HM20A_HUMAN - dbPTM
HM20A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HM20A_HUMAN
UniProt AC Q9NP66
Protein Name High mobility group protein 20A
Gene Name HMG20A
Organism Homo sapiens (Human).
Sequence Length 347
Subcellular Localization Nucleus .
Protein Description Plays a role in neuronal differentiation as chromatin-associated protein. Acts as inhibitor of HMG20B. Overcomes the repressive effects of the neuronal silencer REST and induces the activation of neuronal-specific genes. Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4 (By similarity)..
Protein Sequence MENLMTSSTLPPLFADEDGSKESNDLATTGLNHPEVPYSSGATSSTNNPEFVEDLSQGQLLQSESSNAAEGNEQRHEDEQRSKRGGWSKGRKRKKPLRDSNAPKSPLTGYVRFMNERREQLRAKRPEVPFPEITRMLGNEWSKLPPEEKQRYLDEADRDKERYMKELEQYQKTEAYKVFSRKTQDRQKGKSHRQDAARQATHDHEKETEVKERSVFDIPIFTEEFLNHSKAREAELRQLRKSNMEFEERNAALQKHVESMRTAVEKLEVDVIQERSRNTVLQQHLETLRQVLTSSFASMPLPGSGETPTVDTIDSYMNRLHSIILANPQDNENFIATVREVVNRLDR
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
6Phosphorylation--MENLMTSSTLPPL
--CCCCCCCCCCCCC
23.77-
7Phosphorylation-MENLMTSSTLPPLF
-CCCCCCCCCCCCCC
13.8328348404
8PhosphorylationMENLMTSSTLPPLFA
CCCCCCCCCCCCCCC
25.4628348404
9PhosphorylationENLMTSSTLPPLFAD
CCCCCCCCCCCCCCC
42.9528348404
20PhosphorylationLFADEDGSKESNDLA
CCCCCCCCCCCCCCC
45.6425159151
100PhosphorylationRKKPLRDSNAPKSPL
CCCCCCCCCCCCCCC
28.5825159151
105PhosphorylationRDSNAPKSPLTGYVR
CCCCCCCCCCHHHHH
24.8822167270
108PhosphorylationNAPKSPLTGYVRFMN
CCCCCCCHHHHHHHH
29.8323927012
110PhosphorylationPKSPLTGYVRFMNER
CCCCCHHHHHHHHHH
5.3423927012
152PhosphorylationPPEEKQRYLDEADRD
CHHHHHHHHHHHHHH
18.9322817900
163PhosphorylationADRDKERYMKELEQY
HHHHHHHHHHHHHHH
17.4022817900
165UbiquitinationRDKERYMKELEQYQK
HHHHHHHHHHHHHHH
50.65-
170PhosphorylationYMKELEQYQKTEAYK
HHHHHHHHHHHHHHH
11.5522817900
172AcetylationKELEQYQKTEAYKVF
HHHHHHHHHHHHHHH
43.3226051181
172UbiquitinationKELEQYQKTEAYKVF
HHHHHHHHHHHHHHH
43.32-
173PhosphorylationELEQYQKTEAYKVFS
HHHHHHHHHHHHHHC
15.43-
176PhosphorylationQYQKTEAYKVFSRKT
HHHHHHHHHHHCHHH
11.06-
177AcetylationYQKTEAYKVFSRKTQ
HHHHHHHHHHCHHHH
43.8026051181
177UbiquitinationYQKTEAYKVFSRKTQ
HHHHHHHHHHCHHHH
43.80-
230UbiquitinationEEFLNHSKAREAELR
HHHHCHHHHHHHHHH
43.86-
255UbiquitinationERNAALQKHVESMRT
HHHHHHHHHHHHHHH
50.93-
287PhosphorylationVLQQHLETLRQVLTS
HHHHHHHHHHHHHHH
33.33-

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 HM20A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HM20A_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 HM20A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHP3_HUMANTESCphysical
16189514
MGN2_HUMANMAGOHBphysical
16189514
HM20A_HUMANHMG20Aphysical
16189514
TF2AY_HUMANGTF2A1Lphysical
20211142
HD_HUMANHTTphysical
23275563
HM20A_HUMANHMG20Aphysical
25416956
RPP30_HUMANRPP30physical
25416956
CC136_HUMANCCDC136physical
25416956
SCNM1_HUMANSCNM1physical
25416956
SYTL4_HUMANSYTL4physical
25416956
CFA53_HUMANCFAP53physical
25416956
RSPH9_HUMANRSPH9physical
25416956
HDAC1_HUMANHDAC1physical
26496610
HDAC2_HUMANHDAC2physical
26496610
CH60_HUMANHSPD1physical
26496610
PAWR_HUMANPAWRphysical
26496610
RAD51_HUMANRAD51physical
26496610
RBBP7_HUMANRBBP7physical
26496610
TRI27_HUMANTRIM27physical
26496610
TCF20_HUMANTCF20physical
26496610
MBD2_HUMANMBD2physical
26496610
MTA2_HUMANMTA2physical
26496610
PHF14_HUMANPHF14physical
26496610
HM20B_HUMANHMG20Bphysical
26496610
RAI1_HUMANRAI1physical
26496610
KDM1A_HUMANKDM1Aphysical
26496610
RCOR1_HUMANRCOR1physical
26496610
GSE1_HUMANGSE1physical
26496610
HP1B3_HUMANHP1BP3physical
26496610
PF21A_HUMANPHF21Aphysical
26496610
P66A_HUMANGATAD2Aphysical
26496610
BCOR_HUMANBCORphysical
26496610
URFB1_HUMANUHRF1BP1physical
26496610
RCOR3_HUMANRCOR3physical
26496610
P66B_HUMANGATAD2Bphysical
26496610
HDAC1_HUMANHDAC1physical
28514442
ZC4H2_HUMANZC4H2physical
28514442
PF21A_HUMANPHF21Aphysical
28514442
PHF14_HUMANPHF14physical
28514442
GSE1_HUMANGSE1physical
28514442
SMBT1_HUMANSFMBT1physical
28514442
RCOR2_HUMANRCOR2physical
28514442
DTNA_HUMANDTNAphysical
28514442
SNTB1_HUMANSNTB1physical
28514442
RCOR3_HUMANRCOR3physical
28514442
HMMR_HUMANHMMRphysical
28514442
CEP83_HUMANCEP83physical
28514442
SNTA1_HUMANSNTA1physical
28514442
RCOR1_HUMANRCOR1physical
28514442
SNTB2_HUMANSNTB2physical
28514442
KDM1A_HUMANKDM1Aphysical
28514442
PAWR_HUMANPAWRphysical
28514442
HDAC2_HUMANHDAC2physical
28514442
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
CCHCR_HUMANCCHCR1physical
27173435
YETS4_HUMANYEATS4physical
27173435
TUFT1_HUMANTUFT1physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
RBG10_HUMANRABGAP1Lphysical
27173435
RBG1L_HUMANRABGAP1Lphysical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS53_HUMANVPS53physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
RCOR1_HUMANRCOR1physical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
MS18B_HUMANOIP5physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
PHLB3_HUMANPHLDB3physical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
THA11_HUMANTHAP11physical
27173435
VPS51_HUMANVPS51physical
27173435
KDM1A_HUMANKDM1Aphysical
27173435
EIPR1_HUMANTSSC1physical
27173435

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 HM20A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY.
"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-105, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY.

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