PHF10_HUMAN - dbPTM
PHF10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF10_HUMAN
UniProt AC Q8WUB8
Protein Name PHD finger protein 10
Gene Name PHF10
Organism Homo sapiens (Human).
Sequence Length 498
Subcellular Localization Nucleus.
Protein Description Involved in transcription activity regulation by chromatin remodeling. 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 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)..
Protein Sequence MAAAAGPGAALSPRPCDSDPATPGAQSPKDDNEDNSNDGTQPSKRRRMGSGDSSRSCETSSQDLGFSYYPAENLIEYKWPPDETGEYYMLQEQVSEYLGVTSFKRKYPDLERRDLSHKEKLYLRELNVITETQCTLGLTALRSDEVIDLMIKEYPAKHAEYSVILQEKERQRITDHYKEYSQMQQQNTQKVEASKVPEYIKKAAKKAAEFNSNLNRERMEERRAYFDLQTHVIQVPQGKYKVLPTERTKVSSYPVALIPGQFQEYYKRYSPDELRYLPLNTALYEPPLDPELPALDSDGDSDDGEDGRGDEKRKNKGTSDSSSGNVSEGESPPDSQEDSFQGRQKSKDKAATPRKDGPKRSVLSKSVPGYKPKVIPNAICGICLKGKESNKKGKAESLIHCSQCENSGHPSCLDMTMELVSMIKTYPWQCMECKTCIICGQPHHEEEMMFCDMCDRGYHTFCVGLGAIPSGRWICDCCQRAPPTPRKVGRRGKNSKEG
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------MAAAAGPGA
------CCCCCCCCC		13.0520068231
12PhosphorylationAGPGAALSPRPCDSD
CCCCCCCCCCCCCCC		17.7129255136
18PhosphorylationLSPRPCDSDPATPGA
CCCCCCCCCCCCCCC		52.8125159151
22PhosphorylationPCDSDPATPGAQSPK
CCCCCCCCCCCCCCC		27.8729255136
27PhosphorylationPATPGAQSPKDDNED
CCCCCCCCCCCCCCC		33.1223401153
36PhosphorylationKDDNEDNSNDGTQPS
CCCCCCCCCCCCCCC		48.9329255136
40PhosphorylationEDNSNDGTQPSKRRR
CCCCCCCCCCCHHCC		39.9223663014
43PhosphorylationSNDGTQPSKRRRMGS
CCCCCCCCHHCCCCC		29.0423663014
50PhosphorylationSKRRRMGSGDSSRSC
CHHCCCCCCCCCCCC		30.0423663014
53PhosphorylationRRMGSGDSSRSCETS
CCCCCCCCCCCCCCC		31.0423663014
54PhosphorylationRMGSGDSSRSCETSS
CCCCCCCCCCCCCCC		32.7123663014
56PhosphorylationGSGDSSRSCETSSQD
CCCCCCCCCCCCCCC		20.4625159151
59PhosphorylationDSSRSCETSSQDLGF
CCCCCCCCCCCCCCC		37.7028102081
60PhosphorylationSSRSCETSSQDLGFS
CCCCCCCCCCCCCCC		12.0528102081
61PhosphorylationSRSCETSSQDLGFSY
CCCCCCCCCCCCCCC		34.8223663014
67PhosphorylationSSQDLGFSYYPAENL
CCCCCCCCCCCCCCE		23.2023663014
68PhosphorylationSQDLGFSYYPAENLI
CCCCCCCCCCCCCEE		15.9423663014
69PhosphorylationQDLGFSYYPAENLIE
CCCCCCCCCCCCEEE		8.5123663014
78 (in isoform 2)Ubiquitination-40.2021890473
80 (in isoform 1)Ubiquitination-23.4721890473
95 (in isoform 2)Phosphorylation-21.8820068231
97 (in isoform 2)Phosphorylation-10.9720068231
101 (in isoform 2)Phosphorylation-27.0120068231
102PhosphorylationSEYLGVTSFKRKYPD
HHHHCCCCHHHHCCC		26.7720068231
102 (in isoform 2)Phosphorylation-26.7720068231
107PhosphorylationVTSFKRKYPDLERRD
CCCHHHHCCCHHHCC		13.1520068231
107 (in isoform 2)Phosphorylation-13.1520068231
122PhosphorylationLSHKEKLYLRELNVI
CCHHHHHHHHHHCCC		18.12-
134GlutathionylationNVITETQCTLGLTAL
CCCCCCCCCEECHHH		4.4122555962
139PhosphorylationTQCTLGLTALRSDEV
CCCCEECHHHCCHHH		23.1124719451
149 (in isoform 2)Ubiquitination-2.3521890473
150SulfoxidationSDEVIDLMIKEYPAK
CHHHHHHHHHHCCCC		3.5021406390
151 (in isoform 1)Ubiquitination-3.8921890473
159 (in isoform 2)Ubiquitination-19.4021890473
161PhosphorylationYPAKHAEYSVILQEK
CCCCCCEEEEEECHH		14.7127642862
161 (in isoform 1)Ubiquitination-14.7121890473
166UbiquitinationAEYSVILQEKERQRI
CEEEEEECHHHHHHH		48.9021890473
168UbiquitinationYSVILQEKERQRITD
EEEEECHHHHHHHHH		45.2833845483
168UbiquitinationYSVILQEKERQRITD
EEEEECHHHHHHHHH		45.2821890473
176UbiquitinationERQRITDHYKEYSQM
HHHHHHHHHHHHHHH		27.2429967540
177 (in isoform 2)Ubiquitination-14.3421890473
178UbiquitinationQRITDHYKEYSQMQQ
HHHHHHHHHHHHHHH		46.9129967540
178AcetylationQRITDHYKEYSQMQQ
HHHHHHHHHHHHHHH		46.9126051181
179 (in isoform 1)Ubiquitination-43.1621890473
180PhosphorylationITDHYKEYSQMQQQN
HHHHHHHHHHHHHHH		10.47-
181PhosphorylationTDHYKEYSQMQQQNT
HHHHHHHHHHHHHHH		21.92-
182PhosphorylationDHYKEYSQMQQQNTQ
HHHHHHHHHHHHHHH		32.5718669648
190SumoylationMQQQNTQKVEASKVP
HHHHHHHHHHHHHHH		39.75-
193UbiquitinationQNTQKVEASKVPEYI
HHHHHHHHHHHHHHH		20.0329967540
195SumoylationTQKVEASKVPEYIKK
HHHHHHHHHHHHHHH		69.71-
195SumoylationTQKVEASKVPEYIKK
HHHHHHHHHHHHHHH		69.71-
195UbiquitinationTQKVEASKVPEYIKK
HHHHHHHHHHHHHHH		69.7129967540
204UbiquitinationPEYIKKAAKKAAEFN
HHHHHHHHHHHHHHH		23.8229967540
206MethylationYIKKAAKKAAEFNSN
HHHHHHHHHHHHHHH		48.3798666211
206UbiquitinationYIKKAAKKAAEFNSN
HHHHHHHHHHHHHHH		48.3729967540
209PhosphorylationKAAKKAAEFNSNLNR
HHHHHHHHHHHHCCH		50.6618669648
213PhosphorylationKAAEFNSNLNRERME
HHHHHHHHCCHHHHH		42.3018669648
225PhosphorylationRMEERRAYFDLQTHV
HHHHHHHHHHCCCCE		8.87-
237UbiquitinationTHVIQVPQGKYKVLP
CCEEECCCCCCEECC		63.2521890473
239UbiquitinationVIQVPQGKYKVLPTE
EEECCCCCCEECCCC		36.3321890473
239UbiquitinationVIQVPQGKYKVLPTE
EEECCCCCCEECCCC		36.3321890473
239AcetylationVIQVPQGKYKVLPTE
EEECCCCCCEECCCC		36.3326051181
239PhosphorylationVIQVPQGKYKVLPTE
EEECCCCCCEECCCC		36.3318669648
241SumoylationQVPQGKYKVLPTERT
ECCCCCCEECCCCCC		40.56-
241SumoylationQVPQGKYKVLPTERT
ECCCCCCEECCCCCC		40.5625218447
241UbiquitinationQVPQGKYKVLPTERT
ECCCCCCEECCCCCC		40.5629967540
247UbiquitinationYKVLPTERTKVSSYP
CEECCCCCCCCCCCC		42.1821890473
249UbiquitinationVLPTERTKVSSYPVA
ECCCCCCCCCCCCEE		46.4723000965
249UbiquitinationVLPTERTKVSSYPVA
ECCCCCCCCCCCCEE		46.4721890473
253PhosphorylationERTKVSSYPVALIPG
CCCCCCCCCEEECCC		8.3318083107
265PhosphorylationIPGQFQEYYKRYSPD
CCCHHHHHHHHCCHH		11.9618083107
265UbiquitinationIPGQFQEYYKRYSPD
CCCHHHHHHHHCCHH		11.9621890473
266PhosphorylationPGQFQEYYKRYSPDE
CCHHHHHHHHCCHHH		6.5518083107
267UbiquitinationGQFQEYYKRYSPDEL
CHHHHHHHHCCHHHH		43.9132015554
267UbiquitinationGQFQEYYKRYSPDEL
CHHHHHHHHCCHHHH		43.9121890473
269PhosphorylationFQEYYKRYSPDELRY
HHHHHHHCCHHHHCC		22.0223898821
270PhosphorylationQEYYKRYSPDELRYL
HHHHHHCCHHHHCCC		29.8829255136
276PhosphorylationYSPDELRYLPLNTAL
CCHHHHCCCCCCCCC		25.8720873877
281PhosphorylationLRYLPLNTALYEPPL
HCCCCCCCCCCCCCC		26.2320873877
284PhosphorylationLPLNTALYEPPLDPE
CCCCCCCCCCCCCCC		24.7520873877
297PhosphorylationPELPALDSDGDSDDG
CCCCCCCCCCCCCCC		44.3226503892
301PhosphorylationALDSDGDSDDGEDGR
CCCCCCCCCCCCCCC		43.0326503892
318PhosphorylationEKRKNKGTSDSSSGN
HHHCCCCCCCCCCCC		30.8525022875
319PhosphorylationKRKNKGTSDSSSGNV
HHCCCCCCCCCCCCC		44.1325022875
321PhosphorylationKNKGTSDSSSGNVSE
CCCCCCCCCCCCCCC		26.6022115753
322PhosphorylationNKGTSDSSSGNVSEG
CCCCCCCCCCCCCCC		47.4530278072
323PhosphorylationKGTSDSSSGNVSEGE
CCCCCCCCCCCCCCC		38.0430278072
325PhosphorylationTSDSSSGNVSEGESP
CCCCCCCCCCCCCCC		35.7733259812
327PhosphorylationDSSSGNVSEGESPPD
CCCCCCCCCCCCCCC		43.8325159151
331PhosphorylationGNVSEGESPPDSQED
CCCCCCCCCCCCHHC		53.2222115753
335PhosphorylationEGESPPDSQEDSFQG
CCCCCCCCHHCCCCC		41.0428450419
339PhosphorylationPPDSQEDSFQGRQKS
CCCCHHCCCCCCHHH		20.7928450419
346PhosphorylationSFQGRQKSKDKAATP
CCCCCHHHCCCCCCC		37.44-
347MethylationFQGRQKSKDKAATPR
CCCCHHHCCCCCCCC		70.99116253273
352PhosphorylationKSKDKAATPRKDGPK
HHCCCCCCCCCCCCC		28.6124719451
353UbiquitinationSKDKAATPRKDGPKR
HCCCCCCCCCCCCCC		36.2822817900
355UbiquitinationDKAATPRKDGPKRSV
CCCCCCCCCCCCCCH		69.1422817900
357UbiquitinationAATPRKDGPKRSVLS
CCCCCCCCCCCCHHC		32.4422817900
359UbiquitinationTPRKDGPKRSVLSKS
CCCCCCCCCCHHCCC		63.9422817900
361PhosphorylationRKDGPKRSVLSKSVP
CCCCCCCCHHCCCCC		33.2724719451
363UbiquitinationDGPKRSVLSKSVPGY
CCCCCCHHCCCCCCC		5.8629967540
364PhosphorylationGPKRSVLSKSVPGYK
CCCCCHHCCCCCCCC		22.2626074081
365UbiquitinationPKRSVLSKSVPGYKP
CCCCHHCCCCCCCCC		51.8429967540
365AcetylationPKRSVLSKSVPGYKP
CCCCHHCCCCCCCCC		51.8425953088
366PhosphorylationKRSVLSKSVPGYKPK
CCCHHCCCCCCCCCC		30.1226074081
370PhosphorylationLSKSVPGYKPKVIPN
HCCCCCCCCCCCCCC		20.3224719451
385SumoylationAICGICLKGKESNKK
CCHHEEECCCHHCCC		64.6228112733
391AcetylationLKGKESNKKGKAESL
ECCCHHCCCCCCCHH		72.667493353
484PhosphorylationCCQRAPPTPRKVGRR
HHHCCCCCCCCCCCC		34.3723312004
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 PHF10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF10_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 PHF10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LMBL2_HUMANL3MBTL2physical
16189514
APLP1_HUMANAPLP1physical
16169070
UT14A_HUMANUTP14Aphysical
16169070
SETB1_HUMANSETDB1physical
16169070
U119A_HUMANUNC119physical
16169070
SMCA2_HUMANSMARCA2physical
22334708
SMCA4_HUMANSMARCA4physical
22334708
SMRC1_HUMANSMARCC1physical
22334708
TF65_HUMANRELAphysical
22334708
NFKB1_HUMANNFKB1physical
22334708
SNF5_HUMANSMARCB1physical
22939629
SMCA2_HUMANSMARCA2physical
22939629
SMRD1_HUMANSMARCD1physical
22939629
SMRC2_HUMANSMARCC2physical
22939629
SMRC1_HUMANSMARCC1physical
22939629
SMCA4_HUMANSMARCA4physical
22939629
SMCE1_HUMANSMARCE1physical
22939629
STAM2_HUMANSTAM2physical
21988832
LMBL2_HUMANL3MBTL2physical
25416956
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 PHF10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-301 ANDSER-327, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-331, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-297 ANDSER-301, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASSSPECTROMETRY.
"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-297 AND SER-301, ANDMASS SPECTROMETRY.

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