PHF23_HUMAN - dbPTM
PHF23_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF23_HUMAN
UniProt AC Q9BUL5
Protein Name PHD finger protein 23 {ECO:0000303|PubMed:25484098}
Gene Name PHF23 {ECO:0000303|PubMed:25484098}
Organism Homo sapiens (Human).
Sequence Length 403
Subcellular Localization Nucleus . Cytoplasm . Mainly present in the nucleus and part in the cytoplasm.
Protein Description Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria..
Protein Sequence MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKEESDWPASGSSSPLRGESAADSDGWDSAPSDLRTIQTFVKKAKSSKRRAAQAGPTQPGPPRSTFSRLQAPDSATLLEKMKLKDSLFDLDGPKVASPLSPTSLTHTSRPPAALTPVPLSQGDLSHPPRKKDRKNRKLGPGAGAGFGVLRRPRPTPGDGEKRSRIKKSKKRKLKKAERGDRLPPPGPPQAPPSDTDSEEEEEEEEEEEEEEMATVVGGEAPVPVLPTPPEAPRPPATVHPEGVPPADSESKEVGSTETSQDGDASSSEGEMRVMDEDIMVESGDDSWDLITCYCRKPFAGRPMIECSLCGTWIHLSCAKIKKTNVPDFFYCQKCKELRPEARRLGGPPKSGEP
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
1Acetylation-------MLEAMAEP
-------CCCCCCCC		7.4322814378
9PhosphorylationLEAMAEPSPEDPPPT
CCCCCCCCCCCCCCC		32.2123663014
16PhosphorylationSPEDPPPTLKPETQP
CCCCCCCCCCCCCCC		53.8623663014
21PhosphorylationPPTLKPETQPPEKRR
CCCCCCCCCCCHHHC		55.7023663014
30PhosphorylationPPEKRRRTIEDFNKF
CCHHHCCCHHHHHHH		27.2321815630
55PhosphorylationIPPSKEESDWPASGS
CCCCCCCCCCCCCCC		46.1726074081
60PhosphorylationEESDWPASGSSSPLR
CCCCCCCCCCCCCCC		34.8222167270
62PhosphorylationSDWPASGSSSPLRGE
CCCCCCCCCCCCCCC		25.7522167270
63PhosphorylationDWPASGSSSPLRGES
CCCCCCCCCCCCCCC		39.2322167270
64PhosphorylationWPASGSSSPLRGESA
CCCCCCCCCCCCCCC		29.6522167270
70PhosphorylationSSPLRGESAADSDGW
CCCCCCCCCCCCCCC		31.4230266825
74PhosphorylationRGESAADSDGWDSAP
CCCCCCCCCCCCCCC		33.0430266825
79PhosphorylationADSDGWDSAPSDLRT
CCCCCCCCCCHHHHH		35.2530266825
82PhosphorylationDGWDSAPSDLRTIQT
CCCCCCCHHHHHHHH		49.3323927012
85PhosphorylationDSAPSDLRTIQTFVK
CCCCHHHHHHHHHHH		34.4732142685
92AcetylationRTIQTFVKKAKSSKR
HHHHHHHHHHHHHHH		42.7025953088
107PhosphorylationRAAQAGPTQPGPPRS
HHHHHCCCCCCCCCC		46.6129496963
114PhosphorylationTQPGPPRSTFSRLQA
CCCCCCCCHHHHCCC		39.3128555341
117PhosphorylationGPPRSTFSRLQAPDS
CCCCCHHHHCCCCCH		31.9728555341
124PhosphorylationSRLQAPDSATLLEKM
HHCCCCCHHHHHHHH		23.3028355574
126PhosphorylationLQAPDSATLLEKMKL
CCCCCHHHHHHHHCC		35.5125850435
128UbiquitinationAPDSATLLEKMKLKD
CCCHHHHHHHHCCCC		5.30-
130UbiquitinationDSATLLEKMKLKDSL
CHHHHHHHHCCCCCC		41.1029967540
130UbiquitinationDSATLLEKMKLKDSL
CHHHHHHHHCCCCCC		41.10-
1302-HydroxyisobutyrylationDSATLLEKMKLKDSL
CHHHHHHHHCCCCCC		41.10-
132UbiquitinationATLLEKMKLKDSLFD
HHHHHHHCCCCCCCC		64.55-
134UbiquitinationLLEKMKLKDSLFDLD
HHHHHCCCCCCCCCC		39.4929967540
134SumoylationLLEKMKLKDSLFDLD
HHHHHCCCCCCCCCC		39.49-
134SumoylationLLEKMKLKDSLFDLD
HHHHHCCCCCCCCCC		39.49-
147PhosphorylationLDGPKVASPLSPTSL
CCCCCCCCCCCCCCC		29.3929255136
147 (in isoform 2)Phosphorylation-29.3923879269
148PhosphorylationDGPKVASPLSPTSLT
CCCCCCCCCCCCCCC		27.4132142685
150 (in isoform 2)Phosphorylation-29.5220068231
150PhosphorylationPKVASPLSPTSLTHT
CCCCCCCCCCCCCCC		29.5229255136
152PhosphorylationVASPLSPTSLTHTSR
CCCCCCCCCCCCCCC		32.7529255136
153PhosphorylationASPLSPTSLTHTSRP
CCCCCCCCCCCCCCC		34.3529255136
155PhosphorylationPLSPTSLTHTSRPPA
CCCCCCCCCCCCCCC		23.9125159151
157PhosphorylationSPTSLTHTSRPPAAL
CCCCCCCCCCCCCCC		22.6125159151
158PhosphorylationPTSLTHTSRPPAALT
CCCCCCCCCCCCCCC		34.8725159151
165PhosphorylationSRPPAALTPVPLSQG
CCCCCCCCCCCCCCC		19.9525159151
170PhosphorylationALTPVPLSQGDLSHP
CCCCCCCCCCCCCCC		26.5017525332
175PhosphorylationPLSQGDLSHPPRKKD
CCCCCCCCCCCCHHC		38.3920068231
205PhosphorylationVLRRPRPTPGDGEKR
EECCCCCCCCCCHHH		40.9828555341
211AcetylationPTPGDGEKRSRIKKS
CCCCCCHHHHHHHHH		62.2912624475
218PhosphorylationKRSRIKKSKKRKLKK
HHHHHHHHHHHHHHH		38.1130087585
305PhosphorylationSESKEVGSTETSQDG
CCCCCCCCCCCCCCC		28.3921406692
306PhosphorylationESKEVGSTETSQDGD
CCCCCCCCCCCCCCC		37.0421406692
308PhosphorylationKEVGSTETSQDGDAS
CCCCCCCCCCCCCCC		31.6021406692
309PhosphorylationEVGSTETSQDGDASS
CCCCCCCCCCCCCCC		21.7521406692
315PhosphorylationTSQDGDASSSEGEMR
CCCCCCCCCCCCCEE		38.8525159151
316PhosphorylationSQDGDASSSEGEMRV
CCCCCCCCCCCCEEE		33.8425159151
317PhosphorylationQDGDASSSEGEMRVM
CCCCCCCCCCCEEEE		47.3125159151
332PhosphorylationDEDIMVESGDDSWDL
CCCEEEECCCCCEEE		35.7927422710
336PhosphorylationMVESGDDSWDLITCY
EEECCCCCEEEEEEE		27.5127251275
400PhosphorylationRLGGPPKSGEP----
HHCCCCCCCCC----		54.9129255136
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 PHF23_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF23_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 PHF23_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRSM1_HUMANLRSAM1physical
25484098
SIN3A_HUMANSIN3Aphysical
28514442
SP130_HUMANSAP130physical
28514442
ARI4B_HUMANARID4Bphysical
28514442
SIN3B_HUMANSIN3Bphysical
28514442
SAP30_HUMANSAP30physical
28514442
SDS3_HUMANSUDS3physical
28514442
BRM1L_HUMANBRMS1Lphysical
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 PHF23_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-315, AND MASSSPECTROMETRY.
"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-147; SER-150; THR-152;THR-165; SER-315; SER-316 AND SER-317, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND MASSSPECTROMETRY.

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