PBX1_HUMAN - dbPTM
PBX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PBX1_HUMAN
UniProt AC P40424
Protein Name Pre-B-cell leukemia transcription factor 1
Gene Name PBX1
Organism Homo sapiens (Human).
Sequence Length 430
Subcellular Localization Nucleus .
Protein Description Binds the sequence 5'-ATCAATCAA-3'. Acts as a transcriptional activator of PF4 in complex with MEIS1. Converted into a potent transcriptional activator by the (1;19) translocation. May have a role in steroidogenesis and, subsequently, sexual development and differentiation. Isoform PBX1b as part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Probably in complex with MEIS2, is involved in transcriptional regulation by KLF4. Acts as a transcriptional activator of NKX2-5 and a transcriptional repressor of CDKN2B. Together with NKX2-5, it is required for spleen development through a mechanism that involves CDKN2B repression (By similarity)..
Protein Sequence MDEQPRLMHSHAGVGMAGHPGLSQHLQDGAGGTEGEGGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPTDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGSDNSVEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVTATNVSAHGSQANSPSTPNSAGSSSSFNMSNSGDLFMSVQSLNGDSYQGAQVGANVQSQVDTLRHVISQTGGYSDGLAASQMYSPQGISANGGWQDATTPSSVTSPTEGPGSVHSDTSN
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
87UbiquitinationVLCEIKEKTVLSIRG
HHHHHCCCEEEEEEC		38.64-
111SulfoxidationQLMRLDNMLLAEGVA
HHHHHHHCHHHCCCC		3.0321406390
126PhosphorylationGPEKGGGSAAAAAAA
CCCCCCHHHHHHHHH		20.2928555341
136PhosphorylationAAAAAAASGGAGSDN
HHHHHHHHCCCCCCC		32.7925159151
141PhosphorylationAASGGAGSDNSVEHS
HHHCCCCCCCCCCHH		32.8425159151
144PhosphorylationGGAGSDNSVEHSDYR
CCCCCCCCCCHHHHH		33.6021712546
148PhosphorylationSDNSVEHSDYRAKLS
CCCCCCHHHHHHHHH		23.8822210691
187PhosphorylationMNLLREQSRTRPISP
HHHHHHHHCCCCCCH		30.7622468782
193PhosphorylationQSRTRPISPKEIERM
HHCCCCCCHHHHHHH		32.3824719451
195UbiquitinationRTRPISPKEIERMVS
CCCCCCHHHHHHHHH		65.61-
209PhosphorylationSIIHRKFSSIQMQLK
HHHHHHHHHHHHHHH		29.57-
210PhosphorylationIIHRKFSSIQMQLKQ
HHHHHHHHHHHHHHH		21.70-
305PhosphorylationFQEEANIYAAKTAVT
HHHHHHHHEEECEEE		10.5828674419
309 (in isoform 2)Phosphorylation-22.9530177828
312 (in isoform 2)Phosphorylation-25.8730177828
314 (in isoform 2)Phosphorylation-27.1330177828
317 (in isoform 2)Phosphorylation-19.3330177828
321 (in isoform 2)Phosphorylation-19.0930177828
321PhosphorylationTNVSAHGSQANSPST
ECCCCCCCCCCCCCC		19.0927362937
325 (in isoform 2)Phosphorylation-24.2025849741
325PhosphorylationAHGSQANSPSTPNSA
CCCCCCCCCCCCCCC		24.2027362937
327 (in isoform 2)Phosphorylation-57.2128348404
328 (in isoform 2)Phosphorylation-29.8525159151
328PhosphorylationSQANSPSTPNSAGSS
CCCCCCCCCCCCCCC		29.85-
331PhosphorylationNSPSTPNSAGSSSSF
CCCCCCCCCCCCCCC		34.90-
331 (in isoform 2)Phosphorylation-34.9027251275
335 (in isoform 2)Phosphorylation-29.1427251275
337 (in isoform 2)Phosphorylation-23.6927251275
340 (in isoform 2)Phosphorylation-3.6530177828
379PhosphorylationDTLRHVISQTGGYSD
HHHHHHHHHCCCCCC		22.1720068231
381PhosphorylationLRHVISQTGGYSDGL
HHHHHHHCCCCCCCC		26.2820068231
384PhosphorylationVISQTGGYSDGLAAS
HHHHCCCCCCCCCCH		12.6320068231
385PhosphorylationISQTGGYSDGLAASQ
HHHCCCCCCCCCCHH		28.6020068231
391PhosphorylationYSDGLAASQMYSPQG
CCCCCCCHHCCCCCC		15.1820068231
394PhosphorylationGLAASQMYSPQGISA
CCCCHHCCCCCCCCC		15.0120068231
395PhosphorylationLAASQMYSPQGISAN
CCCHHCCCCCCCCCC		12.8520068231
400PhosphorylationMYSPQGISANGGWQD
CCCCCCCCCCCCCCC		23.6220068231
409PhosphorylationNGGWQDATTPSSVTS
CCCCCCCCCCCCCCC		47.7520068231
410PhosphorylationGGWQDATTPSSVTSP
CCCCCCCCCCCCCCC		23.9320068231
412PhosphorylationWQDATTPSSVTSPTE
CCCCCCCCCCCCCCC		35.0320068231
413PhosphorylationQDATTPSSVTSPTEG
CCCCCCCCCCCCCCC		30.5320068231
415PhosphorylationATTPSSVTSPTEGPG
CCCCCCCCCCCCCCC		30.8220068231
416PhosphorylationTTPSSVTSPTEGPGS
CCCCCCCCCCCCCCC		27.8920068231
418PhosphorylationPSSVTSPTEGPGSVH
CCCCCCCCCCCCCCC		54.0320068231
423PhosphorylationSPTEGPGSVHSDTSN
CCCCCCCCCCCCCCC		21.5723090842
426PhosphorylationEGPGSVHSDTSN---
CCCCCCCCCCCC---		40.1923090842
428PhosphorylationPGSVHSDTSN-----
CCCCCCCCCC-----		32.9323090842
429PhosphorylationGSVHSDTSN------
CCCCCCCCC------		45.6020068231
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
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:23044487
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PBX1_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 PBX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYH10_MOUSEMyh10physical
12724421
HXB7_HUMANHOXB7physical
7729685
HXD4_HUMANHOXD4physical
10523646
MEIS1_HUMANMEIS1physical
10523646
HXD9_HUMANHOXD9physical
10523646
PKNX1_HUMANPKNOX1physical
9482740
HXB1_HUMANHOXB1physical
9482740
MEIS1_HUMANMEIS1physical
10373562
HDAC1_HUMANHDAC1physical
11046157
SIN3B_HUMANSIN3Bphysical
11046157
MEIS1_HUMANMEIS1physical
20237320
PDX1_HUMANPDX1physical
11279116
MEIS2_HUMANMEIS2physical
11279116
HXC8_HUMANHOXC8physical
16637071
KAT2A_HUMANKAT2Aphysical
23044487
MDM2_HUMANMDM2physical
23044487
UCHL3_HUMANUCHL3physical
22939629
PKNX1_HUMANPKNOX1physical
26971355
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PBX1_HUMAN

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Related Literatures of Post-Translational Modification

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