PHF19_HUMAN - dbPTM
PHF19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF19_HUMAN
UniProt AC Q5T6S3
Protein Name PHD finger protein 19
Gene Name PHF19
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Nucleus .
Protein Description Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Probably involved in the transition from an active state to a repressed state in embryonic stem cells: acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting H3K36me3 histone demethylases RIOX1 or KDM2B, leading to demethylation of H3K36 and recruitment of the PRC2 complex that mediates H3K27me3 methylation, followed by de novo silencing. Recruits the PRC2 complex to CpG islands and contributes to embryonic stem cell self-renewal. Also binds dimethylated at 'Lys-36' (H3K36me2). Isoform 1 and isoform 2 inhibit transcription from an HSV-tk promoter..
Protein Sequence MENRALDPGTRDSYGATSHLPNKGALAKVKNNFKDLMSKLTEGQYVLCRWTDGLYYLGKIKRVSSSKQSCLVTFEDNSKYWVLWKDIQHAGVPGEEPKCNICLGKTSGPLNEILICGKCGLGYHQQCHIPIAGSADQPLLTPWFCRRCIFALAVRKGGALKKGAIARTLQAVKMVLSYQPEELEWDSPHRTNQQQCYCYCGGPGEWYLRMLQCYRCRQWFHEACTQCLNEPMMFGDRFYLFFCSVCNQGPEYIERLPLRWVDVVHLALYNLGVQSKKKYFDFEEILAFVNHHWELLQLGKLTSTPVTDRGPHLLNALNSYKSRFLCGKEIKKKKCIFRLRIRVPPNPPGKLLPDKGLLPNENSASSELRKRGKSKPGLLPHEFQQQKRRVYRRKRSKFLLEDAIPSSDFTSAWSTNHHLASIFDFTLDEIQSLKSASSGQTFFSDVDSTDAASTSGSASTSLSYDSRWTVGSRKRKLAAKAYMPLRAKRWAAELDGRCPSDSSAEGASVPERPDEGIDSHTFESISEDDSSLSHLKSSITNYFGAAGRLACGEKYQVLARRVTPEGKVQYLVEWEGTTPY
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
10PhosphorylationNRALDPGTRDSYGAT
CCCCCCCCCCCCCCC		36.3719664994
13PhosphorylationLDPGTRDSYGATSHL
CCCCCCCCCCCCCCC		23.3624732914
14PhosphorylationDPGTRDSYGATSHLP
CCCCCCCCCCCCCCC		18.3124732914
17PhosphorylationTRDSYGATSHLPNKG
CCCCCCCCCCCCCCC		16.5923186163
18PhosphorylationRDSYGATSHLPNKGA
CCCCCCCCCCCCCCH		23.6123186163
23UbiquitinationATSHLPNKGALAKVK
CCCCCCCCCHHHHHH		43.55-
45PhosphorylationSKLTEGQYVLCRWTD
HHHHCCCEEEEEECC		13.2722817900
55PhosphorylationCRWTDGLYYLGKIKR
EEECCCCEEEEEEEE		11.3723917254
56PhosphorylationRWTDGLYYLGKIKRV
EECCCCEEEEEEEEE		17.64-
67UbiquitinationIKRVSSSKQSCLVTF
EEEECCCCCCEEEEE		48.45-
73PhosphorylationSKQSCLVTFEDNSKY
CCCCEEEEECCCCEE		14.3629759185
78PhosphorylationLVTFEDNSKYWVLWK
EEEECCCCEEEEEEE		39.1729759185
105UbiquitinationKCNICLGKTSGPLNE
CCCEECCCCCCCHHH		26.94-
106PhosphorylationCNICLGKTSGPLNEI
CCEECCCCCCCHHHE		36.8018491316
107PhosphorylationNICLGKTSGPLNEIL
CEECCCCCCCHHHEE		41.7318491316
157 (in isoform 2)Phosphorylation-18.9525850435
160 (in isoform 2)Phosphorylation-7.1518691976
161 (in isoform 2)Phosphorylation-48.9417192257
162MethylationRKGGALKKGAIARTL
HCCCHHHCCHHHHHH		55.19116252873
166 (in isoform 2)Phosphorylation-9.6217192257
169 (in isoform 2)Phosphorylation-2.2822199227
170 (in isoform 2)Phosphorylation-43.4222199227
171 (in isoform 2)Phosphorylation-13.1522199227
184 (in isoform 2)Phosphorylation-53.14-
185 (in isoform 2)Ubiquitination-24.81-
187PhosphorylationPEELEWDSPHRTNQQ
HHHCCCCCCCCCCCC		24.5523186163
191PhosphorylationEWDSPHRTNQQQCYC
CCCCCCCCCCCEEEE		34.0527732954
197PhosphorylationRTNQQQCYCYCGGPG
CCCCCEEEEECCCCC		5.1127732954
199PhosphorylationNQQQCYCYCGGPGEW
CCCEEEEECCCCCHH		2.8027732954
207PhosphorylationCGGPGEWYLRMLQCY
CCCCCHHHHHHHHHH		4.7027732954
328UbiquitinationKSRFLCGKEIKKKKC
HHHHCCCCHHCCCEE		56.10-
355UbiquitinationPGKLLPDKGLLPNEN
CCCCCCCCCCCCCCC		49.90-
365PhosphorylationLPNENSASSELRKRG
CCCCCCHHHHHHHCC		24.9425850435
366PhosphorylationPNENSASSELRKRGK
CCCCCHHHHHHHCCC		40.1325850435
374PhosphorylationELRKRGKSKPGLLPH
HHHHCCCCCCCCCCH		47.0828555341
375UbiquitinationLRKRGKSKPGLLPHE
HHHCCCCCCCCCCHH		46.74-
387UbiquitinationPHEFQQQKRRVYRRK
CHHHHHHHHHHHHHH		37.52-
476MethylationTVGSRKRKLAAKAYM
CCCCHHHHHHHHHHC		45.58116252879
508PhosphorylationDSSAEGASVPERPDE
CCCCCCCCCCCCCCC		49.4129759185
537PhosphorylationSSLSHLKSSITNYFG
CHHHHHHHHHHHHCC		33.0825627689
538PhosphorylationSLSHLKSSITNYFGA
HHHHHHHHHHHHCCH		31.6725627689
554UbiquitinationGRLACGEKYQVLARR
HHHHCCCCEEEEEEE		26.68-
563PhosphorylationQVLARRVTPEGKVQY
EEEEEEECCCCCEEE		17.5124719451
577PhosphorylationYLVEWEGTTPY----
EEEEEECCCCC----		17.0624719451
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 PHF19_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF19_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 PHF19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EZH2_HUMANEZH2physical
21143197
EED_HUMANEEDphysical
21143197
PHF19_HUMANPHF19physical
21143197
HIC1_HUMANHIC1physical
22315224
KDM1A_HUMANKDM1Aphysical
23455924
SUV91_HUMANSUV39H1physical
23455924
SUV92_HUMANSUV39H2physical
23455924
H31_HUMANHIST1H3Aphysical
23104054
SUZ12_HUMANSUZ12physical
23104054
EZH2_HUMANEZH2physical
23104054
EED_HUMANEEDphysical
23104054
RBBP7_HUMANRBBP7physical
23104054
RBBP4_HUMANRBBP4physical
23104054
QRIC1_HUMANQRICH1physical
26186194
DCTN3_HUMANDCTN3physical
26186194
MOG1_HUMANRANGRFphysical
26186194
RBM5_HUMANRBM5physical
26186194
SRC_HUMANSRCphysical
26186194
GNA13_HUMANGNA13physical
26186194
RASH_HUMANHRASphysical
26186194
RAP2A_HUMANRAP2Aphysical
26186194
EPCR_HUMANPROCRphysical
26186194
SUZ12_HUMANSUZ12physical
28514442
EZH2_HUMANEZH2physical
28514442
NRBP2_HUMANNRBP2physical
28514442
EZH1_HUMANEZH1physical
28514442
EED_HUMANEEDphysical
28514442
KCC1A_HUMANCAMK1physical
28514442
T2FA_HUMANGTF2F1physical
28514442
GSTCD_HUMANGSTCDphysical
28514442
CHAP1_HUMANCHAMP1physical
28514442
PDLI5_HUMANPDLIM5physical
28514442
TEX10_HUMANTEX10physical
28514442
SENP3_HUMANSENP3physical
28514442
ACTBL_HUMANACTBL2physical
28514442
PELP1_HUMANPELP1physical
28514442
UTRO_HUMANUTRNphysical
28514442
MASU1_HUMANMALSU1physical
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 PHF19_HUMAN

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Related Literatures of Post-Translational Modification

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