NFYA_HUMAN - dbPTM
NFYA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NFYA_HUMAN
UniProt AC P23511
Protein Name Nuclear transcription factor Y subunit alpha
Gene Name NFYA
Organism Homo sapiens (Human).
Sequence Length 347
Subcellular Localization Nucleus.
Protein Description Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors. NF-YA positively regulates the transcription of the core clock component ARNTL/BMAL1..
Protein Sequence MEQYTANSNSSTEQIVVQAGQIQQQQQGGVTAVQLQTEAQVASASGQQVQTLQVVQGQPLMVQVSGGQLITSTGQPIMVQAVPGGQGQTIMQVPVSGTQGLQQIQLVPPGQIQIQGGQAVQVQGQQGQTQQIIIQQPQTAVTAGQTQTQQQIAVQGQQVAQTAEGQTIVYQPVNADGTILQQVTVPVSGMITIPAASLAGAQIVQTGANTNTTSSGQGTVTVTLPVAGNVVNSGGMVMMVPGAGSVPAIQRIPLPGAEMLEEEPLYVNAKQYHRILKRRQARAKLEAEGKIPKERRKYLHESRHRHAMARKRGEGGRFFSPKEKDSPHMQDPNQADEEAMTQIIRVS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
184O-linked_GlycosylationGTILQQVTVPVSGMI
CCEEEEEEEECCCCE
18.1123301498
188O-linked_GlycosylationQQVTVPVSGMITIPA
EEEEEECCCCEEEEH
19.3023301498
192O-linked_GlycosylationVPVSGMITIPAASLA
EECCCCEEEEHHHHC
16.4123301498
197O-linked_GlycosylationMITIPAASLAGAQIV
CEEEEHHHHCCCEEE
22.3623301498
266PhosphorylationMLEEEPLYVNAKQYH
HHCCCCCCCCHHHHH
11.4528674151
270UbiquitinationEPLYVNAKQYHRILK
CCCCCCHHHHHHHHH
46.30-
290AcetylationAKLEAEGKIPKERRK
HHHHHCCCCCHHHHH
47.5425953088
302PhosphorylationRRKYLHESRHRHAMA
HHHHHHHHHHHHHHH
23.7324719451
317MethylationRKRGEGGRFFSPKEK
HHCCCCCCCCCCCCC
40.05115484961
320PhosphorylationGEGGRFFSPKEKDSP
CCCCCCCCCCCCCCC
32.1429496963
322UbiquitinationGGRFFSPKEKDSPHM
CCCCCCCCCCCCCCC
75.97-
324AcetylationRFFSPKEKDSPHMQD
CCCCCCCCCCCCCCC
70.4125953088
326PhosphorylationFSPKEKDSPHMQDPN
CCCCCCCCCCCCCCC
27.9829255136
341PhosphorylationQADEEAMTQIIRVS-
HHCHHHHHHHHCCC-
24.5423403867

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of NFYA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NFYA_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of NFYA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APBP2_HUMANAPPBP2physical
16189514
ZHX1_HUMANZHX1physical
10441475
SRF_HUMANSRFphysical
10571058
ZHX1_HUMANZHX1physical
10571058
HMGA1_HUMANHMGA1physical
9388234
JUN_HUMANJUNphysical
11903046
ATF6A_HUMANATF6physical
11158310
ATF6B_HUMANATF6Bphysical
11158310
NFYB_HUMANNFYBphysical
8051128
SPI1_HUMANSPI1physical
9668064
ELF1_HUMANELF1physical
9668064
NFYB_HUMANNFYBphysical
17098936
PWP1_HUMANPWP1physical
20211142
PAPOG_HUMANPAPOLGphysical
20211142
P53_HUMANTP53physical
15831478
NFYB_HUMANNFYBphysical
15831478
TAF11_HUMANTAF11physical
11689552
TAF12_HUMANTAF12physical
11689552
TAF6_HUMANTAF6physical
11689552
SP1_HUMANSP1physical
10393239
ATF2_HUMANATF2physical
21565167
EP300_HUMANEP300physical
21565167
HDAC1_HUMANHDAC1physical
21565167
JUN_HUMANJUNphysical
21565167
A4_HUMANAPPphysical
21832049
APBP2_HUMANAPPBP2physical
19060904
P53_HUMANTP53physical
16959611
EP300_HUMANEP300physical
16959611
CDK2_HUMANCDK2physical
12857729
CCNA2_HUMANCCNA2physical
12857729
NFYB_HUMANNFYBphysical
12857729
NFYC_HUMANNFYCphysical
12857729
NFYB_HUMANNFYBphysical
25416956
POGZ_HUMANPOGZphysical
25416956
LC7L2_HUMANLUC7L2physical
25416956
MAOX_HUMANME1physical
26186194
UB2D2_HUMANUBE2D2physical
26186194
LASP1_HUMANLASP1physical
26186194
HMCS1_HUMANHMGCS1physical
26186194
NFYC_HUMANNFYCphysical
26186194
IRGQ_HUMANIRGQphysical
26186194
NFYB_HUMANNFYBphysical
26344197
NFYC_HUMANNFYCphysical
26344197
ZC3HA_HUMANZC3H10physical
21516116
TCAF1_HUMANFAM115Aphysical
21516116
ACTN4_HUMANACTN4physical
15364540
NFYC_HUMANNFYCphysical
28514442
IRGQ_HUMANIRGQphysical
28514442
HMCS1_HUMANHMGCS1physical
28514442
4EBP2_HUMANEIF4EBP2physical
28514442
UB2D2_HUMANUBE2D2physical
28514442
FTO_HUMANFTOphysical
28514442
TES_HUMANTESphysical
28514442
ILEU_HUMANSERPINB1physical
28514442
LASP1_HUMANLASP1physical
28514442
UAP1_HUMANUAP1physical
28514442
MAOX_HUMANME1physical
28514442
CHM4A_HUMANCHMP4Aphysical
28514442
CBP_HUMANCREBBPphysical
23908595

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NFYA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASSSPECTROMETRY.

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