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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Acetylation | -----MPKRKAEGDA -----CCCCCCCCCC | 66.29 | 10207070 | |
5 | Acetylation | ---MPKRKAEGDAKG ---CCCCCCCCCCCC | 57.84 | 59699 | |
11 | Acetylation | RKAEGDAKGDKAKVK CCCCCCCCCCHHHCC | 72.83 | 59703 | |
14 | Acetylation | EGDAKGDKAKVKDEP CCCCCCCHHHCCCCH | 59.79 | 70015 | |
14 | Ubiquitination | EGDAKGDKAKVKDEP CCCCCCCHHHCCCCH | 59.79 | 24816145 | |
18 | Acetylation | KGDKAKVKDEPQRRS CCCHHHCCCCHHHHH | 56.52 | 10753971 | |
18 | Sumoylation | KGDKAKVKDEPQRRS CCCHHHCCCCHHHHH | 56.52 | - | |
18 | Ubiquitination | KGDKAKVKDEPQRRS CCCHHHCCCCHHHHH | 56.52 | 33845483 | |
18 | Sumoylation | KGDKAKVKDEPQRRS CCCHHHCCCCHHHHH | 56.52 | 10753971 | |
25 | Phosphorylation | KDEPQRRSARLSAKP CCCHHHHHHHHCCCC | 21.67 | 25159151 | |
29 | ADP-ribosylation | QRRSARLSAKPAPPK HHHHHHHCCCCCCCC | 28.79 | 28190768 | |
29 | Phosphorylation | QRRSARLSAKPAPPK HHHHHHHCCCCCCCC | 28.79 | 23401153 | |
31 | Acetylation | RSARLSAKPAPPKPE HHHHHCCCCCCCCCC | 38.03 | 19608861 | |
31 | Ubiquitination | RSARLSAKPAPPKPE HHHHHCCCCCCCCCC | 38.03 | 23000965 | |
36 | Ubiquitination | SAKPAPPKPEPKPKK CCCCCCCCCCCCCCC | 62.04 | 23000965 | |
36 | Sumoylation | SAKPAPPKPEPKPKK CCCCCCCCCCCCCCC | 62.04 | 19608861 | |
36 | Acetylation | SAKPAPPKPEPKPKK CCCCCCCCCCCCCCC | 62.04 | 23954790 | |
36 | Sumoylation | SAKPAPPKPEPKPKK CCCCCCCCCCCCCCC | 62.04 | - | |
40 | Acetylation | APPKPEPKPKKAPAK CCCCCCCCCCCCCCC | 68.74 | 23749302 | |
40 | Ubiquitination | APPKPEPKPKKAPAK CCCCCCCCCCCCCCC | 68.74 | 29967540 | |
42 | Acetylation | PKPEPKPKKAPAKKG CCCCCCCCCCCCCCC | 68.63 | 10753971 | |
47 | Ubiquitination | KPKKAPAKKGEKVPK CCCCCCCCCCCCCCC | 61.32 | - | |
48 | Ubiquitination | PKKAPAKKGEKVPKG CCCCCCCCCCCCCCC | 74.53 | - | |
48 | Acetylation | PKKAPAKKGEKVPKG CCCCCCCCCCCCCCC | 74.53 | 10753971 | |
51 | Ubiquitination | APAKKGEKVPKGKKG CCCCCCCCCCCCCCC | 72.93 | - | |
54 | Acetylation | KKGEKVPKGKKGKAD CCCCCCCCCCCCCCC | 83.07 | 88049 | |
56 | Acetylation | GEKVPKGKKGKADAG CCCCCCCCCCCCCCC | 65.56 | 88053 | |
57 | Acetylation | EKVPKGKKGKADAGK CCCCCCCCCCCCCCC | 74.45 | 129283 | |
59 | Acetylation | VPKGKKGKADAGKEG CCCCCCCCCCCCCCC | 52.55 | 21339330 | |
59 | Ubiquitination | VPKGKKGKADAGKEG CCCCCCCCCCCCCCC | 52.55 | 22817900 | |
64 | Ubiquitination | KGKADAGKEGNNPAE CCCCCCCCCCCCCCC | 65.26 | 21906983 | |
64 | Acetylation | KGKADAGKEGNNPAE CCCCCCCCCCCCCCC | 65.26 | 23749302 | |
76 | Acetylation | PAENGDAKTDQAQKA CCCCCCCCHHHHHHH | 58.33 | 23749302 | |
76 | Ubiquitination | PAENGDAKTDQAQKA CCCCCCCCHHHHHHH | 58.33 | 21906983 | |
82 | Acetylation | AKTDQAQKAEGAGDA CCHHHHHHHCCCCCC | 51.96 | 19608861 | |
82 | Sumoylation | AKTDQAQKAEGAGDA CCHHHHHHHCCCCCC | 51.96 | - | |
82 | Ubiquitination | AKTDQAQKAEGAGDA CCHHHHHHHCCCCCC | 51.96 | 27667366 | |
82 | Sumoylation | AKTDQAQKAEGAGDA CCHHHHHHHCCCCCC | 51.96 | 25218447 | |
90 | Acetylation | AEGAGDAK------- HCCCCCCC------- | 66.66 | 70023 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
25 | S | Phosphorylation | Kinase | AURKB | Q96GD4 | GPS |
29 | S | Phosphorylation | Kinase | AURKB | Q96GD4 | GPS |
29 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
29 | S | Phosphorylation | Kinase | PKG/CGK_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMGN2_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HMGN2_HUMAN | HMGN2 | physical | 7563062 | |
POL_HV1H2 | gag-pol | physical | 20016921 | |
KLH36_HUMAN | KLHL36 | physical | 28514442 | |
PARP2_HUMAN | PARP2 | physical | 28514442 | |
CHM1A_HUMAN | CHMP1A | physical | 28514442 | |
H2AY_HUMAN | H2AFY | physical | 28514442 | |
PYGB_HUMAN | PYGB | physical | 28514442 | |
GLGB_HUMAN | GBE1 | physical | 28514442 |
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. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |