PIPNB_HUMAN - dbPTM
PIPNB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIPNB_HUMAN
UniProt AC P48739
Protein Name Phosphatidylinositol transfer protein beta isoform
Gene Name PITPNB
Organism Homo sapiens (Human).
Sequence Length 271
Subcellular Localization Cytoplasm. Golgi apparatus.
Protein Description Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes..
Protein Sequence MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHKIYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLGTLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKELANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTMEDIRRMEDETQKELETMRKRGSVRGTSAADV
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
5Acetylation---MVLIKEFRVVLP
---CCEEEEEEEEEE
46.7919608861
5Ubiquitination---MVLIKEFRVVLP
---CCEEEEEEEEEE
46.7923000965
5 (in isoform 2)Ubiquitination-46.79-
13GlutathionylationEFRVVLPCSVQEYQV
EEEEEEEECCEEEEC
5.6422555962
18PhosphorylationLPCSVQEYQVGQLYS
EEECCEEEECCCEEE
7.45-
31UbiquitinationYSVAEASKNETGGGE
EEHHHHHCCCCCCCC
66.8932015554
33UbiquitinationVAEASKNETGGGEGI
HHHHHCCCCCCCCCE
53.1932015554
44UbiquitinationGEGIEVLKNEPYEKD
CCCEEEECCCCCCCC
65.5221906983
44AcetylationGEGIEVLKNEPYEKD
CCCEEEECCCCCCCC
65.5223236377
44 (in isoform 1)Ubiquitination-65.5221890473
46UbiquitinationGIEVLKNEPYEKDGE
CEEEECCCCCCCCCC
47.9029967540
46 (in isoform 2)Ubiquitination-47.9021890473
50UbiquitinationLKNEPYEKDGEKGQY
ECCCCCCCCCCCCCC
66.2522817900
50AcetylationLKNEPYEKDGEKGQY
ECCCCCCCCCCCCCC
66.2522424773
52UbiquitinationNEPYEKDGEKGQYTH
CCCCCCCCCCCCCEE
49.9722817900
54UbiquitinationPYEKDGEKGQYTHKI
CCCCCCCCCCCEEEE
57.7722817900
56UbiquitinationEKDGEKGQYTHKIYH
CCCCCCCCCEEEEEE
51.5222817900
57PhosphorylationKDGEKGQYTHKIYHL
CCCCCCCCEEEEEEH
21.3422817900
58PhosphorylationDGEKGQYTHKIYHLK
CCCCCCCEEEEEEHH
14.5922817900
60UbiquitinationEKGQYTHKIYHLKSK
CCCCCEEEEEEHHHC
36.8429967540
62UbiquitinationGQYTHKIYHLKSKVP
CCCEEEEEEHHHCCC
13.1029967540
65UbiquitinationTHKIYHLKSKVPAFV
EEEEEEHHHCCCEEE
34.6129967540
67UbiquitinationKIYHLKSKVPAFVRM
EEEEHHHCCCEEEEE
51.1332142685
67 (in isoform 2)Ubiquitination-51.13-
69UbiquitinationYHLKSKVPAFVRMIA
EEHHHCCCEEEEEEC
24.5832142685
74SulfoxidationKVPAFVRMIAPEGSL
CCCEEEEEECCCCCE
2.2921406390
80PhosphorylationRMIAPEGSLVFHEKA
EEECCCCCEEEECCC
21.5023532336
86UbiquitinationGSLVFHEKAWNAYPY
CCEEEECCCHHHCCC
50.5623000965
86 (in isoform 2)Ubiquitination-50.56-
86AcetylationGSLVFHEKAWNAYPY
CCEEEECCCHHHCCC
50.5626051181
86 (in isoform 1)Ubiquitination-50.5621890473
88UbiquitinationLVFHEKAWNAYPYCR
EEEECCCHHHCCCEE
10.8923000965
88UbiquitinationLVFHEKAWNAYPYCR
EEEECCCHHHCCCEE
10.8921890473
88 (in isoform 2)Ubiquitination-10.8921890473
91PhosphorylationHEKAWNAYPYCRTIV
ECCCHHHCCCEEEEE
7.4828152594
93PhosphorylationKAWNAYPYCRTIVTN
CCHHHCCCEEEEECC
5.0620090780
96PhosphorylationNAYPYCRTIVTNEYM
HHCCCEEEEECCCHH
19.08-
104MethylationIVTNEYMKDDFFIKI
EECCCHHCCCEEEEE
53.9244498999
104UbiquitinationIVTNEYMKDDFFIKI
EECCCHHCCCEEEEE
53.9223000965
104 (in isoform 2)Ubiquitination-53.92-
104 (in isoform 1)Ubiquitination-53.9221890473
106UbiquitinationTNEYMKDDFFIKIET
CCCHHCCCEEEEEEE
34.5321890473
106UbiquitinationTNEYMKDDFFIKIET
CCCHHCCCEEEEEEE
34.5321890473
106 (in isoform 2)Ubiquitination-34.5321890473
110UbiquitinationMKDDFFIKIETWHKP
HCCCEEEEEEEECCC
29.3623000965
110 (in isoform 1)Ubiquitination-29.3621890473
112UbiquitinationDDFFIKIETWHKPDL
CCEEEEEEEECCCCC
40.6223000965
112UbiquitinationDDFFIKIETWHKPDL
CCEEEEEEEECCCCC
40.6221890473
112 (in isoform 2)Ubiquitination-40.6221890473
116UbiquitinationIKIETWHKPDLGTLE
EEEEEECCCCCCCEE
31.6129967540
116AcetylationIKIETWHKPDLGTLE
EEEEEECCCCCCCEE
31.6126051181
118UbiquitinationIETWHKPDLGTLENV
EEEECCCCCCCEECC
63.6329967540
146MethylationVHIDIADRSQVEPAD
EEEECCCHHHCCCCC
21.70115487603
154PhosphorylationSQVEPADYKADEDPA
HHCCCCCCCCCCCHH
15.35-
155UbiquitinationQVEPADYKADEDPAL
HCCCCCCCCCCCHHH
50.3221906983
155 (in isoform 2)Ubiquitination-50.32-
155 (in isoform 1)Ubiquitination-50.3221890473
157UbiquitinationEPADYKADEDPALFQ
CCCCCCCCCCHHHHH
57.5921963094
157UbiquitinationEPADYKADEDPALFQ
CCCCCCCCCCHHHHH
57.5921890473
157 (in isoform 2)Ubiquitination-57.5921890473
167UbiquitinationPALFQSVKTKRGPLG
HHHHHHHCCCCCCCC
54.2821906983
167 (in isoform 1)Ubiquitination-54.2821890473
169UbiquitinationLFQSVKTKRGPLGPN
HHHHHCCCCCCCCCC
50.0324816145
169 (in isoform 2)Ubiquitination-50.0321890473
169UbiquitinationLFQSVKTKRGPLGPN
HHHHHCCCCCCCCCC
50.0321890473
178UbiquitinationGPLGPNWKKELANSP
CCCCCCHHHHHCCCC
42.9023000965
179UbiquitinationPLGPNWKKELANSPD
CCCCCHHHHHCCCCC
49.9623000965
179 (in isoform 2)Ubiquitination-49.96-
179 (in isoform 1)Ubiquitination-49.9621890473
180UbiquitinationLGPNWKKELANSPDC
CCCCHHHHHCCCCCC
49.7623000965
181UbiquitinationGPNWKKELANSPDCP
CCCHHHHHCCCCCCH
8.2023000965
181UbiquitinationGPNWKKELANSPDCP
CCCHHHHHCCCCCCH
8.2021890473
181 (in isoform 2)Ubiquitination-8.2021890473
184PhosphorylationWKKELANSPDCPQMC
HHHHHCCCCCCHHHH
19.2625159151
193PhosphorylationDCPQMCAYKLVTIKF
CCHHHHHHHEEEEEH
10.4218083107
194AcetylationCPQMCAYKLVTIKFK
CHHHHHHHEEEEEHH
20.2526051181
199UbiquitinationAYKLVTIKFKWWGLQ
HHHEEEEEHHHHCCH
31.3723000965
199AcetylationAYKLVTIKFKWWGLQ
HHHEEEEEHHHHCCH
31.3725953088
201UbiquitinationKLVTIKFKWWGLQSK
HEEEEEHHHHCCHHH
36.7123000965
201 (in isoform 2)Ubiquitination-36.71-
201AcetylationKLVTIKFKWWGLQSK
HEEEEEHHHHCCHHH
36.7125953088
201 (in isoform 1)Ubiquitination-36.7121890473
203UbiquitinationVTIKFKWWGLQSKVE
EEEEHHHHCCHHHHH
9.7523000965
203UbiquitinationVTIKFKWWGLQSKVE
EEEEHHHHCCHHHHH
9.7521890473
203 (in isoform 2)Ubiquitination-9.7521890473
208UbiquitinationKWWGLQSKVENFIQK
HHHCCHHHHHHHHHH
40.3823000965
208 (in isoform 2)Ubiquitination-40.38-
208 (in isoform 1)Ubiquitination-40.3821890473
210UbiquitinationWGLQSKVENFIQKQE
HCCHHHHHHHHHHHH
50.5923000965
210UbiquitinationWGLQSKVENFIQKQE
HCCHHHHHHHHHHHH
50.5921890473
210 (in isoform 2)Ubiquitination-50.5921890473
215AcetylationKVENFIQKQEKRIFT
HHHHHHHHHHHHHHH
56.4619608861
215UbiquitinationKVENFIQKQEKRIFT
HHHHHHHHHHHHHHH
56.4623000965
215 (in isoform 2)Ubiquitination-56.46-
215 (in isoform 1)Ubiquitination-56.4621890473
217UbiquitinationENFIQKQEKRIFTNF
HHHHHHHHHHHHHHH
51.8723000965
217UbiquitinationENFIQKQEKRIFTNF
HHHHHHHHHHHHHHH
51.8721890473
217AcetylationENFIQKQEKRIFTNF
HHHHHHHHHHHHHHH
51.8719608861
217 (in isoform 2)Ubiquitination-51.8721890473
218UbiquitinationNFIQKQEKRIFTNFH
HHHHHHHHHHHHHHH
48.5823000965
218 (in isoform 2)Ubiquitination-48.58-
220UbiquitinationIQKQEKRIFTNFHRQ
HHHHHHHHHHHHHHH
8.0623000965
220UbiquitinationIQKQEKRIFTNFHRQ
HHHHHHHHHHHHHHH
8.06-
240SulfoxidationDKWIDLTMEDIRRME
HHHHCCCHHHHHHCC
5.9130846556
244MethylationDLTMEDIRRMEDETQ
CCCHHHHHHCCHHHH
44.19115487611
250PhosphorylationIRRMEDETQKELETM
HHHCCHHHHHHHHHH
58.2120068231
252UbiquitinationRMEDETQKELETMRK
HCCHHHHHHHHHHHH
72.2329967540
252 (in isoform 1)Ubiquitination-72.2321890473
254UbiquitinationEDETQKELETMRKRG
CHHHHHHHHHHHHHC
9.5221890473
254UbiquitinationEDETQKELETMRKRG
CHHHHHHHHHHHHHC
9.5221890473
254 (in isoform 2)Ubiquitination-9.5221890473
256PhosphorylationETQKELETMRKRGSV
HHHHHHHHHHHHCCC
34.5920068231
262PhosphorylationETMRKRGSVRGTSAA
HHHHHHCCCCCCCCC
16.8128355574
266PhosphorylationKRGSVRGTSAADV--
HHCCCCCCCCCCC--
12.4825159151
267PhosphorylationRGSVRGTSAADV---
HCCCCCCCCCCC---
25.0423403867

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 PIPNB_HUMAN !!

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

-

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_HUMAN !!

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

Oops, there are no PPI records of PIPNB_HUMAN !!

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 PIPNB_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-215, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57, AND MASSSPECTROMETRY.

TOP