MYT1L_HUMAN - dbPTM
MYT1L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYT1L_HUMAN
UniProt AC Q9UL68
Protein Name Myelin transcription factor 1-like protein {ECO:0000303|Ref.1}
Gene Name MYT1L {ECO:0000303|Ref.1, ECO:0000312|HGNC:HGNC:7623}
Organism Homo sapiens (Human).
Sequence Length 1186
Subcellular Localization Nucleus . Chromosome . Preferentially binds to DNA binding sites that are in an open chromatin configuration.
Protein Description Transcription factor that plays a key role in neuronal differentiation by specifically repressing expression of non-neuronal genes during neuron differentiation. In contrast to other transcription repressors that inhibit specific lineages, mediates repression of multiple differentiation programs. Also represses expression of negative regulators of neurogenesis, such as members of the Notch signaling pathway, including HES1. The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro. Directly binds the 5'-AAGTT-3' core motif present on the promoter of target genes and represses transcription by recruiting a multiprotein complex containing SIN3B. The 5'-AAGTT-3' core motif is absent from the promoter of neural genes..
Protein Sequence MEVDTEEKRHRTRSKGVRVPVEPAIQELFSCPTPGCDGSGHVSGKYARHRSVYGCPLAKKRKTQDKQPQEPAPKRKPFAVKADSSSVDECDDSDGTEDMDEKEEDEGEEYSEDNDEPGDEDEEDEEGDREEEEEIEEEDEDDDEDGEDVEDEEEEEEEEEEEEEEEENEDHQMNCHNTRIMQDTEKDDNNNDEYDNYDELVAKSLLNLGKIAEDAAYRARTESEMNSNTSNSLEDDSDKNENLGRKSELSLDLDSDVVRETVDSLKLLAQGHGVVLSENMNDRNYADSMSQQDSRNMNYVMLGKPMNNGLMEKMVEESDEEVCLSSLECLRNQCFDLARKLSETNPQERNPQQNMNIRQHVRPEEDFPGRTPDRNYSDMLNLMRLEEQLSPRSRVFASCAKEDGCHERDDDTTSVNSDRSEEVFDMTKGNLTLLEKAIALETERAKAMREKMAMEAGRRDNMRSYEDQSPRQLPGEDRKPKSSDSHVKKPYYGKDPSRTEKKESKCPTPGCDGTGHVTGLYPHHRSLSGCPHKDRVPPEILAMHESVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAKAQEKHQSCDVSKSSQASDRVLRPMCFVKQLEIPQYGYRNNVPTTTPRSNLAKELEKYSKTSFEYNSYDNHTYGKRAIAPKVQTRDISPKGYDDAKRYCKDPSPSSSSTSSYAPSSSSNLSCGGGSSASSTCSKSSFDYTHDMEAAHMAATAILNLSTRCREMPQNLSTKPQDLCATRNPDMEVDENGTLDLSMNKQRPRDSCCPILTPLEPMSPQQQAVMNNRCFQLGEGDCWDLPVDYTKMKPRRIDEDESKDITPEDLDPFQEALEERRYPGEVTIPSPKPKYPQCKESKKDLITLSGCPLADKSIRSMLATSSQELKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGIRIAQSKEDKEDQEPIRCPVPGCDGQGHITGKYASHRSASGCPLAAKRQKDGYLNGSQFSWKSVKTEGMSCPTPGCDGSGHVSGSFLTHRSLSGCPRATSAMKKAKLSGEQMLTIKQRASNGIENDEEIKQLDEEIKELNESNSQMEADMIKLRTQITTMESNLKTIEEENKVIEQQNESLLHELANLSQSLIHSLANIQLPHMDPINEQNFDAYVTTLTEMYTNQDRYQSPENKALLENIKQAVRGIQV
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
221PhosphorylationDAAYRARTESEMNSN
HHHHHHHCHHHHCCC
42.76-
223PhosphorylationAYRARTESEMNSNTS
HHHHHCHHHHCCCCC
41.34-
237PhosphorylationSNSLEDDSDKNENLG
CCCCCCCCCCCCCCC
63.91-
250PhosphorylationLGRKSELSLDLDSDV
CCCHHHHHCCCCHHH
18.78-
325PhosphorylationSDEEVCLSSLECLRN
CCHHHHHHHHHHHHH
27.9622817900
342PhosphorylationFDLARKLSETNPQER
HHHHHHHHHCCCCCC
45.4722817900
390PhosphorylationMRLEEQLSPRSRVFA
HHHHHHCCCCHHHHH
20.2627732954
442PhosphorylationEKAIALETERAKAMR
HHHHHHHHHHHHHHH
31.4624114839
464PhosphorylationGRRDNMRSYEDQSPR
HCHHCHHCCCCCCCC
23.3128122231
465PhosphorylationRRDNMRSYEDQSPRQ
CHHCHHCCCCCCCCC
17.1128122231
469PhosphorylationMRSYEDQSPRQLPGE
HHCCCCCCCCCCCCC
34.0828122231
526PhosphorylationGLYPHHRSLSGCPHK
CCCCCCCCCCCCCCC
23.6427251275
528PhosphorylationYPHHRSLSGCPHKDR
CCCCCCCCCCCCCCC
39.3327251275
570PhosphorylationSNRNSHRSLSGCPIA
CCCCCCCCCCCCHHH
22.8227732954
572PhosphorylationRNSHRSLSGCPIAAA
CCCCCCCCCCHHHHH
39.3327732954
619PhosphorylationKQLEIPQYGYRNNVP
EEECCCCCCCCCCCC
15.6925262027
621PhosphorylationLEIPQYGYRNNVPTT
ECCCCCCCCCCCCCC
12.7725262027
632PhosphorylationVPTTTPRSNLAKELE
CCCCCCCCHHHHHHH
37.08-
641PhosphorylationLAKELEKYSKTSFEY
HHHHHHHHCCCCCEE
13.1624129246
642PhosphorylationAKELEKYSKTSFEYN
HHHHHHHCCCCCEEC
40.2924129246
644PhosphorylationELEKYSKTSFEYNSY
HHHHHCCCCCEECCC
32.4824129246
645PhosphorylationLEKYSKTSFEYNSYD
HHHHCCCCCEECCCC
21.5924129246
648PhosphorylationYSKTSFEYNSYDNHT
HCCCCCEECCCCCCC
13.8529759185
650PhosphorylationKTSFEYNSYDNHTYG
CCCCEECCCCCCCCC
32.7224129246
651PhosphorylationTSFEYNSYDNHTYGK
CCCEECCCCCCCCCC
19.6829759185
655PhosphorylationYNSYDNHTYGKRAIA
ECCCCCCCCCCCCCC
39.9824129246
656PhosphorylationNSYDNHTYGKRAIAP
CCCCCCCCCCCCCCC
17.0724129246
689PhosphorylationCKDPSPSSSSTSSYA
CCCCCCCCCCCCCCC
31.52-
694PhosphorylationPSSSSTSSYAPSSSS
CCCCCCCCCCCCCCC
25.96-
699PhosphorylationTSSYAPSSSSNLSCG
CCCCCCCCCCCCCCC
36.41-
704PhosphorylationPSSSSNLSCGGGSSA
CCCCCCCCCCCCCCC
18.24-
709PhosphorylationNLSCGGGSSASSTCS
CCCCCCCCCCCCCCC
26.46-
712PhosphorylationCGGGSSASSTCSKSS
CCCCCCCCCCCCCCC
28.29-
716PhosphorylationSSASSTCSKSSFDYT
CCCCCCCCCCCCCCC
35.34-
734PhosphorylationEAAHMAATAILNLST
HHHHHHHHHHHHHHH
12.51-
753AcetylationMPQNLSTKPQDLCAT
CCCCCCCCHHHHCCC
36.997667007
854PhosphorylationFQEALEERRYPGEVT
HHHHHHHCCCCCCCC
33.7724719451
856PhosphorylationEALEERRYPGEVTIP
HHHHHCCCCCCCCCC
23.0824719451
859PhosphorylationEERRYPGEVTIPSPK
HHCCCCCCCCCCCCC
31.8024719451
861PhosphorylationRRYPGEVTIPSPKPK
CCCCCCCCCCCCCCC
23.9124719451
864PhosphorylationPGEVTIPSPKPKYPQ
CCCCCCCCCCCCCCC
41.5324117733
869PhosphorylationIPSPKPKYPQCKESK
CCCCCCCCCCCCCCC
13.68-
875PhosphorylationKYPQCKESKKDLITL
CCCCCCCCCCCEEEE
30.42-
925PhosphorylationGNYASHRSLSGCPRA
CCCCCCCCCCCCCCH
22.82-
1006PhosphorylationSVKTEGMSCPTPGCD
ECEECCCCCCCCCCC
28.0030576142
1009PhosphorylationTEGMSCPTPGCDGSG
ECCCCCCCCCCCCCC
36.3230576142
1015PhosphorylationPTPGCDGSGHVSGSF
CCCCCCCCCCCCCCC
16.6924043423
1019PhosphorylationCDGSGHVSGSFLTHR
CCCCCCCCCCCCCCC
24.0524043423
1021PhosphorylationGSGHVSGSFLTHRSL
CCCCCCCCCCCCCCC
15.0224043423
1024PhosphorylationHVSGSFLTHRSLSGC
CCCCCCCCCCCCCCC
17.1530576142
1044PhosphorylationAMKKAKLSGEQMLTI
HHHHHCCCCCCCHHH
39.3126074081

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 MYT1L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYT1L_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 MYT1L_HUMAN !!

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

Oops, there are no PPI records of MYT1L_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 MYT1L_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP