AN32E_HUMAN - dbPTM
AN32E_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MEMKKKIN
-------CCCHHHHC
11.6522814378
5Ubiquitination---MEMKKKINLELR
---CCCHHHHCHHHC
58.54-
6Sumoylation--MEMKKKINLELRN
--CCCHHHHCHHHCC
31.17-
6Ubiquitination--MEMKKKINLELRN
--CCCHHHHCHHHCC
31.17-
6Sumoylation--MEMKKKINLELRN
--CCCHHHHCHHHCC
31.17-
62-Hydroxyisobutyrylation--MEMKKKINLELRN
--CCCHHHHCHHHCC
31.17-
12MethylationKKINLELRNRSPEEV
HHHCHHHCCCCHHHH
27.43115481755
15PhosphorylationNLELRNRSPEEVTEL
CHHHCCCCHHHHHHH
39.9722468782
17UbiquitinationELRNRSPEEVTELVL
HHCCCCHHHHHHHHH
67.3621890473
53UbiquitinationFLSMANVELSSLARL
HHHHHCCCHHHHCCC
42.6221890473
56PhosphorylationMANVELSSLARLPSL
HHCCCHHHHCCCCCH
38.3830387612
62PhosphorylationSSLARLPSLNKLRKL
HHHCCCCCHHHHHCC
49.5228464451
65AcetylationARLPSLNKLRKLELS
CCCCCHHHHHCCCCC
55.7725953088
65UbiquitinationARLPSLNKLRKLELS
CCCCCHHHHHCCCCC
55.7721890473
65UbiquitinationARLPSLNKLRKLELS
CCCCCHHHHHCCCCC
55.7721890473
652-HydroxyisobutyrylationARLPSLNKLRKLELS
CCCCCHHHHHCCCCC
55.77-
68SumoylationPSLNKLRKLELSDNI
CCHHHHHCCCCCCCC
57.6728112733
68UbiquitinationPSLNKLRKLELSDNI
CCHHHHHCCCCCCCC
57.6721890473
68SumoylationPSLNKLRKLELSDNI
CCHHHHHCCCCCCCC
57.67-
682-HydroxyisobutyrylationPSLNKLRKLELSDNI
CCHHHHHCCCCCCCC
57.67-
77PhosphorylationELSDNIISGGLEVLA
CCCCCCHHHHHHHHH
24.0228348404
86UbiquitinationGLEVLAEKCPNLTYL
HHHHHHHHCCCCEEE
49.76-
91PhosphorylationAEKCPNLTYLNLSGN
HHHCCCCEEEECCCC
32.3828152594
92PhosphorylationEKCPNLTYLNLSGNK
HHCCCCEEEECCCCC
9.2128152594
96PhosphorylationNLTYLNLSGNKIKDL
CCEEEECCCCCCCCC
38.9728152594
99UbiquitinationYLNLSGNKIKDLSTV
EEECCCCCCCCCHHH
55.4421906983
99SumoylationYLNLSGNKIKDLSTV
EEECCCCCCCCCHHH
55.44-
99AcetylationYLNLSGNKIKDLSTV
EEECCCCCCCCCHHH
55.4425953088
99SumoylationYLNLSGNKIKDLSTV
EEECCCCCCCCCHHH
55.44-
1012-HydroxyisobutyrylationNLSGNKIKDLSTVEA
ECCCCCCCCCHHHHH
54.98-
101SumoylationNLSGNKIKDLSTVEA
ECCCCCCCCCHHHHH
54.98-
101UbiquitinationNLSGNKIKDLSTVEA
ECCCCCCCCCHHHHH
54.9821890473
101SumoylationNLSGNKIKDLSTVEA
ECCCCCCCCCHHHHH
54.98-
104PhosphorylationGNKIKDLSTVEALQN
CCCCCCCHHHHHHHH
40.3125159151
105PhosphorylationNKIKDLSTVEALQNL
CCCCCCHHHHHHHHH
29.6621712546
1132-HydroxyisobutyrylationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.72-
113SuccinylationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.7223954790
113SumoylationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.72-
113UbiquitinationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.7221890473
113SumoylationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.72-
113AcetylationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.7223954790
116UbiquitinationLQNLKNLKSLDLFNC
HHHHHCCCCCCCCCC
59.3721906983
117PhosphorylationQNLKNLKSLDLFNCE
HHHHCCCCCCCCCCE
30.2221712546
219PhosphorylationGEEEVGLSYLMKEEI
CHHHHHHHHHHHHHH
15.4226074081
220PhosphorylationEEEVGLSYLMKEEIQ
HHHHHHHHHHHHHHC
18.8326074081
223SumoylationVGLSYLMKEEIQDEE
HHHHHHHHHHHCCCC
49.99-
235PhosphorylationDEEDDDDYVEEGEEE
CCCCCCCCHHCCHHH
19.4328674151
254UbiquitinationEGGLRGEKRKRDAED
HCCCCCHHHCCCCCC
67.072190698
254AcetylationEGGLRGEKRKRDAED
HCCCCCHHHCCCCCC
67.0726051181
256SumoylationGLRGEKRKRDAEDDG
CCCCHHHCCCCCCCC
66.74-
256SumoylationGLRGEKRKRDAEDDG
CCCCHHHCCCCCCCC
66.74-

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 AN32E_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AN32E_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 AN32E_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS2_HUMANRPS2physical
22939629
SNX2_HUMANSNX2physical
22863883
SNX6_HUMANSNX6physical
22863883
SAHH2_HUMANAHCYL1physical
26344197
SAHH3_HUMANAHCYL2physical
26344197
DMAP1_HUMANDMAP1physical
26344197
PAPP1_HUMANPAPPAphysical
26344197
VPS72_HUMANVPS72physical
26344197

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 AN32E_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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