ANR39_HUMAN - dbPTM
ANR39_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANR39_HUMAN
UniProt AC Q53RE8
Protein Name Ankyrin repeat domain-containing protein 39
Gene Name ANKRD39
Organism Homo sapiens (Human).
Sequence Length 183
Subcellular Localization
Protein Description
Protein Sequence MATPRPCADGPCCSHPSAVLGVQQTLEEMDFERGIWSAALNGDLGRVKHLIQKAEDPSQPDSAGYTALHYASRNGHYAVCQFLLESGAKCDAQTHGGATALHRASYCGHTEIARLLLSHGSNPRVVDDDGMTSLHKAAERGHGDICSLLLQHSPALKAIRDRKARLACDLLPCNSDLRDLLSS
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
48UbiquitinationNGDLGRVKHLIQKAE
CCCHHHHHHHHHHCC
31.1929967540
53UbiquitinationRVKHLIQKAEDPSQP
HHHHHHHHCCCCCCC
46.9132015554
62PhosphorylationEDPSQPDSAGYTALH
CCCCCCCCCCHHHHH
30.2128152594
65PhosphorylationSQPDSAGYTALHYAS
CCCCCCCHHHHHHHH
6.6424927040
66PhosphorylationQPDSAGYTALHYASR
CCCCCCHHHHHHHHH
23.0930835493
70PhosphorylationAGYTALHYASRNGHY
CCHHHHHHHHHCCCH
13.7124927040
72PhosphorylationYTALHYASRNGHYAV
HHHHHHHHHCCCHHH
21.0728152594
105PhosphorylationATALHRASYCGHTEI
CHHHHCHHHCCHHHH
22.4028857561
106PhosphorylationTALHRASYCGHTEIA
HHHHCHHHCCHHHHH
11.0622817900
121PhosphorylationRLLLSHGSNPRVVDD
HHHHHCCCCCEEECC
37.9368740257
136UbiquitinationDGMTSLHKAAERGHG
CCCCHHHHHHHCCCH
55.3621906983
147PhosphorylationRGHGDICSLLLQHSP
CCCHHHHHHHHHCCH
23.5329214152
153PhosphorylationCSLLLQHSPALKAIR
HHHHHHCCHHHHHHH
10.0225159151
157UbiquitinationLQHSPALKAIRDRKA
HHCCHHHHHHHHHHH
43.82-

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 ANR39_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANR39_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 ANR39_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

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 ANR39_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65, AND MASSSPECTROMETRY.

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