS; CCDS455.1; -. [Q13952-2]
DR CCDS; CCDS81305.1; -. [Q13952-1]
DR CCDS; CCDS81306.1; -. [Q13952-3]
DR RefSeq; NP_001136059.1; NM_001142587.1. [Q13952-7]
DR RefSeq; NP_001136060.1; NM_001142588.1. [Q13952-5]
DR RefSeq; NP_001136061.1; NM_001142589.1. [Q13952-4]
DR RefSeq; NP_001136062.1; NM_001142590.1. [Q13952-6]
DR RefSeq; NP_001295043.1; NM_001308114.1. [Q13952-1]
DR RefSeq; NP_001295044.1; NM_001308115.1. [Q13952-3]
DR RefSeq; NP_055038.2; NM_014223.4. [Q13952-2]
DR RefSeq; XP_005270951.1; XM_005270894.1. [Q13952-1]
DR RefSeq; XP_005270952.3; XM_005270895.3.
DR RefSeq; XP_006710721.2; XM_006710658.2. [Q13952-3]
DR RefSeq; XP_006710723.2; XM_006710660.2. [Q13952-5]
DR RefSeq; XP_006710724.1; XM_006710661.1. [Q13952-3]
DR RefSeq; XP_006710725.2; XM_006710662.2.
DR RefSeq; XP_011539818.1; XM_011541516.1. [Q13952-1]
DR RefSeq; XP_016856854.1; XM_017001365.1. [Q13952-1]
DR RefSeq; XP_016856856.1; XM_017001367.1. [Q13952-5]
DR RefSeq; XP_016856857.1; XM_017001368.1. [Q13952-2]
DR RefSeq; XP_016856858.1; XM_017001369.1. [Q13952-2]
DR PDB; 1N1J; X-ray; 1.67 A; B=27-120.
DR PDB; 4AWL; X-ray; 3.08 A; C=27-120.
DR PDB; 4CSR; X-ray; 1.50 A; B=27-120.
DR PDB; 6QMP; X-ray; 2.00 A; C=27-120.
DR PDB; 6QMQ; X-ray; 2.50 A; C=27-120.
DR PDB; 6QMS; X-ray; 1.80 A; C=27-120.
DR PDB; 7AH8; X-ray; 2.70 A; B/D=41-120.
DR PDBsum; 1N1J; -.
DR PDBsum; 4AWL; -.
DR PDBsum; 4CSR; -.
DR PDBsum; 6QMP; -.
DR PDBsum; 6QMQ; -.
DR PDBsum; 6QMS; -.
DR PDBsum; 7AH8; -.
DR AlphaFoldDB; Q13952; -.
DR SASBDB; Q13952; -.
DR SMR; Q13952; -.
DR BioGRID; 110868; 168.
DR ComplexPortal; CPX-1956; CCAAT-binding factor complex.
DR CORUM; Q13952; -.
DR IntAct; Q13952; 104.
DR MINT; Q13952; -.
DR GlyGen; Q13952; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; Q13952; -.
DR MetOSite; Q13952; -.
DR PhosphoSitePlus; Q13952; -.
DR BioMuta; NFYC; -.
DR DMDM; 20137773; -.
DR EPD; Q13952; -.
DR jPOST; Q13952; -.
DR MassIVE; Q13952; -.
DR MaxQB; Q13952; -.
DR PaxDb; Q13952; -.
DR PeptideAtlas; Q13952; -.
DR PRIDE; Q13952; -.
DR ProteomicsDB; 28993; -.
DR ProteomicsDB; 59772; -. [Q13952-1]
DR ProteomicsDB; 59773; -. [Q13952-2]
DR ProteomicsDB; 59774; -. [Q13952-3]
DR ProteomicsDB; 59775; -. [Q13952-4]
DR ProteomicsDB; 59776; -. [Q13952-5]
DR ProteomicsDB; 59777; -. [Q13952-6]
DR Antibodypedia; 18017; 260 antibodies from 29 providers.
DR DNASU; 4802; -.
DR Ensembl; ENST00000308733.9; ENSP00000312617.5; ENSG00000066136.21. [Q13952-1]
DR Ensembl; ENST00000372651.5; ENSP00000361734.1; ENSG00000066136.21. [Q13952-2]
DR Ensembl; ENST00000372652.5; ENSP00000361736.1; ENSG00000066136.21. [Q13952-3]
DR Ensembl; ENST00000372653.5; ENSP00000361737.1; ENSG00000066136.21. [Q13952-6]
DR Ensembl; ENST00000372654.5; ENSP00000361738.1; ENSG00000066136.21. [Q13952-2]
DR Ensembl; ENST00000425457.6; ENSP00000396620.2; ENSG00000066136.21. [Q13952-5]
DR Ensembl; ENST00000427410.6; ENSP00000408315.2; ENSG00000066136.21. [Q13952-4]
DR Ensembl; ENST00000440226.7; ENSP00000414299.2; ENSG00000066136.21. [Q13952-2]
DR Ensembl; ENST00000447388.8; ENSP00000404427.3; ENSG00000066136.21. [Q13952-2]
DR Ensembl; ENST00000456393.6; ENSP00000408867.2; ENSG00000066136.21. [Q13952-7]
DR GeneID; 4802; -.
DR KEGG; hsa:4802; -.
DR MANE-Select; ENST00000447388.8; ENSP00000404427.3; NM_014223.5; NP_055038.2. [Q13952-2]
DR UCSC; uc001cfx.6; human. [Q13952-1]
DR CTD; 4802; -.
DR DisGeNET; 4802; -.
DR GeneCards; NFYC; -.
DR HGNC; HGNC:7806; NFYC.
DR HPA; ENSG00000066136; Low tissue specificity.
DR MIM; 605344; gene.
DR neXtProt; NX_Q13952; -.
DR OpenTargets; ENSG00000066136; -.
DR PharmGKB; PA31611; -.
DR VEuPathDB; HostDB:ENSG00000066136; -.
DR eggNOG; KOG1657; Eukaryota.
DR GeneTree; ENSGT00940000155689; -.
DR HOGENOM; CLU_045277_2_1_1; -.
DR InParanoid; Q13952; -.
DR OMA; DIAQPMF; -.
DR OrthoDB; 1558176at2759; -.
DR PhylomeDB; Q13952; -.
DR TreeFam; TF354207; -.
DR PathwayCommons; Q13952; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress.
DR Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
DR Reactome; R-HSA-9614657; FOXO-mediated transcription of cell death genes.
DR SignaLink; Q13952; -.
DR SIGNOR; Q13952; -.
DR BioGRID-ORCS; 4802; 649 hits in 1108 CRISPR screens.
DR ChiTaRS; NFYC; human.
DR EvolutionaryTrace; Q13952; -.
DR GeneWiki; NFYC; -.
DR GenomeRNAi; 4802; -.
DR Pharos; Q13952; Tbio.
DR PRO; PR:Q13952; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13952; protein.
DR Bgee; ENSG00000066136; Expressed in buccal mucosa cell and 212 other tissues.
DR ExpressionAtlas; Q13952; baseline and differential.
DR Genevisible; Q13952; HS.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0035065; P:regulation of histone acetylation; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR Pfam; PF00125; Histone; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..458
FT /note="Nuclear transcription factor Y subunit gamma"
FT /id="PRO_0000218246"
FT REGION 305..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 60..97
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043348"
FT VAR_SEQ 186..219
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043349"
FT VAR_SEQ 277..295
FT /note="Missing (in isoform 1, isoform 2, isoform 4, isoform
FT 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10446203,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8910521, ECO:0000303|PubMed:9249075,
FT ECO:0000303|PubMed:9332362, ECO:0000303|Ref.7,
FT ECO:0000303|Ref.8"
FT /id="VSP_000851"
FT VAR_SEQ 315
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_046350"
FT VAR_SEQ 316..419
FT /note="Missing (in isoform 1, isoform 4, isoform 5, isoform
FT 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10446203,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8910521, ECO:0000303|PubMed:9249075,
FT ECO:0000303|PubMed:9332362, ECO:0000303|Ref.7,
FT ECO:0000303|Ref.8"
FT /id="VSP_000852"
FT VARIANT 165
FT /note="Q -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035702"
FT CONFLICT 52
FT /note="M -> I (in Ref. 3; CAA99055)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="D -> N (in Ref. 4; BAA14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="V -> L (in Ref. 1; AAC50816)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="Q -> H (in Ref. 4; BAA14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="T -> N (in Ref. 4; BAA14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="P -> A (in Ref. 1; AAC50816)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="I -> F (in Ref. 4; BAA14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="G -> S (in Ref. 4; BAA12818/BAA14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Q -> K (in Ref. 4; BAA12818)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="QS -> HN (in Ref. 4; BAA14051)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="L -> V (in Ref. 1; AAC50816)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="A -> V (in Ref. 1; AAC50816)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="Q -> K (in Ref. 4; BAA14051)"
FT /evidence="ECO:0000305"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4CSR"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4CSR"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4AWL"
FT HELIX 64..90
FT /evidence="ECO:0007829|PDB:4CSR"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4CSR"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:4CSR"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:4CSR"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4CSR"
SQ SEQUENCE 458 AA; 50302 MW; B17B2C7F622653B9 CRC64;
MSTEGGFGGT SSSDAQQSLQ SFWPRVMEEI RNLTVKDFRV QELPLARIKK IMKLDEDVKM
ISAEAPVLFA KAAQIFITEL TLRAWIHTED NKRRTLQRND IAMAITKFDQ FDFLIDIVPR
DELKPPKRQE EVRQSVTPAE PVQYYFTLAQ QPTAVQVQGQ QQGQQTTSST TTIQPGQIII
AQPQQGQTTP VTMQVGEGQQ VQIVQAQPQG QAQQAQSGTG QTMQVMQQII TNTGEIQQIP
VQLNAGQLQY IRLAQPVSGT QVVQGQIQTL ATNAQQGQRN ASQGKPRRCL KETLQITQTE
VQQGQQQFSQ FTDGQRNSVQ QARVSELTGE AEPREVKATG NSTPCTSSLP TTHPPSHRAG
ASCVCCSQPQ QSSTSPPPSD ALQWVVVEVS GTPNQLETHR ELHAPLPGMT SLSPLHPSQQ
LYQIQQVTMP AGQDLAQPMF IQSANQPSDG QAPQVTGD
