H31T_HUMAN - dbPTM
H31T_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H31T_HUMAN
UniProt AC Q16695
Protein Name Histone H3.1t
Gene Name HIST3H3
Organism Homo sapiens (Human).
Sequence Length 136
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..
Protein Sequence MARTKQTARKSTGGKAPRKQLATKVARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLMREIAQDFKTDLRFQSSAVMALQEACESYLVGLFEDTNLCVIHAKRVTIMPKDIQLARRIRGERA
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
----CCCCCHHHHHC
20.2617938195
5Allysine---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Acetylation---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Deamination---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Methylation---MARTKQTARKST
---CCCCCHHHHHCC
39.8515628137
5Other---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
6Formation of an isopeptide bond--MARTKQTARKSTG
--CCCCCHHHHHCCC
39.52-
6Serotonylation--MARTKQTARKSTG
--CCCCCHHHHHCCC
39.52-
7Phosphorylation-MARTKQTARKSTGG
-CCCCCHHHHHCCCC
29.9520228790
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.52-
9CitrullinationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.52-
9MethylationARTKQTARKSTGGKA
CCCCHHHHHCCCCCC
36.52-
10"N6,N6,N6-trimethyllysine"RTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10AcetylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.329854409
10LactoylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10MethylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10OtherRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10UbiquitinationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3222817900
11ADP-ribosylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.08-
11PhosphorylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.0810469656
12PhosphorylationKQTARKSTGGKAPRK
CHHHHHCCCCCCCHH
53.6526074081
15SumoylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15AcetylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.479854417
15GlutarylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15LactoylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15MethylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15OtherARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.47-
15SuccinylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4710911985
15SumoylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4710911985
15UbiquitinationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4727667366
18Asymmetric dimethylarginineSTGGKAPRKQLATKV
CCCCCCCHHHHHHHH
44.18-
18CitrullinationSTGGKAPRKQLATKV
CCCCCCCHHHHHHHH
44.18-
18MethylationSTGGKAPRKQLATKV
CCCCCCCHHHHHHHH
44.18-
19AcetylationTGGKAPRKQLATKVA
CCCCCCHHHHHHHHH
48.9119608861
19ButyrylationTGGKAPRKQLATKVA
CCCCCCHHHHHHHHH
48.91-
19GlutarylationTGGKAPRKQLATKVA
CCCCCCHHHHHHHHH
48.91-
19LactoylationTGGKAPRKQLATKVA
CCCCCCHHHHHHHHH
48.91-
19MethylationTGGKAPRKQLATKVA
CCCCCCHHHHHHHHH
48.91-
19OtherTGGKAPRKQLATKVA
CCCCCCHHHHHHHHH
48.91-
19UbiquitinationTGGKAPRKQLATKVA
CCCCCCHHHHHHHHH
48.9122817900
24AcetylationPRKQLATKVARKSAP
CHHHHHHHHHHHCCC
28.4319608861
24ButyrylationPRKQLATKVARKSAP
CHHHHHHHHHHHCCC
28.43-
24GlutarylationPRKQLATKVARKSAP
CHHHHHHHHHHHCCC
28.43-
24LactoylationPRKQLATKVARKSAP
CHHHHHHHHHHHCCC
28.43-
24MethylationPRKQLATKVARKSAP
CHHHHHHHHHHHCCC
28.43-
24OtherPRKQLATKVARKSAP
CHHHHHHHHHHHCCC
28.43-
24UbiquitinationPRKQLATKVARKSAP
CHHHHHHHHHHHCCC
28.4322817900
27CitrullinationQLATKVARKSAPATG
HHHHHHHHHCCCCCC
36.13-
27CitrullinationQLATKVARKSAPATG
HHHHHHHHHCCCCCC
36.13-
28"N6,N6,N6-trimethyllysine"LATKVARKSAPATGG
HHHHHHHHCCCCCCC
41.03-
28AcetylationLATKVARKSAPATGG
HHHHHHHHCCCCCCC
41.0311478441
28GlutarylationLATKVARKSAPATGG
HHHHHHHHCCCCCCC
41.03-
28LactoylationLATKVARKSAPATGG
HHHHHHHHCCCCCCC
41.03-
28MethylationLATKVARKSAPATGG
HHHHHHHHCCCCCCC
41.0319608861
28OtherLATKVARKSAPATGG
HHHHHHHHCCCCCCC
41.03-
28UbiquitinationLATKVARKSAPATGG
HHHHHHHHCCCCCCC
41.0324816145
29ADP-ribosylationATKVARKSAPATGGV
HHHHHHHCCCCCCCC
33.65-
29PhosphorylationATKVARKSAPATGGV
HHHHHHHCCCCCCCC
33.6525159151
33PhosphorylationARKSAPATGGVKKPH
HHHCCCCCCCCCCCC
33.1528176443
37"N6,N6,N6-trimethyllysine"APATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
37AcetylationAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9511619301
37MethylationAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
37OtherAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.95-
37UbiquitinationAPATGGVKKPHRYRP
CCCCCCCCCCCCCCC
64.9523000965
38"N6,N6-dimethyllysine"PATGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.58-
38MethylationPATGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.58-
38UbiquitinationPATGGVKKPHRYRPG
CCCCCCCCCCCCCCC
43.5823000965
41DimethylationGGVKKPHRYRPGTVA
CCCCCCCCCCCCCHH
37.37-
41MethylationGGVKKPHRYRPGTVA
CCCCCCCCCCCCCHH
37.3754548177
42NitrationGVKKPHRYRPGTVAL
CCCCCCCCCCCCHHH
20.37-
42PhosphorylationGVKKPHRYRPGTVAL
CCCCCCCCCCCCHHH
20.3728152594
43MethylationVKKPHRYRPGTVALR
CCCCCCCCCCCHHHH
24.11-
46PhosphorylationPHRYRPGTVALREIR
CCCCCCCCHHHHHHH
12.8030266825
50MethylationRPGTVALREIRRYQK
CCCCHHHHHHHHHHH
27.79-
55PhosphorylationALREIRRYQKSTELL
HHHHHHHHHHCHHHH
15.5022817900
57"N6,N6,N6-trimethyllysine"REIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57AcetylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8715628137
57GlutarylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57LactoylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57MethylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57OtherREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57SuccinylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8721890473
57SumoylationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.87-
57UbiquitinationREIRRYQKSTELLIR
HHHHHHHHCHHHHHH
50.8723000965
58PhosphorylationEIRRYQKSTELLIRK
HHHHHHHCHHHHHHH
16.1623401153
59PhosphorylationIRRYQKSTELLIRKL
HHHHHHCHHHHHHHC
37.3730266825
64MethylationKSTELLIRKLPFQRL
HCHHHHHHHCHHHHH
34.13-
65MethylationSTELLIRKLPFQRLM
CHHHHHHHCHHHHHH
54.22-
65OtherSTELLIRKLPFQRLM
CHHHHHHHCHHHHHH
54.22-
80"N6,N6,N6-trimethyllysine"REIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80AcetylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.799854425
80GlutarylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80LactoylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80MethylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80OtherREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80SuccinylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7921890473
80SumoylationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.79-
80UbiquitinationREIAQDFKTDLRFQS
HHHHHHHCCCHHHHH
49.7923000965
81PhosphorylationEIAQDFKTDLRFQSS
HHHHHHCCCHHHHHH
40.0123401153
84MethylationQDFKTDLRFQSSAVM
HHHCCCHHHHHHHHH
30.30-
87PhosphorylationKTDLRFQSSAVMALQ
CCCHHHHHHHHHHHH
19.97-
88PhosphorylationTDLRFQSSAVMALQE
CCHHHHHHHHHHHHH
17.69-
99PhosphorylationALQEACESYLVGLFE
HHHHHHHHHHHHHHC
24.53-
108PhosphorylationLVGLFEDTNLCVIHA
HHHHHCCCCEEEEEE
23.93-
116AcetylationNLCVIHAKRVTIMPK
CEEEEEEEECEECHH
32.99-
116GlutarylationNLCVIHAKRVTIMPK
CEEEEEEEECEECHH
32.99-
119PhosphorylationVIHAKRVTIMPKDIQ
EEEEEECEECHHHHH
18.6520068231
121SulfoxidationHAKRVTIMPKDIQLA
EEEECEECHHHHHHH
2.1728183972
123SumoylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123AcetylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5111381985
123GlutarylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123MethylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123OtherKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123SuccinylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5121890473
123SumoylationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.51-
123UbiquitinationKRVTIMPKDIQLARR
EECEECHHHHHHHHH
50.5123000965
129MethylationPKDIQLARRIRGERA
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
4TPhosphorylationKinaseGSG2Q8TF76
GPS
7TPhosphorylationKinasePKC-Uniprot
11SPhosphorylationKinaseALTERNATE-Uniprot
12TPhosphorylationKinasePKC-Uniprot
29SPhosphorylationKinaseAURKBQ96GD4
GPS
29SPhosphorylationKinaseAURKCQ9UQB9
GPS
29SPhosphorylationKinaseRPS6KA5O75582
GPS
29SPhosphorylationKinaseALTERNATE-Uniprot
-KUbiquitinationE3 ubiquitin ligaseRAG1P15918
PMID:20122409

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

-
11SAcetylation

-
11SAcetylation

30257210
11SMethylation

-
11SMethylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

-
11SPhosphorylation

30257210
12TPhosphorylation

-
12TMethylation

-
12TPhosphorylation

-
18RCitrullination

-
18RAcetylation

-
18RMethylation

-
18RMethylation

-
18RMethylation

-
19KMethylation

19608861
19KAcetylation

19608861
24KMethylation

19608861
24KAcetylation

19608861
28KMethylation

-
28KMethylation

-
29SPhosphorylation

18691976
37KMethylation

-
57KMethylation

-
80KMethylation

-
80KMethylation

-
80KMethylation

-
80Kubiquitylation

-
80KSuccinylation

29211711
120Kubiquitylation

-
120KMethylation

-
123KSuccinylation

27436229
123KAcetylation

-

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 H31T_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAF1A_HUMANTAF1Aphysical
11163245
SET_HUMANSETphysical
11163245
AN32A_HUMANANP32Aphysical
11163245
HAT1_HUMANHAT1physical
20953179
RBBP7_HUMANRBBP7physical
20953179
HSP7C_HUMANHSPA8physical
20953179
HS90A_HUMANHSP90AA1physical
20953179
IPO4_HUMANIPO4physical
20953179
ASF1B_HUMANASF1Bphysical
20953179
RBBP4_HUMANRBBP4physical
20953179
CAF1B_HUMANCHAF1Bphysical
20953179
MCM7_HUMANMCM7physical
20953179
ASF1A_HUMANASF1Aphysical
17242207
TDRD3_HUMANTDRD3physical
21172665
SMN_HUMANSMN1physical
21172665
SPF30_HUMANSMNDC1physical
21172665
SPF30_SCHPOspf30physical
21172665
KMT2A_HUMANKMT2Aphysical
21135039
WDR5_HUMANWDR5physical
21135039
CBX3_HUMANCBX3physical
21047797
CBX7_HUMANCBX7physical
21047797
CBX8_HUMANCBX8physical
21047797
CBX1_HUMANCBX1physical
21047797
CBX2_HUMANCBX2physical
21047797
CBX5_HUMANCBX5physical
21047797
CBX6_HUMANCBX6physical
21047797
PHF8_HUMANPHF8physical
21029866
SUZ12_HUMANSUZ12physical
21029866
CBX5_HUMANCBX5physical
21029866
PRS8_HUMANPSMC5physical
18662994
CBX5_HUMANCBX5physical
23281010
BIRC5_HUMANBIRC5physical
23281010
ERAP1_HUMANERAP1physical
23281010
KIF2C_HUMANKIF2Cphysical
23281010
KIF2A_HUMANKIF2Aphysical
23281010
PPM1G_HUMANPPM1Gphysical
23281010
MBD3_HUMANMBD3physical
23281010
JADE2_HUMANJADE2physical
23281010
RBBP7_HUMANRBBP7physical
23281010
HAT1_HUMANHAT1physical
23281010
JADE3_HUMANJADE3physical
23281010
RBBP4_HUMANRBBP4physical
23281010
UHRF1_HUMANUHRF1physical
23281010
MTA1_HUMANMTA1physical
23281010
MTA2_HUMANMTA2physical
23281010
REQU_HUMANDPF2physical
23281010
TAF1_HUMANTAF1physical
17884155
CBX5_HUMANCBX5physical
17884155
TAF1B_HUMANTAF1Bphysical
17884155
TAF2_HUMANTAF2physical
17884155
TAF3_HUMANTAF3physical
17884155
TAF4_HUMANTAF4physical
17884155
TAF4B_HUMANTAF4Bphysical
17884155
TAF5_HUMANTAF5physical
17884155
TAF6_HUMANTAF6physical
17884155
TAF7_HUMANTAF7physical
17884155
TAF8_HUMANTAF8physical
17884155
TAF9_HUMANTAF9physical
17884155
TAF9B_HUMANTAF9Bphysical
17884155
TAF10_HUMANTAF10physical
17884155
TAF11_HUMANTAF11physical
17884155
TAF12_HUMANTAF12physical
17884155
TAF13_HUMANTAF13physical
17884155
TAF3_HUMANTAF3physical
20953165
AIRE_HUMANAIREphysical
20953165
PF21A_HUMANPHF21Aphysical
20953165
PHF2_HUMANPHF2physical
20953165
PHF8_HUMANPHF8physical
20953165
BPTF_HUMANBPTFphysical
20953165
ING2_HUMANING2physical
20953165
ING4_HUMANING4physical
20953165
TAF5_HUMANTAF5physical
20953165
TAF6_HUMANTAF6physical
20953165
PHF7_HUMANPHF7physical
22595675
ING2_HUMANING2physical
22595675
NSD3_HUMANWHSC1L1physical
23269674
UHRF1_HUMANUHRF1physical
24813945
WDR5_HUMANWDR5physical
24793694
ASH2L_HUMANASH2Lphysical
24793694
RET5_HUMANRBP5physical
24793694
POGZ_HUMANPOGZphysical
20850016
CBX5_HUMANCBX5physical
20850016
KAT2A_HUMANKAT2Aphysical
20850016
SGF29_HUMANCCDC101physical
20850016
PHF8_HUMANPHF8physical
20850016
GLYR1_HUMANGLYR1physical
20850016
TAF13_HUMANTAF13physical
20850016
TAF11_HUMANTAF11physical
20850016
TAF8_HUMANTAF8physical
20850016
TAF6_HUMANTAF6physical
20850016
TAF12_HUMANTAF12physical
20850016
TAF7_HUMANTAF7physical
20850016
TAF5_HUMANTAF5physical
20850016
TAF4_HUMANTAF4physical
20850016
TAF4B_HUMANTAF4Bphysical
20850016
TAF1_HUMANTAF1physical
20850016
TAF3_HUMANTAF3physical
20850016
TAF9_HUMANTAF9physical
20850016
TAF2_HUMANTAF2physical
20850016
TAF10_HUMANTAF10physical
20850016
HMGX4_HUMANHMGXB4physical
20850016
PPIB_HUMANPPIBphysical
20850016
BPTF_HUMANBPTFphysical
20850016
TAF9B_HUMANTAF9Bphysical
20850016
BAP18_HUMANC17orf49physical
20850016
SUPT3_HUMANSUPT3Hphysical
20850016
TAF5L_HUMANTAF5Lphysical
20850016
TADA1_HUMANTADA1physical
20850016
TAF6L_HUMANTAF6Lphysical
20850016
SP20H_HUMANSUPT20Hphysical
20850016
CHD1_HUMANCHD1physical
20850016
SIN3A_HUMANSIN3Aphysical
20850016
DPY30_HUMANDPY30physical
20850016
TADA3_HUMANTADA3physical
20850016
DIDO1_HUMANDIDO1physical
20850016
KDM5A_HUMANKDM5Aphysical
20850016
SIN3B_HUMANSIN3Bphysical
20850016
PHF12_HUMANPHF12physical
20850016
GATD1_HUMANGATAD1physical
20850016
EMSY_HUMANC11orf30physical
20850016
CHD6_HUMANCHD6physical
20850016
TBP_HUMANTBPphysical
20850016
DEK_HUMANDEKphysical
20850016
MO4L1_HUMANMORF4L1physical
20850016
RBBP4_HUMANRBBP4physical
20850016
HDAC1_HUMANHDAC1physical
20850016
RBP56_HUMANTAF15physical
20850016
CDYL_HUMANCDYLphysical
20850016
CDYL2_HUMANCDYL2physical
20850016
CBX3_HUMANCBX3physical
20850016
PTBP1_HUMANPTBP1physical
20850016
PHC2_HUMANPHC2physical
20850016
CHAP1_HUMANCHAMP1physical
20850016
BMI1_HUMANBMI1physical
20850016
LRIF1_HUMANLRIF1physical
20850016
LRWD1_HUMANLRWD1physical
20850016
CAF1A_HUMANCHAF1Aphysical
20850016
ORC2_HUMANORC2physical
20850016
PCGF6_HUMANPCGF6physical
20850016
ORC3_HUMANORC3physical
20850016
CBX4_HUMANCBX4physical
20850016
ORC4_HUMANORC4physical
20850016
CAF1B_HUMANCHAF1Bphysical
20850016
ORC5_HUMANORC5physical
20850016
RING2_HUMANRNF2physical
20850016
NONO_HUMANNONOphysical
20850016
PHC3_HUMANPHC3physical
20850016
MIER1_HUMANMIER1physical
20850016
CBX1_HUMANCBX1physical
20850016
RING1_HUMANRING1physical
20850016
ADNP_HUMANADNPphysical
20850016
ROAA_HUMANHNRNPABphysical
20850016
CBX8_HUMANCBX8physical
20850016
ROA1_HUMANHNRNPA1physical
20850016
MGAP_HUMANMGAphysical
20850016
NUCL_HUMANNCLphysical
20850016
HNRPK_HUMANHNRNPKphysical
20850016
SFPQ_HUMANSFPQphysical
20850016
HNRPL_HUMANHNRNPLphysical
20850016
ROA2_HUMANHNRNPA2B1physical
20850016
HNRPR_HUMANHNRNPRphysical
20850016
AHDC1_HUMANAHDC1physical
20850016
ZMYM4_HUMANZMYM4physical
20850016
CHD4_HUMANCHD4physical
20850016
CBX2_HUMANCBX2physical
20850016
NSD2_HUMANWHSC1physical
20850016
PHF1_HUMANPHF1physical
23273982
H2AY_HUMANH2AFYphysical
25306110
PHRF1_HUMANPHRF1physical
25855964
ANM5_HUMANPRMT5physical
25713080
NBN_HUMANNBNphysical
25823024
MRE11_HUMANMRE11Aphysical
25823024
RAD50_HUMANRAD50physical
25823024

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 H31T_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-19 AND LYS-24, AND MASSSPECTROMETRY.
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT LYS-28, 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-58 AND THR-81.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.

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