PBX2_HUMAN - dbPTM
PBX2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PBX2_HUMAN
UniProt AC P40425
Protein Name Pre-B-cell leukemia transcription factor 2
Gene Name PBX2
Organism Homo sapiens (Human).
Sequence Length 430
Subcellular Localization Nucleus .
Protein Description Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1..
Protein Sequence MDERLLGPPPPGGGRGGLGLVSGEPGGPGEPPGGGDPGGGSGGVPGGRGKQDIGDILQQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRSSQEEEPVDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGGVSPDNSIEHSDYRSKLAQIRHIYHSELEKYEQACNEFTTHVMNLLREQSRTRPVAPKEMERMVSIIHRKFSAIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEVLNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAVKTAVSVTQGGHSRTSSPTPPSSAGSGGSFNLSGSGDMFLGMPGLNGDSYSASQVESLRHSMGPGGYGDNLGGGQMYSPREMRANGSWQEAVTPSSVTSPTEGPGSVHSDTSN
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
15MethylationPPPPGGGRGGLGLVS
CCCCCCCCCCCCCCC		39.00115486571
41PhosphorylationGGDPGGGSGGVPGGR
CCCCCCCCCCCCCCC		35.3325850435
89PhosphorylationRMKPALFSVLCEIKE
HHCHHHHHHHHHHHH		18.2824719451
97UbiquitinationVLCEIKEKTGLSIRS
HHHHHHHHHCCCCCC		42.78-
98PhosphorylationLCEIKEKTGLSIRSS
HHHHHHHHCCCCCCC		44.4328450419
101PhosphorylationIKEKTGLSIRSSQEE
HHHHHCCCCCCCCCC		19.8028464451
104PhosphorylationKTGLSIRSSQEEEPV
HHCCCCCCCCCCCCC		34.4030631047
105PhosphorylationTGLSIRSSQEEEPVD
HCCCCCCCCCCCCCC		31.5917525332
116SulfoxidationEPVDPQLMRLDNMLL
CCCCHHHHHHHHHHH		3.1721406390
136PhosphorylationGPEKGGGSAAAAAAA
CCCCCCHHHHHHHHH		20.2922115753
146PhosphorylationAAAAAAASGGGVSPD
HHHHHHHHCCCCCCC		32.9923401153
151PhosphorylationAASGGGVSPDNSIEH
HHHCCCCCCCCCCCC		29.7929255136
155PhosphorylationGGVSPDNSIEHSDYR
CCCCCCCCCCCHHHH		36.4129255136
159PhosphorylationPDNSIEHSDYRSKLA
CCCCCCCHHHHHHHH		24.4423401153
161PhosphorylationNSIEHSDYRSKLAQI
CCCCCHHHHHHHHHH		21.5722115753
164UbiquitinationEHSDYRSKLAQIRHI
CCHHHHHHHHHHHHH		38.55-
308UbiquitinationRYKKNIGKFQEEANI
EEECCCCHHHHHHCE		39.83-
316PhosphorylationFQEEANIYAVKTAVS
HHHHHCEEEEEEEEE		12.7329978859
320PhosphorylationANIYAVKTAVSVTQG
HCEEEEEEEEEECCC		26.2023403867
323PhosphorylationYAVKTAVSVTQGGHS
EEEEEEEEECCCCCC		19.5829978859
325O-linked_GlycosylationVKTAVSVTQGGHSRT
EEEEEEECCCCCCCC		17.6230059200
325PhosphorylationVKTAVSVTQGGHSRT
EEEEEEECCCCCCCC		17.6223927012
330PhosphorylationSVTQGGHSRTSSPTP
EECCCCCCCCCCCCC		40.2925159151
332PhosphorylationTQGGHSRTSSPTPPS
CCCCCCCCCCCCCCC		36.2526074081
333PhosphorylationQGGHSRTSSPTPPSS
CCCCCCCCCCCCCCC		32.9626074081
334PhosphorylationGGHSRTSSPTPPSSA
CCCCCCCCCCCCCCC		31.9826074081
336PhosphorylationHSRTSSPTPPSSAGS
CCCCCCCCCCCCCCC		50.1826074081
339PhosphorylationTSSPTPPSSAGSGGS
CCCCCCCCCCCCCCC		33.7426074081
340PhosphorylationSSPTPPSSAGSGGSF
CCCCCCCCCCCCCCE		42.2826074081
343PhosphorylationTPPSSAGSGGSFNLS
CCCCCCCCCCCEECC		39.4326074081
346PhosphorylationSSAGSGGSFNLSGSG
CCCCCCCCEECCCCC		17.9426074081
378PhosphorylationQVESLRHSMGPGGYG
HHHHHHHHCCCCCCC		20.9923403867
384PhosphorylationHSMGPGGYGDNLGGG
HHCCCCCCCCCCCCC		27.5023403867
394PhosphorylationNLGGGQMYSPREMRA
CCCCCCCCCHHHHHC		13.9730108239
395PhosphorylationLGGGQMYSPREMRAN
CCCCCCCCHHHHHCC		16.4923401153
404PhosphorylationREMRANGSWQEAVTP
HHHHCCCCCCCCCCC		25.9523090842
410PhosphorylationGSWQEAVTPSSVTSP
CCCCCCCCCCCCCCC		25.2227251275
412PhosphorylationWQEAVTPSSVTSPTE
CCCCCCCCCCCCCCC		28.2427251275
413PhosphorylationQEAVTPSSVTSPTEG
CCCCCCCCCCCCCCC		30.5327251275
415PhosphorylationAVTPSSVTSPTEGPG
CCCCCCCCCCCCCCC		30.8227251275
416PhosphorylationVTPSSVTSPTEGPGS
CCCCCCCCCCCCCCC		27.8928450419
418PhosphorylationPSSVTSPTEGPGSVH
CCCCCCCCCCCCCCC		54.0328450419
423PhosphorylationSPTEGPGSVHSDTSN
CCCCCCCCCCCCCCC		21.5728450419
426PhosphorylationEGPGSVHSDTSN---
CCCCCCCCCCCC---		40.1928450419
428PhosphorylationPGSVHSDTSN-----
CCCCCCCCCC-----		32.9328450419
429PhosphorylationGSVHSDTSN------
CCCCCCCCC------		45.6028450419
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 PBX2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PBX2_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 PBX2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CARD9_HUMANCARD9physical
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 PBX2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-330, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY.

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