PP2BB_HUMAN - dbPTM
PP2BB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP2BB_HUMAN
UniProt AC P16298
Protein Name Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
Gene Name PPP3CB
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Cytoplasm .
Protein Description Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. [PubMed: 19154138]
Protein Sequence MAAPEPARAAPPPPPPPPPPPGADRVVKAVPFPPTHRLTSEEVFDLDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLSICSDDELMTEGEDQFDGSAAARKEIIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLAGGRQTLQSATVEAIEAEKAIRGFSPPHRICSFEEAKGLDRINERMPPRKDAVQQDGFNSLNTAHATENHGTGNHTAQ
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
2Acetylation------MAAPEPARA
------CCCCCCCCC		31.5519413330
35PhosphorylationKAVPFPPTHRLTSEE
EECCCCCCCCCCCCC		21.62-
56 (in isoform 4)Ubiquitination-42.01-
56UbiquitinationIPRVDVLKNHLVKEG
CCCHHHHHCCCHHCC		42.01-
56 (in isoform 1)Ubiquitination-42.0121890473
56 (in isoform 3)Ubiquitination-42.0121890473
56 (in isoform 2)Ubiquitination-42.0121890473
61UbiquitinationVLKNHLVKEGRVDEE
HHHCCCHHCCCCCHH		61.89-
116PhosphorylationKLFEVGGSPANTRYL
HHHCCCCCCCCCEEE		18.2124076635
128PhosphorylationRYLFLGDYVDRGYFS
EEEECCCCCCCCCCH		11.49-
168PhosphorylationECRHLTEYFTFKQEC
HHHHHHHEEEECCHH		11.59-
172 (in isoform 4)Ubiquitination-41.97-
172UbiquitinationLTEYFTFKQECKIKY
HHHEEEECCHHHCCC		41.97-
302UbiquitinationAGYRMYRKSQTTGFP
HCCCCHHHHCCCCCC		29.45-
332 (in isoform 3)Ubiquitination-43.8721890473
332 (in isoform 1)Ubiquitination-43.8721890473
332 (in isoform 4)Ubiquitination-43.87-
332UbiquitinationNNKAAVLKYENNVMN
CCCEEEEEEECCEEC		43.8721890473
332UbiquitinationNNKAAVLKYENNVMN
CCCEEEEEEECCEEC		43.8721890473
350 (in isoform 2)Ubiquitination-19.2821890473
414AcetylationNKIRAIGKMARVFSV
HHHHHHHHHHHHHHH		24.2325953088
420PhosphorylationGKMARVFSVLREESE
HHHHHHHHHHHHHCC		19.8624247654
421PhosphorylationKMARVFSVLREESES
HHHHHHHHHHHHCCC		3.8727251275
433UbiquitinationSESVLTLKGLTPTGM
CCCEEEECCCCCCCC		46.792190698
433 (in isoform 1)Ubiquitination-46.7921890473
434 (in isoform 3)Ubiquitination-37.5821890473
434 (in isoform 4)Ubiquitination-37.58-
436PhosphorylationVLTLKGLTPTGMLPS
EEEECCCCCCCCCCC		27.7227251275
437PhosphorylationLTLKGLTPTGMLPSG
EEECCCCCCCCCCCC		31.8127251275
451 (in isoform 2)Ubiquitination-50.2521890473
465UbiquitinationVEAIEAEKAIRGFSP
HHHHHHHHHHCCCCC		57.04-
471PhosphorylationEKAIRGFSPPHRICS
HHHHCCCCCCCCCCC		40.1023401153
472PhosphorylationKAIRGFSPPHRICSF
HHHCCCCCCCCCCCH		26.8427251275
478PhosphorylationSPPHRICSFEEAKGL
CCCCCCCCHHHHCCH		33.0623401153
479PhosphorylationPPHRICSFEEAKGLD
CCCCCCCHHHHCCHH		9.4924719451
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 PP2BB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP2BB_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 PP2BB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JUN_HUMANJUNphysical
17952113
PDE4D_HUMANPDE4Dphysical
20647544
GRP75_HUMANHSPA9physical
26496610
RAD51_HUMANRAD51physical
26496610
COX5A_HUMANCOX5Aphysical
26496610
RSRC1_HUMANRSRC1physical
26496610
PHF5A_HUMANPHF5Aphysical
26496610
SPF45_HUMANRBM17physical
26496610
AHNK_HUMANAHNAKphysical
27880917
ARMT1_HUMANC6orf211physical
27880917
GSK3A_HUMANGSK3Aphysical
27880917
LBH_HUMANLBHphysical
27880917
CANB1_HUMANPPP3R1physical
27880917
RCAN1_HUMANRCAN1physical
27880917
RCAN3_HUMANRCAN3physical
27880917
ZYX_HUMANZYXphysical
27880917
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 PP2BB_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory