DPF3_HUMAN - dbPTM
DPF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPF3_HUMAN
UniProt AC Q92784
Protein Name Zinc finger protein DPF3
Gene Name DPF3
Organism Homo sapiens (Human).
Sequence Length 378
Subcellular Localization Nucleus .
Protein Description Belongs to the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic 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 post-mitotic 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). Muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Specifically binds acetylated lysines on histone 3 and 4 (H3K14ac, H3K9ac, H4K5ac, H4K8ac, H4K12ac, H4K16ac). In the complex, it acts as a tissue-specific anchor between histone acetylations and methylations and chromatin remodeling. It thereby probably plays an essential role in heart and skeletal muscle development..
Protein Sequence MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDPKLRLLEIKPEVELPLKKDGFTSESTTLEALLRGEGVEKKVDAREEESIQEIQRVLENDENVEEGNEEEDLEEDIPKRKNRTRGRARGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA
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
46PhosphorylationLPFLDSQTGVAQNNC
CCEECCCCCCCCCCE
37.26-
92UbiquitinationLHPPEDPKLRLLEIK
CCCCCCCCCCEEEEC
59.57-
99SumoylationKLRLLEIKPEVELPL
CCCEEEECCCEECCC
26.2528112733
107AcetylationPEVELPLKKDGFTSE
CCEECCCCCCCCCCC
47.0525953088
108UbiquitinationEVELPLKKDGFTSES
CEECCCCCCCCCCCC
71.42-
138PhosphorylationVDAREEESIQEIQRV
CCCCHHHHHHHHHHH
32.62-
235PhosphorylationDEAQDQETRSPPNHR
CCCCCCCCCCCCCCC
30.7128348404
237PhosphorylationAQDQETRSPPNHRNE
CCCCCCCCCCCCCCC
52.7228348404
255PhosphorylationPQKGPDGTVIPNNYC
CCCCCCCCCCCCCCC
23.7329978859
261PhosphorylationGTVIPNNYCDFCLGG
CCCCCCCCCCCCCCC
10.4729978859
269PhosphorylationCDFCLGGSNMNKKSG
CCCCCCCCCCCCCCC
30.9829978859
309 (in isoform 2)Phosphorylation-12.4324275569
316 (in isoform 2)Phosphorylation-1.6724275569
317 (in isoform 2)Phosphorylation-35.2624275569
318 (in isoform 2)Phosphorylation-20.3224275569
319 (in isoform 5)Phosphorylation-1.3624275569
320 (in isoform 2)Phosphorylation-4.6224275569
323 (in isoform 2)Phosphorylation-28.9124275569
326 (in isoform 5)Phosphorylation-65.6024275569
327 (in isoform 5)Phosphorylation-58.9024275569
328 (in isoform 5)Phosphorylation-40.7724275569
330 (in isoform 5)Phosphorylation-42.8224275569
333 (in isoform 5)Phosphorylation-6.1224275569
344 (in isoform 2)Phosphorylation-4.77-
348 (in isoform 2)Phosphorylation-16.2824719451
350 (in isoform 2)Phosphorylation-11.26-
354 (in isoform 5)Phosphorylation-50.51-
358 (in isoform 5)Phosphorylation-18.8124719451
360 (in isoform 5)Phosphorylation-2.00-
364 (in isoform 3)Phosphorylation-12.9624275569
371 (in isoform 3)Phosphorylation-13.7424275569
372 (in isoform 3)Phosphorylation-34.8924275569
373 (in isoform 3)Phosphorylation-15.0924275569
375 (in isoform 3)Phosphorylation-11.4424275569
378 (in isoform 3)Phosphorylation-26.0124275569
399 (in isoform 3)Phosphorylation--
403 (in isoform 3)Phosphorylation-24719451
405 (in isoform 3)Phosphorylation--

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
348SPhosphorylationKinaseCSNK2A1P68400
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPF3_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 DPF3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF65_HUMANRELAphysical
22334708
NFKB1_HUMANNFKB1physical
22334708
SMCA4_HUMANSMARCA4physical
22334708
SMCA2_HUMANSMARCA2physical
22334708
SMRC1_HUMANSMARCC1physical
22334708
SMRD1_HUMANSMARCD1physical
22334708
SNF5_HUMANSMARCB1physical
22334708
ARI1A_HUMANARID1Aphysical
26186194
ARI1B_HUMANARID1Bphysical
26186194
SMRC2_HUMANSMARCC2physical
26186194
SMRC1_HUMANSMARCC1physical
26186194
SMCA2_HUMANSMARCA2physical
26186194
SMCA4_HUMANSMARCA4physical
26186194
SMRD3_HUMANSMARCD3physical
26186194
SMRD2_HUMANSMARCD2physical
26186194
SMRD1_HUMANSMARCD1physical
26186194
ARID2_HUMANARID2physical
26186194
PB1_HUMANPBRM1physical
26186194
SNF5_HUMANSMARCB1physical
26186194
BRD7_HUMANBRD7physical
26186194
SMCE1_HUMANSMARCE1physical
26186194
BCL7A_HUMANBCL7Aphysical
26186194
BCL7C_HUMANBCL7Cphysical
26186194
BCL7B_HUMANBCL7Bphysical
26186194
ACL6A_HUMANACTL6Aphysical
26186194
ACL6B_HUMANACTL6Bphysical
26186194
SSXT_HUMANSS18physical
26186194
CREST_HUMANSS18L1physical
26186194
SPEB_HUMANAGMATphysical
26186194
ARI1A_HUMANARID1Aphysical
26344197
ARI1B_HUMANARID1Bphysical
26344197
CSK21_HUMANCSNK2A1physical
26582913
CSK22_HUMANCSNK2A2physical
26582913
CSK2B_HUMANCSNK2Bphysical
26582913
U520_HUMANSNRNP200physical
26582913
UBR5_HUMANUBR5physical
26582913
UBR4_HUMANUBR4physical
26582913
HDGR3_HUMANHDGFRP3physical
26582913
HS71L_HUMANHSPA1Lphysical
26582913
AIFM1_HUMANAIFM1physical
26582913
TECR_HUMANTECRphysical
26582913
TBA3E_HUMANTUBA3Ephysical
26582913
XPOT_HUMANXPOTphysical
26582913
EF1A2_HUMANEEF1A2physical
26582913
TIM50_HUMANTIMM50physical
26582913
AHSA1_HUMANAHSA1physical
26582913
SMRD1_HUMANSMARCD1physical
28514442
SMRC2_HUMANSMARCC2physical
28514442
ARI1B_HUMANARID1Bphysical
28514442
BRD7_HUMANBRD7physical
28514442
SMRD3_HUMANSMARCD3physical
28514442
SMCA2_HUMANSMARCA2physical
28514442
SMRD2_HUMANSMARCD2physical
28514442
SMCE1_HUMANSMARCE1physical
28514442
ARID2_HUMANARID2physical
28514442
SSXT_HUMANSS18physical
28514442
BCL7B_HUMANBCL7Bphysical
28514442
SNF5_HUMANSMARCB1physical
28514442
PB1_HUMANPBRM1physical
28514442
SMCA4_HUMANSMARCA4physical
28514442
SMRC1_HUMANSMARCC1physical
28514442
ARI1A_HUMANARID1Aphysical
28514442
CREST_HUMANSS18L1physical
28514442
ACL6B_HUMANACTL6Bphysical
28514442
DCX_HUMANDCXphysical
28514442
ACL6A_HUMANACTL6Aphysical
28514442
SPEB_HUMANAGMATphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPF3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP