PIPNB_MOUSE - dbPTM
PIPNB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIPNB_MOUSE
UniProt AC P53811
Protein Name Phosphatidylinositol transfer protein beta isoform
Gene Name Pitpnb
Organism Mus musculus (Mouse).
Sequence Length 271
Subcellular Localization Cytoplasm. Golgi apparatus.
Protein Description Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes..
Protein Sequence MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYENDGEKGQYTHKIYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLGTLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFHSVKTKRGPLGPNWKKELANTPDCPRMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNLHRQLFCWIDKWIDLTMEDIRRMEDETQKELETMRKKGSVRGTSAADA
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
5Ubiquitination---MVLIKEFRVVLP
---CCEEEEEEEEEE
46.79-
5Acetylation---MVLIKEFRVVLP
---CCEEEEEEEEEE
46.7922826441
13S-palmitoylationEFRVVLPCSVQEYQV
EEEEEEEECCEEEEC
5.6428526873
44AcetylationGEGIEVLKNEPYEND
CCCEEEECCCCCCCC
65.5223954790
54AcetylationPYENDGEKGQYTHKI
CCCCCCCCCCCCHHH
57.7723954790
54UbiquitinationPYENDGEKGQYTHKI
CCCCCCCCCCCCHHH
57.77-
65AcetylationTHKIYHLKSKVPAFV
CHHHEEHHHCCCEEE
34.6122826441
86UbiquitinationGSLVFHEKAWNAYPY
CCEEEECCCHHHCCC
50.56-
94S-nitrosocysteineAWNAYPYCRTIVTNE
CHHHCCCEEEEECCC
2.40-
94S-palmitoylationAWNAYPYCRTIVTNE
CHHHCCCEEEEECCC
2.4028526873
94S-nitrosylationAWNAYPYCRTIVTNE
CHHHCCCEEEEECCC
2.4021278135
165PhosphorylationEDPALFHSVKTKRGP
CCCHHHCCCCCCCCC
20.2711953429
179MalonylationPLGPNWKKELANTPD
CCCCCHHHHHCCCCC
49.9626320211
187S-palmitoylationELANTPDCPRMCAYK
HHCCCCCCHHHCHHE
2.1328526873
187S-nitrosylationELANTPDCPRMCAYK
HHCCCCCCHHHCHHE
2.1321278135
187S-nitrosocysteineELANTPDCPRMCAYK
HHCCCCCCHHHCHHE
2.13-
194AcetylationCPRMCAYKLVTIKFK
CHHHCHHEEEEEEHH
20.2522826441
199AcetylationAYKLVTIKFKWWGLQ
HHEEEEEEHHHHCCH
31.3722826441
201AcetylationKLVTIKFKWWGLQSK
EEEEEEHHHHCCHHH
36.7122826441
201UbiquitinationKLVTIKFKWWGLQSK
EEEEEEHHHHCCHHH
36.71-
215MalonylationKVENFIQKQEKRIFT
HHHHHHHHHHHHHHH
56.4626320211
215AcetylationKVENFIQKQEKRIFT
HHHHHHHHHHHHHHH
56.4622826441
230S-nitrosylationNLHRQLFCWIDKWID
HHHHHHHHHHHHHHC
4.1821278135
230S-nitrosocysteineNLHRQLFCWIDKWID
HHHHHHHHHHHHHHC
4.18-
230S-palmitoylationNLHRQLFCWIDKWID
HHHHHHHHHHHHHHC
4.1828526873
262PhosphorylationETMRKKGSVRGTSAA
HHHHHHCCCCCCCCC
19.9526824392
266PhosphorylationKKGSVRGTSAADA--
HHCCCCCCCCCCC--
12.4818846507
267PhosphorylationKGSVRGTSAADA---
HCCCCCCCCCCC---
25.0418846507

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
165SPhosphorylationKinasePRKCAP20444
GPS
165SPhosphorylationKinasePKC-FAMILY-GPS
262SPhosphorylationKinasePRKCAP20444
GPS
262SPhosphorylationKinasePKC-FAMILY-GPS
262SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
262SPhosphorylation

11953429

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 PIPNB_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PIPNB_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIPNB_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The Golgi localization of phosphatidylinositol transfer protein betarequires the protein kinase C-dependent phosphorylation of serine 262and is essential for maintaining plasma membrane sphingomyelinlevels.";
van Tiel C.M., Westerman J., Paasman M.A., Hoebens M.M., Wirtz K.W.,Snoek G.T.;
J. Biol. Chem. 277:22447-22452(2002).
Cited for: PHOSPHORYLATION AT SER-262, MUTAGENESIS OF SER-165 AND SER-262, ANDMASS SPECTROMETRY.

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