PHAR3_HUMAN - dbPTM
PHAR3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHAR3_HUMAN
UniProt AC Q96KR7
Protein Name Phosphatase and actin regulator 3
Gene Name PHACTR3
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization Nucleus matrix. Localized to the nuclear matrix-intermediate filament scaffold. Isoform 2 is also found in some cytoplasmic extensions.
Protein Description
Protein Sequence MAASEDGSGCLVSRGRSQSDPSVLTDSSATSSADAGENPDEMDQTPPARPEYLVSGIRTPPVRRNSKLATLGRIFKPWKWRKKKNEKLKQTTSALEKKMAGRQGREELIKKGLLEMMEQDAESKTCNPDGGPRSVQSEPPTPKSETLTSEDAQPGSPLATGTDQVSLDKPLSSAAHLDDAAKMPSASSGEEADAGSLLPTTNELSQALAGADSLDSPPRPLERSVGQLPSPPLLPTPPPKASSKTTKNVTGQATLFQASSMKSADPSLRGQLSTPTGSPHLTTVHRPLPPSRVIEELHRALATKHRQDSFQGRESKGSPKKRLDVRLSRTSSVERGKEREEAWSFDGALENKRTAAKESEENKENLIINSELKDDLLLYQDEEALNDSIISGTLPRKCKKELLAVKLRNRPSKQELEDRNIFPRRTDEERQEIRQQIEMKLSKRLSQRPAVEELERRNILKQRNDQTEQEERREIKQRLTRKLNQRPTVDELRDRKILIRFSDYVEVAKAQDYDRRADKPWTRLSAADKAAIRKELNEYKSNEMEVHASSKHLTRFHRP
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
19PhosphorylationVSRGRSQSDPSVLTD
EECCCCCCCCCCCCC		53.3824076635
45PhosphorylationNPDEMDQTPPARPEY
CHHHCCCCCCCCCHH		27.2925072903
52PhosphorylationTPPARPEYLVSGIRT
CCCCCCHHHHCCCCC		18.3225072903
55PhosphorylationARPEYLVSGIRTPPV
CCCHHHHCCCCCCCC		26.3825072903
66PhosphorylationTPPVRRNSKLATLGR
CCCCCCCCHHHHHHH		27.51-
70PhosphorylationRRNSKLATLGRIFKP
CCCCHHHHHHHHHCC		39.9317693683
93PhosphorylationEKLKQTTSALEKKMA
HHHHHHHHHHHHHHC		33.9521964256
123PhosphorylationMMEQDAESKTCNPDG
HHHHHHHHCCCCCCC		34.6820201521
144PhosphorylationSEPPTPKSETLTSED
CCCCCCCCCCCCCCC		36.7028450419
146PhosphorylationPPTPKSETLTSEDAQ
CCCCCCCCCCCCCCC		42.2928450419
148PhosphorylationTPKSETLTSEDAQPG
CCCCCCCCCCCCCCC		37.1728450419
149PhosphorylationPKSETLTSEDAQPGS
CCCCCCCCCCCCCCC		36.2728450419
156PhosphorylationSEDAQPGSPLATGTD
CCCCCCCCCCCCCCC		24.3528450419
160PhosphorylationQPGSPLATGTDQVSL
CCCCCCCCCCCCCCC		48.5828450419
162PhosphorylationGSPLATGTDQVSLDK
CCCCCCCCCCCCCCC		20.9228450419
166PhosphorylationATGTDQVSLDKPLSS
CCCCCCCCCCCCCCC		25.8028450419
172PhosphorylationVSLDKPLSSAAHLDD
CCCCCCCCCCCCHHH		26.8528450419
173PhosphorylationSLDKPLSSAAHLDDA
CCCCCCCCCCCHHHH		36.8428450419
216PhosphorylationAGADSLDSPPRPLER
HCCCCCCCCCCCCCC		41.9424076635
224PhosphorylationPPRPLERSVGQLPSP
CCCCCCCCCCCCCCC		22.6328450419
230PhosphorylationRSVGQLPSPPLLPTP
CCCCCCCCCCCCCCC		47.9828450419
236PhosphorylationPSPPLLPTPPPKASS
CCCCCCCCCCCCCCC		48.6927732954
245PhosphorylationPPKASSKTTKNVTGQ
CCCCCCCCCCCCCCC		44.97-
250PhosphorylationSKTTKNVTGQATLFQ
CCCCCCCCCCEEEEE		32.7322210691
254PhosphorylationKNVTGQATLFQASSM
CCCCCCEEEEEHHHC		21.8824719451
259PhosphorylationQATLFQASSMKSADP
CEEEEEHHHCCCCCH		21.8522210691
273PhosphorylationPSLRGQLSTPTGSPH
HHHCCCCCCCCCCCC		25.1824117733
274PhosphorylationSLRGQLSTPTGSPHL
HHCCCCCCCCCCCCE		33.2024117733
276PhosphorylationRGQLSTPTGSPHLTT
CCCCCCCCCCCCEEE		50.8324117733
278PhosphorylationQLSTPTGSPHLTTVH
CCCCCCCCCCEEEEC		16.1824117733
282PhosphorylationPTGSPHLTTVHRPLP
CCCCCCEEEECCCCC		24.6024117733
283PhosphorylationTGSPHLTTVHRPLPP
CCCCCEEEECCCCCH		22.2224117733
291PhosphorylationVHRPLPPSRVIEELH
ECCCCCHHHHHHHHH		36.9224117733
303PhosphorylationELHRALATKHRQDSF
HHHHHHHHHHCHHCC		28.3829759185
309PhosphorylationATKHRQDSFQGRESK
HHHHCHHCCCCCCCC		15.9029449344
315PhosphorylationDSFQGRESKGSPKKR
HCCCCCCCCCCCCHH		40.7429449344
318PhosphorylationQGRESKGSPKKRLDV
CCCCCCCCCCHHHHH		36.9621487013
328PhosphorylationKRLDVRLSRTSSVER
HHHHHHHCCCCCCHH		23.9729449344
391PhosphorylationALNDSIISGTLPRKC
HHHHCCCCCCCCHHH		24.85-
393PhosphorylationNDSIISGTLPRKCKK
HHCCCCCCCCHHHCH		27.14-
488PhosphorylationRKLNQRPTVDELRDR
HHHHCCCCHHHHHCC		42.66-
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
318SPhosphorylationKinaseCDK5Q00535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHAR3_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 PHAR3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP1A_HUMANPPP1CAphysical
12925532
EF1G_HUMANEEF1Gphysical
16169070
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 PHAR3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND MASSSPECTROMETRY.

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