UniProt ID | AN32E_HUMAN | |
---|---|---|
UniProt AC | Q9BTT0 | |
Protein Name | Acidic leucine-rich nuclear phosphoprotein 32 family member E | |
Gene Name | ANP32E | |
Organism | Homo sapiens (Human). | |
Sequence Length | 268 | |
Subcellular Localization | Cytoplasm. Nucleus. | |
Protein Description | Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AFZ from the nucleosome: removes H2A.Z/H2AFZ from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AFZ in the nucleosome. May stabilize the evicted H2A.Z/H2AFZ-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state. [PubMed: 24463511 Inhibits activity of protein phosphatase 2A (PP2A Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis.] | |
Protein Sequence | MEMKKKINLELRNRSPEEVTELVLDNCLCVNGEIEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQITYLDGFDQEDNEAPDSEEEDDEDGDEDDEEEEENEAGPPEGYEEEEEEEEEEDEDEDEDEDEAGSELGEGEEEVGLSYLMKEEIQDEEDDDDYVEEGEEEEEEEEGGLRGEKRKRDAEDDGEEEDD | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MEMKKKIN -------CCCHHHHC | 11.65 | 22814378 | |
5 | Ubiquitination | ---MEMKKKINLELR ---CCCHHHHCHHHC | 58.54 | - | |
6 | Sumoylation | --MEMKKKINLELRN --CCCHHHHCHHHCC | 31.17 | - | |
6 | Ubiquitination | --MEMKKKINLELRN --CCCHHHHCHHHCC | 31.17 | - | |
6 | Sumoylation | --MEMKKKINLELRN --CCCHHHHCHHHCC | 31.17 | - | |
6 | 2-Hydroxyisobutyrylation | --MEMKKKINLELRN --CCCHHHHCHHHCC | 31.17 | - | |
12 | Methylation | KKINLELRNRSPEEV HHHCHHHCCCCHHHH | 27.43 | 115481755 | |
15 | Phosphorylation | NLELRNRSPEEVTEL CHHHCCCCHHHHHHH | 39.97 | 22468782 | |
17 | Ubiquitination | ELRNRSPEEVTELVL HHCCCCHHHHHHHHH | 67.36 | 21890473 | |
53 | Ubiquitination | FLSMANVELSSLARL HHHHHCCCHHHHCCC | 42.62 | 21890473 | |
56 | Phosphorylation | MANVELSSLARLPSL HHCCCHHHHCCCCCH | 38.38 | 30387612 | |
62 | Phosphorylation | SSLARLPSLNKLRKL HHHCCCCCHHHHHCC | 49.52 | 28464451 | |
65 | Acetylation | ARLPSLNKLRKLELS CCCCCHHHHHCCCCC | 55.77 | 25953088 | |
65 | Ubiquitination | ARLPSLNKLRKLELS CCCCCHHHHHCCCCC | 55.77 | 21890473 | |
65 | Ubiquitination | ARLPSLNKLRKLELS CCCCCHHHHHCCCCC | 55.77 | 21890473 | |
65 | 2-Hydroxyisobutyrylation | ARLPSLNKLRKLELS CCCCCHHHHHCCCCC | 55.77 | - | |
68 | Sumoylation | PSLNKLRKLELSDNI CCHHHHHCCCCCCCC | 57.67 | 28112733 | |
68 | Ubiquitination | PSLNKLRKLELSDNI CCHHHHHCCCCCCCC | 57.67 | 21890473 | |
68 | Sumoylation | PSLNKLRKLELSDNI CCHHHHHCCCCCCCC | 57.67 | - | |
68 | 2-Hydroxyisobutyrylation | PSLNKLRKLELSDNI CCHHHHHCCCCCCCC | 57.67 | - | |
77 | Phosphorylation | ELSDNIISGGLEVLA CCCCCCHHHHHHHHH | 24.02 | 28348404 | |
86 | Ubiquitination | GLEVLAEKCPNLTYL HHHHHHHHCCCCEEE | 49.76 | - | |
91 | Phosphorylation | AEKCPNLTYLNLSGN HHHCCCCEEEECCCC | 32.38 | 28152594 | |
92 | Phosphorylation | EKCPNLTYLNLSGNK HHCCCCEEEECCCCC | 9.21 | 28152594 | |
96 | Phosphorylation | NLTYLNLSGNKIKDL CCEEEECCCCCCCCC | 38.97 | 28152594 | |
99 | Ubiquitination | YLNLSGNKIKDLSTV EEECCCCCCCCCHHH | 55.44 | 21906983 | |
99 | Sumoylation | YLNLSGNKIKDLSTV EEECCCCCCCCCHHH | 55.44 | - | |
99 | Acetylation | YLNLSGNKIKDLSTV EEECCCCCCCCCHHH | 55.44 | 25953088 | |
99 | Sumoylation | YLNLSGNKIKDLSTV EEECCCCCCCCCHHH | 55.44 | - | |
101 | 2-Hydroxyisobutyrylation | NLSGNKIKDLSTVEA ECCCCCCCCCHHHHH | 54.98 | - | |
101 | Sumoylation | NLSGNKIKDLSTVEA ECCCCCCCCCHHHHH | 54.98 | - | |
101 | Ubiquitination | NLSGNKIKDLSTVEA ECCCCCCCCCHHHHH | 54.98 | 21890473 | |
101 | Sumoylation | NLSGNKIKDLSTVEA ECCCCCCCCCHHHHH | 54.98 | - | |
104 | Phosphorylation | GNKIKDLSTVEALQN CCCCCCCHHHHHHHH | 40.31 | 25159151 | |
105 | Phosphorylation | NKIKDLSTVEALQNL CCCCCCHHHHHHHHH | 29.66 | 21712546 | |
113 | 2-Hydroxyisobutyrylation | VEALQNLKNLKSLDL HHHHHHHHCCCCCCC | 68.72 | - | |
113 | Succinylation | VEALQNLKNLKSLDL HHHHHHHHCCCCCCC | 68.72 | 23954790 | |
113 | Sumoylation | VEALQNLKNLKSLDL HHHHHHHHCCCCCCC | 68.72 | - | |
113 | Ubiquitination | VEALQNLKNLKSLDL HHHHHHHHCCCCCCC | 68.72 | 21890473 | |
113 | Sumoylation | VEALQNLKNLKSLDL HHHHHHHHCCCCCCC | 68.72 | - | |
113 | Acetylation | VEALQNLKNLKSLDL HHHHHHHHCCCCCCC | 68.72 | 23954790 | |
116 | Ubiquitination | LQNLKNLKSLDLFNC HHHHHCCCCCCCCCC | 59.37 | 21906983 | |
117 | Phosphorylation | QNLKNLKSLDLFNCE HHHHCCCCCCCCCCE | 30.22 | 21712546 | |
219 | Phosphorylation | GEEEVGLSYLMKEEI CHHHHHHHHHHHHHH | 15.42 | 26074081 | |
220 | Phosphorylation | EEEVGLSYLMKEEIQ HHHHHHHHHHHHHHC | 18.83 | 26074081 | |
223 | Sumoylation | VGLSYLMKEEIQDEE HHHHHHHHHHHCCCC | 49.99 | - | |
235 | Phosphorylation | DEEDDDDYVEEGEEE CCCCCCCCHHCCHHH | 19.43 | 28674151 | |
254 | Ubiquitination | EGGLRGEKRKRDAED HCCCCCHHHCCCCCC | 67.07 | 2190698 | |
254 | Acetylation | EGGLRGEKRKRDAED HCCCCCHHHCCCCCC | 67.07 | 26051181 | |
256 | Sumoylation | GLRGEKRKRDAEDDG CCCCHHHCCCCCCCC | 66.74 | - | |
256 | Sumoylation | GLRGEKRKRDAEDDG CCCCHHHCCCCCCCC | 66.74 | - |
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 AN32E_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AN32E_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 AN32E_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RS2_HUMAN | RPS2 | physical | 22939629 | |
SNX2_HUMAN | SNX2 | physical | 22863883 | |
SNX6_HUMAN | SNX6 | physical | 22863883 | |
SAHH2_HUMAN | AHCYL1 | physical | 26344197 | |
SAHH3_HUMAN | AHCYL2 | physical | 26344197 | |
DMAP1_HUMAN | DMAP1 | physical | 26344197 | |
PAPP1_HUMAN | PAPPA | physical | 26344197 | |
VPS72_HUMAN | VPS72 | physical | 26344197 |
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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Phosphorylation | |
Reference | PubMed |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-235, AND MASSSPECTROMETRY. |