PBIP1_HUMAN - dbPTM
PBIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PBIP1_HUMAN
UniProt AC Q96AQ6
Protein Name Pre-B-cell leukemia transcription factor-interacting protein 1
Gene Name PBXIP1
Organism Homo sapiens (Human).
Sequence Length 731
Subcellular Localization Cytoplasm, cytoskeleton . Nucleus . Shuttles between the nucleus and the cytosol (PubMed:12360403). Mainly localized in the cytoplasm, associated with microtubules (PubMed:10825160, PubMed:12360403). Detected in small amounts in the nucleus (PubMed:1
Protein Description Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling..
Protein Sequence MASCPDSDNSWVLAGSESLPVETLGPASRMDPESERALQAPHSPSKTDGKELAGTMDGEGTLFQTESPQSGSILTEETEVKGTLEGDVCGVEPPGPGDTVVQGDLQETTVVTGLGPDTQDLEGQSPPQSLPSTPKAAWIREEGRCSSSDDDTDVDMEGLRRRRGREAGPPQPMVPLAVENQAGGEGAGGELGISLNMCLLGALVLLGLGVLLFSGGLSESETGPMEEVERQVLPDPEVLEAVGDRQDGLREQLQAPVPPDSVPSLQNMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLMHQPKGLEEENAQLRGALQQGEAFQRALESELQQLRARLQGLEADCVRGPDGVCLSGGRGPQGDKAIREQGPREQEPELSFLKQKEQLEAEAQALRQELERQRRLLGSVQQDLERSLQDASRGDPAHAGLAELGHRLAQKLQGLENWGQDPGVSANASKAWHQKSHFQNSREWSGKEKWWDGQRDRKAEHWKHKKEESGRERKKNWGGQEDREPAGRWKEGRPRVEESGSKKEGKRQGPKEPPRKSGSFHSSGEKQKQPRWREGTKDSHDPLPSWAELLRPKYRAPQGCSGVDECARQEGLTFFGTELAPVRQQELASLLRTYLARLPWAGQLTKELPLSPAFFGEDGIFRHDRLRFRDFVDALEDSLEEVAVQQTGDDDEVDDFEDFIFSHFFGDKALKKRSGKKDKHSQSPRAAGPREGHSHSHHHHHRG
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
3Phosphorylation-----MASCPDSDNS
-----CCCCCCCCCC		25.5328348404
7Phosphorylation-MASCPDSDNSWVLA
-CCCCCCCCCCEEEC		24.6727251275
10PhosphorylationSCPDSDNSWVLAGSE
CCCCCCCCEEECCCC		24.4524719451
14 (in isoform 2)Phosphorylation-15.1725849741
16PhosphorylationNSWVLAGSESLPVET
CCEEECCCCCCCCCC		20.5727251275
23PhosphorylationSESLPVETLGPASRM
CCCCCCCCCCCHHHC		36.93-
34PhosphorylationASRMDPESERALQAP
HHHCCHHHHHHHHCC		37.4624144214
43PhosphorylationRALQAPHSPSKTDGK
HHHHCCCCCCCCCCC		29.7923927012
45PhosphorylationLQAPHSPSKTDGKEL
HHCCCCCCCCCCCCC		51.7222167270
47PhosphorylationAPHSPSKTDGKELAG
CCCCCCCCCCCCCCC		55.0823927012
55PhosphorylationDGKELAGTMDGEGTL
CCCCCCCEECCCCCE		13.3923927012
61PhosphorylationGTMDGEGTLFQTESP
CEECCCCCEEECCCC		21.7923927012
65PhosphorylationGEGTLFQTESPQSGS
CCCCEEECCCCCCCC		30.9722199227
67PhosphorylationGTLFQTESPQSGSIL
CCEEECCCCCCCCEE		31.4622199227
70PhosphorylationFQTESPQSGSILTEE
EECCCCCCCCEEEEE		37.5822199227
72PhosphorylationTESPQSGSILTEETE
CCCCCCCCEEEEEEE		21.4822199227
75PhosphorylationPQSGSILTEETEVKG
CCCCCEEEEEEEEEC		30.0627251275
125PhosphorylationTQDLEGQSPPQSLPS
CCCCCCCCCCCCCCC		49.7826074081
129PhosphorylationEGQSPPQSLPSTPKA
CCCCCCCCCCCCCCE		48.2826074081
132PhosphorylationSPPQSLPSTPKAAWI
CCCCCCCCCCCEEEE		63.7426074081
133PhosphorylationPPQSLPSTPKAAWIR
CCCCCCCCCCEEEEC		27.2026074081
146PhosphorylationIREEGRCSSSDDDTD
ECCCCCCCCCCCCCC		31.3622617229
147PhosphorylationREEGRCSSSDDDTDV
CCCCCCCCCCCCCCC		41.2222617229
148PhosphorylationEEGRCSSSDDDTDVD
CCCCCCCCCCCCCCC		28.8522617229
152PhosphorylationCSSSDDDTDVDMEGL
CCCCCCCCCCCHHHH		44.9421082442
274UbiquitinationNMGLLLDKLAKENQD
HHHHHHHHHHHHCHH		50.76-
277UbiquitinationLLLDKLAKENQDIRL
HHHHHHHHHCHHHHH		68.58-
293UbiquitinationQAQLQAQKEELQSLM
HHHHHHHHHHHHHHH		57.05-
304UbiquitinationQSLMHQPKGLEEENA
HHHHHCCCCHHHHHH		70.34-
355PhosphorylationGPDGVCLSGGRGPQG
CCCCCEECCCCCCCH		33.7926437602
3642-HydroxyisobutyrylationGRGPQGDKAIREQGP
CCCCCHHHHHHHHCC		53.16-
379PhosphorylationREQEPELSFLKQKEQ
CCCCCCHHHHHHHHH		27.2024719451
382UbiquitinationEPELSFLKQKEQLEA
CCCHHHHHHHHHHHH		58.26-
384UbiquitinationELSFLKQKEQLEAEA
CHHHHHHHHHHHHHH		45.93-
407PhosphorylationRQRRLLGSVQQDLER
HHHHHHHHHHHHHHH		19.4026437602
415PhosphorylationVQQDLERSLQDASRG
HHHHHHHHHHHHHCC		22.4722210691
420PhosphorylationERSLQDASRGDPAHA
HHHHHHHHCCCHHHH		45.1222210691
463UbiquitinationASKAWHQKSHFQNSR
HHHHHHHHHHCCCCC		32.77-
464PhosphorylationSKAWHQKSHFQNSRE
HHHHHHHHHCCCCCC		23.9827080861
469PhosphorylationQKSHFQNSREWSGKE
HHHHCCCCCCCCCCC		22.3123401153
473PhosphorylationFQNSREWSGKEKWWD
CCCCCCCCCCCCCCC		34.9227080861
531MethylationVEESGSKKEGKRQGP
CCCCCCCCCCCCCCC		73.69-
534AcetylationSGSKKEGKRQGPKEP
CCCCCCCCCCCCCCC		42.5119829955
539AcetylationEGKRQGPKEPPRKSG
CCCCCCCCCCCCCCC		85.0030591147
539MethylationEGKRQGPKEPPRKSG
CCCCCCCCCCCCCCC		85.00-
545PhosphorylationPKEPPRKSGSFHSSG
CCCCCCCCCCCCCCC		40.7329691806
547PhosphorylationEPPRKSGSFHSSGEK
CCCCCCCCCCCCCCC		27.2029691806
550PhosphorylationRKSGSFHSSGEKQKQ
CCCCCCCCCCCCCCC		37.7229691806
551 (in isoform 3)Phosphorylation-42.2629116813
551PhosphorylationKSGSFHSSGEKQKQP
CCCCCCCCCCCCCCC		42.2626699800
564PhosphorylationQPRWREGTKDSHDPL
CCCCCCCCCCCCCCC		27.2527080861
567PhosphorylationWREGTKDSHDPLPSW
CCCCCCCCCCCCCHH		31.20-
605 (in isoform 2)Ubiquitination-23.7521906983
617PhosphorylationVRQQELASLLRTYLA
CCHHHHHHHHHHHHH		40.3324719451
634UbiquitinationPWAGQLTKELPLSPA
CCCCHHCCCCCCCHH		66.882190698
634 (in isoform 1)Ubiquitination-66.8821906983
639PhosphorylationLTKELPLSPAFFGED
HCCCCCCCHHHCCCC		16.55-
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
147SPhosphorylationKinaseIKKEQ14164
PSP
147SPhosphorylationKinaseTBK1Q9UHD2
PSP
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:24488098
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PBIP1_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 PBIP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPPA2_HUMANDPPA2physical
16189514
PHS2_HUMANPCBD2physical
20211142
WASC3_HUMANCCDC53physical
19060904
MDFI_HUMANMDFIphysical
19060904
PKCB1_HUMANZMYND8physical
21988832
GMCL1_HUMANGMCL1physical
25416956
GMCL1_HUMANGMCL1physical
21516116
TBK1_HUMANTBK1physical
24488098
MDM2_HUMANMDM2physical
24488098
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 PBIP1_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-146; SER-147 ANDSER-148, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-146; SER-147;SER-148 AND THR-152, AND MASS SPECTROMETRY.

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