PBX3_HUMAN - dbPTM
PBX3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PBX3_HUMAN
UniProt AC P40426
Protein Name Pre-B-cell leukemia transcription factor 3
Gene Name PBX3
Organism Homo sapiens (Human).
Sequence Length 434
Subcellular Localization Nucleus .
Protein Description Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'..
Protein Sequence MDDQSRMLQTLAGVNLAGHSVQGGMALPPPPHGHEGADGDGRKQDIGDILHQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRGAQEEDPPDPQLMRLDNMLLAEGVSGPEKGGGSAAAAAAAAASGGSSDNSIEHSDYRAKLTQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVGIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEILNEYFYSHLSNPYPSEEAKEELAKKCSITVSQVSNWFGNKRIRYKKNIGKFQEEANLYAAKTAVTAAHAVAAAVQNNQTNSPTTPNSGSSGSFNLPNSGDMFMNMQSLNGDSYQGSQVGANVQSQVDTLRHVINQTGGYSDGLGGNSLYSPHNLNANGGWQDATTPSSVTSPTEGPGSVHSDTSN
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
82PhosphorylationRMKPALFSVLCEIKE
HHCHHHHHHHHHHHH
18.2824719451
90UbiquitinationVLCEIKEKTGLSIRG
HHHHHHHHHCCCCCC
42.78-
121PhosphorylationMLLAEGVSGPEKGGG
CHHHCCCCCCCCCCH
60.5318187866
129PhosphorylationGPEKGGGSAAAAAAA
CCCCCCHHHHHHHHH
20.2923186163
139PhosphorylationAAAAAAASGGSSDNS
HHHHHHHHCCCCCCC
38.6728555341
189PhosphorylationMNLLREQSRTRPISP
HHHHHHHHCCCCCCH
30.7622468782
195PhosphorylationQSRTRPISPKEIERM
HHCCCCCCHHHHHHH
32.3824719451
197UbiquitinationRTRPISPKEIERMVG
CCCCCCHHHHHHHHH
65.61-
211PhosphorylationGIIHRKFSSIQMQLK
HHHHHHHCHHHHHHH
29.57-
212PhosphorylationIIHRKFSSIQMQLKQ
HHHHHHCHHHHHHHH
21.70-
307PhosphorylationFQEEANLYAAKTAVT
HHHHHHHHHHHHHHH
12.3425159151
427PhosphorylationSPTEGPGSVHSDTSN
CCCCCCCCCCCCCCC
21.5723090842
430PhosphorylationEGPGSVHSDTSN---
CCCCCCCCCCCC---
40.1923090842
432PhosphorylationPGSVHSDTSN-----
CCCCCCCCCC-----
32.9323090842
433PhosphorylationGSVHSDTSN------
CCCCCCCCC------
45.6023090842

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 PBX3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PBX3_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 PBX3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATRAP_HUMANAGTRAPphysical
16189514
ZNHI3_HUMANZNHIT3physical
20211142
ATRAP_HUMANAGTRAPphysical
19060904
PRAF1_HUMANRABAC1physical
19060904
TPM3_HUMANTPM3physical
25416956
TRAF1_HUMANTRAF1physical
25416956
AR6P1_HUMANARL6IP1physical
25416956
MAGC2_HUMANMAGEC2physical
25416956
TRI44_HUMANTRIM44physical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
MAL2_HUMANMAL2physical
25416956
FSD2_HUMANFSD2physical
25416956

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 PBX3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASSSPECTROMETRY.

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