AN32E_RAT - dbPTM
AN32E_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AN32E_RAT
UniProt AC Q5XIE0
Protein Name Acidic leucine-rich nuclear phosphoprotein 32 family member E
Gene Name Anp32e
Organism Rattus norvegicus (Rat).
Sequence Length 258
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. Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis (By similarity)..
Protein Sequence MEMKKKINMELKNRAPEEVTELVLDNCLCVNGEIEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQITYLDGFDQEDNEAPDSEEEEEDEDGDEDEEDEEEDEAGPPEGYEDEDEDEDEAGSEVGEGEEEVGLSYLMKEEIQDEEDDDDYVDEGEEEEEEEEEGPRGEKRKRDAEDDGEEDDD
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
11.65-
4Acetylation----MEMKKKINMEL
----CCCHHHHCHHH
37.2922902405
5Acetylation---MEMKKKINMELK
---CCCHHHHCHHHH
58.5422902405
6Acetylation--MEMKKKINMELKN
--CCCHHHHCHHHHH
33.5222902405
62PhosphorylationSSLARLPSLNKLRKL
HHHCCCCCHHHHHCC
49.5222673903
65AcetylationARLPSLNKLRKLELS
CCCCCHHHHHCCCCC
55.7722902405
91PhosphorylationAEKCPNLTYLNLSGN
HHHCCCCEEEECCCC
32.3823984901
92PhosphorylationEKCPNLTYLNLSGNK
HHCCCCEEEECCCCC
9.2123984901
96PhosphorylationNLTYLNLSGNKIKDL
CCEEEECCCCCCCCC
38.9723984901
104PhosphorylationGNKIKDLSTVEALQN
CCCCCCCHHHHHHHH
40.3123984901
105PhosphorylationNKIKDLSTVEALQNL
CCCCCCHHHHHHHHH
29.6623984901
113AcetylationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.7222902405
113UbiquitinationVEALQNLKNLKSLDL
HHHHHHHHCCCCCCC
68.72-
225PhosphorylationDEEDDDDYVDEGEEE
CCCCCCCCCCCCHHH
19.4522276854

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AN32E_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AN32E_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AN32E_RAT

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Related Literatures of Post-Translational Modification

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