LMBL1_HUMAN - dbPTM
LMBL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LMBL1_HUMAN
UniProt AC Q9Y468
Protein Name Lethal(3)malignant brain tumor-like protein 1
Gene Name L3MBTL1
Organism Homo sapiens (Human).
Sequence Length 840
Subcellular Localization Nucleus . Excluded from the nucleolus. Does not colocalizes with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex.
Protein Description Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor by recognizing and binding mono- and dimethylated histone H1b/HIST1H1E at 'Lys-26' (H1bK26me1 and H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading to condense chromatin and repress transcription. Recognizes and binds p53/TP53 monomethylated at 'Lys-382', leading to repress p53/TP53-target genes. Also recognizes and binds RB1/RB monomethylated at 'Lys-860'. Participates in the ETV6-mediated repression. Probably plays a role in cell proliferation. Overexpression induces multinucleated cells, suggesting that it is required to accomplish normal mitosis..
Protein Sequence MHLVAGDSPGSGPHLPATAFIIPASSATLGLPSSALDVSCFPREPIHVGAPEQVAGCEPVSATVLPQLSAGPASSSTSTVRLLEWTEAAAPPPGGGLRFRISEYKPLNMAGVEQPPSPELRQEGVTEYEDGGAPAGDGEAGPQQAEDHPQNPPEDPNQDPPEDDSTCQCQACGPHQAAGPDLGSSNDGCPQLFQERSVIVENSSGSTSASELLKPMKKRKRREYQSPSEEESEPEAMEKQEEGKDPEGQPTASTPESEEWSSSQPATGEKKECWSWESYLEEQKAITAPVSLFQDSQAVTHNKNGFKLGMKLEGIDPQHPSMYFILTVAEVCGYRLRLHFDGYSECHDFWVNANSPDIHPAGWFEKTGHKLQPPKGYKEEEFSWSQYLRSTRAQAAPKHLFVSQSHSPPPLGFQVGMKLEAVDRMNPSLVCVASVTDVVDSRFLVHFDNWDDTYDYWCDPSSPYIHPVGWCQKQGKPLTPPQDYPDPDNFCWEKYLEETGASAVPTWAFKVRPPHSFLVNMKLEAVDRRNPALIRVASVEDVEDHRIKIHFDGWSHGYDFWIDADHPDIHPAGWCSKTGHPLQPPLGPREPSSASPGGCPPLSYRSLPHTRTSKYSFHHRKCPTPGCDGSGHVTGKFTAHHCLSGCPLAERNQSRLKAELSDSEASARKKNLSGFSPRKKPRHHGRIGRPPKYRKIPQEDFQTLTPDVVHQSLFMSALSAHPDRSLSVCWEQHCKLLPGVAGISASTVAKWTIDEVFGFVQTLTGCEDQARLFKDEARIVRVTHVSGKTLVWTVAQLGDLVCSDHLQEGKGILETGVHSLLCSLPTHLLAKLSFASDSQY
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
49PhosphorylationPREPIHVGAPEQVAG
CCCCCCCCCHHHHCC
37.3823401153
117PhosphorylationAGVEQPPSPELRQEG
CCCCCCCCHHHHHCC
36.8223186163
160PhosphorylationPEDPNQDPPEDDSTC
CCCCCCCCCCCCCCC
63.9928348404
164PhosphorylationNQDPPEDDSTCQCQA
CCCCCCCCCCCCCCC
62.8328348404
199PhosphorylationLFQERSVIVENSSGS
HHHCCEEEEECCCCC
53.1828674151
232PhosphorylationQSPSEEESEPEAMEK
CCCCHHHCCHHHHHH
23.81-
299PhosphorylationLFQDSQAVTHNKNGF
HHCCCCCCCCCCCCC
37.0024260401
605PhosphorylationGCPPLSYRSLPHTRT
CCCCCCCCCCCCCCC
47.3823403867
728PhosphorylationHPDRSLSVCWEQHCK
CCCCCHHHHHHHHHH
21.4124719451

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 LMBL1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LMBL1_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 LMBL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMBL1_HUMANL3MBTL1physical
12588862
ETV7_HUMANETV7physical
12588862
RB_HUMANRB1physical
17540172
CBX3_HUMANCBX3physical
17540172
CBX5_HUMANCBX5physical
17540172
SETD7_HUMANSETD7physical
18408754
H14_HUMANHIST1H1Ephysical
19144645
P53_HUMANTP53physical
20870725
KMT5A_HUMANSETD8physical
20870725
MCM2_HUMANMCM2physical
21149733
MCM3_HUMANMCM3physical
21149733
MCM4_HUMANMCM4physical
21149733
MCM5_HUMANMCM5physical
21149733
MCM6_HUMANMCM6physical
21149733
MCM7_HUMANMCM7physical
21149733
CDC45_HUMANCDC45physical
21149733
PCNA_HUMANPCNAphysical
21149733
TERA_HUMANVCPphysical
22120668
TERA_HUMANVCPphysical
23652004
ZN644_HUMANZNF644physical
28514442
SATB2_HUMANSATB2physical
28514442
SAM11_HUMANSAMD11physical
28514442
F208B_HUMANFAM208Bphysical
28514442
WIZ_HUMANWIZphysical
28514442
EHMT2_HUMANEHMT2physical
28514442
ZN195_HUMANZNF195physical
28514442
APC1_HUMANANAPC1physical
28514442
EHMT1_HUMANEHMT1physical
28514442
CBX2_HUMANCBX2physical
28514442
PPHLN_HUMANPPHLN1physical
28514442
APC5_HUMANANAPC5physical
28514442
ZBT34_HUMANZBTB34physical
28514442
BCOR_HUMANBCORphysical
28514442
ZN281_HUMANZNF281physical
28514442
EVI1_HUMANMECOMphysical
28514442
SP16H_HUMANSUPT16Hphysical
28514442
NSE4A_HUMANNSMCE4Aphysical
28514442
P73_HUMANTP73physical
28514442
MCM4_HUMANMCM4physical
28514442
PHF10_HUMANPHF10physical
28514442
BRCA2_HUMANBRCA2physical
28514442
Z324A_HUMANZNF324physical
28514442
SALL2_HUMANSALL2physical
28514442
MCM2_HUMANMCM2physical
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 LMBL1_HUMAN

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Related Literatures of Post-Translational Modification

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