ACL6A_HUMAN - dbPTM
ACL6A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACL6A_HUMAN
UniProt AC O96019
Protein Name Actin-like protein 6A
Gene Name ACTL6A
Organism Homo sapiens (Human).
Sequence Length 429
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. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. 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 (By similarity). Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair..
Protein Sequence MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGDKGKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPVLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKRKEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQSFTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP
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
2Acetylation------MSGGVYGGD
------CCCCCCCCC		44.2322814378
2Phosphorylation------MSGGVYGGD
------CCCCCCCCC		44.2328348404
6Phosphorylation--MSGGVYGGDEVGA
--CCCCCCCCCCCCE		20.7528464451
18 (in isoform 2)Ubiquitination-2.4121890473
18UbiquitinationVGALVFDIGSYTVRA
CCEEEEEECCEEEEE		2.4123000965
20UbiquitinationALVFDIGSYTVRAGY
EEEEEECCEEEEECC		20.2623000965
20 (in isoform 2)Ubiquitination-20.2621890473
34AcetylationYAGEDCPKVDFPTAI
CCCCCCCCCCCCCEE		61.8526051181
47UbiquitinationAIGMVVERDDGSTLM
EEEEEEECCCCCEEE		35.3929967540
51PhosphorylationVVERDDGSTLMEIDG
EEECCCCCEEEEECC		25.9328348404
52PhosphorylationVERDDGSTLMEIDGD
EECCCCCEEEEECCC		35.3428348404
54SulfoxidationRDDGSTLMEIDGDKG
CCCCCEEEEECCCCC		4.2628465586
60 (in isoform 1)Ubiquitination-73.8121890473
60UbiquitinationLMEIDGDKGKQGGPT
EEEECCCCCCCCCCE		73.8123000965
60AcetylationLMEIDGDKGKQGGPT
EEEECCCCCCCCCCE		73.8125953088
62SumoylationEIDGDKGKQGGPTYY
EECCCCCCCCCCEEE		52.0628112733
62 (in isoform 1)Ubiquitination-52.0621890473
62UbiquitinationEIDGDKGKQGGPTYY
EECCCCCCCCCCEEE		52.0623000965
62AcetylationEIDGDKGKQGGPTYY
EECCCCCCCCCCEEE		52.0626051181
67PhosphorylationKGKQGGPTYYIDTNA
CCCCCCCEEEEECCC		32.0328152594
68PhosphorylationGKQGGPTYYIDTNAL
CCCCCCEEEEECCCC		11.1028152594
69PhosphorylationKQGGPTYYIDTNALR
CCCCCEEEEECCCCC		8.5228152594
70UbiquitinationQGGPTYYIDTNALRV
CCCCEEEEECCCCCC		3.5729967540
72PhosphorylationGPTYYIDTNALRVPR
CCEEEEECCCCCCCH		16.9128152594
86PhosphorylationRENMEAISPLKNGMV
HHHHHHHCCCCCCCC		31.0929255136
89UbiquitinationMEAISPLKNGMVEDW
HHHHCCCCCCCCCCH		55.6429967540
90UbiquitinationEAISPLKNGMVEDWD
HHHCCCCCCCCCCHH		52.0229967540
93UbiquitinationSPLKNGMVEDWDSFQ
CCCCCCCCCCHHHHH		6.8221963094
112UbiquitinationHTYKMHVKSEASLHP
HCEECCCCCHHHCCC		28.0929967540
116PhosphorylationMHVKSEASLHPVLMS
CCCCCHHHCCCHHHC		24.1424719451
129PhosphorylationMSEAPWNTRAKREKL
HCCCCCCHHHHHHHH		28.3024719451
132UbiquitinationAPWNTRAKREKLTEL
CCCCHHHHHHHHHHH		58.7729967540
135UbiquitinationNTRAKREKLTELMFE
CHHHHHHHHHHHHHH		65.8221963094
152UbiquitinationNIPAFFLCKTAVLTA
CCCHHHHHHHHHHHH		2.8821963094
184UbiquitinationTTAIPVHDGYVLQQG
CEEEEECCCEEEEEC		50.8021963094
184 (in isoform 2)Ubiquitination-50.8021890473
186PhosphorylationAIPVHDGYVLQQGIV
EEEECCCEEEEECEE		12.21-
191PhosphorylationDGYVLQQGIVKSPLA
CCEEEEECEECCCCC		17.4432645325
191 (in isoform 2)Phosphorylation-17.44-
194UbiquitinationVLQQGIVKSPLAGDF
EEEECEECCCCCCCE		44.4221963094
196UbiquitinationQQGIVKSPLAGDFIT
EECEECCCCCCCEEH		22.1023000965
198UbiquitinationGIVKSPLAGDFITMQ
CEECCCCCCCEEHHH		20.9223000965
200UbiquitinationVKSPLAGDFITMQCR
ECCCCCCCEEHHHHH		26.6023000965
204SulfoxidationLAGDFITMQCRELFQ
CCCCEEHHHHHHHHH		2.7921406390
226 (in isoform 1)Ubiquitination-40.4421890473
226UbiquitinationPPYMIASKEAVREGS
CCEEEECHHHHHCCC		40.4421906983
233PhosphorylationKEAVREGSPANWKRK
HHHHHCCCCCCCCCH		18.9822167270
238UbiquitinationEGSPANWKRKEKLPQ
CCCCCCCCCHHHCCC		54.0923000965
238MethylationEGSPANWKRKEKLPQ
CCCCCCCCCHHHCCC		54.09-
240UbiquitinationSPANWKRKEKLPQVT
CCCCCCCHHHCCCCC		56.3123000965
240AcetylationSPANWKRKEKLPQVT
CCCCCCCHHHCCCCC		56.3119816129
242UbiquitinationANWKRKEKLPQVTRS
CCCCCHHHCCCCCHH		69.3823000965
247PhosphorylationKEKLPQVTRSWHNYM
HHHCCCCCHHHHHHH		17.4620068231
261UbiquitinationMCNCVIQDFQASVLQ
HHHHHHHHHHHHEEE		26.8821963094
261 (in isoform 2)Ubiquitination-26.8821890473
303 (in isoform 1)Ubiquitination-63.5421890473
303UbiquitinationDFGAERLKIPEGLFD
CCCCHHCCCCCCCCC		63.5421906983
329UbiquitinationMLGVSHVVTTSVGMC
EEECEEEEEECCEEC		3.9621963094
329 (in isoform 2)Ubiquitination-3.9621890473
337 (in isoform 2)Ubiquitination-32.4721890473
337UbiquitinationTTSVGMCDIDIRPGL
EECCEECCCCCCCCC		32.4721890473
369PhosphorylationDRLNRELSQKTPPSM
HHHHHHHHCCCCCHH		25.5229083192
371MalonylationLNRELSQKTPPSMRL
HHHHHHCCCCCHHHE		60.6732601280
371 (in isoform 1)Ubiquitination-60.6721890473
371UbiquitinationLNRELSQKTPPSMRL
HHHHHHCCCCCHHHE		60.6721906983
372PhosphorylationNRELSQKTPPSMRLK
HHHHHCCCCCHHHEE		32.5620860994
375PhosphorylationLSQKTPPSMRLKLIA
HHCCCCCHHHEEEHH		20.1020860994
379MalonylationTPPSMRLKLIANNTT
CCCHHHEEEHHCCCC		27.7326320211
379 (in isoform 1)Ubiquitination-27.7321890473
379UbiquitinationTPPSMRLKLIANNTT
CCCHHHEEEHHCCCC		27.7327667366
379AcetylationTPPSMRLKLIANNTT
CCCHHHEEEHHCCCC		27.7323954790
392PhosphorylationTTVERRFSSWIGGSI
CCHHHHHHHHHHHHH		23.9722210691
393PhosphorylationTVERRFSSWIGGSIL
CHHHHHHHHHHHHHH		21.7222210691
405PhosphorylationSILASLGTFQQMWIS
HHHHHHCHHHHHHHC		24.4622210691
421UbiquitinationQEYEEGGKQCVERKC
HHHHCCHHCCCCCCC		51.9230230243
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 ACL6A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACL6A_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 ACL6A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EWS_HUMANEWSR1physical
16189514
KAT2A_HUMANKAT2Aphysical
11839798
TRRAP_HUMANTRRAPphysical
11839798
KAT5_HUMANKAT5physical
11839798
RUVB1_HUMANRUVBL1physical
11839798
FLII_HUMANFLIIphysical
19720835
TYY1_HUMANYY1physical
18026119
P53_HUMANTP53physical
17878219
SMRC1_HUMANSMARCC1physical
21699904
SMCA4_HUMANSMARCA4physical
21699904
SMCA4_HUMANSMARCA4physical
22939629
RUVB1_HUMANRUVBL1physical
22939629
TRRAP_HUMANTRRAPphysical
22939629
SMCA2_HUMANSMARCA2physical
22939629
SMCE1_HUMANSMARCE1physical
22939629
SMRC1_HUMANSMARCC1physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
ARI1A_HUMANARID1Aphysical
22939629
ARI1B_HUMANARID1Bphysical
22939629
UCHL5_HUMANUCHL5physical
22939629
NB5R3_HUMANCYB5R3physical
26186194
RAB1B_HUMANRAB1Bphysical
26186194
PHLP_HUMANPDCLphysical
26186194
SF01_HUMANSF1physical
26186194
ERF1_HUMANETF1physical
26186194
EFTS_HUMANTSFMphysical
26186194
MAP2_HUMANMETAP2physical
26186194
SF3A1_HUMANSF3A1physical
26186194
RAB14_HUMANRAB14physical
26186194
RPR1B_HUMANRPRD1Bphysical
26186194
LYRIC_HUMANMTDHphysical
26186194
USO1_HUMANUSO1physical
26186194
VIGLN_HUMANHDLBPphysical
26186194
MP2K2_HUMANMAP2K2physical
26186194
RIC8B_HUMANRIC8Bphysical
26186194
DDRGK_HUMANDDRGK1physical
26186194
TCPH_HUMANCCT7physical
26186194
TCPG_HUMANCCT3physical
26186194
HDGR2_HUMANHDGFRP2physical
26186194
TCPW_HUMANCCT6Bphysical
26186194
TCPZ_HUMANCCT6Aphysical
26186194
TCPB_HUMANCCT2physical
26186194
HINT1_HUMANHINT1physical
26186194
TCPA_HUMANTCP1physical
26186194
TCPD_HUMANCCT4physical
26186194
TBL1R_HUMANTBL1XR1physical
26344197
TCPB_HUMANCCT2physical
28514442
HDGR2_HUMANHDGFRP2physical
28514442
RUVB1_HUMANRUVBL1physical
28514442
HINT1_HUMANHINT1physical
28514442
RPR1B_HUMANRPRD1Bphysical
28514442
FEN1_HUMANFEN1physical
28514442
NB5R3_HUMANCYB5R3physical
28514442
SMRC2_HUMANSMARCC2physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPG_HUMANCCT3physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
MYCL_HUMANMYCLphysical
29028833
RUVB2_HUMANRUVBL2physical
29028833
DMAP1_HUMANDMAP1physical
29028833
KAT5_HUMANKAT5physical
29028833
TRRAP_HUMANTRRAPphysical
29028833
EP400_HUMANEP400physical
29028833
VPS72_HUMANVPS72physical
29028833
MAX_HUMANMAXphysical
29028833
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 ACL6A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND MASSSPECTROMETRY.

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