MYBA_HUMAN - dbPTM
MYBA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYBA_HUMAN
UniProt AC P10243
Protein Name Myb-related protein A {ECO:0000303|PubMed:7987850, ECO:0000303|PubMed:8058310}
Gene Name MYBL1
Organism Homo sapiens (Human).
Sequence Length 752
Subcellular Localization Nucleus .
Protein Description Transcription factor that specifically recognizes the sequence 5'-YAAC[GT]G-3'. [PubMed: 8058310]
Protein Sequence MAKRSRSEDEDDDLQYADHDYEVPQQKGLKKLWNRVKWTRDEDDKLKKLVEQHGTDDWTLIASHLQNRSDFQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSLIAKHLKGRIGKQCRERWHNHLNPEVKKSSWTEEEDRIIYEAHKRLGNRWAEIAKLLPGRTDNSIKNHWNSTMRRKVEQEGYLQDGIKSERSSSKLQHKPCAAMDHMQTQNQFYIPVQIPGYQYVSPEGNCIEHVQPTSAFIQQPFIDEDPDKEKKIKELEMLLMSAENEVRRKRIPSQPGSFSSWSGSFLMDDNMSNTLNSLDEHTSEFYSMDENQPVSAQQNSPTKFLAVEANAVLSSLQTIPEFAETLELIESDPVAWSDVTSFDISDAAASPIKSTPVKLMRIQHNEGAMECQFNVSLVLEGKKNTCNGGNSEAVPLTSPNIAKFSTPPAILRKKRKMRVGHSPGSELRDGSLNDGGNMALKHTPLKTLPFSPSQFFNTCPGNEQLNIENPSFTSTPICGQKALITTPLHKETTPKDQKENVGFRTPTIRRSILGTTPRTPTPFKNALAAQEKKYGPLKIVSQPLAFLEEDIREVLKEETGTDLFLKEEDEPAYKSCKQENTASGKKVRKSLVLDNWEKEESGTQLLTEDISDMQSENRFTTSLLMIPLLEIHDNRCNLIPEKQDINSTNKTYTLTKKKPNPNTSKVVKLEKNLQSNCEWETVVYGKTEDQLIMTEQARRYLSTYTATSSTSRALIL
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
5Phosphorylation---MAKRSRSEDEDD
---CCCCCCCCCCCC		39.1825159151
7Phosphorylation-MAKRSRSEDEDDDL
-CCCCCCCCCCCCCC		51.1225159151
16PhosphorylationDEDDDLQYADHDYEV
CCCCCCCCCCCCCCC		22.6928985074
21PhosphorylationLQYADHDYEVPQQKG
CCCCCCCCCCCHHHC		18.5327642862
79UbiquitinationQCQHRWQKVLNPELI
CCHHHHHHHHCHHHH		41.5521890473
79UbiquitinationQCQHRWQKVLNPELI
CCHHHHHHHHCHHHH		41.5521890473
87UbiquitinationVLNPELIKGPWTKEE
HHCHHHHCCCCCHHH		72.11-
92UbiquitinationLIKGPWTKEEDQRVI
HHCCCCCHHHHHHHH		56.06-
104UbiquitinationRVIELVQKYGPKRWS
HHHHHHHHHCHHHHH		44.7021890473
104UbiquitinationRVIELVQKYGPKRWS
HHHHHHHHHCHHHHH		44.7021890473
108UbiquitinationLVQKYGPKRWSLIAK
HHHHHCHHHHHHHHH		63.24-
138SumoylationNHLNPEVKKSSWTEE
HHCCHHHHHCCCCHH		45.32-
138UbiquitinationNHLNPEVKKSSWTEE
HHCCHHHHHCCCCHH		45.32-
138SumoylationNHLNPEVKKSSWTEE
HHCCHHHHHCCCCHH		45.32-
166UbiquitinationNRWAEIAKLLPGRTD
CHHHHHHHHCCCCCC		57.10-
199SumoylationGYLQDGIKSERSSSK
CCCHHCCCCCCCCCC		52.3628112733
199UbiquitinationGYLQDGIKSERSSSK
CCCHHCCCCCCCCCC		52.36-
394AcetylationPIKSTPVKLMRIQHN
CCCCCCEEEEEEECC		37.4619608861
418AcetylationVSLVLEGKKNTCNGG
EEEEEECCCCCCCCC		33.2125953088
433PhosphorylationNSEAVPLTSPNIAKF
CCCCCCCCCCCHHHC		35.7525627689
434PhosphorylationSEAVPLTSPNIAKFS
CCCCCCCCCCHHHCC		24.5125850435
441PhosphorylationSPNIAKFSTPPAILR
CCCHHHCCCCHHHHH		39.0222210691
442PhosphorylationPNIAKFSTPPAILRK
CCHHHCCCCHHHHHH		36.1027050516
458PhosphorylationRKMRVGHSPGSELRD
CCCCCCCCCCCCCCC		25.6530266825
461PhosphorylationRVGHSPGSELRDGSL
CCCCCCCCCCCCCCC		36.5227732954
477AcetylationDGGNMALKHTPLKTL
CCCCCCCCCCCCCCC		35.5725953088
479PhosphorylationGNMALKHTPLKTLPF
CCCCCCCCCCCCCCC		28.8227251275
521PhosphorylationCGQKALITTPLHKET
CCCEEEEECCCCCCC		24.1830266825
522PhosphorylationGQKALITTPLHKETT
CCEEEEECCCCCCCC		19.5030266825
541PhosphorylationKENVGFRTPTIRRSI
HCCCCCCCHHHHHHH		23.6323312004
543PhosphorylationNVGFRTPTIRRSILG
CCCCCCHHHHHHHCC		26.8823312004
547PhosphorylationRTPTIRRSILGTTPR
CCHHHHHHHCCCCCC		16.5922199227
551PhosphorylationIRRSILGTTPRTPTP
HHHHHCCCCCCCCCC		30.1322199227
552PhosphorylationRRSILGTTPRTPTPF
HHHHCCCCCCCCCCC		14.6922199227
555PhosphorylationILGTTPRTPTPFKNA
HCCCCCCCCCCCCHH		32.4922199227
557PhosphorylationGTTPRTPTPFKNALA
CCCCCCCCCCCHHHH		40.529417069
560AcetylationPRTPTPFKNALAAQE
CCCCCCCCHHHHHHH		42.3825953088
592SumoylationEDIREVLKEETGTDL
HHHHHHHHHHHCCCC		59.6928112733
602SumoylationTGTDLFLKEEDEPAY
HCCCCEECCCCCHHH		52.2928112733
602SumoylationTGTDLFLKEEDEPAY
HCCCCEECCCCCHHH		52.29-
617PhosphorylationKSCKQENTASGKKVR
HHHCCCCCCCCCCCH		22.8128555341
619PhosphorylationCKQENTASGKKVRKS
HCCCCCCCCCCCHHH		49.4528555341
621AcetylationQENTASGKKVRKSLV
CCCCCCCCCCHHHHH		45.6730586621
626PhosphorylationSGKKVRKSLVLDNWE
CCCCCHHHHHHCCCC		17.1022199227
643PhosphorylationESGTQLLTEDISDMQ
CHHCEEEECCHHHHH		39.9624043423
647PhosphorylationQLLTEDISDMQSENR
EEEECCHHHHHCCCC		39.0824043423
651PhosphorylationEDISDMQSENRFTTS
CCHHHHHCCCCCCCH		30.1524043423
678AcetylationRCNLIPEKQDINSTN
CCCCCCCCCCCCCCC		48.1726051181
683PhosphorylationPEKQDINSTNKTYTL
CCCCCCCCCCCEEEE		33.4229978859
684PhosphorylationEKQDINSTNKTYTLT
CCCCCCCCCCEEEEE		35.9229978859
686UbiquitinationQDINSTNKTYTLTKK
CCCCCCCCEEEEEEC		42.89-
687PhosphorylationDINSTNKTYTLTKKK
CCCCCCCEEEEEECC		24.6529978859
688PhosphorylationINSTNKTYTLTKKKP
CCCCCCEEEEEECCC		11.0229978859
689PhosphorylationNSTNKTYTLTKKKPN
CCCCCEEEEEECCCC		32.9329978859
691PhosphorylationTNKTYTLTKKKPNPN
CCCEEEEEECCCCCC		32.7729978859
704AcetylationPNTSKVVKLEKNLQS
CCHHHHEEEHHHHHH		54.6520167786
743PhosphorylationYLSTYTATSSTSRAL
HHHHHCCCCCCCCEE		18.5328555341
745PhosphorylationSTYTATSSTSRALIL
HHHCCCCCCCCEECC		26.5068696077
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
7SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYBA_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 MYBA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUCL_HUMANNCLphysical
10660576
LIN9_HUMANLIN9physical
28514442
LIN52_HUMANLIN52physical
28514442
LIN54_HUMANLIN54physical
28514442
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 MYBA_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-394, AND MASS SPECTROMETRY.

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