PAXB1_HUMAN - dbPTM
PAXB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAXB1_HUMAN
UniProt AC Q9Y5B6
Protein Name PAX3- and PAX7-binding protein 1
Gene Name PAXBP1
Organism Homo sapiens (Human).
Sequence Length 917
Subcellular Localization Nucleus.
Protein Description Adapter protein linking the transcription factors PAX3 and PAX7 to the histone methylation machinery and involved in myogenesis. Associates with a histone methyltransferase complex that specifically mediates dimethylation and trimethylation of 'Lys-4' of histone H3. Mediates the recruitment of that complex to the transcription factors PAX3 and PAX7 on chromatin to regulate the expression of genes involved in muscle progenitor cells proliferation including ID3 and CDC20 (By similarity)..
Protein Sequence MFRKARRVNVRKRNDSEEEERERDEEQEPPPLLPPPGTGEEAGPGGGDRAPGGESLLGPGPSPPSALTPGLGAEAGGGFPGGAEPGNGLKPRKRPRENKEVPRASLLSFQDEEEENEEVFKVKKSSYSKKIVKLLKKEYKEDLEKSKIKTELNSSAESEQPLDKTGHVKDTNQEDGVIISEHGEDEMDMESEKEEEKPKTGGAFSNALSSLNVLRPGEIPDAAFIHAARKKRQMARELGDFTPHDNEPGKGRLVREDENDASDDEDDDEKRRIVFSVKEKSQRQKIAEEIGIEGSDDDALVTGEQDEELSRWEQEQIRKGINIPQVQASQPAEVNMYYQNTYQTMPYGSSYGIPYSYTAYGSSDAKSQKTDNTVPFKTPSNEMTPVTIDLVKKQLKDRLDSMKELHKTNRQQHEKHLQSRVDSTRAIERLEGSSGGIGERYKFLQEMRGYVQDLLECFSEKVPLINELESAIHQLYKQRASRLVQRRQDDIKDESSEFSSHSNKALMAPNLDSFGRDRALYQEHAKRRIAEREARRTRRRQAREQTGKMADHLEGLSSDDEETSTDITNFNLEKDRISKESGKVFEDVLESFYSIDCIKSQFEAWRSKYYTSYKDAYIGLCLPKLFNPLIRLQLLTWTPLEAKCRDFENMLWFESLLFYGCEEREQEKDDVDVALLPTIVEKVILPKLTVIAENMWDPFSTTQTSRMVGITLKLINGYPSVVNAENKNTQVYLKALLLRMRRTLDDDVFMPLYPKNVLENKNSGPYLFFQRQFWSSVKLLGNFLQWYGIFSNKTLQELSIDGLLNRYILMAFQNSEYGDDSIKKAQNVINCFPKQWFMNLKGERTISQLENFCRYLVHLADTIYRNSIGCSDVEKRNARENIKQIVKLLASVRALDHAMSVASDHNVKEFKSLIEGK
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
16PhosphorylationNVRKRNDSEEEERER
CCCCCCCCHHHHHHH
28355574
38PhosphorylationPLLPPPGTGEEAGPG
CCCCCCCCCCCCCCC
20873877
55PhosphorylationDRAPGGESLLGPGPS
CCCCCCCCCCCCCCC
25850435
62PhosphorylationSLLGPGPSPPSALTP
CCCCCCCCCCCCCCC
26055452
65PhosphorylationGPGPSPPSALTPGLG
CCCCCCCCCCCCCCC
25850435
68PhosphorylationPSPPSALTPGLGAEA
CCCCCCCCCCCCCCC
25850435
108PhosphorylationVPRASLLSFQDEEEE
CCHHHHHCCCCCHHH
25159151
121MethylationEENEEVFKVKKSSYS
HHCHHHEEECHHHHH
-
123MethylationNEEVFKVKKSSYSKK
CHHHEEECHHHHHHH
-
149SumoylationDLEKSKIKTELNSSA
HHHHHHCCHHHCCCC
-
149SumoylationDLEKSKIKTELNSSA
HHHHHHCCHHHCCCC
25114211
150PhosphorylationLEKSKIKTELNSSAE
HHHHHCCHHHCCCCC
21712546
154PhosphorylationKIKTELNSSAESEQP
HCCHHHCCCCCCCCC
25159151
155PhosphorylationIKTELNSSAESEQPL
CCHHHCCCCCCCCCC
25159151
158PhosphorylationELNSSAESEQPLDKT
HHCCCCCCCCCCCCC
25159151
164AcetylationESEQPLDKTGHVKDT
CCCCCCCCCCCCCCC
23236377
171PhosphorylationKTGHVKDTNQEDGVI
CCCCCCCCCCCCCEE
21955146
180PhosphorylationQEDGVIISEHGEDEM
CCCCEEEECCCCCCC
30576142
191PhosphorylationEDEMDMESEKEEEKP
CCCCCCHHHCHHCCC
21955146
193AcetylationEMDMESEKEEEKPKT
CCCCHHHCHHCCCCC
7339679
197SumoylationESEKEEEKPKTGGAF
HHHCHHCCCCCCCHH
-
197SumoylationESEKEEEKPKTGGAF
HHHCHHCCCCCCCHH
-
210PhosphorylationAFSNALSSLNVLRPG
HHHHHHHHCCCCCCC
28555341
242PhosphorylationARELGDFTPHDNEPG
HHHHCCCCCCCCCCC
26657352
250AcetylationPHDNEPGKGRLVRED
CCCCCCCCCCCCCCC
25953088
262PhosphorylationREDENDASDDEDDDE
CCCCCCCCCCCCCHH
20201521
276PhosphorylationEKRRIVFSVKEKSQR
HHHHHEEEECCHHHH
23312004
278AcetylationRRIVFSVKEKSQRQK
HHHEEEECCHHHHHH
23749302
295PhosphorylationEEIGIEGSDDDALVT
HHHCCCCCCCCCEEC
30266825
302PhosphorylationSDDDALVTGEQDEEL
CCCCCEECCCCCHHH
28176443
377AcetylationTDNTVPFKTPSNEMT
CCCCCCCCCCCCCCC
25953088
378PhosphorylationDNTVPFKTPSNEMTP
CCCCCCCCCCCCCCC
20068231
380PhosphorylationTVPFKTPSNEMTPVT
CCCCCCCCCCCCCCH
20068231
383SulfoxidationFKTPSNEMTPVTIDL
CCCCCCCCCCCHHHH
21406390
384PhosphorylationKTPSNEMTPVTIDLV
CCCCCCCCCCHHHHH
27732954
387PhosphorylationSNEMTPVTIDLVKKQ
CCCCCCCHHHHHHHH
20068231
401O-linked_GlycosylationQLKDRLDSMKELHKT
HHHHHHHHHHHHHHH
30379171
433PhosphorylationAIERLEGSSGGIGER
HHHHHHCCCCCHHHH
20860994
434PhosphorylationIERLEGSSGGIGERY
HHHHHCCCCCHHHHH
26699800
441PhosphorylationSGGIGERYKFLQEMR
CCCHHHHHHHHHHHH
26699800
442UbiquitinationGGIGERYKFLQEMRG
CCHHHHHHHHHHHHH
-
476PhosphorylationESAIHQLYKQRASRL
HHHHHHHHHHHHHHH
-
492AcetylationQRRQDDIKDESSEFS
HHHHHHCCCCCHHCH
26051181
492SumoylationQRRQDDIKDESSEFS
HHHHHHCCCCCHHCH
-
492SumoylationQRRQDDIKDESSEFS
HHHHHHCCCCCHHCH
-
495PhosphorylationQDDIKDESSEFSSHS
HHHCCCCCHHCHHHC
20873877
496PhosphorylationDDIKDESSEFSSHSN
HHCCCCCHHCHHHCC
20873877
507SulfoxidationSHSNKALMAPNLDSF
HHCCCCEECCCHHHC
21406390
513PhosphorylationLMAPNLDSFGRDRAL
EECCCHHHCCCHHHH
28555341
521PhosphorylationFGRDRALYQEHAKRR
CCCHHHHHHHHHHHH
27642862
546PhosphorylationRRQAREQTGKMADHL
HHHHHHHHHCHHHHH
22468782
557PhosphorylationADHLEGLSSDDEETS
HHHHCCCCCCCCCCC
20201521
558PhosphorylationDHLEGLSSDDEETST
HHHCCCCCCCCCCCC
20201521
563PhosphorylationLSSDDEETSTDITNF
CCCCCCCCCCCCCCC
21955146
564PhosphorylationSSDDEETSTDITNFN
CCCCCCCCCCCCCCC
30278072
565PhosphorylationSDDEETSTDITNFNL
CCCCCCCCCCCCCCH
25022875
568PhosphorylationEETSTDITNFNLEKD
CCCCCCCCCCCHHHH
23403867
624UbiquitinationYIGLCLPKLFNPLIR
CHHHHHHHHHCHHHH
-
682 (in isoform 2)Ubiquitination-21890473
682 (in isoform 1)Ubiquitination-21890473
682UbiquitinationLLPTIVEKVILPKLT
HHHHHHHHCHHHCCE
21890473
718PhosphorylationTLKLINGYPSVVNAE
EEEECCCCCCCCCCC
23403867
720PhosphorylationKLINGYPSVVNAENK
EECCCCCCCCCCCCC
23403867
729PhosphorylationVNAENKNTQVYLKAL
CCCCCCCHHHHHHHH
22461510
732PhosphorylationENKNTQVYLKALLLR
CCCCHHHHHHHHHHH
23612710
807PhosphorylationIDGLLNRYILMAFQN
HHHHHHHHHHHHHHC
26270265
815PhosphorylationILMAFQNSEYGDDSI
HHHHHHCCCCCCHHH
26270265
817PhosphorylationMAFQNSEYGDDSIKK
HHHHCCCCCCHHHHH
26270265
834AcetylationNVINCFPKQWFMNLK
HHHHHCCHHHHHHCC
26051181
855PhosphorylationQLENFCRYLVHLADT
HHHHHHHHHHHHHHH
20068231
875AcetylationIGCSDVEKRNARENI
CCCCHHHHHHHHHHH
26051181
887AcetylationENIKQIVKLLASVRA
HHHHHHHHHHHHHHH
25953088

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 PAXB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAXB1_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 PAXB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PAXB1_HUMAN !!

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 PAXB1_HUMAN

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Related Literatures of Post-Translational Modification

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