HMGN2_HUMAN - dbPTM
HMGN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMGN2_HUMAN
UniProt AC P05204
Protein Name Non-histone chromosomal protein HMG-17
Gene Name HMGN2
Organism Homo sapiens (Human).
Sequence Length 90
Subcellular Localization Nucleus . Cytoplasm . Cytoplasmic enrichment upon phosphorylation.
Protein Description Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity)..
Protein Sequence MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK
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
3Acetylation-----MPKRKAEGDA
-----CCCCCCCCCC
66.2910207070
5Acetylation---MPKRKAEGDAKG
---CCCCCCCCCCCC
57.8459699
11AcetylationRKAEGDAKGDKAKVK
CCCCCCCCCCHHHCC
72.8359703
14AcetylationEGDAKGDKAKVKDEP
CCCCCCCHHHCCCCH
59.7970015
14UbiquitinationEGDAKGDKAKVKDEP
CCCCCCCHHHCCCCH
59.7924816145
18AcetylationKGDKAKVKDEPQRRS
CCCHHHCCCCHHHHH
56.5210753971
18SumoylationKGDKAKVKDEPQRRS
CCCHHHCCCCHHHHH
56.52-
18UbiquitinationKGDKAKVKDEPQRRS
CCCHHHCCCCHHHHH
56.5233845483
18SumoylationKGDKAKVKDEPQRRS
CCCHHHCCCCHHHHH
56.5210753971
25PhosphorylationKDEPQRRSARLSAKP
CCCHHHHHHHHCCCC
21.6725159151
29ADP-ribosylationQRRSARLSAKPAPPK
HHHHHHHCCCCCCCC
28.7928190768
29PhosphorylationQRRSARLSAKPAPPK
HHHHHHHCCCCCCCC
28.7923401153
31AcetylationRSARLSAKPAPPKPE
HHHHHCCCCCCCCCC
38.0319608861
31UbiquitinationRSARLSAKPAPPKPE
HHHHHCCCCCCCCCC
38.0323000965
36UbiquitinationSAKPAPPKPEPKPKK
CCCCCCCCCCCCCCC
62.0423000965
36SumoylationSAKPAPPKPEPKPKK
CCCCCCCCCCCCCCC
62.0419608861
36AcetylationSAKPAPPKPEPKPKK
CCCCCCCCCCCCCCC
62.0423954790
36SumoylationSAKPAPPKPEPKPKK
CCCCCCCCCCCCCCC
62.04-
40AcetylationAPPKPEPKPKKAPAK
CCCCCCCCCCCCCCC
68.7423749302
40UbiquitinationAPPKPEPKPKKAPAK
CCCCCCCCCCCCCCC
68.7429967540
42AcetylationPKPEPKPKKAPAKKG
CCCCCCCCCCCCCCC
68.6310753971
47UbiquitinationKPKKAPAKKGEKVPK
CCCCCCCCCCCCCCC
61.32-
48UbiquitinationPKKAPAKKGEKVPKG
CCCCCCCCCCCCCCC
74.53-
48AcetylationPKKAPAKKGEKVPKG
CCCCCCCCCCCCCCC
74.5310753971
51UbiquitinationAPAKKGEKVPKGKKG
CCCCCCCCCCCCCCC
72.93-
54AcetylationKKGEKVPKGKKGKAD
CCCCCCCCCCCCCCC
83.0788049
56AcetylationGEKVPKGKKGKADAG
CCCCCCCCCCCCCCC
65.5688053
57AcetylationEKVPKGKKGKADAGK
CCCCCCCCCCCCCCC
74.45129283
59AcetylationVPKGKKGKADAGKEG
CCCCCCCCCCCCCCC
52.5521339330
59UbiquitinationVPKGKKGKADAGKEG
CCCCCCCCCCCCCCC
52.5522817900
64UbiquitinationKGKADAGKEGNNPAE
CCCCCCCCCCCCCCC
65.2621906983
64AcetylationKGKADAGKEGNNPAE
CCCCCCCCCCCCCCC
65.2623749302
76AcetylationPAENGDAKTDQAQKA
CCCCCCCCHHHHHHH
58.3323749302
76UbiquitinationPAENGDAKTDQAQKA
CCCCCCCCHHHHHHH
58.3321906983
82AcetylationAKTDQAQKAEGAGDA
CCHHHHHHHCCCCCC
51.9619608861
82SumoylationAKTDQAQKAEGAGDA
CCHHHHHHHCCCCCC
51.96-
82UbiquitinationAKTDQAQKAEGAGDA
CCHHHHHHHCCCCCC
51.9627667366
82SumoylationAKTDQAQKAEGAGDA
CCHHHHHHHCCCCCC
51.9625218447
90AcetylationAEGAGDAK-------
HCCCCCCC-------
66.6670023

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
25SPhosphorylationKinaseAURKBQ96GD4
GPS
29SPhosphorylationKinaseAURKBQ96GD4
GPS
29SPhosphorylationKinasePKG-FAMILY-GPS
29SPhosphorylationKinasePKG/CGK_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HMGN2_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 HMGN2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMGN2_HUMANHMGN2physical
7563062
POL_HV1H2gag-polphysical
20016921
KLH36_HUMANKLHL36physical
28514442
PARP2_HUMANPARP2physical
28514442
CHM1A_HUMANCHMP1Aphysical
28514442
H2AY_HUMANH2AFYphysical
28514442
PYGB_HUMANPYGBphysical
28514442
GLGB_HUMANGBE1physical
28514442

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 HMGN2_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-82, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphorylation and subcellular redistribution of high mobility groupproteins 14 and 17, analyzed by mass spectrometry.";
Louie D.F., Gloor K.K., Galasinski S.C., Resing K.A., Ahn N.G.;
Protein Sci. 9:170-179(2000).
Cited for: PROTEIN SEQUENCE OF 19-31, PHOSPHORYLATION AT SER-25 AND SER-29,SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.

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