H3C_HUMAN - dbPTM
H3C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H3C_HUMAN
UniProt AC Q6NXT2
Protein Name Histone H3.3C
Gene Name H3F3C
Organism Homo sapiens (Human).
Sequence Length 135
Subcellular Localization Nucleus. Chromosome.
Protein Description Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes..
Protein Sequence MARTKQTARKSTGGKAPRKQLATKAARKSTPSTCGVKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFNTDLRFQSAAVGALQEASEAYLVGLLEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
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
3Asymmetric dimethylarginine-----MARTKQTARK
-----CCCCCHHHHH
40.95-
3Citrullination-----MARTKQTARK
-----CCCCCHHHHH
40.95-
3Methylation-----MARTKQTARK
-----CCCCCHHHHH
40.95-
4Phosphorylation----MARTKQTARKS
----CCCCCHHHHHH
20.2617938195
5Allysine---MARTKQTARKST
---CCCCCHHHHHHC
39.85-
5Acetylation---MARTKQTARKST
---CCCCCHHHHHHC
39.85-
5Deamination---MARTKQTARKST
---CCCCCHHHHHHC
39.85-
5Methylation---MARTKQTARKST
---CCCCCHHHHHHC
39.85-
5Other---MARTKQTARKST
---CCCCCHHHHHHC
39.85-
6Formation of an isopeptide bond--MARTKQTARKSTG
--CCCCCHHHHHHCC
39.52-
6Serotonylation--MARTKQTARKSTG
--CCCCCHHHHHHCC
39.52-
7Phosphorylation-MARTKQTARKSTGG
-CCCCCHHHHHHCCC
29.9520228790
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHHCCCCC
36.52-
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHHCCCCC
36.52-
9MethylationARTKQTARKSTGGKA
CCCCHHHHHHCCCCC
36.52-
10"N6,N6,N6-trimethyllysine"RTKQTARKSTGGKAP
CCCHHHHHHCCCCCC
50.32-
10AcetylationRTKQTARKSTGGKAP
CCCHHHHHHCCCCCC
50.3254236075
10LactoylationRTKQTARKSTGGKAP
CCCHHHHHHCCCCCC
50.32-
10MethylationRTKQTARKSTGGKAP
CCCHHHHHHCCCCCC
50.32-
10OtherRTKQTARKSTGGKAP
CCCHHHHHHCCCCCC
50.32-
10UbiquitinationRTKQTARKSTGGKAP
CCCHHHHHHCCCCCC
50.3222817900
11ADP-ribosylationTKQTARKSTGGKAPR
CCHHHHHHCCCCCCH
27.08-
11PhosphorylationTKQTARKSTGGKAPR
CCHHHHHHCCCCCCH
27.0810469656
12PhosphorylationKQTARKSTGGKAPRK
CHHHHHHCCCCCCHH
53.6526074081
15SumoylationARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.47-
15AcetylationARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.4754236071
15GlutarylationARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.47-
15LactoylationARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.47-
15OtherARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.47-
15SuccinylationARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.4721890473
15SumoylationARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.47-
15UbiquitinationARKSTGGKAPRKQLA
HHHHCCCCCCHHHHH
57.4723000965
18Asymmetric dimethylarginineSTGGKAPRKQLATKA
HCCCCCCHHHHHHHH
44.18-
18CitrullinationSTGGKAPRKQLATKA
HCCCCCCHHHHHHHH
44.18-
18MethylationSTGGKAPRKQLATKA
HCCCCCCHHHHHHHH
44.18-
19SumoylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19AcetylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9166741851
19ButyrylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19GlutarylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19LactoylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19MethylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19OtherTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19SumoylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.91-
19UbiquitinationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9123000965
24SumoylationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.15-
24AcetylationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.1566724869
24ButyrylationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.15-
24GlutarylationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.15-
24LactoylationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.15-
24MethylationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.15-
24OtherPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.15-
24SumoylationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.15-
24UbiquitinationPRKQLATKAARKSTP
CHHHHHHHHHHHCCC
34.1523000965
27CitrullinationQLATKAARKSTPSTC
HHHHHHHHHCCCCCC
38.01-
27CitrullinationQLATKAARKSTPSTC
HHHHHHHHHCCCCCC
38.01-
28"N6,N6,N6-trimethyllysine"LATKAARKSTPSTCG
HHHHHHHHCCCCCCC
54.69-
28AcetylationLATKAARKSTPSTCG
HHHHHHHHCCCCCCC
54.69-
28GlutarylationLATKAARKSTPSTCG
HHHHHHHHCCCCCCC
54.69-
28LactoylationLATKAARKSTPSTCG
HHHHHHHHCCCCCCC
54.69-
28MethylationLATKAARKSTPSTCG
HHHHHHHHCCCCCCC
54.69-
28OtherLATKAARKSTPSTCG
HHHHHHHHCCCCCCC
54.69-
28UbiquitinationLATKAARKSTPSTCG
HHHHHHHHCCCCCCC
54.6922817900
29ADP-ribosylationATKAARKSTPSTCGV
HHHHHHHCCCCCCCC
39.74-
29PhosphorylationATKAARKSTPSTCGV
HHHHHHHCCCCCCCC
39.74-
32PhosphorylationAARKSTPSTCGVKPH
HHHHCCCCCCCCCCC
36.10-
37MethylationTPSTCGVKPHRYRPG
CCCCCCCCCCCCCCC
22.01-
41PhosphorylationCGVKPHRYRPGTVAL
CCCCCCCCCCCCHHH
20.3728152594
42MethylationGVKPHRYRPGTVALR
CCCCCCCCCCCHHHH
24.11-
45PhosphorylationPHRYRPGTVALREIR
CCCCCCCCHHHHHHH
12.8030266825
49MethylationRPGTVALREIRRYQK
CCCCHHHHHHHHHHH
27.79-
54PhosphorylationALREIRRYQKSTELL
HHHHHHHHHHCHHHH
15.5022817900
56"N6,N6,N6-trimethyllysine"REIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
56AcetylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8766739507
56GlutarylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
56LactoylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
56MethylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
56OtherREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
56SuccinylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8721890473
56SumoylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
56UbiquitinationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8723000965
57PhosphorylationEIRRYQKSTELLIRK
HHHHHHHCHHHHHHH
16.1623401153
58PhosphorylationIRRYQKSTELLIRKL
HHHHHHCHHHHHHHC
37.3730266825
63MethylationKSTELLIRKLPFQRL
HCHHHHHHHCCHHHH
34.13-
64MethylationSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.22-
64OtherSTELLIRKLPFQRLV
CHHHHHHHCCHHHHH
54.22-
80O-linked_GlycosylationEIAQDFNTDLRFQSA
HHHHHCCCCHHHHHH
36.0821224338
80PhosphorylationEIAQDFNTDLRFQSA
HHHHHCCCCHHHHHH
36.0820850016
86PhosphorylationNTDLRFQSAAVGALQ
CCCHHHHHHHHHHHH
18.58-
107PhosphorylationLVGLLEDTNLCAIHA
HHHHHCCCCCEEEEE
22.25-
115AcetylationNLCAIHAKRVTIMPK
CCEEEEEEECEECHH
32.99-
115GlutarylationNLCAIHAKRVTIMPK
CCEEEEEEECEECHH
32.99-
118PhosphorylationAIHAKRVTIMPKDIQ
EEEEEECEECHHHHH
18.6520068231
122SumoylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
122AcetylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5154236079
122GlutarylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
122MethylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
122OtherKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
122SuccinylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5121890473
122SumoylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
122UbiquitinationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5123000965
128MethylationPKDIQLARRIRGERA
HHHHHHHHHHHCCCC
43.05-

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
4TPhosphorylationKinaseHASPINQ8TF76
Uniprot
7TPhosphorylationKinasePKC-Uniprot
11SPhosphorylationKinaseALTERNATE-Uniprot
12TPhosphorylationKinasePKC-Uniprot
29SPhosphorylationKinaseALTERNATE-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
3RMethylation

-
4TPhosphorylation

-
5Kubiquitylation

-
5KAcetylation

-
5KMethylation

-
5KMethylation

-
5KMethylation

-
5KMethylation

-
5KPhosphorylation

-
5KMethylation

-
7TPhosphorylation

-
7TMethylation

-
9RMethylation

-
9RMethylation

-
9RMethylation

-
9RCitrullination

-
9RAcetylation

-
10KPhosphorylation

-
10KPhosphorylation

30257210
10KPhosphorylation

-
10KPhosphorylation

-
10KMethylation

-
10KMethylation

-
10KMethylation

-
10KAcetylation

-
10KAcetylation

-
10KAcetylation

-
10KAcetylation

30257210
10KMethylation

-
10KMethylation

-
10KMethylation

-
11SAcetylation

30257210
11SAcetylation

-
11SAcetylation

-
11SMethylation

-
11SMethylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

30257210
12TPhosphorylation

-
12TMethylation

-
12TPhosphorylation

-
18RCitrullination

-
18RMethylation

-
18RMethylation

-
18RMethylation

-
18RAcetylation

-
19KMethylation

-
19KAcetylation

-
24KMethylation

-
24KAcetylation

-
28KMethylation

-
28KMethylation

-
29SPhosphorylation

-
56KMethylation

-
120Kubiquitylation

-
120KMethylation

-
122KSuccinylation

-
122KAcetylation

-

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 H3C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
KDM4B_HUMANKDM4Bphysical
23455924
ANM5_HUMANPRMT5physical
23455924
ANM6_HUMANPRMT6physical
23455924
ANM7_HUMANPRMT7physical
23455924
SETMR_HUMANSETMARphysical
23455924
SMYD1_HUMANSMYD1physical
23455924
SMYD3_HUMANSMYD3physical
23455924
SUV91_HUMANSUV39H1physical
23455924
NSD3_HUMANWHSC1L1physical
23455924

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 H3C_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-15; LYS-19; LYS-24;LYS-56 AND LYS-122, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative interaction proteomics and genome-wide profiling ofepigenetic histone marks and their readers.";
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,Mann M.;
Cell 142:967-980(2010).
Cited for: PHOSPHORYLATION AT SER-57 AND THR-80.

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