AEN_HUMAN - dbPTM
AEN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AEN_HUMAN
UniProt AC Q8WTP8
Protein Name Apoptosis-enhancing nuclease
Gene Name AEN
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization Nucleus. Nucleus, nucleolus. Localized predomintly in the nucleolus. Translocates from the nucleolus to the nucleoplasm upon apoptosis induction.
Protein Description Exonuclease with activity against single- and double-stranded DNA and RNA. Mediates p53-induced apoptosis. When induced by p53 following DNA damage, digests double-stranded DNA to form single-stranded DNA and amplifies DNA damage signals, leading to enhancement of apoptosis..
Protein Sequence MVPREAPESAQCLCPSLTIPNAKDVLRKRHKRRSRQHQRFMARKALLQEQGLLSMPPEPGSSPLPTPFGAATATEAASSGKQCLRAGSGSAPCSRRPAPGKASGPLPSKCVAIDCEMVGTGPRGRVSELARCSIVSYHGNVLYDKYIRPEMPIADYRTRWSGITRQHMRKAVPFQVAQKEILKLLKGKVVVGHALHNDFQALKYVHPRSQTRDTTYVPNFLSEPGLHTRARVSLKDLALQLLHKKIQVGQHGHSSVEDATTAMELYRLVEVQWEQQEARSLWTCPEDREPDSSTDMEQYMEDQYWPDDLAHGSRGGAREAQDRRN
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
101 (in isoform 1)Ubiquitination-38.0221906983
101 (in isoform 2)Ubiquitination-38.0221906983
101UbiquitinationSRRPAPGKASGPLPS
CCCCCCCCCCCCCCC
38.0221906983
108PhosphorylationKASGPLPSKCVAIDC
CCCCCCCCCEEEEEC
46.5024719451
109 (in isoform 2)Ubiquitination-30.68-
109UbiquitinationASGPLPSKCVAIDCE
CCCCCCCCEEEEECE
30.68-
120PhosphorylationIDCEMVGTGPRGRVS
EECEEECCCCCCCHH
32.3850563817
136PhosphorylationLARCSIVSYHGNVLY
HHCCEEEEEECCEEE
15.1128450419
137PhosphorylationARCSIVSYHGNVLYD
HCCEEEEEECCEEEE
11.6728450419
143PhosphorylationSYHGNVLYDKYIRPE
EEECCEEEECCCCCC
13.2028450419
164PhosphorylationRTRWSGITRQHMRKA
CCCCCCCCHHHHHHH
28.0029449344
170UbiquitinationITRQHMRKAVPFQVA
CCHHHHHHHCCHHHH
46.2729967540
204PhosphorylationNDFQALKYVHPRSQT
CHHHHHHHCCCCCCC
12.5822210691
209PhosphorylationLKYVHPRSQTRDTTY
HHHCCCCCCCCCCCC
40.1122210691
214PhosphorylationPRSQTRDTTYVPNFL
CCCCCCCCCCCCCCC
19.4122210691
215PhosphorylationRSQTRDTTYVPNFLS
CCCCCCCCCCCCCCC
27.1522210691
235UbiquitinationTRARVSLKDLALQLL
CCHHCCHHHHHHHHH
43.0922817900
235 (in isoform 1)Ubiquitination-43.0921906983
235 (in isoform 2)Ubiquitination-43.0921906983
245UbiquitinationALQLLHKKIQVGQHG
HHHHHHHHCCCCCCC
27.8529967540
280PhosphorylationWEQQEARSLWTCPED
HHHHHHHHHCCCCCC
34.9946159971
283PhosphorylationQEARSLWTCPEDREP
HHHHHHCCCCCCCCC
24.3946159977

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 AEN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AEN_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 AEN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNPTA_HUMANGNPTABphysical
25416956
LZTS2_HUMANLZTS2physical
25416956
TRI41_HUMANTRIM41physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
K1C40_HUMANKRT40physical
25416956
RALYL_HUMANRALYLphysical
25416956
RBY1F_HUMANRBMY1Fphysical
25416956
KHDR2_HUMANKHDRBS2physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
AAMP_HUMANAAMPphysical
26186194
PKN1_HUMANPKN1physical
28514442
PPID_HUMANPPIDphysical
28514442
CRIP2_HUMANCRIP2physical
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 AEN_HUMAN

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Related Literatures of Post-Translational Modification

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