PHF6_HUMAN - dbPTM
PHF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHF6_HUMAN
UniProt AC Q8IWS0
Protein Name PHD finger protein 6
Gene Name PHF6
Organism Homo sapiens (Human).
Sequence Length 365
Subcellular Localization Nucleus. Nucleus, nucleolus. Chromosome, centromere, kinetochore . Nuclear, it particularly localizes to the nucleolus.
Protein Description Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription..
Protein Sequence MSSSVEQKKGPTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEADLEESFNEHELEPSSPKSKKKSRKGRPRKTNFKGLSEDTRSTSSHGTDEMESSSYRDRSPHRSSPSDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNHSGNDERDEEDEERESKSRGKVEIDQQQLTQQQLNGN
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------MSSSVEQKK
------CCCCCCCCC		31.1822814378
4Phosphorylation----MSSSVEQKKGP
----CCCCCCCCCCC		23.5121130716
8UbiquitinationMSSSVEQKKGPTRQR
CCCCCCCCCCCCCCC		46.31-
8UbiquitinationMSSSVEQKKGPTRQR
CCCCCCCCCCCCCCC		46.31-
8SumoylationMSSSVEQKKGPTRQR
CCCCCCCCCCCCCCC		46.31-
8SumoylationMSSSVEQKKGPTRQR
CCCCCCCCCCCCCCC		46.31-
8UbiquitinationMSSSVEQKKGPTRQR
CCCCCCCCCCCCCCC		46.3133845483
12PhosphorylationVEQKKGPTRQRKCGF
CCCCCCCCCCCCCCC		48.3721130716
21AcetylationQRKCGFCKSNRDKEC
CCCCCCCCCCCCCHH		48.8025953088
21UbiquitinationQRKCGFCKSNRDKEC
CCCCCCCCCCCCCHH		48.8024816145
26AcetylationFCKSNRDKECGQLLI
CCCCCCCCHHHCEEE		52.2225953088
26UbiquitinationFCKSNRDKECGQLLI
CCCCCCCCHHHCEEE		52.2233845483
38UbiquitinationLLISENQKVAAHHKC
EEECCCHHHHHHHHH		45.48-
38UbiquitinationLLISENQKVAAHHKC
EEECCCHHHHHHHHH		45.48-
38UbiquitinationLLISENQKVAAHHKC
EEECCCHHHHHHHHH		45.4829967540
49PhosphorylationHHKCMLFSSALVSSH
HHHHHHHHHHHHCCC		15.6730624053
50PhosphorylationHKCMLFSSALVSSHS
HHHHHHHHHHHCCCC		20.4930624053
54PhosphorylationLFSSALVSSHSDNES
HHHHHHHCCCCCCCC		24.1528450419
55PhosphorylationFSSALVSSHSDNESL
HHHHHHCCCCCCCCC		21.3828450419
57PhosphorylationSALVSSHSDNESLGG
HHHHCCCCCCCCCCC		44.0428464451
61PhosphorylationSSHSDNESLGGFSIE
CCCCCCCCCCCCCHH		38.2730624053
78UbiquitinationQKEIKRGTKLMCSLC
HHHHHHCCCEEHHHH		25.66-
79AcetylationKEIKRGTKLMCSLCH
HHHHHCCCEEHHHHC		36.7325953088
79UbiquitinationKEIKRGTKLMCSLCH
HHHHHCCCEEHHHHC		36.7329967540
83PhosphorylationRGTKLMCSLCHCPGA
HCCCEEHHHHCCCCC		21.7727080861
84UbiquitinationGTKLMCSLCHCPGAT
CCCEEHHHHCCCCCE		1.65-
91PhosphorylationLCHCPGATIGCDVKT
HHCCCCCEEECCEEC		24.6627080861
97AcetylationATIGCDVKTCHRTYH
CEEECCEECCCHHEE		31.9825953088
112UbiquitinationYHCALHDKAQIREKP
EHHHCCCHHHHHCCC		31.29-
1122-HydroxyisobutyrylationYHCALHDKAQIREKP
EHHHCCCHHHHHCCC		31.29-
112UbiquitinationYHCALHDKAQIREKP
EHHHCCCHHHHHCCC		31.29-
118UbiquitinationDKAQIREKPSQGIYM
CHHHHHCCCCCCEEE		39.87-
118AcetylationDKAQIREKPSQGIYM
CHHHHHCCCCCCEEE		39.8725953088
118UbiquitinationDKAQIREKPSQGIYM
CHHHHHCCCCCCEEE		39.87-
120PhosphorylationAQIREKPSQGIYMVY
HHHHCCCCCCEEEEE		52.7017525332
124PhosphorylationEKPSQGIYMVYCRKH
CCCCCCEEEEEECCC		6.3220068231
127PhosphorylationSQGIYMVYCRKHKKT
CCCEEEEEECCCCCC		3.0920068231
128GlutathionylationQGIYMVYCRKHKKTA
CCEEEEEECCCCCCC		2.9622555962
134PhosphorylationYCRKHKKTAHNSEAD
EECCCCCCCCCCHHH		37.6430266825
134 (in isoform 2)Phosphorylation-37.6423927012
138PhosphorylationHKKTAHNSEADLEES
CCCCCCCCHHHHHHH		25.0522167270
138 (in isoform 2)Phosphorylation-25.0523927012
139UbiquitinationKKTAHNSEADLEESF
CCCCCCCHHHHHHHH		52.07-
145PhosphorylationSEADLEESFNEHELE
CHHHHHHHHCHHCCC		24.8129255136
146 (in isoform 2)Phosphorylation-16.3923927012
154PhosphorylationNEHELEPSSPKSKKK
CHHCCCCCCCCCCCC		50.3129255136
155PhosphorylationEHELEPSSPKSKKKS
HHCCCCCCCCCCCCC		47.2429255136
155 (in isoform 2)Phosphorylation-47.2426503892
156PhosphorylationHELEPSSPKSKKKSR
HCCCCCCCCCCCCCC		49.6432142685
156 (in isoform 2)Phosphorylation-49.6430266825
158PhosphorylationLEPSSPKSKKKSRKG
CCCCCCCCCCCCCCC		53.7623927012
159 (in isoform 2)Phosphorylation-71.0521949786
162PhosphorylationSPKSKKKSRKGRPRK
CCCCCCCCCCCCCCC		48.37-
169MethylationSRKGRPRKTNFKGLS
CCCCCCCCCCCCCCC		50.97115974937
173SumoylationRPRKTNFKGLSEDTR
CCCCCCCCCCCCCCC		62.10-
173AcetylationRPRKTNFKGLSEDTR
CCCCCCCCCCCCCCC		62.1026051181
173MethylationRPRKTNFKGLSEDTR
CCCCCCCCCCCCCCC		62.1066729685
173SumoylationRPRKTNFKGLSEDTR
CCCCCCCCCCCCCCC		62.1025218447
173UbiquitinationRPRKTNFKGLSEDTR
CCCCCCCCCCCCCCC		62.1032015554
174UbiquitinationPRKTNFKGLSEDTRS
CCCCCCCCCCCCCCC		30.23-
174UbiquitinationPRKTNFKGLSEDTRS
CCCCCCCCCCCCCCC		30.2332015554
176PhosphorylationKTNFKGLSEDTRSTS
CCCCCCCCCCCCCCC		41.9430624053
179PhosphorylationFKGLSEDTRSTSSHG
CCCCCCCCCCCCCCC		23.5930576142
181PhosphorylationGLSEDTRSTSSHGTD
CCCCCCCCCCCCCCC		34.4323927012
182PhosphorylationLSEDTRSTSSHGTDE
CCCCCCCCCCCCCCC		30.8423927012
183PhosphorylationSEDTRSTSSHGTDEM
CCCCCCCCCCCCCCC		22.9126503892
184PhosphorylationEDTRSTSSHGTDEME
CCCCCCCCCCCCCCC		26.4826503892
185 (in isoform 2)Phosphorylation-42.8318669648
187PhosphorylationRSTSSHGTDEMESSS
CCCCCCCCCCCCCCC		24.3025159151
192PhosphorylationHGTDEMESSSYRDRS
CCCCCCCCCCCCCCC		24.2323401153
193UbiquitinationGTDEMESSSYRDRSP
CCCCCCCCCCCCCCC		20.34-
193PhosphorylationGTDEMESSSYRDRSP
CCCCCCCCCCCCCCC		20.3426503892
194PhosphorylationTDEMESSSYRDRSPH
CCCCCCCCCCCCCCC		33.2023927012
195PhosphorylationDEMESSSYRDRSPHR
CCCCCCCCCCCCCCC		20.6220201521
199PhosphorylationSSSYRDRSPHRSSPS
CCCCCCCCCCCCCCC		29.3720201521
200PhosphorylationSSYRDRSPHRSSPSD
CCCCCCCCCCCCCCC		28.0132645325
203PhosphorylationRDRSPHRSSPSDTRP
CCCCCCCCCCCCCCC		43.5030278072
204PhosphorylationDRSPHRSSPSDTRPK
CCCCCCCCCCCCCCC		28.5120201521
206PhosphorylationSPHRSSPSDTRPKCG
CCCCCCCCCCCCCCC		54.2721955146
208PhosphorylationHRSSPSDTRPKCGFC
CCCCCCCCCCCCCCC		53.8920201521
211UbiquitinationSPSDTRPKCGFCHVG
CCCCCCCCCCCCCCC		43.6429967540
212UbiquitinationPSDTRPKCGFCHVGE
CCCCCCCCCCCCCCC		5.8329967540
227SumoylationEENEARGKLHIFNAK
CCCCCCCCEEEECHH		31.19-
227AcetylationEENEARGKLHIFNAK
CCCCCCCCEEEECHH		31.1925953088
227SumoylationEENEARGKLHIFNAK
CCCCCCCCEEEECHH		31.1928112733
227UbiquitinationEENEARGKLHIFNAK
CCCCCCCCEEEECHH		31.1932015554
228UbiquitinationENEARGKLHIFNAKK
CCCCCCCEEEECHHH		4.11-
228UbiquitinationENEARGKLHIFNAKK
CCCCCCCEEEECHHH		4.1132015554
232UbiquitinationRGKLHIFNAKKAAAH
CCCEEEECHHHHHHH		50.69-
2342-HydroxyisobutyrylationKLHIFNAKKAAAHYK
CEEEECHHHHHHHCE		44.01-
234AcetylationKLHIFNAKKAAAHYK
CEEEECHHHHHHHCE		44.0125953088
234UbiquitinationKLHIFNAKKAAAHYK
CEEEECHHHHHHHCE		44.0129967540
235UbiquitinationLHIFNAKKAAAHYKC
EEEECHHHHHHHCEE		40.6329967540
239UbiquitinationNAKKAAAHYKCMLFS
CHHHHHHHCEEEEEE		20.19-
245UbiquitinationAHYKCMLFSSGTVQL
HHCEEEEEECCEEEE		1.86-
247PhosphorylationYKCMLFSSGTVQLTT
CEEEEEECCEEEEEE		31.02-
266SumoylationEFGDFDIKTVLQEIK
HHCCCCHHHHHHHHH		34.13-
266SumoylationEFGDFDIKTVLQEIK
HHCCCCHHHHHHHHH		34.13-
266UbiquitinationEFGDFDIKTVLQEIK
HHCCCCHHHHHHHHH		34.1332015554
267UbiquitinationFGDFDIKTVLQEIKR
HCCCCHHHHHHHHHC		27.12-
267UbiquitinationFGDFDIKTVLQEIKR
HCCCCHHHHHHHHHC		27.1232015554
2732-HydroxyisobutyrylationKTVLQEIKRGKRMKC
HHHHHHHHCCCCCEE		55.11-
273AcetylationKTVLQEIKRGKRMKC
HHHHHHHHCCCCCEE		55.1125953088
273UbiquitinationKTVLQEIKRGKRMKC
HHHHHHHHCCCCCEE		55.1133845483
274UbiquitinationTVLQEIKRGKRMKCT
HHHHHHHCCCCCEEE		62.62-
276UbiquitinationLQEIKRGKRMKCTLC
HHHHHCCCCCEEEEC		54.04-
278UbiquitinationEIKRGKRMKCTLCSQ
HHHCCCCCEEEECCC		4.81-
279UbiquitinationIKRGKRMKCTLCSQP
HHCCCCCEEEECCCC		28.2722505724
280UbiquitinationKRGKRMKCTLCSQPG
HCCCCCEEEECCCCC		2.28-
281PhosphorylationRGKRMKCTLCSQPGA
CCCCCEEEECCCCCC		25.8629083192
284PhosphorylationRMKCTLCSQPGATIG
CCEEEECCCCCCCEE		42.3929083192
289PhosphorylationLCSQPGATIGCEIKA
ECCCCCCCEEEEEEE		24.6629083192
295AcetylationATIGCEIKACVKTYH
CCEEEEEEEEEEHHC		17.2826051181
295UbiquitinationATIGCEIKACVKTYH
CCEEEEEEEEEEHHC		17.2832015554
299AcetylationCEIKACVKTYHYHCG
EEEEEEEEHHCCCCC		43.1626051181
310AcetylationYHCGVQDKAKYIENM
CCCCCHHHHHHHHHH		29.6826051181
310UbiquitinationYHCGVQDKAKYIENM
CCCCCHHHHHHHHHH		29.6829967540
311UbiquitinationHCGVQDKAKYIENMS
CCCCHHHHHHHHHHH		20.41-
312AcetylationCGVQDKAKYIENMSR
CCCHHHHHHHHHHHH		53.1325953088
312UbiquitinationCGVQDKAKYIENMSR
CCCHHHHHHHHHHHH		53.1329967540
313UbiquitinationGVQDKAKYIENMSRG
CCHHHHHHHHHHHHH		20.51-
315UbiquitinationQDKAKYIENMSRGIY
HHHHHHHHHHHHHHH		43.73-
319MethylationKYIENMSRGIYKLYC
HHHHHHHHHHHHHHC		25.43115487435
322PhosphorylationENMSRGIYKLYCKNH
HHHHHHHHHHHCCCC		9.5829496907
323AcetylationNMSRGIYKLYCKNHS
HHHHHHHHHHCCCCC		30.9325953088
323UbiquitinationNMSRGIYKLYCKNHS
HHHHHHHHHHCCCCC		30.9329967540
325PhosphorylationSRGIYKLYCKNHSGN
HHHHHHHHCCCCCCC		9.3829496907
327UbiquitinationGIYKLYCKNHSGNDE
HHHHHHCCCCCCCCC		44.1029967540
335MethylationNHSGNDERDEEDEER
CCCCCCCCCHHHHHH		60.55115487427
344PhosphorylationEEDEERESKSRGKVE
HHHHHHHHHHCCCCE		42.0019562805
345SumoylationEDEERESKSRGKVEI
HHHHHHHHHCCCCEE		39.14-
345SumoylationEDEERESKSRGKVEI
HHHHHHHHHCCCCEE		39.14-
346PhosphorylationDEERESKSRGKVEID
HHHHHHHHCCCCEEC		56.3922617229
349SumoylationRESKSRGKVEIDQQQ
HHHHHCCCCEECHHH		35.27-
349AcetylationRESKSRGKVEIDQQQ
HHHHHCCCCEECHHH		35.2726051181
349SumoylationRESKSRGKVEIDQQQ
HHHHHCCCCEECHHH		35.27-
349UbiquitinationRESKSRGKVEIDQQQ
HHHHHCCCCEECHHH		35.2724816145
358O-linked_GlycosylationEIDQQQLTQQQLNGN
EECHHHHHHHHHCCC		21.7228510447
358PhosphorylationEIDQQQLTQQQLNGN
EECHHHHHHHHHCCC		21.7217525332
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 PHF6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHF6_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 PHF6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBBP4_HUMANRBBP4physical
22720776
HDAC1_HUMANHDAC1physical
22720776
CHD4_HUMANCHD4physical
22720776
CHD3_HUMANCHD3physical
22720776
RBBP7_HUMANRBBP7physical
22720776
H12_HUMANHIST1H1Cphysical
22720776
H2B1B_HUMANHIST1H2BBphysical
22720776
H2AZ_HUMANH2AFZphysical
22720776
U520_HUMANSNRNP200physical
22720776
PRP8_HUMANPRPF8physical
22720776
ROA2_HUMANHNRNPA2B1physical
22720776
HNRH3_HUMANHNRNPH3physical
22720776
HNRPU_HUMANHNRNPUphysical
22720776
RALY_HUMANRALYphysical
22720776
ROA3_HUMANHNRNPA3physical
22720776
PCBP2_HUMANPCBP2physical
22720776
HNRPC_HUMANHNRNPCphysical
22720776
MGN_HUMANMAGOHphysical
22720776
RLA0_HUMANRPLP0physical
22720776
RS18_HUMANRPS18physical
22720776
RS25_HUMANRPS25physical
22720776
RL22_HUMANRPL22physical
22720776
RL4_HUMANRPL4physical
22720776
RL30_HUMANRPL30physical
22720776
LYAR_HUMANLYARphysical
22720776
FBRL_HUMANFBLphysical
22720776
NPM_HUMANNPM1physical
22720776
TBA1C_HUMANTUBA1Cphysical
22720776
PIP_HUMANPIPphysical
22720776
SRP14_HUMANSRP14physical
22720776
RBBP4_HUMANRBBP4physical
25601084
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
301900Boerjeson-Forssman-Lehmann syndrome (BFLS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHF6_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-138 AND SER-145, ANDMASS 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-154 AND SER-155, 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-138; SER-145; SER-154AND SER-155, 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-120 AND THR-358, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-145; SER-154;SER-155; SER-199 AND SER-204, AND MASS SPECTROMETRY.
"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-199 AND SER-203, ANDMASS SPECTROMETRY.

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