MYB_HUMAN - dbPTM
MYB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYB_HUMAN
UniProt AC P10242
Protein Name Transcriptional activator Myb
Gene Name MYB
Organism Homo sapiens (Human).
Sequence Length 640
Subcellular Localization Nucleus .
Protein Description Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells..
Protein Sequence MARRPRHSIYSSDEDDEDFEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQESSKASQPAVATSFQKNSHLMGFAQAPPTAQLPATGQPTVNNDYSYYHISEAQNVSSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQVLPTQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGEHHSTPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSDLEMPSLTSTPLIGHKLTVTTPFHRDQTVKTQKENTVFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHLVEDLQDVIKQESDESGIVAEFQENGPPLLKKIKQEVESPTDKSGNFFCSHHWEGDSLNTQLFTQTSPVADAPNILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQPCSSTWEPASCGKMEEQMTSSSQARKYVNAFSARTLVM
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
8PhosphorylationMARRPRHSIYSSDED
CCCCCCCCCCCCCCC
25.2230576142
10PhosphorylationRRPRHSIYSSDEDDE
CCCCCCCCCCCCCCC
12.7227251275
11PhosphorylationRPRHSIYSSDEDDED
CCCCCCCCCCCCCCC
29.6411522824
11 (in isoform 4)Phosphorylation-29.6427642862
12PhosphorylationPRHSIYSSDEDDEDF
CCCCCCCCCCCCCCC
28.2211522824
12 (in isoform 4)Phosphorylation-28.2227642862
26 (in isoform 4)Phosphorylation-14.4327642862
26PhosphorylationFEMCDHDYDGLLPKS
CCCCCCCCCCCCCCC
14.4327251275
44 (in isoform 4)Phosphorylation-25.5524719451
44PhosphorylationHLGKTRWTREEDEKL
CCCCCCCCHHHHHHH
25.5524719451
53UbiquitinationEEDEKLKKLVEQNGT
HHHHHHHHHHHHHCC
69.10-
53 (in isoform 4)Ubiquitination-69.10-
69PhosphorylationDWKVIANYLPNRTDV
CHHHHHHHCCCCCCC
17.95-
84UbiquitinationQCQHRWQKVLNPELI
CCHHHHHHHHCHHHH
41.5521890473
84 (in isoform 4)Ubiquitination-41.5521890473
84 (in isoform 1)Ubiquitination-41.5521890473
84 (in isoform 2)Ubiquitination-41.5521890473
84 (in isoform 3)Ubiquitination-41.5521890473
84 (in isoform 5)Ubiquitination-41.5521890473
84 (in isoform 6)Ubiquitination-41.5521890473
84UbiquitinationQCQHRWQKVLNPELI
CCHHHHHHHHCHHHH
41.5521890473
84UbiquitinationQCQHRWQKVLNPELI
CCHHHHHHHHCHHHH
41.5521890473
92UbiquitinationVLNPELIKGPWTKEE
HHCHHHHCCCCCHHH
72.11-
92 (in isoform 4)Ubiquitination-72.11-
97UbiquitinationLIKGPWTKEEDQRVI
HHCCCCCHHHHHHHH
56.06-
97 (in isoform 4)Ubiquitination-56.06-
109UbiquitinationRVIELVQKYGPKRWS
HHHHHHHHHCCHHHH
44.702189047
109 (in isoform 4)Ubiquitination-44.7021890473
109 (in isoform 1)Ubiquitination-44.7021890473
109 (in isoform 2)Ubiquitination-44.7021890473
109 (in isoform 3)Ubiquitination-44.7021890473
109 (in isoform 5)Ubiquitination-44.7021890473
109 (in isoform 6)Ubiquitination-44.7021890473
109UbiquitinationRVIELVQKYGPKRWS
HHHHHHHHHCCHHHH
44.7021890473
109UbiquitinationRVIELVQKYGPKRWS
HHHHHHHHHCCHHHH
44.7021890473
113UbiquitinationLVQKYGPKRWSVIAK
HHHHHCCHHHHHHHH
63.24-
120UbiquitinationKRWSVIAKHLKGRIG
HHHHHHHHHHHHHHH
38.04-
120 (in isoform 4)Ubiquitination-38.04-
130S-nitrosocysteineKGRIGKQCRERWHNH
HHHHHHHHHHHHHHH
5.78-
130S-nitrosylationKGRIGKQCRERWHNH
HHHHHHHHHHHHHHH
5.7822178444
143SumoylationNHLNPEVKKTSWTEE
HHCCHHHHCCCCCHH
48.98-
143SumoylationNHLNPEVKKTSWTEE
HHCCHHHHCCCCCHH
48.98-
143UbiquitinationNHLNPEVKKTSWTEE
HHCCHHHHCCCCCHH
48.98-
160UbiquitinationRIIYQAHKRLGNRWA
HHHHHHHHHHHCHHH
52.94-
160 (in isoform 4)Ubiquitination-52.94-
171UbiquitinationNRWAEIAKLLPGRTD
CHHHHHHHHCCCCCC
57.10-
171 (in isoform 4)Ubiquitination-57.10-
182UbiquitinationGRTDNAIKNHWNSTM
CCCCHHHHHHHHHHH
40.11-
182 (in isoform 4)Ubiquitination-40.11-
192UbiquitinationWNSTMRRKVEQEGYL
HHHHHHHHHHHCCCC
39.50-
192 (in isoform 4)Ubiquitination-39.50-
204UbiquitinationGYLQESSKASQPAVA
CCCCCCCCCCCCCCH
62.43-
204 (in isoform 4)Ubiquitination-62.43-
291UbiquitinationYNDEDPEKEKRIKEL
CCCCCHHHHHHHHHH
74.13-
291 (in isoform 4)Ubiquitination-74.13-
293UbiquitinationDEDPEKEKRIKELEL
CCCHHHHHHHHHHHH
71.18-
296UbiquitinationPEKEKRIKELELLLM
HHHHHHHHHHHHHHH
61.35-
296 (in isoform 4)Ubiquitination-61.35-
304PhosphorylationELELLLMSTENELKG
HHHHHHHHCCCCCCC
32.3229083192
305PhosphorylationLELLLMSTENELKGQ
HHHHHHHCCCCCCCC
28.9430576142
333PhosphorylationGWHSTTIADHTRPHG
CCEECEECCCCCCCC
10.63-
363PhosphorylationSLPADPGSLPEESAS
CCCCCCCCCCHHHCC
46.2526074081
368PhosphorylationPGSLPEESASPARCM
CCCCCHHHCCCCEEE
32.1726074081
370PhosphorylationSLPEESASPARCMIV
CCCHHHCCCCEEEEE
28.5026074081
381PhosphorylationCMIVHQGTILDNVKN
EEEEECCCHHHHHHH
16.2826074081
386AcetylationQGTILDNVKNLLEFA
CCCHHHHHHHHHHHH
4.3119608861
386UbiquitinationQGTILDNVKNLLEFA
CCCHHHHHHHHHHHH
4.3119608861
395AcetylationNLLEFAETLQFIDSF
HHHHHHHHHHHHHHH
23.5619608861
395UbiquitinationNLLEFAETLQFIDSF
HHHHHHHHHHHHHHH
23.5619608861
400AcetylationAETLQFIDSFLNTSS
HHHHHHHHHHHCCCC
34.3310656693
405PhosphorylationFIDSFLNTSSNHENS
HHHHHHCCCCCCCCC
35.3626074081
406PhosphorylationIDSFLNTSSNHENSD
HHHHHCCCCCCCCCC
28.2426074081
407PhosphorylationDSFLNTSSNHENSDL
HHHHCCCCCCCCCCC
39.9226074081
418PhosphorylationNSDLEMPSLTSTPLI
CCCCCCCCCCCCCCC
42.86-
420PhosphorylationDLEMPSLTSTPLIGH
CCCCCCCCCCCCCCC
34.59-
432PhosphorylationIGHKLTVTTPFHRDQ
CCCEEEEECCCCCCC
24.4227251275
433PhosphorylationGHKLTVTTPFHRDQT
CCEEEEECCCCCCCC
21.4427251275
436AcetylationLTVTTPFHRDQTVKT
EEEECCCCCCCCCCC
33.3419608861
436UbiquitinationLTVTTPFHRDQTVKT
EEEECCCCCCCCCCC
33.3419608861
442UbiquitinationFHRDQTVKTQKENTV
CCCCCCCCCCCCCCE
48.93-
445AcetylationDQTVKTQKENTVFRT
CCCCCCCCCCCEECC
59.1523749302
445UbiquitinationDQTVKTQKENTVFRT
CCCCCCCCCCCEECC
59.1519608861
448PhosphorylationVKTQKENTVFRTPAI
CCCCCCCCEECCHHH
23.3224719451
450AcetylationTQKENTVFRTPAIKR
CCCCCCEECCHHHHH
7.2910656693
452PhosphorylationKENTVFRTPAIKRSI
CCCCEECCHHHHHHH
12.9528348404
457MethylationFRTPAIKRSILESSP
ECCHHHHHHHHHCCC
23.86115384183
457 (in isoform 8)Phosphorylation-23.8622210691
458PhosphorylationRTPAIKRSILESSPR
CCHHHHHHHHHCCCC
26.9028111955
458 (in isoform 8)Phosphorylation-26.9022210691
462PhosphorylationIKRSILESSPRTPTP
HHHHHHHCCCCCCCC
42.0426074081
463PhosphorylationKRSILESSPRTPTPF
HHHHHHCCCCCCCCC
14.7126074081
465MethylationSILESSPRTPTPFKH
HHHHCCCCCCCCCHH
56.11115384193
466PhosphorylationILESSPRTPTPFKHA
HHHCCCCCCCCCHHH
34.5926074081
468PhosphorylationESSPRTPTPFKHALA
HCCCCCCCCCHHHHH
40.5226074081
468AcetylationESSPRTPTPFKHALA
HCCCCCCCCCHHHHH
40.5219608861
468UbiquitinationESSPRTPTPFKHALA
HCCCCCCCCCHHHHH
40.5219608861
470 (in isoform 7)Phosphorylation-11.3022210691
471MethylationPRTPTPFKHALAAQE
CCCCCCCHHHHHHCC
29.2260111
471AcetylationPRTPTPFKHALAAQE
CCCCCCCHHHHHHCC
29.2219608861
471UbiquitinationPRTPTPFKHALAAQE
CCCCCCCHHHHHHCC
29.2219608861
471 (in isoform 7)Phosphorylation-29.2222210691
473 (in isoform 4)Phosphorylation-10.2522210691
474 (in isoform 4)Phosphorylation-3.9822210691
477AcetylationFKHALAAQEIKYGPL
CHHHHHHCCCCCCCC
47.5419608861
477UbiquitinationFKHALAAQEIKYGPL
CHHHHHHCCCCCCCC
47.5419608861
480AcetylationALAAQEIKYGPLKML
HHHHCCCCCCCCCCC
43.3219608861
480SumoylationALAAQEIKYGPLKML
HHHHCCCCCCCCCCC
43.32-
480UbiquitinationALAAQEIKYGPLKML
HHHHCCCCCCCCCCC
43.3219608861
480SumoylationALAAQEIKYGPLKML
HHHHCCCCCCCCCCC
43.3228112733
482AcetylationAAQEIKYGPLKMLPQ
HHCCCCCCCCCCCCC
18.9610656693
485AcetylationEIKYGPLKMLPQTPS
CCCCCCCCCCCCCHH
41.3410656693
485UbiquitinationEIKYGPLKMLPQTPS
CCCCCCCCCCCCCHH
41.34-
490PhosphorylationPLKMLPQTPSHLVED
CCCCCCCCHHHHHHH
25.4828634298
492PhosphorylationKMLPQTPSHLVEDLQ
CCCCCCHHHHHHHHH
32.6128634298
503SumoylationEDLQDVIKQESDESG
HHHHHHHHHHCCCCC
48.11-
503SumoylationEDLQDVIKQESDESG
HHHHHHHHHHCCCCC
48.11-
527SumoylationPPLLKKIKQEVESPT
CHHHHHHHHHHCCCC
49.65-
527SumoylationPPLLKKIKQEVESPT
CHHHHHHHHHHCCCC
49.65-
532PhosphorylationKIKQEVESPTDKSGN
HHHHHHCCCCCCCCC
37.9723401153
534PhosphorylationKQEVESPTDKSGNFF
HHHHCCCCCCCCCEE
66.402202948
553 (in isoform 4)Phosphorylation-31.7627251275
557PhosphorylationSLNTQLFTQTSPVAD
CCCCEEEEECCCCCC
39.2626074081
559PhosphorylationNTQLFTQTSPVADAP
CCEEEEECCCCCCCC
31.7526074081
560PhosphorylationTQLFTQTSPVADAPN
CEEEEECCCCCCCCC
13.9426074081
563 (in isoform 4)Ubiquitination-15.61-
566 (in isoform 4)Ubiquitination-29.01-
573 (in isoform 4)Phosphorylation-4.1927251275
576AcetylationLTSSVLMAPASEDED
CCCCEEECCCCCCCC
7.7319608861
576UbiquitinationLTSSVLMAPASEDED
CCCCEEECCCCCCCC
7.7319608861
584 (in isoform 4)Phosphorylation-38.6927251275
585AcetylationASEDEDNVLKAFTVP
CCCCCCCCCHHEECC
10.0519608861
585UbiquitinationASEDEDNVLKAFTVP
CCCCCCCCCHHEECC
10.0519608861
587 (in isoform 4)Phosphorylation-36.8524719451
589AcetylationEDNVLKAFTVPKNRS
CCCCCHHEECCCCCC
7.2719608861
589UbiquitinationEDNVLKAFTVPKNRS
CCCCCHHEECCCCCC
7.2719608861
590AcetylationDNVLKAFTVPKNRSL
CCCCHHEECCCCCCC
40.5310656693
592 (in isoform 4)Ubiquitination-25.75-
592AcetylationVLKAFTVPKNRSLAS
CCHHEECCCCCCCCC
25.7519608861
592UbiquitinationVLKAFTVPKNRSLAS
CCHHEECCCCCCCCC
25.7519608861
593UbiquitinationLKAFTVPKNRSLASP
CHHEECCCCCCCCCC
61.73-
596PhosphorylationFTVPKNRSLASPLQP
EECCCCCCCCCCCCC
37.3728464451
598AcetylationVPKNRSLASPLQPCS
CCCCCCCCCCCCCCC
15.4519608861
598UbiquitinationVPKNRSLASPLQPCS
CCCCCCCCCCCCCCC
15.4519608861
599PhosphorylationPKNRSLASPLQPCSS
CCCCCCCCCCCCCCC
31.2823401153
601 (in isoform 4)Ubiquitination-9.10-
601AcetylationNRSLASPLQPCSSTW
CCCCCCCCCCCCCCC
9.1019608861
601UbiquitinationNRSLASPLQPCSSTW
CCCCCCCCCCCCCCC
9.1019608861
603AcetylationSLASPLQPCSSTWEP
CCCCCCCCCCCCCCC
27.8610656693
605PhosphorylationASPLQPCSSTWEPAS
CCCCCCCCCCCCCCC
37.1726552605
606PhosphorylationSPLQPCSSTWEPASC
CCCCCCCCCCCCCCC
44.2326552605
606AcetylationSPLQPCSSTWEPASC
CCCCCCCCCCCCCCC
44.2310656693
607PhosphorylationPLQPCSSTWEPASCG
CCCCCCCCCCCCCCC
19.9726552605
612PhosphorylationSSTWEPASCGKMEEQ
CCCCCCCCCCCCHHH
33.8326552605
615UbiquitinationWEPASCGKMEEQMTS
CCCCCCCCCHHHHCC
47.68-
615AcetylationWEPASCGKMEEQMTS
CCCCCCCCCHHHHCC
47.6825953088
621PhosphorylationGKMEEQMTSSSQARK
CCCHHHHCCHHHHHH
25.75-
624PhosphorylationEEQMTSSSQARKYVN
HHHHCCHHHHHHHHH
27.85-
628UbiquitinationTSSSQARKYVNAFSA
CCHHHHHHHHHHHHH
57.47-
653 (in isoform 4)Phosphorylation-24719451
680 (in isoform 4)Phosphorylation-27251275
714 (in isoform 4)Ubiquitination--
720 (in isoform 4)Phosphorylation-24719451
736 (in isoform 4)Ubiquitination--
749 (in isoform 4)Ubiquitination--

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
11SPhosphorylationKinaseCSNK2A1P68400
GPS
11SPhosphorylationKinaseCK2-FAMILY-GPS
11SPhosphorylationKinaseCK2_GROUP-PhosphoELM
12SPhosphorylationKinaseCSNK2A1P68400
GPS
12SPhosphorylationKinaseCK2-FAMILY-GPS
12SPhosphorylationKinaseCK2_GROUP-PhosphoELM
532SPhosphorylationKinaseMAPK3P27361
GPS
532SPhosphorylationKinaseMAPK-FAMILY-GPS
532SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:18765672
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:10747903

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYB_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 MYB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBP_HUMANCREBBPgenetic
11423988
NUCL_HUMANNCLphysical
10660576
CEBPB_HUMANCEBPBphysical
11792321
CEBPE_HUMANCEBPEphysical
10233885
MAF_HUMANMAFphysical
9566892
SND1_HUMANSND1physical
8756344
PAX5_HUMANPAX5physical
11781241
FBXW7_HUMANFBXW7physical
18765672
ZMY11_HUMANZMYND11physical
11244510
KMT2A_HUMANKMT2Aphysical
20093773
WDR5_HUMANWDR5physical
20093773
RBBP5_HUMANRBBP5physical
20093773
ASH2L_HUMANASH2Lphysical
20093773
MEN1_HUMANMEN1physical
20093773
SP100_HUMANSP100physical
20211142
PARP1_HUMANPARP1physical
18945670
HIPK2_HUMANHIPK2physical
15082531
EP300_HUMANEP300physical
11585920
TIF1B_HUMANTRIM28physical
14761981
SKI_HUMANSKIphysical
14761981
SIN3A_HUMANSIN3Aphysical
14761981
NCOR1_HUMANNCOR1physical
14761981
UBC9_HUMANUBE2Iphysical
11779867
CHD3_HUMANCHD3physical
17344210
EP300_HUMANEP300physical
20364308
KAT2B_HUMANKAT2Bphysical
20364308
FBXW7_MOUSEFbxw7physical
19421138
KAT5_HUMANKAT5physical
22110127
TRAF6_HUMANTRAF6physical
18093978
FBXW5_HUMANFBXW5physical
22910413
DDB1_HUMANDDB1physical
22910413
CUL4A_HUMANCUL4Aphysical
22910413
PIAS1_HUMANPIAS1physical
21338522
MYOZ2_HUMANMYOZ2physical
21988832
PPM1K_HUMANPPM1Kphysical
21988832
ERC2_HUMANERC2physical
20195357
RENT2_HUMANUPF2physical
20195357
FBXW7_HUMANFBXW7physical
21092141
PIAS1_HUMANPIAS1physical
27032383

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 MYB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-480, AND MASSSPECTROMETRY.

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