PRUN1_HUMAN - dbPTM
PRUN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRUN1_HUMAN
UniProt AC Q86TP1
Protein Name Exopolyphosphatase PRUNE1
Gene Name PRUNE1 {ECO:0000312|HGNC:HGNC:13420}
Organism Homo sapiens (Human).
Sequence Length 453
Subcellular Localization Cytoplasm. Nucleus. Cell junction, focal adhesion. In some transfected cells a nuclear staining is also observed.
Protein Description Phosphodiesterase (PDE) that has higher activity toward cAMP than cGMP, as substrate. Plays a role in cell proliferation, migration and differentiation, and acts as a negative regulator of NME1. Plays a role in the regulation of neurogenesis. [PubMed: 28334956 Involved in the regulation of microtubule polymerization]
Protein Sequence MEDYLQGCRAALQESRPLHVVLGNEACDLDSTVSALALAFYLAKTTEAEEVFVPVLNIKRSELPLRGDIVFFLQKVHIPESILIFRDEIDLHALYQAGQLTLILVDHHILSKSDTALEEAVAEVLDHRPIEPKHCPPCHVSVELVGSCATLVTERILQGAPEILDRQTAALLHGTIILDCVNMDLKIGKATPKDSKYVEKLEALFPDLPKRNDIFDSLQKAKFDVSGLTTEQMLRKDQKTIYRQGVKVAISAIYMDLEAFLQRSNLLADLHAFCQAHSYDVLVAMTIFFNTHNEPVRQLAIFCPHVALQTTICEVLERSHSPPLKLTPASSTHPNLHAYLQGNTQVSRKKLLPLLQEALSAYFDSMKIPSGQPETADVSREQVDKELDRASNSLISGLSQDEEDPPLPPTPMNSLVDECPLDQGLPKLSAEAVFEKCSQISLSQSTTASLSKK
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-------MEDYLQGC
-------CHHHHHHH
22814378
18UbiquitinationALQESRPLHVVLGNE
HHHHCCCCEEEECCC
29967540
28UbiquitinationVLGNEACDLDSTVSA
EECCCCCCCHHHHHH
29967540
40UbiquitinationVSALALAFYLAKTTE
HHHHHHHHHHHCCCC
29967540
200UbiquitinationKDSKYVEKLEALFPD
CCCHHHHHHHHHCCC
29967540
210UbiquitinationALFPDLPKRNDIFDS
HHCCCCCCCCCHHHH
29967540
220UbiquitinationDIFDSLQKAKFDVSG
CHHHHHHHHCCCCCC
-
222UbiquitinationFDSLQKAKFDVSGLT
HHHHHHHCCCCCCCC
29967540
226PhosphorylationQKAKFDVSGLTTEQM
HHHCCCCCCCCHHHH
27174698
229PhosphorylationKFDVSGLTTEQMLRK
CCCCCCCCHHHHHHH
27174698
230PhosphorylationFDVSGLTTEQMLRKD
CCCCCCCHHHHHHHC
27174698
319PhosphorylationICEVLERSHSPPLKL
HHHHHHHCCCCCCCC
29396449
321PhosphorylationEVLERSHSPPLKLTP
HHHHHCCCCCCCCCC
25849741
331PhosphorylationLKLTPASSTHPNLHA
CCCCCCCCCCCCHHH
-
332PhosphorylationKLTPASSTHPNLHAY
CCCCCCCCCCCHHHH
-
360PhosphorylationPLLQEALSAYFDSMK
HHHHHHHHHHHHHCC
29083192
362PhosphorylationLQEALSAYFDSMKIP
HHHHHHHHHHHCCCC
29083192
365PhosphorylationALSAYFDSMKIPSGQ
HHHHHHHHCCCCCCC
29083192
379PhosphorylationQPETADVSREQVDKE
CCCCCCCCHHHHHHH
28555341
391PhosphorylationDKELDRASNSLISGL
HHHHHHHHHHHHHCC
28060719
393PhosphorylationELDRASNSLISGLSQ
HHHHHHHHHHHCCCC
28060719
396PhosphorylationRASNSLISGLSQDEE
HHHHHHHHCCCCCCC
28060719
399PhosphorylationNSLISGLSQDEEDPP
HHHHHCCCCCCCCCC
28102081
410PhosphorylationEDPPLPPTPMNSLVD
CCCCCCCCCCHHHCC
28060719
414PhosphorylationLPPTPMNSLVDECPL
CCCCCCHHHCCCCCC
28060719

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 PRUN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRUN1_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 PRUN1_HUMAN !!

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

Oops, there are no PPI records of PRUN1_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRUN1_HUMAN

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Related Literatures of Post-Translational Modification

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