H2A1H_HUMAN - dbPTM
H2A1H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2A1H_HUMAN
UniProt AC Q96KK5
Protein Name Histone H2A type 1-H
Gene Name HIST1H2AH
Organism Homo sapiens (Human).
Sequence Length 128
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 MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAK
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
2Phosphorylation------MSGRGKQGG
------CCCCCCCCC		36.8815823041
2Acetylation------MSGRGKQGG
------CCCCCCCCC		36.8815823041
4Citrullination----MSGRGKQGGKA
----CCCCCCCCCHH		41.66-
4Methylation----MSGRGKQGGKA
----CCCCCCCCCHH		41.66-
4Citrullination----MSGRGKQGGKA
----CCCCCCCCCHH		41.6615823041
6Methylation--MSGRGKQGGKARA
--CCCCCCCCCHHCH		44.39-
6Acetylation--MSGRGKQGGKARA
--CCCCCCCCCHHCH		44.39-
6Other--MSGRGKQGGKARA
--CCCCCCCCCHHCH		44.3924681537
10AcetylationGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.3422389435
10LactoylationGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.34-
10OtherGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.3427105115
10SuccinylationGRGKQGGKARAKAKT
CCCCCCCHHCHHHHH		41.3422389435
14AcetylationQGGKARAKAKTRSSR
CCCHHCHHHHHHHHC		44.88-
14UbiquitinationQGGKARAKAKTRSSR
CCCHHCHHHHHHHHC		44.8822980979
14OtherQGGKARAKAKTRSSR
CCCHHCHHHHHHHHC		44.8827105115
16UbiquitinationGKARAKAKTRSSRAG
CHHCHHHHHHHHCCC		43.7122980979
17PhosphorylationKARAKAKTRSSRAGL
HHCHHHHHHHHCCCC		40.4123882029
19PhosphorylationRAKAKTRSSRAGLQF
CHHHHHHHHCCCCCC		29.4323312004
20PhosphorylationAKAKTRSSRAGLQFP
HHHHHHHHCCCCCCC		23.9027966365
21MethylationKAKTRSSRAGLQFPV
HHHHHHHCCCCCCCH		33.64-
30MethylationGLQFPVGRVHRLLRK
CCCCCHHHHHHHHHC		22.69-
37N6-crotonyl-L-lysineRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.02-
37UbiquitinationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.02-
37CrotonylationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.0221925322
37OtherRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC		52.0227105115
40PhosphorylationRLLRKGNYAERVGAG
HHHHCCCHHHHCCCC		20.6428152594
58PhosphorylationYLAAVLEYLTAEILE
HHHHHHHHHHHHHHH		12.75-
75OtherGNAARDNKKTRIIPR
CHHHHCCCCCCEEHH		60.8724681537
76OtherNAARDNKKTRIIPRH
HHHHCCCCCCEEHHH		49.6524681537
77PhosphorylationAARDNKKTRIIPRHL
HHHCCCCCCEEHHHH		28.8023882029
82MethylationKKTRIIPRHLQLAIR
CCCCEEHHHHHHHHC		32.51-
89MethylationRHLQLAIRNDEELNK
HHHHHHHCCHHHHHH		38.65-
96GlutarylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6831542297
96OtherRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6827105115
96AcetylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6855169283
96SuccinylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6822389435
96UbiquitinationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE		58.6822389435
100GlutarylationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC		35.8531542297
100UbiquitinationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC		35.8521906983
102PhosphorylationNKLLGKVTIAQGGVL
HHHHCCEEECCCCCC		17.6824732914
105MethylationLGKVTIAQGGVLPNI
HCCEEECCCCCCCCE		45.3724352239
119N6-crotonyl-L-lysineIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.76-
119UbiquitinationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.76-
119OtherIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7627105115
119SumoylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.76-
119GlutarylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7631542297
119CrotonylationIQAVLLPKKTESHHK
EEEEECCCCCCCCCC		72.7621925322
120SumoylationQAVLLPKKTESHHKA
EEEECCCCCCCCCCC		56.43-
120CrotonylationQAVLLPKKTESHHKA
EEEECCCCCCCCCCC		56.4321925322
120UbiquitinationQAVLLPKKTESHHKA
EEEECCCCCCCCCCC		56.4325470042
120N6-crotonyl-L-lysineQAVLLPKKTESHHKA
EEEECCCCCCCCCCC		56.43-
120GlutarylationQAVLLPKKTESHHKA
EEEECCCCCCCCCCC		56.4331542297
121PhosphorylationAVLLPKKTESHHKAK
EEECCCCCCCCCCCC		49.1722617229
123PhosphorylationLLPKKTESHHKAK--
ECCCCCCCCCCCC--		35.8022617229
126UbiquitinationKKTESHHKAK-----
CCCCCCCCCC-----		53.07-
126N6-crotonyl-L-lysineKKTESHHKAK-----
CCCCCCCCCC-----		53.07-
126GlutarylationKKTESHHKAK-----
CCCCCCCCCC-----		53.0731542297
126CrotonylationKKTESHHKAK-----
CCCCCCCCCC-----		53.0721925322
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
2SPhosphorylationKinaseRPS6KA5O75582
Uniprot
121TPhosphorylationKinaseDCAF1Q9Y4B6
Uniprot
-KUbiquitinationE3 ubiquitin ligasePRC1O43663
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseBMI1P35226
PMID:16359901
-KUbiquitinationE3 ubiquitin ligaseBMI1#RNF2P35226#Q99496
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2SAcetylation

15010469
2SPhosphorylation

15010469
2SPhosphorylation

15010469
2SPhosphorylation

15010469
4RMethylation

15823041
14Kubiquitylation

22980979
14Kubiquitylation

22980979
16Kubiquitylation

22980979
16Kubiquitylation

22980979
27KMethylation

15386022
27Kubiquitylation

15386022
63Kubiquitylation

15386022
105QMethylation

24352239
120Kubiquitylation

15386022
120Kubiquitylation

15386022
121TPhosphorylation

15078818
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 H2A1H_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H2A1H_HUMAN !!
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 H2A1H_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Deimination of histone H2A and H4 at arginine 3 in HL-60granulocytes.";
Hagiwara T., Hidaka Y., Yamada M.;
Biochemistry 44:5827-5834(2005).
Cited for: ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation of histone H2A inhibits transcription on chromatintemplates.";
Zhang Y., Griffin K., Mondal N., Parvin J.D.;
J. Biol. Chem. 279:21866-21872(2004).
Cited for: PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2.
"Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 duringmitosis in the early Drosophila embryo.";
Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N.,Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
Genes Dev. 18:877-888(2004).
Cited for: PHOSPHORYLATION AT THR-121.
Ubiquitylation
ReferencePubMed
"DNA damage triggers nucleotide excision repair-dependentmonoubiquitylation of histone H2A.";
Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M.,de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B.,Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.;
Genes Dev. 20:1343-1352(2006).
Cited for: UBIQUITINATION AT LYS-120.
"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox genesilencing.";
Cao R., Tsukada Y., Zhang Y.;
Mol. Cell 20:845-854(2005).
Cited for: UBIQUITINATION AT LYS-120.
"Role of histone H2A ubiquitination in Polycomb silencing.";
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,Jones R.S., Zhang Y.;
Nature 431:873-878(2004).
Cited for: UBIQUITINATION AT LYS-120.

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