H12_BOVIN - dbPTM
H12_BOVIN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H12_BOVIN
UniProt AC P02253
Protein Name Histone H1.2
Gene Name HIST1H1C
Organism Bos taurus (Bovine).
Sequence Length 213
Subcellular Localization Nucleus. Chromosome. Mainly localizes in euchromatin..
Protein Description Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)..
Protein Sequence MSETAPAAPAAAPPAEKTPVKKKAAKKPAGARRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAATGEAKPKAKKAGAAKPKKAAGAAKKTKKATGAATPKKTAKKTPKKAKKPAAAAVTKKVAKSPKKAKAAKPKKAAKSAAKAVKPKAAKPKVAKPKKAAPKKK
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
2Acetylation------MSETAPAAP
------CCCCCCCCC
-
2Phosphorylation------MSETAPAAP
------CCCCCCCCC
-
17AcetylationAAAPPAEKTPVKKKA
CCCCCHHHCCCCHHH
-
18PhosphorylationAAPPAEKTPVKKKAA
CCCCHHHCCCCHHHC
-
23OtherEKTPVKKKAAKKPAG
HHCCCCHHHCCCCCC
-
26MethylationPVKKKAAKKPAGARR
CCCHHHCCCCCCCCC
-
26AcetylationPVKKKAAKKPAGARR
CCCHHHCCCCCCCCC
-
26OtherPVKKKAAKKPAGARR
CCCHHHCCCCCCCCC
-
27OtherVKKKAAKKPAGARRK
CCHHHCCCCCCCCCC
-
34CrotonylationKPAGARRKASGPPVS
CCCCCCCCCCCCCHH
-
34OtherKPAGARRKASGPPVS
CCCCCCCCCCCCCHH
-
34N6-crotonyl-L-lysineKPAGARRKASGPPVS
CCCCCCCCCCCCCHH
-
34MethylationKPAGARRKASGPPVS
CCCCCCCCCCCCCHH
-
35PhosphorylationPAGARRKASGPPVSE
CCCCCCCCCCCCHHH
1137958
36PhosphorylationAGARRKASGPPVSEL
CCCCCCCCCCCHHHH
1137958
41PhosphorylationKASGPPVSELITKAV
CCCCCCHHHHHHHHH
-
46AcetylationPVSELITKAVAASKE
CHHHHHHHHHHHCHH
-
46OtherPVSELITKAVAASKE
CHHHHHHHHHHHCHH
-
52OtherTKAVAASKERSGVSL
HHHHHHCHHCCCCCH
-
54CitrullinationAVAASKERSGVSLAA
HHHHCHHCCCCCHHH
-
54CitrullinationAVAASKERSGVSLAA
HHHHCHHCCCCCHHH
-
63OtherGVSLAALKKALAAAG
CCCHHHHHHHHHHCC
-
64N6-crotonyl-L-lysineVSLAALKKALAAAGY
CCHHHHHHHHHHCCC
-
64OtherVSLAALKKALAAAGY
CCHHHHHHHHHHCCC
-
64CrotonylationVSLAALKKALAAAGY
CCHHHHHHHHHHCCC
-
75OtherAAGYDVEKNNSRIKL
HCCCCCHHCCCCCCC
-
75AcetylationAAGYDVEKNNSRIKL
HCCCCCHHCCCCCCC
-
81OtherEKNNSRIKLGLKSLV
HHCCCCCCCCHHHHH
-
85CrotonylationSRIKLGLKSLVSKGT
CCCCCCHHHHHHCCC
-
85OtherSRIKLGLKSLVSKGT
CCCCCCHHHHHHCCC
-
85N6-crotonyl-L-lysineSRIKLGLKSLVSKGT
CCCCCCHHHHHHCCC
-
90CrotonylationGLKSLVSKGTLVQTK
CHHHHHHCCCEEEEC
-
90OtherGLKSLVSKGTLVQTK
CHHHHHHCCCEEEEC
-
90AcetylationGLKSLVSKGTLVQTK
CHHHHHHCCCEEEEC
-
90N6-crotonyl-L-lysineGLKSLVSKGTLVQTK
CHHHHHHCCCEEEEC
-
97SuccinylationKGTLVQTKGTGASGS
CCCEEEECCCCCCCC
-
97N6-crotonyl-L-lysineKGTLVQTKGTGASGS
CCCEEEECCCCCCCC
-
97CrotonylationKGTLVQTKGTGASGS
CCCEEEECCCCCCCC
-
97OtherKGTLVQTKGTGASGS
CCCEEEECCCCCCCC
-
103PhosphorylationTKGTGASGSFKLNKK
ECCCCCCCCEEECCC
3134256
104PhosphorylationKGTGASGSFKLNKKA
CCCCCCCCEEECCCC
3134256
106OtherTGASGSFKLNKKAAT
CCCCCCEEECCCCCC
-
110OtherGSFKLNKKAATGEAK
CCEEECCCCCCCCCC
-
117OtherKAATGEAKPKAKKAG
CCCCCCCCHHHHHCC
-
121OtherGEAKPKAKKAGAAKP
CCCCHHHHHCCCCCC
-
129OtherKAGAAKPKKAAGAAK
HCCCCCCCHHHCCCH
-
136OtherKKAAGAAKKTKKATG
CHHHCCCHHCCCCCC
-
146PhosphorylationKKATGAATPKKTAKK
CCCCCCCCCCCCCCC
-
148OtherATGAATPKKTAKKTP
CCCCCCCCCCCCCCC
-
154PhosphorylationPKKTAKKTPKKAKKP
CCCCCCCCCCCCCCH
-
159CrotonylationKKTPKKAKKPAAAAV
CCCCCCCCCHHHHHH
-
159N6-crotonyl-L-lysineKKTPKKAKKPAAAAV
CCCCCCCCCHHHHHH
-
159OtherKKTPKKAKKPAAAAV
CCCCCCCCCHHHHHH
-
168CrotonylationPAAAAVTKKVAKSPK
HHHHHHHHHHHCCHH
-
168AcetylationPAAAAVTKKVAKSPK
HHHHHHHHHHHCCHH
-
168N6-crotonyl-L-lysinePAAAAVTKKVAKSPK
HHHHHHHHHHHCCHH
-
168OtherPAAAAVTKKVAKSPK
HHHHHHHHHHHCCHH
-
173PhosphorylationVTKKVAKSPKKAKAA
HHHHHHCCHHHHHHC
-
187MethylationAKPKKAAKSAAKAVK
CCHHHHHHHHHHHHC
-
188ADP-ribosylationKPKKAAKSAAKAVKP
CHHHHHHHHHHHHCC
-
188PhosphorylationKPKKAAKSAAKAVKP
CHHHHHHHHHHHHCC
-

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
35SPhosphorylationKinasePKA-FAMILY-GPS
35SPhosphorylationKinasePKA_GROUP-PhosphoELM
36SPhosphorylationKinasePRKACAP00517
GPS
36SPhosphorylationKinasePRKG1P00516
GPS
36SPhosphorylationKinasePKG1Q13976
PSP
36SPhosphorylationKinasePRKCAP04409
GPS
103SPhosphorylationKinasePKC-FAMILY-GPS
103SPhosphorylationKinasePKC_GROUP-PhosphoELM
104SPhosphorylationKinasePRKCAP05696
GPS
104SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H12_BOVIN !!

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 H12_BOVIN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H12_BOVIN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H12_BOVIN

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Related Literatures of Post-Translational Modification

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