P4R3B_HUMAN - dbPTM
P4R3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P4R3B_HUMAN
UniProt AC Q5MIZ7
Protein Name Serine/threonine-protein phosphatase 4 regulatory subunit 3B
Gene Name PPP4R3B {ECO:0000312|HGNC:HGNC:29267}
Organism Homo sapiens (Human).
Sequence Length 849
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Nucleus . In interphase localized in the cytoplasm and (with higher levels) the nucleus. During metaphase located in pericentriolar regions.
Protein Description Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers..
Protein Sequence MSDTRRRVKVYTLNEDRQWDDRGTGHVSSTYVEELKGMSLLVRAESDGSLLLESKINPNTAYQKQQDTLIVWSEAENYDLALSFQEKAGCDEIWEKICQVQGKDPSVEVTQDLIDESEEERFEEMPETSHLIDLPTCELNKLEEIADLVTSVLSSPIRREKLALALENEGYIKKLLQLFQACENLENTEGLHHLYEIIRGILFLNKATLFEVMFSDECIMDVVGCLEYDPALAQPKRHREFLTKTAKFKEVIPITDSELRQKIHQTYRVQYIQDIILPTPSVFEENFLSTLTSFIFFNKVEIVSMLQEDEKFLSEVFAQLTDEATDDDKRRELVNFFKEFCAFSQTLQPQNRDAFFKTLAKLGILPALEIVMGMDDLQVRSAATDIFSYLVEFSPSMVREFVMQEAQQSDDDILLINVVIEQMICDTDPELGGAVQLMGLLRTLIDPENMLATTNKTEKSEFLNFFYNHCMHVLTAPLLTNTSEDKCEKDFFLKHYRYSWSFICTPSHSHSHSTPSSSISQDNIVGSNKNNTICPDNYQTAQLLALILELLTFCVEHHTYHIKNYIMNKDLLRRVLVLMNSKHTFLALCALRFMRRIIGLKDEFYNRYITKGNLFEPVINALLDNGTRYNLLNSAVIELFEFIRVEDIKSLTAHIVENFYKALESIEYVQTFKGLKTKYEQEKDRQNQKLNSVPSILRSNRFRRDAKALEEDEEMWFNEDEEEEGKAVVAPVEKPKPEDDFPDNYEKFMETKKAKESEDKENLPKRTSPGGFKFTFSHSASAANGTNSKSVVAQIPPATSNGSSSKTTNLPTSVTATKGSLVGLVDYPDDEEEDEEEESSPRKRPRLGS
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
9UbiquitinationSDTRRRVKVYTLNED
CCCCCCEEEEEECCC		27.93-
11PhosphorylationTRRRVKVYTLNEDRQ
CCCCEEEEEECCCCC		10.3728985074
12PhosphorylationRRRVKVYTLNEDRQW
CCCEEEEEECCCCCC		26.5428985074
17MethylationVYTLNEDRQWDDRGT
EEEECCCCCCCCCCC		33.05-
46PhosphorylationSLLVRAESDGSLLLE
EEEEEEECCCCEEEE		46.4130108239
49PhosphorylationVRAESDGSLLLESKI
EEEECCCCEEEEEEC		22.3430108239
54PhosphorylationDGSLLLESKINPNTA
CCCEEEEEECCCCCC		38.5130108239
55UbiquitinationGSLLLESKINPNTAY
CCEEEEEECCCCCCC		36.8129967540
96UbiquitinationGCDEIWEKICQVQGK
CCHHHHHHHHHHCCC		33.51-
110PhosphorylationKDPSVEVTQDLIDES
CCCCCCCHHHHCCCC		11.6730301811
117 (in isoform 3)Phosphorylation-46.70-
117PhosphorylationTQDLIDESEEERFEE
HHHHCCCCHHHHHHH		46.7019664994
128PhosphorylationRFEEMPETSHLIDLP
HHHHCCCCCCCCCCC		18.6427251275
129PhosphorylationFEEMPETSHLIDLPT
HHHCCCCCCCCCCCC		18.0327251275
150PhosphorylationEEIADLVTSVLSSPI
HHHHHHHHHHHCCHH		22.0328348404
151PhosphorylationEIADLVTSVLSSPIR
HHHHHHHHHHCCHHH		17.3728348404
154PhosphorylationDLVTSVLSSPIRREK
HHHHHHHCCHHHHHH		31.7325159151
155PhosphorylationLVTSVLSSPIRREKL
HHHHHHCCHHHHHHH		21.8625159151
161UbiquitinationSSPIRREKLALALEN
CCHHHHHHHHHHHCC		36.93-
1612-HydroxyisobutyrylationSSPIRREKLALALEN
CCHHHHHHHHHHHCC		36.93-
171PhosphorylationLALENEGYIKKLLQL
HHHCCCHHHHHHHHH		11.9119658100
244UbiquitinationRHREFLTKTAKFKEV
HHHHHHHHHCCCCEE		48.94-
249UbiquitinationLTKTAKFKEVIPITD
HHHHCCCCEEEECCC		50.8229967540
264UbiquitinationSELRQKIHQTYRVQY
HHHHHHHHHHHHHHH		22.4421890473
274UbiquitinationYRVQYIQDIILPTPS
HHHHHHHHHCCCCCC		21.9723000965
296UbiquitinationSTLTSFIFFNKVEIV
HHHHHHHHCCCHHHH		5.3421890473
306UbiquitinationKVEIVSMLQEDEKFL
CHHHHHHHHHCHHHH		3.8223000965
308UbiquitinationEIVSMLQEDEKFLSE
HHHHHHHHCHHHHHH		65.2621890473
318UbiquitinationKFLSEVFAQLTDEAT
HHHHHHHHHHCCCCC		14.5123000965
329UbiquitinationDEATDDDKRRELVNF
CCCCCHHHHHHHHHH		61.4229967540
361UbiquitinationAFFKTLAKLGILPAL
HHHHHHHHCCCHHHH		50.8121890473
371UbiquitinationILPALEIVMGMDDLQ
CHHHHHHHHCCCHHH		1.6623000965
393UbiquitinationIFSYLVEFSPSMVRE
HHHHHHHCCHHHHHH		11.5221890473
403UbiquitinationSMVREFVMQEAQQSD
HHHHHHHHHHHHHCC		3.4623000965
456AcetylationNMLATTNKTEKSEFL
HHHCCCCCCCHHHHH		56.8425953088
457PhosphorylationMLATTNKTEKSEFLN
HHCCCCCCCHHHHHH		51.20-
459UbiquitinationATTNKTEKSEFLNFF
CCCCCCCHHHHHHHH		61.59-
482PhosphorylationTAPLLTNTSEDKCEK
HHHHCCCCCCCHHCC		28.40-
483PhosphorylationAPLLTNTSEDKCEKD
HHHCCCCCCCHHCCC		45.96-
489UbiquitinationTSEDKCEKDFFLKHY
CCCCHHCCCHHHHHC		70.1129967540
494UbiquitinationCEKDFFLKHYRYSWS
HCCCHHHHHCEEEEE		33.1733845483
495 (in isoform 3)Phosphorylation-17.91-
495 (in isoform 2)Phosphorylation-17.91-
500 (in isoform 3)Phosphorylation-6.58-
516UbiquitinationSHSHSTPSSSISQDN
CCCCCCCCCCCCCCC		36.4821890473
526UbiquitinationISQDNIVGSNKNNTI
CCCCCCCCCCCCCCC		23.0023000965
548UbiquitinationAQLLALILELLTFCV
HHHHHHHHHHHHHHH		3.8421890473
558UbiquitinationLTFCVEHHTYHIKNY
HHHHHHHHHHHHHHH		18.0223000965
569UbiquitinationIKNYIMNKDLLRRVL
HHHHHCCHHHHHHHH		32.1621890473
579UbiquitinationLRRVLVLMNSKHTFL
HHHHHHHHCCHHHHH		4.0823000965
594 (in isoform 3)Phosphorylation-1.97-
6012-HydroxyisobutyrylationMRRIIGLKDEFYNRY
HHHHHCCCHHHHHHC		50.42-
601UbiquitinationMRRIIGLKDEFYNRY
HHHHHCCCHHHHHHC		50.4221890473
611UbiquitinationFYNRYITKGNLFEPV
HHHHCCCCCCCHHHH		35.9223000965
673AcetylationIEYVQTFKGLKTKYE
HHHHHHHCCHHHHHH		67.727429247
676AcetylationVQTFKGLKTKYEQEK
HHHHCCHHHHHHHHH		52.197429255
677PhosphorylationQTFKGLKTKYEQEKD
HHHCCHHHHHHHHHH		43.8524719451
679PhosphorylationFKGLKTKYEQEKDRQ
HCCHHHHHHHHHHHH		28.2417924679
683 (in isoform 3)Phosphorylation-58.88-
692PhosphorylationRQNQKLNSVPSILRS
HHHHHHHHHHHHHHC		45.9328555341
695PhosphorylationQKLNSVPSILRSNRF
HHHHHHHHHHHCCCH		31.9026434776
726SumoylationEDEEEEGKAVVAPVE
CCHHHCCCEEEEECC		41.09-
745PhosphorylationEDDFPDNYEKFMETK
CCCCCCCHHHHHHHH		28.0728796482
754 (in isoform 3)Phosphorylation-23.54-
755PhosphorylationFMETKKAKESEDKEN
HHHHHHHHHCCCCCC		71.3233259812
755AcetylationFMETKKAKESEDKEN
HHHHHHHHHCCCCCC		71.3218585219
755 (in isoform 3)Phosphorylation-71.32-
767PhosphorylationKENLPKRTSPGGFKF
CCCCCCCCCCCCEEE		45.4520068231
768PhosphorylationENLPKRTSPGGFKFT
CCCCCCCCCCCEEEE		26.1120068231
777PhosphorylationGGFKFTFSHSASAAN
CCEEEEEECCCCCCC		17.3028555341
779PhosphorylationFKFTFSHSASAANGT
EEEEEECCCCCCCCC		23.7928555341
781PhosphorylationFTFSHSASAANGTNS
EEEECCCCCCCCCCC		30.8128555341
808PhosphorylationNGSSSKTTNLPTSVT
CCCCCCCCCCCCEEE		38.1933259812
820PhosphorylationSVTATKGSLVGLVDY
EEEECCCCEEEEECC		22.8028450419
827PhosphorylationSLVGLVDYPDDEEED
CEEEEECCCCCHHHC		10.9023927012
839PhosphorylationEEDEEEESSPRKRPR
HHCCHHCCCCCCCCC		49.2630278072
840PhosphorylationEDEEEESSPRKRPRL
HCCHHCCCCCCCCCC		31.8130278072
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 P4R3B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P4R3B_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 P4R3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FEZ1_HUMANFEZ1physical
16169070
CAN1_HUMANCAPN1physical
22863883
CNDP2_HUMANCNDP2physical
22863883
SIAS_HUMANNANSphysical
22863883
RL23_HUMANRPL23physical
22863883
NHRF1_HUMANSLC9A3R1physical
22863883
TGM2_HUMANTGM2physical
22863883
1433T_HUMANYWHAQphysical
22863883
HNRPU_HUMANHNRNPUphysical
26344197
OSBL8_HUMANOSBPL8physical
26344197
PP4C_HUMANPPP4Cphysical
26344197
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 P4R3B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-679, AND MASSSPECTROMETRY.

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