PF21A_HUMAN - dbPTM
PF21A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PF21A_HUMAN
UniProt AC Q96BD5
Protein Name PHD finger protein 21A
Gene Name PHF21A
Organism Homo sapiens (Human).
Sequence Length 680
Subcellular Localization Nucleus.
Protein Description Component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it may act as a scaffold. Inhibits KDM1A-mediated demethylation of 'Lys-4' of histone H3 in vitro, suggesting a role in demethylation regulation..
Protein Sequence MELQTLQEALKVEIQVHQKLVAQMKQDPQNADLKKQLHELQAKITALSEKQKRVVEQLRKNLIVKQEQPDKFQIQPLPQSENKLQTAQQQPLQQLQQQQQYHHHHAQQSAAASPNLTASQKTVTTASMITTKTLPLVLKAATATMPASVVGQRPTIAMVTAINSQKAVLSTDVQNTPVNLQTSSKVTGPGAEAVQIVAKNTVTLVQATPPQPIKVPQFIPPPRLTPRPNFLPQVRPKPVAQNNIPIAPAPPPMLAAPQLIQRPVMLTKFTPTTLPTSQNSIHPVRVVNGQTATIAKTFPMAQLTSIVIATPGTRLAGPQTVQLSKPSLEKQTVKSHTETDEKQTESRTITPPAAPKPKREENPQKLAFMVSLGLVTHDHLEEIQSKRQERKRRTTANPVYSGAVFEPERKKSAVTYLNSTMHPGTRKRGRPPKYNAVLGFGALTPTSPQSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTDGDIHEDFCSVCRKSGQLLMCDTCSRVYHLDCLDPPLKTIPKGMWICPRCQDQMLKKEEAIPWPGTLAIVHSYIAYKAAKEEEKQKLLKWSSDLKQEREQLEQKVKQLSNSISKCMEMKNTILARQKEMHSSLEKVKQLIRLIHGIDLSKPVDSEATVGAISNGPDCTPPANAATSTPAPSPSSQSCTANCNQGEETK
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
25 (in isoform 3)Ubiquitination-39.20-
25UbiquitinationQKLVAQMKQDPQNAD
HHHHHHHHHCCCCHH		39.2029967540
35UbiquitinationPQNADLKKQLHELQA
CCCHHHHHHHHHHHH		66.4429967540
43UbiquitinationQLHELQAKITALSEK
HHHHHHHHHHHCHHH		27.8529967540
48PhosphorylationQAKITALSEKQKRVV
HHHHHHCHHHHHHHH		40.04-
50UbiquitinationKITALSEKQKRVVEQ
HHHHCHHHHHHHHHH		58.7129967540
65SumoylationLRKNLIVKQEQPDKF
HHHHCCCCCCCCCCC		40.92-
65UbiquitinationLRKNLIVKQEQPDKF
HHHHCCCCCCCCCCC		40.9229967540
65SumoylationLRKNLIVKQEQPDKF
HHHHCCCCCCCCCCC		40.9228112733
71UbiquitinationVKQEQPDKFQIQPLP
CCCCCCCCCCCCCCC		45.9429967540
80PhosphorylationQIQPLPQSENKLQTA
CCCCCCCCCHHHHHH		40.9925159151
109O-linked_GlycosylationHHHHAQQSAAASPNL
HHHHHHHHHHHCCCC		14.06OGP
122PhosphorylationNLTASQKTVTTASMI
CCCCCCCCCCCCHHH		18.5628634298
122O-linked_GlycosylationNLTASQKTVTTASMI
CCCCCCCCCCCCHHH		18.5630059200
124PhosphorylationTASQKTVTTASMITT
CCCCCCCCCCHHHHC		23.1323401153
124O-linked_GlycosylationTASQKTVTTASMITT
CCCCCCCCCCHHHHC		23.1330059200
125PhosphorylationASQKTVTTASMITTK
CCCCCCCCCHHHHCC		16.6423401153
125O-linked_GlycosylationASQKTVTTASMITTK
CCCCCCCCCHHHHCC		16.6430059200
127PhosphorylationQKTVTTASMITTKTL
CCCCCCCHHHHCCCH		14.5028634298
130PhosphorylationVTTASMITTKTLPLV
CCCCHHHHCCCHHHH		17.3828634298
131PhosphorylationTTASMITTKTLPLVL
CCCHHHHCCCHHHHH		15.8828634298
133PhosphorylationASMITTKTLPLVLKA
CHHHHCCCHHHHHHH		31.3628634298
142PhosphorylationPLVLKAATATMPASV
HHHHHHHHCCCCHHH		27.7622210691
144PhosphorylationVLKAATATMPASVVG
HHHHHHCCCCHHHHC		21.2322210691
155PhosphorylationSVVGQRPTIAMVTAI
HHHCCCCEEEEEEEC		24.4522210691
176PhosphorylationLSTDVQNTPVNLQTS
EECCCCCCCCCEECC		16.1225159151
185UbiquitinationVNLQTSSKVTGPGAE
CCEECCCCCCCCCHH		43.5129967540
185 (in isoform 3)Ubiquitination-43.51-
201 (in isoform 2)Phosphorylation-17.7320068231
201 (in isoform 3)Phosphorylation-17.7320068231
201PhosphorylationVQIVAKNTVTLVQAT
EEEEEECEEEEEECC		17.7320068231
203 (in isoform 2)Phosphorylation-21.1220068231
203 (in isoform 3)Phosphorylation-21.1220068231
208PhosphorylationTVTLVQATPPQPIKV
EEEEEECCCCCCCCC		20.5728555341
209 (in isoform 2)Phosphorylation-28.6620068231
209 (in isoform 3)Phosphorylation-28.6620068231
270O-linked_GlycosylationPVMLTKFTPTTLPTS
CEEEEECCCCCCCCC		22.6830059200
272O-linked_GlycosylationMLTKFTPTTLPTSQN
EEEECCCCCCCCCCC		37.6030059200
273O-linked_GlycosylationLTKFTPTTLPTSQNS
EEECCCCCCCCCCCC		31.7630059200
273PhosphorylationLTKFTPTTLPTSQNS
EEECCCCCCCCCCCC		31.76-
276O-linked_GlycosylationFTPTTLPTSQNSIHP
CCCCCCCCCCCCCCC		46.1630059200
276PhosphorylationFTPTTLPTSQNSIHP
CCCCCCCCCCCCCCC		46.16-
277O-linked_GlycosylationTPTTLPTSQNSIHPV
CCCCCCCCCCCCCCE		25.9830059200
277PhosphorylationTPTTLPTSQNSIHPV
CCCCCCCCCCCCCCE		25.98-
297PhosphorylationQTATIAKTFPMAQLT
CEEEEEECCCHHHEE		24.7721406692
304PhosphorylationTFPMAQLTSIVIATP
CCCHHHEEEEEEECC		12.3420068231
305PhosphorylationFPMAQLTSIVIATPG
CCHHHEEEEEEECCC		24.3721406692
310PhosphorylationLTSIVIATPGTRLAG
EEEEEEECCCCCCCC		15.8921406692
313PhosphorylationIVIATPGTRLAGPQT
EEEECCCCCCCCCCE		24.5821406692
314MethylationVIATPGTRLAGPQTV
EEECCCCCCCCCCEE		28.5854557969
320PhosphorylationTRLAGPQTVQLSKPS
CCCCCCCEEECCCCC		17.2221406692
324PhosphorylationGPQTVQLSKPSLEKQ
CCCEEECCCCCHHHH		25.9821406692
325UbiquitinationPQTVQLSKPSLEKQT
CCEEECCCCCHHHHH		47.41-
326 (in isoform 3)Ubiquitination-40.55-
334UbiquitinationSLEKQTVKSHTETDE
CHHHHHCCCCCCCCC		39.65-
335 (in isoform 3)Ubiquitination-31.16-
339PhosphorylationTVKSHTETDEKQTES
HCCCCCCCCCCCCCC		51.09-
344PhosphorylationTETDEKQTESRTITP
CCCCCCCCCCCCCCC		47.17-
348PhosphorylationEKQTESRTITPPAAP
CCCCCCCCCCCCCCC		38.1823403867
350PhosphorylationQTESRTITPPAAPKP
CCCCCCCCCCCCCCC		23.7023401153
351PhosphorylationTESRTITPPAAPKPK
CCCCCCCCCCCCCCC		16.8132142685
371PhosphorylationQKLAFMVSLGLVTHD
HHHHHHHHHCCCCHH		12.6322964224
376PhosphorylationMVSLGLVTHDHLEEI
HHHHCCCCHHHHHHH		26.9922964224
394PhosphorylationRQERKRRTTANPVYS
HHHHHHHHCCCCCCC		34.0023186163
395PhosphorylationQERKRRTTANPVYSG
HHHHHHHCCCCCCCC		23.7223186163
400PhosphorylationRTTANPVYSGAVFEP
HHCCCCCCCCCCCCC		11.5718083107
412PhosphorylationFEPERKKSAVTYLNS
CCCCHHHCHHHHCCC		30.8928555341
434PhosphorylationKRGRPPKYNAVLGFG
CCCCCCCCCEEEEEC		17.7123403867
444PhosphorylationVLGFGALTPTSPQSS
EEEECCCCCCCCCCC		24.8030278072
446PhosphorylationGFGALTPTSPQSSHP
EECCCCCCCCCCCCC		48.0526503892
447PhosphorylationFGALTPTSPQSSHPD
ECCCCCCCCCCCCCC		23.3428355574
450PhosphorylationLTPTSPQSSHPDSPE
CCCCCCCCCCCCCCC		33.7230278072
451PhosphorylationTPTSPQSSHPDSPEN
CCCCCCCCCCCCCCC		33.5229255136
455PhosphorylationPQSSHPDSPENEKTE
CCCCCCCCCCCCCCE		38.2726503892
475PhosphorylationPAPVQPVSLPSPTST
CCCCCCCCCCCCCCC		41.0428122231
478PhosphorylationVQPVSLPSPTSTDGD
CCCCCCCCCCCCCCC		46.2125159151
480PhosphorylationPVSLPSPTSTDGDIH
CCCCCCCCCCCCCCC		48.9028122231
481PhosphorylationVSLPSPTSTDGDIHE
CCCCCCCCCCCCCCH		28.0827251275
482PhosphorylationSLPSPTSTDGDIHED
CCCCCCCCCCCCCHH		46.6228122231
492PhosphorylationDIHEDFCSVCRKSGQ
CCCHHHHHHHHHCCC		25.0128122231
497PhosphorylationFCSVCRKSGQLLMCD
HHHHHHHCCCEEEEE		16.6627499020
525UbiquitinationPLKTIPKGMWICPRC
CCCCCCCCCEECHHH		15.9929967540
531UbiquitinationKGMWICPRCQDQMLK
CCCEECHHHHHHHCC		26.7329967540
542UbiquitinationQMLKKEEAIPWPGTL
HHCCHHHCCCCCCHH		17.7829967540
571UbiquitinationEEKQKLLKWSSDLKQ
HHHHHHHHHCHHHHH		56.3029967540
577UbiquitinationLKWSSDLKQEREQLE
HHHCHHHHHHHHHHH		55.9229967540
578 (in isoform 3)Ubiquitination-63.38-
588UbiquitinationEQLEQKVKQLSNSIS
HHHHHHHHHHHHHHH		53.1929967540
591PhosphorylationEQKVKQLSNSISKCM
HHHHHHHHHHHHHHH		26.4929083192
593PhosphorylationKVKQLSNSISKCMEM
HHHHHHHHHHHHHHH		25.5129083192
595PhosphorylationKQLSNSISKCMEMKN
HHHHHHHHHHHHHHH		21.4424850871
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 PF21A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PF21A_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 PF21A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
12032298
KDM1A_HUMANKDM1Aphysical
12032298
HM20B_HUMANHMG20Bphysical
12032298
RCOR1_HUMANRCOR1physical
12032298
HDAC2_HUMANHDAC2physical
12032298
GTF2I_HUMANGTF2Iphysical
12493763
ESCO2_HUMANESCO2physical
18501190
H32_HUMANHIST2H3Cphysical
17687328
BANP_HUMANBANPphysical
25416956
K1C40_HUMANKRT40physical
25416956
BMAL1_HUMANARNTLphysical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
CAVN1_HUMANPTRFphysical
27173435
VPS50_HUMANCCDC132physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
PSMD9_HUMANPSMD9physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
GOGA5_HUMANGOLGA5physical
27173435
YETS4_HUMANYEATS4physical
27173435
TFPT_HUMANTFPTphysical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
PKN3_HUMANPKN3physical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
JUN_HUMANJUNphysical
27173435
EIPR1_HUMANTSSC1physical
27173435
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 PF21A_HUMAN

loading...

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 THR-444 AND SER-447, 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-447 AND SER-455, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory