PHAR1_HUMAN - dbPTM
PHAR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHAR1_HUMAN
UniProt AC Q9C0D0
Protein Name Phosphatase and actin regulator 1
Gene Name PHACTR1
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Cytoplasm. Cell junction, synapse. Nucleus. Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import (By similarity)..
Protein Description Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. Plays a role in cell motility. Plays a role in the formation of tubules by endothelial cells. Regulates PPP1CA activity. Required for normal cell survival..
Protein Sequence MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQARRATLLLPPTLMAASSEDDIDRRPIRRVRSKSDTPYLAEARISFNLGAAEEVERLAAMRSDSLVPGTHTPPIRRRSKFANLGRIFKPWKWRKKKSEKFKHTSAALERKISMRQSREELIKRGVLKEIYDKDGELSISNEEDSLENGQSLSSSQLSLPALSEMEPVPMPRDPCSYEVLQPSDIMDGPDPGAPVKLPCLPVKLSPPLPPKKVMICMPVGGPDLSLVSYTAQKSGQQGVAQHHHTVLPSQIQHQLQYGSHGQHLPSTTGSLPMHPSGCRMIDELNKTLAMTMQRLESSEQRVPCSTSYHSSGLHSGDGVTKAGPMGLPEIRQVPTVVIECDDNKENVPHESDYEDSSCLYTREEEEEEEDEDDDSSLYTSSLAMKVCRKDSLAIKLSNRPSKRELEEKNILPRQTDEERLELRQQIGTKLTRRLSQRPTAEELEQRNILKPRNEQEEQEEKREIKRRLTRKLSQRPTVEELRERKILIRFSDYVEVADAQDYDRRADKPWTRLTAADKAAIRKELNEFKSTEMEVHELSRHLTRFHRP
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
65PhosphorylationRPIRRVRSKSDTPYL
CCCHHCCCCCCCCCE
33.3827732954
67PhosphorylationIRRVRSKSDTPYLAE
CHHCCCCCCCCCEEE
48.2225307156
69PhosphorylationRVRSKSDTPYLAEAR
HCCCCCCCCCEEEEH
22.4127732954
78PhosphorylationYLAEARISFNLGAAE
CEEEEHHEECCCCHH
11.5227251275
95PhosphorylationERLAAMRSDSLVPGT
HHHHHHCCCCCCCCC
20.6128857561
97PhosphorylationLAAMRSDSLVPGTHT
HHHHCCCCCCCCCCC
32.2928857561
102PhosphorylationSDSLVPGTHTPPIRR
CCCCCCCCCCCCCCC
19.2628857561
104PhosphorylationSLVPGTHTPPIRRRS
CCCCCCCCCCCCCCH
30.5120886841
145PhosphorylationAALERKISMRQSREE
HHHHHHHHHHHCHHH
15.7924719451
149PhosphorylationRKISMRQSREELIKR
HHHHHHHCHHHHHHC
31.1521712546
237PhosphorylationPCLPVKLSPPLPPKK
CEEECCCCCCCCCCE
20.8222985185
467PhosphorylationTKLTRRLSQRPTAEE
HHHHHHHHCCCCHHH
23.4922777824
471PhosphorylationRRLSQRPTAEELEQR
HHHHCCCCHHHHHHC
49.2223186163
501PhosphorylationREIKRRLTRKLSQRP
HHHHHHHHHHHHCCC
24.77-
505PhosphorylationRRLTRKLSQRPTVEE
HHHHHHHHCCCCHHH
27.4623401153
509PhosphorylationRKLSQRPTVEELRER
HHHHCCCCHHHHHHC
42.6229255136
525PhosphorylationILIRFSDYVEVADAQ
EEEECHHCEEECCHH
9.4130257219
562PhosphorylationKELNEFKSTEMEVHE
HHHHHHHCCHHHHHH
34.6129083192
563PhosphorylationELNEFKSTEMEVHEL
HHHHHHCCHHHHHHH
39.6829083192
571PhosphorylationEMEVHELSRHLTRFH
HHHHHHHHHHHHHHC
18.0529083192

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 PHAR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHAR1_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 PHAR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTS_HUMANACTA1physical
15107502
PP1A_HUMANPPP1CAphysical
15107502

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 PHAR1_HUMAN

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Related Literatures of Post-Translational Modification

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