ENDD1_HUMAN - dbPTM
ENDD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENDD1_HUMAN
UniProt AC O94919
Protein Name Endonuclease domain-containing 1 protein
Gene Name ENDOD1
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Secreted .
Protein Description May act as a DNase and a RNase..
Protein Sequence MGTARWLALGSLFALAGLLEGRLVGEEEAGFGECDKFFYAGTPPAGLAADSHVKICQRAEGAERFATLYSTRDRIPVYSAFRAPRPAPGGAEQRWLVEPQIDDPNSNLEEAINEAEAITSVNSLGSKQALNTDYLDSDYQRGQLYPFSLSSDVQVATFTLTNSAPMTQSFQERWYVNLHSLMDRALTPQCGSGEDLYILTGTVPSDYRVKDKVAVPEFVWLAACCAVPGGGWAMGFVKHTRDSDIIEDVMVKDLQKLLPFNPQLFQNNCGETEQDTEKMKKILEVVNQIQDEERMVQSQKSSSPLSSTRSKRSTLLPPEASEGSSSFLGKLMGFIATPFIKLFQLIYYLVVAILKNIVYFLWCVTKQVINGIESCLYRLGSATISYFMAIGEELVSIPWKVLKVVAKVIRALLRILCCLLKAICRVLSIPVRVLVDVATFPVYTMGAIPIVCKDIALGLGGTVSLLFDTAFGTLGGLFQVVFSVCKRIGYKVTFDNSGEL
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
137PhosphorylationLNTDYLDSDYQRGQL
CCCCCCCCCCCCCCC
35.31-
207PhosphorylationTGTVPSDYRVKDKVA
ECCCCCCCCCCCCCC
22.95-
250SulfoxidationSDIIEDVMVKDLQKL
CCCCHHHHHHHHHHH
4.8521406390
300UbiquitinationERMVQSQKSSSPLSS
HHHHHCCCCCCCCCC
58.5121906983
301PhosphorylationRMVQSQKSSSPLSST
HHHHCCCCCCCCCCC
28.5426437602
301O-linked_GlycosylationRMVQSQKSSSPLSST
HHHHCCCCCCCCCCC
28.54OGP
302PhosphorylationMVQSQKSSSPLSSTR
HHHCCCCCCCCCCCC
42.9028857561
303PhosphorylationVQSQKSSSPLSSTRS
HHCCCCCCCCCCCCC
36.6328857561
306PhosphorylationQKSSSPLSSTRSKRS
CCCCCCCCCCCCCCC
32.8022817900
307PhosphorylationKSSSPLSSTRSKRST
CCCCCCCCCCCCCCC
35.2122817900
308PhosphorylationSSSPLSSTRSKRSTL
CCCCCCCCCCCCCCC
35.2726437602
310PhosphorylationSPLSSTRSKRSTLLP
CCCCCCCCCCCCCCC
32.2922817900
313PhosphorylationSSTRSKRSTLLPPEA
CCCCCCCCCCCCCCC
27.43-
314PhosphorylationSTRSKRSTLLPPEAS
CCCCCCCCCCCCCCC
36.03-
407AcetylationKVLKVVAKVIRALLR
HHHHHHHHHHHHHHH
26.9519608861
490PhosphorylationSVCKRIGYKVTFDNS
HHHHHHCCEEEECCC
10.4224719451

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 ENDD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENDD1_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 ENDD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STOM_HUMANSTOMphysical
27173435

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 ENDD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-407, AND MASS SPECTROMETRY.

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