PHLP1_HUMAN - dbPTM
PHLP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHLP1_HUMAN
UniProt AC O60346
Protein Name PH domain leucine-rich repeat-containing protein phosphatase 1
Gene Name PHLPP1
Organism Homo sapiens (Human).
Sequence Length 1717
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Nucleus. In colorectal cancer tissue, expression is concentrated at the lateral membrane of epithelial cells.
Isoform 2: Cell membrane .
Protein Description Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA. [PubMed: 15808505]
Protein Sequence MEPAAAATVQRLPELGREDRASAPAAAAAAAAAAAAAAAALAAAAGGGRSPEPALTPAAPSGGNGSGSGAREEAPGEAPPGPLPGRAGGAGRRRRRGAPQPIAGGAAPVPGAGGGANSLLLRRGRLKRNLSAAAAAASSSSSSSAAAASHSPGAAGLPASCSASASLCTRSLDRKTLLLKHRQTLQLQPSDRDWVRHQLQRGCVHVFDRHMASTYLRPVLCTLDTTAGEVAARLLQLGHKGGGVVKVLGQGPGAAAAREPAEPPPEAGPRLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGSCEEKAAAAVAPGGLQSTPGRSGVTAEKAPPPPPPPTLYVQLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKPHSTGSSERIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSLTGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVASQRISSVDLSCCSLEHLPANLFYSQDLTHLNLKQNFLRQNPSLPAARGLNELQRFTKLKSLNLSNNHLGDFPLAVCSIPTLAELNVSCNALRSVPAAVGVMHNLQTFLLDGNFLQSLPAELENMKQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMSGNCVETLRLQALRKMPHIKHVDLRLNVIRKLIADEVDFLQHVTQLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTLDICGYFLKALYASSNELVQLDVYPVPNYLSYMDVSRNRLENVPEWVCESRKLEVLDIGHNQICELPARLFCNSSLRKLLAGHNQLARLPERLERTSVEVLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNSILQELYLTNNSLTDKCVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVMQLPEIKCVDLSCNELSEVTLPENLPPKLQELDLTGNPRLVLDHKTLELLNNIRCFKIDQPSTGDASGAPAVWSHGYTEASGVKNKLCVAALSVNNFCDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNEEEYMVNTFIVMQRKLGTAGQKLGGAAVLCHIKHDPVDPGGSFTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQHKAIITEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNVPDALAAAKKLCTLAQSYGCHDSISAVVVQLSVTEDSFCCCELSAGGAVPPPSPGIFPPSVNMVIKDRPSDGLGVPSSSSGMASEISSELSTSEMSSEVGSTASDEPPPGALSENSPAYPSEQRCMLHPICLSNSFQRQLSSATFSSAFSDNGLDSDDEEPIEGVFTNGSRVEVEVDIHCSRAKEKEKQQHLLQVPAEASDEGIVISANEDEPGLPRKADFSAVGTIGRRRANGSVAPQERSHNVIEVATDAPLRKPGGYFAAPAQPDPDDQFIIPPELEEEVKEIMKHHQEQQQQQQPPPPPQLQPQLPRHYQLDQLPDYYDTPL
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-------MEPAAAAT
-------CCHHHHHH
53.6322814378
50PhosphorylationAAAGGGRSPEPALTP
HHHCCCCCCCCCCCC
36.5728348404
56PhosphorylationRSPEPALTPAAPSGG
CCCCCCCCCCCCCCC
17.0028348404
118PhosphorylationGAGGGANSLLLRRGR
CCCCCHHHHHHHCCH
21.6225850435
131PhosphorylationGRLKRNLSAAAAAAS
CHHHHHHHHHHHHHH
21.2928450419
138PhosphorylationSAAAAAASSSSSSSA
HHHHHHHHCCCHHHH
26.4827080861
139PhosphorylationAAAAAASSSSSSSAA
HHHHHHHCCCHHHHH
29.5229970186
140PhosphorylationAAAAASSSSSSSAAA
HHHHHHCCCHHHHHH
31.5729970186
141PhosphorylationAAAASSSSSSSAAAA
HHHHHCCCHHHHHHH
35.8729970186
142PhosphorylationAAASSSSSSSAAAAS
HHHHCCCHHHHHHHH
30.2029970186
143PhosphorylationAASSSSSSSAAAASH
HHHCCCHHHHHHHHC
26.4125627689
144PhosphorylationASSSSSSSAAAASHS
HHCCCHHHHHHHHCC
24.71-
149PhosphorylationSSSAAAASHSPGAAG
HHHHHHHHCCCCCCC
21.5525627689
151PhosphorylationSAAAASHSPGAAGLP
HHHHHHCCCCCCCCC
23.6425627689
169PhosphorylationSASASLCTRSLDRKT
CCCHHHHHCCCCCCH
28.69-
171PhosphorylationSASLCTRSLDRKTLL
CHHHHHCCCCCCHHH
19.2330576142
176PhosphorylationTRSLDRKTLLLKHRQ
HCCCCCCHHHHHCCC
24.4330576142
184PhosphorylationLLLKHRQTLQLQPSD
HHHHCCCCCCCCCCC
19.2121406692
190PhosphorylationQTLQLQPSDRDWVRH
CCCCCCCCCHHHHHH
32.1121406692
222O-linked_GlycosylationYLRPVLCTLDTTAGE
HHHCEEEECCCCHHH
24.41OGP
240UbiquitinationRLLQLGHKGGGVVKV
HHHHCCCCCCCEEEE
58.4130230243
246UbiquitinationHKGGGVVKVLGQGPG
CCCCCEEEECCCCCC
29.3621890473
279PhosphorylationAPPEPRDSEVPPARS
CCCCCCCCCCCCCCC
41.60-
313PhosphorylationVGGPGGWSRRASPAP
CCCCCCCCCCCCCCC
18.3724719451
317PhosphorylationGGWSRRASPAPSDSS
CCCCCCCCCCCCCCC
21.5629255136
321PhosphorylationRRASPAPSDSSPGEP
CCCCCCCCCCCCCCC
52.8321815630
323PhosphorylationASPAPSDSSPGEPFV
CCCCCCCCCCCCCCC
42.6529255136
324PhosphorylationSPAPSDSSPGEPFVG
CCCCCCCCCCCCCCC
41.7529255136
335PhosphorylationPFVGGPVSSPRAPRP
CCCCCCCCCCCCCCC
37.4529255136
336PhosphorylationFVGGPVSSPRAPRPV
CCCCCCCCCCCCCCC
20.7429255136
409PhosphorylationQPLPLPQTASSPQPQ
CCCCCCCCCCCCCCC
26.9423663014
411PhosphorylationLPLPQTASSPQPQQK
CCCCCCCCCCCCCCC
46.0325159151
412PhosphorylationPLPQTASSPQPQQKA
CCCCCCCCCCCCCCC
25.7025159151
425PhosphorylationKAPRAIDSPGGAVRE
CCCCCCCCCCCCCCC
21.2330266825
434PhosphorylationGGAVREGSCEEKAAA
CCCCCCCCHHHHHHH
17.3822210691
450PhosphorylationVAPGGLQSTPGRSGV
HCCCCCCCCCCCCCC
41.4325159151
451PhosphorylationAPGGLQSTPGRSGVT
CCCCCCCCCCCCCCC
19.4621815630
524PhosphorylationIGCLIRFYAGKPHST
HHEEEEEECCCCCCC
12.4722210691
534PhosphorylationKPHSTGSSERIQLSG
CCCCCCCCCCEEECC
32.0422210691
691PhosphorylationLNELQRFTKLKSLNL
HHHHHHHHHCHHCCC
37.3422210691
797O-linked_GlycosylationMSGNCVETLRLQALR
HCCCHHHHHHHHHHH
9.2230379171
1071UbiquitinationEIDLSGNKLKAIPTT
EECCCCCCCCCCCHH
55.6929967540
1077PhosphorylationNKLKAIPTTIMNCRR
CCCCCCCHHHHHHHH
23.8823403867
1078PhosphorylationKLKAIPTTIMNCRRM
CCCCCCHHHHHHHHC
16.9323403867
1146UbiquitinationPRLVLDHKTLELLNN
CEEEECHHHHHHHHC
55.2422817900
1147O-linked_GlycosylationRLVLDHKTLELLNNI
EEEECHHHHHHHHCC
23.2630379171
1206PhosphorylationCDNREALYGVFDGDR
CCCHHHHHCEECCCC
20.4927642862
1242PhosphorylationKTKNEEEYMVNTFIV
HCCCHHHHHHHHHHH
15.0527732954
1246PhosphorylationEEEYMVNTFIVMQRK
HHHHHHHHHHHHHHH
11.8827732954
1323UbiquitinationLKRIKQHKAIITEDG
HHHHHHCCEEECCCC
38.4929967540
1359PhosphorylationVPRPHVQSVLLTPQD
CCCCCCCEEEECCCC
17.4019797085
1363PhosphorylationHVQSVLLTPQDEFFI
CCCEEEECCCCEEEE
18.1019797085
1379PhosphorylationGSKGLWDSLSVEEAV
CCCCHHHCCCHHHHH
15.8019797085
1381PhosphorylationKGLWDSLSVEEAVEA
CCHHHCCCHHHHHHH
31.2819797085
1400UbiquitinationPDALAAAKKLCTLAQ
HHHHHHHHHHHHHHH
41.3629967540
1524PhosphorylationMLHPICLSNSFQRQL
CCCHHHHCHHHHHHH
26.4728450419
1526PhosphorylationHPICLSNSFQRQLSS
CHHHHCHHHHHHHHH
21.2728450419
1617PhosphorylationADFSAVGTIGRRRAN
CCCCCCCCCCCCCCC
17.4129255136
1651PhosphorylationPLRKPGGYFAAPAQP
CCCCCCCCCCCCCCC
8.9227642862
1704PhosphorylationQPQLPRHYQLDQLPD
CCCCCCCCCHHHCCC
16.4327642862
1712PhosphorylationQLDQLPDYYDTPL--
CHHHCCCCCCCCC--
10.9919060867
1713PhosphorylationLDQLPDYYDTPL---
HHHCCCCCCCCC---
22.2627642862

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
1359SPhosphorylationKinaseGSK3BP49841
PSP
1359SPhosphorylationKinaseCSNK1A1P48729
GPS
1363TPhosphorylationKinaseGSK3BP49841
PSP
1363TPhosphorylationKinaseCSNK1A1P48729
GPS
1379SPhosphorylationKinaseGSK3BP49841
PSP
1379SPhosphorylationKinaseCSNK1A1P48729
GPS
1381SPhosphorylationKinaseGSK3BP49841
PSP
1381SPhosphorylationKinaseCSNK1A1P48729
GPS
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:24658274

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHLP1_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 PHLP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBW1A_HUMANBTRCphysical
19797085
FKBP5_HUMANFKBP5physical
19615732
PPP5_HUMANPPP5Cphysical
19615732
UBP1_HUMANUSP1physical
19615732
NHRF2_HUMANSLC9A3R2physical
19615732
SGT1_HUMANSUGT1physical
19615732
PHLP2_HUMANPHLPP2physical
19615732
SCRIB_HUMANSCRIBphysical
19615732
WDR48_HUMANWDR48physical
19615732
RBM15_HUMANRBM15physical
19615732
UBP46_HUMANUSP46physical
19615732
SNX27_HUMANSNX27physical
19615732
WDR20_HUMANWDR20physical
19615732
UBP12_HUMANUSP12physical
19615732
AKT1_HUMANAKT1physical
20605778
UBP46_HUMANUSP46physical
22391563
UBP1_HUMANUSP1physical
22426999
SNX6_HUMANSNX6physical
22939629
BUD23_HUMANWBSCR22physical
22939629
AKT1_HUMANAKT1physical
15808505
UBP12_HUMANUSP12physical
25216524
WDR48_HUMANWDR48physical
25216524
WDR20_HUMANWDR20physical
25216524
NHRF1_HUMANSLC9A3R1physical
21804599
BAG2_HUMANBAG2physical
27880917
FKBP4_HUMANFKBP4physical
27880917
FKBP5_HUMANFKBP5physical
27880917
MCMBP_HUMANMCMBPphysical
27880917
NUDC3_HUMANNUDCD3physical
27880917
PHLP2_HUMANPHLPP2physical
27880917
2AAA_HUMANPPP2R1Aphysical
27880917
2ABA_HUMANPPP2R2Aphysical
27880917
RPAP3_HUMANRPAP3physical
27880917
NHRF2_HUMANSLC9A3R2physical
27880917
SGT1_HUMANSUGT1physical
27880917
UBP1_HUMANUSP1physical
27880917
UBP12_HUMANUSP12physical
27880917
UBP46_HUMANUSP46physical
27880917
WDR20_HUMANWDR20physical
27880917
WDR48_HUMANWDR48physical
27880917
AIP_HUMANAIPphysical
27880917
CBPC1_HUMANAGTPBP1physical
27880917
NUDC_HUMANNUDCphysical
27880917
RBM15_HUMANRBM15physical
27880917
GLMN_HUMANGLMNphysical
27880917
FANCI_HUMANFANCIphysical
27097374
AKT1_HUMANAKT1physical
27097374
WDR48_HUMANWDR48physical
24145035
CHIP_HUMANSTUB1physical
24145035
COA1_HUMANCOA1physical
24145035
SGT1_HUMANSUGT1physical
24145035
UBP12_HUMANUSP12physical
24145035
UBP1_HUMANUSP1physical
24145035
UBP46_HUMANUSP46physical
24145035
SCRIB_HUMANSCRIBphysical
24145035
IRS4_HUMANIRS4physical
24145035

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 PHLP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1712, AND MASSSPECTROMETRY.

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