BBX_HUMAN - dbPTM
BBX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BBX_HUMAN
UniProt AC Q8WY36
Protein Name HMG box transcription factor BBX
Gene Name BBX
Organism Homo sapiens (Human).
Sequence Length 941
Subcellular Localization Nucleus .
Protein Description Transcription factor that is necessary for cell cycle progression from G1 to S phase..
Protein Sequence MKGSNRNKDHSAEGEGVGKRPKRKCLQWHPLLAKKLLDFSEEEEEEDEEEDIDKVQLLGADGLEQDVGETEDDESPEQRARRPMNAFLLFCKRHRSLVRQEHPRLDNRGATKILADWWAVLDPKEKQKYTDMAKEYKDAFMKANPGYKWCPTTNKPVKSPTPTVNPRKKLWAFPSDSSRDLPSPKKAKTEEMPQLNFGMADPTQMGGLSMLLLAGEHALGTPEVSSGTCRPDVSESPELRQKSPLFQFAEISSSTSHSDASTKQCQTSALFQFAEISSNTSQLGGAEPVKRCGKSALFQLAEMCLASEGMKMEESKLIKAKESDGGRIKELEKGKEEKEIKMEKTDETRLQKEAEFEKSAKENLRDSKELRNFEALQIDDIMAIKMEDPKEIRKEELEEDHKCSHFPDFSYSASSKIIISDVPSRKDHMCHPHGIMIIEDPAALNKPEKLKKKKKKSKMDRHGNDKSTPKKTCKKRQSSESDIESVIYTIEAVAKGDWGIEKLGDTPRKKVRTSSSGKGSILDAKPPKKKVKSREKKMSKEKSSDTTKESRPPDFISISASKNISGETPEGIKAEPLTPMEDALPPSLSGQAKPEDSDCHRKIETCGSRKSERSCKGALYKTLVSEGMLTSLRANVDRGKRSSGKGNSSDHEGCWNEESWTFSQSGTSGSKKFKKTKPKEDCLLGSAKLDEEFEKKFNSLPQYSPVTFDRKCVPVPRKKKKTGNVSSEPTKTSKGPFQSQKKNLFHKIVSKYKHKKEKPNVPEKGSGDKWSNKQLFLDAIHPTEAIFSEDRNTMEPVHKVKNIPSIFNTPEPTTTQEPLVGSQKRKARKTKITHLVRTADGRVSPAGGTLDDKPKEQLQRSLPKATETDCNDKCSHNTEVGETRSSTPEMPAVSAFFSLAALAEVAAMENVHRGQRSTPLTHDGQPKEMPQAPVLISCADQ
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
11PhosphorylationSNRNKDHSAEGEGVG
CCCCCCCCCCCCCCC
37.8420068231
34AcetylationQWHPLLAKKLLDFSE
HHCHHHHHHHHCCCH
43.8825953088
40PhosphorylationAKKLLDFSEEEEEED
HHHHHCCCHHHHCCC
43.7125159151
70PhosphorylationLEQDVGETEDDESPE
CCCCCCCCCCCCCHH
38.4927732954
75PhosphorylationGETEDDESPEQRARR
CCCCCCCCHHHHHHC
40.5127732954
96PhosphorylationLFCKRHRSLVRQEHP
HHHHHHHHHHHCCCC
25.70-
130PhosphorylationPKEKQKYTDMAKEYK
HHHHHHHHHHHHHHH
26.7420860994
137SumoylationTDMAKEYKDAFMKAN
HHHHHHHHHHHHHHC
43.61-
137SumoylationTDMAKEYKDAFMKAN
HHHHHHHHHHHHHHC
43.61-
152PhosphorylationPGYKWCPTTNKPVKS
CCCCCCCCCCCCCCC
39.6023927012
153PhosphorylationGYKWCPTTNKPVKSP
CCCCCCCCCCCCCCC
26.7923927012
155AcetylationKWCPTTNKPVKSPTP
CCCCCCCCCCCCCCC
49.4426051181
159PhosphorylationTTNKPVKSPTPTVNP
CCCCCCCCCCCCCCC
33.9529255136
161PhosphorylationNKPVKSPTPTVNPRK
CCCCCCCCCCCCCCC
38.3929255136
163PhosphorylationPVKSPTPTVNPRKKL
CCCCCCCCCCCCCCE
35.0823927012
169SumoylationPTVNPRKKLWAFPSD
CCCCCCCCEECCCCC
51.01-
169SumoylationPTVNPRKKLWAFPSD
CCCCCCCCEECCCCC
51.01-
169UbiquitinationPTVNPRKKLWAFPSD
CCCCCCCCEECCCCC
51.01-
175PhosphorylationKKLWAFPSDSSRDLP
CCEECCCCCCCCCCC
43.6125159151
177PhosphorylationLWAFPSDSSRDLPSP
EECCCCCCCCCCCCC
31.4525159151
178PhosphorylationWAFPSDSSRDLPSPK
ECCCCCCCCCCCCCC
34.5025159151
183PhosphorylationDSSRDLPSPKKAKTE
CCCCCCCCCCCCCCC
57.5628355574
189PhosphorylationPSPKKAKTEEMPQLN
CCCCCCCCCCCCCCC
41.8826074081
234PhosphorylationGTCRPDVSESPELRQ
CCCCCCCCCCHHHHH
39.4726074081
236PhosphorylationCRPDVSESPELRQKS
CCCCCCCCHHHHHCC
19.0326074081
243O-linked_GlycosylationSPELRQKSPLFQFAE
CHHHHHCCCCEEEEE
20.6330059200
243PhosphorylationSPELRQKSPLFQFAE
CHHHHHCCCCEEEEE
20.6325159151
252O-linked_GlycosylationLFQFAEISSSTSHSD
CEEEEECCCCCCCCC
15.1130059200
252PhosphorylationLFQFAEISSSTSHSD
CEEEEECCCCCCCCC
15.1123927012
253PhosphorylationFQFAEISSSTSHSDA
EEEEECCCCCCCCCC
43.2123927012
254PhosphorylationQFAEISSSTSHSDAS
EEEECCCCCCCCCCC
27.4323927012
255PhosphorylationFAEISSSTSHSDAST
EEECCCCCCCCCCCC
32.1923927012
256O-linked_GlycosylationAEISSSTSHSDASTK
EECCCCCCCCCCCCC
23.9630059200
256PhosphorylationAEISSSTSHSDASTK
EECCCCCCCCCCCCC
23.9622199227
258O-linked_GlycosylationISSSTSHSDASTKQC
CCCCCCCCCCCCCHH
34.3430059200
258PhosphorylationISSSTSHSDASTKQC
CCCCCCCCCCCCCHH
34.3424117733
261PhosphorylationSTSHSDASTKQCQTS
CCCCCCCCCCHHHHH
40.9224117733
262PhosphorylationTSHSDASTKQCQTSA
CCCCCCCCCHHHHHH
27.1924117733
295PhosphorylationPVKRCGKSALFQLAE
CCCCCCHHHHHHHHH
18.5828348404
316UbiquitinationGMKMEESKLIKAKES
CCCHHHHHCEEEHHH
58.47-
352UbiquitinationTDETRLQKEAEFEKS
CHHHHHHHHHHHHHH
64.58-
361SumoylationAEFEKSAKENLRDSK
HHHHHHHHHHHHCCH
54.98-
361SumoylationAEFEKSAKENLRDSK
HHHHHHHHHHHHCCH
54.98-
367PhosphorylationAKENLRDSKELRNFE
HHHHHHCCHHHHCCE
22.9220860994
385SumoylationIDDIMAIKMEDPKEI
HHHEEEEECCCHHHH
27.05-
385SumoylationIDDIMAIKMEDPKEI
HHHEEEEECCCHHHH
27.0528112733
412PhosphorylationHFPDFSYSASSKIII
CCCCCCCCCCCCEEE
22.0728555341
420PhosphorylationASSKIIISDVPSRKD
CCCCEEEECCCCCCC
23.3429083192
424PhosphorylationIIISDVPSRKDHMCH
EEEECCCCCCCCCCC
52.3829083192
449AcetylationAALNKPEKLKKKKKK
HHHCCHHHHHHHHHH
74.3020055403
452AcetylationNKPEKLKKKKKKSKM
CCHHHHHHHHHHHHC
79.0420055399
454AcetylationPEKLKKKKKKSKMDR
HHHHHHHHHHHHCCC
74.4520055407
467PhosphorylationDRHGNDKSTPKKTCK
CCCCCCCCCCHHHHC
53.4530576142
468PhosphorylationRHGNDKSTPKKTCKK
CCCCCCCCCHHHHCC
44.8828176443
478PhosphorylationKTCKKRQSSESDIES
HHHCCCCCCHHHHHH
39.8630278072
479PhosphorylationTCKKRQSSESDIESV
HHCCCCCCHHHHHHH
32.5530278072
481PhosphorylationKKRQSSESDIESVIY
CCCCCCHHHHHHHHH
45.9230278072
485PhosphorylationSSESDIESVIYTIEA
CCHHHHHHHHHHHHH
17.7230278072
488PhosphorylationSDIESVIYTIEAVAK
HHHHHHHHHHHHHHC
10.2523663014
489PhosphorylationDIESVIYTIEAVAKG
HHHHHHHHHHHHHCC
10.9623663014
502UbiquitinationKGDWGIEKLGDTPRK
CCCCCCCCCCCCCCC
56.71-
506PhosphorylationGIEKLGDTPRKKVRT
CCCCCCCCCCCEEEC
24.1627422710
513PhosphorylationTPRKKVRTSSSGKGS
CCCCEEECCCCCCCC
35.6323312004
514PhosphorylationPRKKVRTSSSGKGSI
CCCEEECCCCCCCCC
16.3721601212
515PhosphorylationRKKVRTSSSGKGSIL
CCEEECCCCCCCCCC
42.3629214152
516PhosphorylationKKVRTSSSGKGSILD
CEEECCCCCCCCCCC
44.2723532336
520O-linked_GlycosylationTSSSGKGSILDAKPP
CCCCCCCCCCCCCCC
24.3830059200
520PhosphorylationTSSSGKGSILDAKPP
CCCCCCCCCCCCCCC
24.3821601212
557PhosphorylationSRPPDFISISASKNI
CCCCCEEEEECCCCC
15.5228555341
559PhosphorylationPPDFISISASKNISG
CCCEEEEECCCCCCC
21.5025159151
565PhosphorylationISASKNISGETPEGI
EECCCCCCCCCCCCC
39.7130266825
568PhosphorylationSKNISGETPEGIKAE
CCCCCCCCCCCCCCC
30.1130266825
573SumoylationGETPEGIKAEPLTPM
CCCCCCCCCCCCCCH
58.5128112733
576 (in isoform 3)Phosphorylation-46.5230206219
578PhosphorylationGIKAEPLTPMEDALP
CCCCCCCCCHHHCCC
31.1626657352
587PhosphorylationMEDALPPSLSGQAKP
HHHCCCCCCCCCCCC
32.9725002506
589PhosphorylationDALPPSLSGQAKPED
HCCCCCCCCCCCCCC
32.9525002506
625PhosphorylationALYKTLVSEGMLTSL
HHHHHHHCCCHHHHH
31.3928555341
630PhosphorylationLVSEGMLTSLRANVD
HHCCCHHHHHHHHCC
19.4728555341
631PhosphorylationVSEGMLTSLRANVDR
HCCCHHHHHHHHCCC
16.3428555341
648PhosphorylationRSSGKGNSSDHEGCW
CCCCCCCCCCCCCCC
45.9023927012
649PhosphorylationSSGKGNSSDHEGCWN
CCCCCCCCCCCCCCC
47.1623927012
659PhosphorylationEGCWNEESWTFSQSG
CCCCCCCCEEEECCC
25.8228450419
661PhosphorylationCWNEESWTFSQSGTS
CCCCCCEEEECCCCC
23.7630108239
663PhosphorylationNEESWTFSQSGTSGS
CCCCEEEECCCCCCC
18.9627080861
665PhosphorylationESWTFSQSGTSGSKK
CCEEEECCCCCCCCC
42.7223927012
667PhosphorylationWTFSQSGTSGSKKFK
EEEECCCCCCCCCCC
34.8527080861
668PhosphorylationTFSQSGTSGSKKFKK
EEECCCCCCCCCCCC
44.5920068231
670PhosphorylationSQSGTSGSKKFKKTK
ECCCCCCCCCCCCCC
32.2323927012
676PhosphorylationGSKKFKKTKPKEDCL
CCCCCCCCCCHHHCC
53.84-
686PhosphorylationKEDCLLGSAKLDEEF
HHHCCCCCCCCCHHH
23.3821815630
696SumoylationLDEEFEKKFNSLPQY
CCHHHHHHHHCCCCC
42.45-
696SumoylationLDEEFEKKFNSLPQY
CCHHHHHHHHCCCCC
42.4528112733
696UbiquitinationLDEEFEKKFNSLPQY
CCHHHHHHHHCCCCC
42.45-
699PhosphorylationEFEKKFNSLPQYSPV
HHHHHHHCCCCCCCC
44.5523927012
703PhosphorylationKFNSLPQYSPVTFDR
HHHCCCCCCCCCCCC
17.0129255136
704PhosphorylationFNSLPQYSPVTFDRK
HHCCCCCCCCCCCCC
13.9829255136
707PhosphorylationLPQYSPVTFDRKCVP
CCCCCCCCCCCCCEE
24.1729255136
726PhosphorylationKKKTGNVSSEPTKTS
CCCCCCCCCCCCCCC
32.7422964224
727PhosphorylationKKTGNVSSEPTKTSK
CCCCCCCCCCCCCCC
43.22-
736 (in isoform 2)Phosphorylation-28.0424719451
750PhosphorylationNLFHKIVSKYKHKKE
HHHHHHHHHHCCCCC
33.4726270265
752PhosphorylationFHKIVSKYKHKKEKP
HHHHHHHHCCCCCCC
15.7226270265
773UbiquitinationSGDKWSNKQLFLDAI
CCCCCCCCEEHHHHH
42.75-
805PhosphorylationHKVKNIPSIFNTPEP
CHHCCCCCCCCCCCC
35.6925850435
809PhosphorylationNIPSIFNTPEPTTTQ
CCCCCCCCCCCCCCC
20.4825159151
813PhosphorylationIFNTPEPTTTQEPLV
CCCCCCCCCCCCCCC
40.5925850435
814PhosphorylationFNTPEPTTTQEPLVG
CCCCCCCCCCCCCCC
36.8825850435
815PhosphorylationNTPEPTTTQEPLVGS
CCCCCCCCCCCCCCC
33.1525850435
822PhosphorylationTQEPLVGSQKRKARK
CCCCCCCCHHHHCCC
25.6725159151
833PhosphorylationKARKTKITHLVRTAD
HCCCCCCCEEEECCC
15.6528555341
838PhosphorylationKITHLVRTADGRVSP
CCCEEEECCCCCCCC
22.9425159151
844PhosphorylationRTADGRVSPAGGTLD
ECCCCCCCCCCCCCC
13.9929255136
849PhosphorylationRVSPAGGTLDDKPKE
CCCCCCCCCCCCHHH
26.5420201521
873AcetylationTETDCNDKCSHNTEV
CCCCCCCCCCCCCCC
24.5226051181
885PhosphorylationTEVGETRSSTPEMPA
CCCCCCCCCCCCCHH
46.0828450419
886PhosphorylationEVGETRSSTPEMPAV
CCCCCCCCCCCCHHH
44.6928450419
887PhosphorylationVGETRSSTPEMPAVS
CCCCCCCCCCCHHHH
25.2328464451
898PhosphorylationPAVSAFFSLAALAEV
HHHHHHHHHHHHHHH
15.6228464451
917PhosphorylationNVHRGQRSTPLTHDG
CCCCCCCCCCCCCCC
26.8725159151
918PhosphorylationVHRGQRSTPLTHDGQ
CCCCCCCCCCCCCCC
25.2229978859
921PhosphorylationGQRSTPLTHDGQPKE
CCCCCCCCCCCCCCC
21.0829978859

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 BBX_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BBX_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 BBX_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SPAG1_HUMANSPAG1physical
27173435

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 BBX_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND MASSSPECTROMETRY.
"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-479; SER-485; THR-809AND SER-822, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND MASSSPECTROMETRY.
"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-159 AND THR-161, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-568, AND MASSSPECTROMETRY.

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