ACL6B_HUMAN - dbPTM
ACL6B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACL6B_HUMAN
UniProt AC O94805
Protein Name Actin-like protein 6B
Gene Name ACTL6B
Organism Homo sapiens (Human).
Sequence Length 426
Subcellular Localization Nucleus .
Protein Description Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex), as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion, and is required for postmitotic neural development and dendritic outgrowth. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. ACTL6B/BAF53B is not essential for assembly of the nBAF complex but is required for targeting the complex and CREST to the promoter of genes essential for dendritic growth (By similarity)..
Protein Sequence MSGGVYGGDEVGALVFDIGSFSVRAGYAGEDCPKADFPTTVGLLAAEEGGGLELEGDKEKKGKIFHIDTNALHVPRDGAEVMSPLKNGMIEDWECFRAILDHTYSKHVKSEPNLHPVLMSEAPWNTRAKREKLTELMFEQYNIPAFFLCKTAVLTAFANGRSTGLVLDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFISMQCRELFQEMAIDIIPPYMIAAKEPVREGAPPNWKKKEKLPQVSKSWHNYMCNEVIQDFQASVLQVSDSPYDEQVAAQMPTVHYEMPNGYNTDYGAERLRIPEGLFDPSNVKGLSGNTMLGVGHVVTTSIGMCDIDIRPGLYGSVIVTGGNTLLQGFTDRLNRELSQKTPPSMRLKLIASNSTMERKFSPWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP
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
2Phosphorylation------MSGGVYGGD
------CCCCCCCCC
44.23-
2Acetylation------MSGGVYGGD
------CCCCCCCCC
44.23-
6Phosphorylation--MSGGVYGGDEVGA
--CCCCCCCCCCCEE
20.7518491316
83PhosphorylationRDGAEVMSPLKNGMI
CCCCCCCCCCCCCCC
32.05-
104PhosphorylationRAILDHTYSKHVKSE
HHHHHHCHHHCCCCC
16.5925884760
126PhosphorylationMSEAPWNTRAKREKL
CCCCCCCHHHHHHHH
28.30-
134PhosphorylationRAKREKLTELMFEQY
HHHHHHHHHHHHHHC
37.8324719451
141PhosphorylationTELMFEQYNIPAFFL
HHHHHHHCCCCHHHH
14.0927174698
155PhosphorylationLCKTAVLTAFANGRS
HHHHHHHHHHHCCCC
17.0924719451
183PhosphorylationAIPVHDGYVLQQGIV
EEEECCCEEEEECEE
12.21-
191AcetylationVLQQGIVKSPLAGDF
EEEECEECCCCCCCH
44.4226051181
204MethylationDFISMQCRELFQEMA
CHHHHHHHHHHHHHH
27.11-
244PhosphorylationKEKLPQVSKSWHNYM
HHHCCCCCHHHHHHH
18.7420068231
366PhosphorylationDRLNRELSQKTPPSM
HHHHHHHHHCCCCHH
25.5229083192
368UbiquitinationLNRELSQKTPPSMRL
HHHHHHHCCCCHHHE
60.6721906983
368AcetylationLNRELSQKTPPSMRL
HHHHHHHCCCCHHHE
60.6725953088
369PhosphorylationNRELSQKTPPSMRLK
HHHHHHCCCCHHHEE
32.5620860994
372PhosphorylationLSQKTPPSMRLKLIA
HHHCCCCHHHEEEHH
20.1020860994
382PhosphorylationLKLIASNSTMERKFS
EEEHHCCCCCCCCCC
27.0023403867
383PhosphorylationKLIASNSTMERKFSP
EEHHCCCCCCCCCCC
27.5723403867
395PhosphorylationFSPWIGGSILASLGT
CCCCCCHHHHHHHHH
14.8222210691
399PhosphorylationIGGSILASLGTFQQM
CCHHHHHHHHHHHHH
24.7222210691
413PhosphorylationMWISKQEYEEGGKQC
HHHCHHHHHCCHHCC
19.4522210691
418UbiquitinationQEYEEGGKQCVERKC
HHHHCCHHCCCCCCC
51.9230230243
418AcetylationQEYEEGGKQCVERKC
HHHHCCHHCCCCCCC
51.9226051181

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 ACL6B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACL6B_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 ACL6B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBP1_HUMANCTBP1genetic
12565893
CTBP1_HUMANCTBP1physical
12565893
A4_HUMANAPPphysical
21832049
MED14_HUMANMED14physical
26344197

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 ACL6B_HUMAN

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Related Literatures of Post-Translational Modification

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