dbPTM

PHF12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PHF12_HUMAN
UniProt AC	Q96QT6
Protein Name	PHD finger protein 12
Gene Name	PHF12 {ECO:0000312\|HGNC:HGNC:20816}
Organism	Homo sapiens (Human).
Sequence Length	1004
Subcellular Localization	Nucleus .
Protein Description	Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional AES complexes to DNA..
Protein Sequence	MWEKMETKTIVYDLDTSGGLMEQIQALLAPPKTDEAEKRSRKPEKEPRRSGRATNHDSCDSCKEGGDLLCCDHCPAAFHLQCCNPPLSEEMLPPGEWMCHRCTVRRKKREQKKELGHVNGLVDKSGKRTTSPSSDTDLLDRSASKTELKAIAHARILERRASRPGTPTSSASTETPTSEQNDVDEDIIDVDEEPVAAEPDYVQPQLRRPFELLIAAAMERNPTQFQLPNELTCTTALPGSSKRRRKEETTGKNVKKTQHELDHNGLVPLPVKVCFTCNRSCRVAPLIQCDYCPLLFHMDCLEPPLTAMPLGRWMCPNHIEHVVLNQKNMTLSNRCQVFDRFQDTVSQHVVKVDFLNRIHKKHPPNRRVLQSVKRRSLKVPDAIKSQYQFPPPLIAPAAIRDGELICNGIPEESQMHLLNSEHLATQAEQQEWLCSVVALQCSILKHLSAKQMPSHWDSEQTEKADIKPVIVTDSSVTTSLQTADKTPTPSHYPLSCPSGISTQNSLSCSPPHQSPALEDIGCSSCAEKSKKTPCGTANGPVNTEVKANGPHLYSSPTDSTDPRRLPGANTPLPGLSHRQGWPRPLTPPAAGGLQNHTVGIIVKTENATGPSSCPQRSLVPVPSLPPSIPSSCASIENTSTLQRKTVQSQIGPPLTDSRPLGSPPNATRVLTPPQAAGDGILATTANQRFSSPAPSSDGKVSPGTLSIGSALTVPSFPANSTAMVDLTNSLRAFMDVNGEIEINMLDEKLIKFLALQRIHQLFPSRVQPSPGSVGTHQLASGGHHIEVQRKEVQARAVFYPLLGLGGAVNMCYRTLYIGTGADMDVCLTNYGHCNYVSGKHACIFYDENTKHYELLNYSEHGTTVDNVLYSCDFSEKTPPTPPSSIVAKVQSVIRRRRHQKQDEEPSEEAAMMSSQAQGPQRRPCNCKASSSSLIGGSGAGWEGTALLHHGSYIKLGCLQFVFSITEFATKQPKGDASLLQDGVLAEKLSLKPHQGPVLRSNSVP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	WEKMETKTIVYDLDT CCCCCCEEEEEECCC	24.08	22468782
17	Phosphorylation	IVYDLDTSGGLMEQI EEEECCCCCCHHHHH	30.45	22468782
33	Phosphorylation	ALLAPPKTDEAEKRS HHHCCCCCCHHHHHC	44.86	22468782
125	Phosphorylation	VNGLVDKSGKRTTSP CCCCCCCCCCCCCCC	45.12	-
129	Phosphorylation	VDKSGKRTTSPSSDT CCCCCCCCCCCCCCC	34.80	30266825
130	Phosphorylation	DKSGKRTTSPSSDTD CCCCCCCCCCCCCCC	42.55	29255136
130 (in isoform 2)	Phosphorylation	-	42.55	-
131	Phosphorylation	KSGKRTTSPSSDTDL CCCCCCCCCCCCCCH	23.36	29255136
131 (in isoform 2)	Phosphorylation	-	23.36	-
133	Phosphorylation	GKRTTSPSSDTDLLD CCCCCCCCCCCCHHH	40.38	25159151
133 (in isoform 2)	Phosphorylation	-	40.38	-
134	Phosphorylation	KRTTSPSSDTDLLDR CCCCCCCCCCCHHHC	48.16	25159151
134 (in isoform 2)	Phosphorylation	-	48.16	-
136	Phosphorylation	TTSPSSDTDLLDRSA CCCCCCCCCHHHCCC	30.41	23401153
136 (in isoform 2)	Phosphorylation	-	30.41	-
142	Phosphorylation	DTDLLDRSASKTELK CCCHHHCCCCHHHHH	36.24	30108239
144	Phosphorylation	DLLDRSASKTELKAI CHHHCCCCHHHHHHH	41.16	27251275
146	Phosphorylation	LDRSASKTELKAIAH HHCCCCHHHHHHHHH	44.02	30108239
162	Phosphorylation	RILERRASRPGTPTS HHHHHHHCCCCCCCC	36.88	28348404
166	Phosphorylation	RRASRPGTPTSSAST HHHCCCCCCCCCCCC	26.52	28348404
168	Phosphorylation	ASRPGTPTSSASTET HCCCCCCCCCCCCCC	34.84	28348404
169	Phosphorylation	SRPGTPTSSASTETP CCCCCCCCCCCCCCC	25.72	28348404
170	Phosphorylation	RPGTPTSSASTETPT CCCCCCCCCCCCCCC	28.81	28348404
172	Phosphorylation	GTPTSSASTETPTSE CCCCCCCCCCCCCCC	28.82	28348404
173	Phosphorylation	TPTSSASTETPTSEQ CCCCCCCCCCCCCCC	43.53	28348404
175	Phosphorylation	TSSASTETPTSEQND CCCCCCCCCCCCCCC	31.77	28348404
177	Phosphorylation	SASTETPTSEQNDVD CCCCCCCCCCCCCCC	52.92	29496963
178	Phosphorylation	ASTETPTSEQNDVDE CCCCCCCCCCCCCCC	38.09	29496963
240	Phosphorylation	CTTALPGSSKRRRKE ECCCCCCCHHHCCCH	30.65	21712546
241	Phosphorylation	TTALPGSSKRRRKEE CCCCCCCHHHCCCHH	35.78	21712546
337 (in isoform 4)	Ubiquitination	-	6.53	21890473
373	Ubiquitination	RRVLQSVKRRSLKVP HHHHHHHHHHCCCCC	47.55	-
376	Phosphorylation	LQSVKRRSLKVPDAI HHHHHHHCCCCCHHH	36.25	30624053
420	Phosphorylation	SQMHLLNSEHLATQA HHHHHHCHHHHHHHH	26.77	24043423
425	Phosphorylation	LNSEHLATQAEQQEW HCHHHHHHHHHHHHH	34.37	24043423
435	Phosphorylation	EQQEWLCSVVALQCS HHHHHHHHHHHHHHH	19.91	24043423
442	Phosphorylation	SVVALQCSILKHLSA HHHHHHHHHHHHHCC	20.28	24719451
450	Ubiquitination	ILKHLSAKQMPSHWD HHHHHCCCCCCCCCC	43.69	-
467	Sumoylation	QTEKADIKPVIVTDS HHHCCCCCCEEEECC	33.51	-
467	Sumoylation	QTEKADIKPVIVTDS HHHCCCCCCEEEECC	33.51	28112733
486	Phosphorylation	SLQTADKTPTPSHYP CEECCCCCCCCCCCC	32.70	27080861
488	Phosphorylation	QTADKTPTPSHYPLS ECCCCCCCCCCCCCC	42.53	26074081
490	Phosphorylation	ADKTPTPSHYPLSCP CCCCCCCCCCCCCCC	37.82	26074081
492	Phosphorylation	KTPTPSHYPLSCPSG CCCCCCCCCCCCCCC	15.37	26074081
495	Phosphorylation	TPSHYPLSCPSGIST CCCCCCCCCCCCCCC	21.34	27080861
498	Phosphorylation	HYPLSCPSGISTQNS CCCCCCCCCCCCCCC	53.75	27080861
501	Phosphorylation	LSCPSGISTQNSLSC CCCCCCCCCCCCCCC	27.71	27080861
502	Phosphorylation	SCPSGISTQNSLSCS CCCCCCCCCCCCCCC	29.83	27080861
505	Phosphorylation	SGISTQNSLSCSPPH CCCCCCCCCCCCCCC	16.31	26074081
507	Phosphorylation	ISTQNSLSCSPPHQS CCCCCCCCCCCCCCC	16.63	23401153
509	Phosphorylation	TQNSLSCSPPHQSPA CCCCCCCCCCCCCCC	37.78	30576142
514	Phosphorylation	SCSPPHQSPALEDIG CCCCCCCCCCHHHCC	14.76	27080861
523	Phosphorylation	ALEDIGCSSCAEKSK CHHHCCCHHHCHHCC	24.20	27080861
524	Phosphorylation	LEDIGCSSCAEKSKK HHHCCCHHHCHHCCC	22.79	27080861
532	Phosphorylation	CAEKSKKTPCGTANG HCHHCCCCCCCCCCC	27.78	21815630
536	Phosphorylation	SKKTPCGTANGPVNT CCCCCCCCCCCCCCC	24.54	25627689
553	Phosphorylation	KANGPHLYSSPTDST ECCCCCCCCCCCCCC	12.22	24732914
554	Phosphorylation	ANGPHLYSSPTDSTD CCCCCCCCCCCCCCC	35.88	25849741
555	Phosphorylation	NGPHLYSSPTDSTDP CCCCCCCCCCCCCCC	20.47	30266825
557	Phosphorylation	PHLYSSPTDSTDPRR CCCCCCCCCCCCCCC	44.52	30266825
559	Phosphorylation	LYSSPTDSTDPRRLP CCCCCCCCCCCCCCC	36.87	30266825
560	Phosphorylation	YSSPTDSTDPRRLPG CCCCCCCCCCCCCCC	53.48	30266825
570	Phosphorylation	RRLPGANTPLPGLSH CCCCCCCCCCCCCCC	26.18	24732914
586	Phosphorylation	QGWPRPLTPPAAGGL CCCCCCCCCCCCCCC	29.88	27273156
586 (in isoform 2)	Phosphorylation	-	29.88	-
597	Phosphorylation	AGGLQNHTVGIIVKT CCCCCCCEEEEEEEE	28.16	27251275
645	Phosphorylation	TSTLQRKTVQSQIGP CCCCCHHHHHHHCCC	26.43	23312004
648	Phosphorylation	LQRKTVQSQIGPPLT CCHHHHHHHCCCCCC	21.30	29396449
655	Phosphorylation	SQIGPPLTDSRPLGS HHCCCCCCCCCCCCC	37.39	30266825
657	Phosphorylation	IGPPLTDSRPLGSPP CCCCCCCCCCCCCCC	30.48	30266825
662	Phosphorylation	TDSRPLGSPPNATRV CCCCCCCCCCCCCEE	44.88	30266825
667	Phosphorylation	LGSPPNATRVLTPPQ CCCCCCCCEECCCCC	28.13	30266825
671	Phosphorylation	PNATRVLTPPQAAGD CCCCEECCCCCCCCC	30.02	29255136
671 (in isoform 2)	Phosphorylation	-	30.02	-
683	Phosphorylation	AGDGILATTANQRFS CCCCEEEEECCCCCC	24.01	23403867
684	Phosphorylation	GDGILATTANQRFSS CCCEEEEECCCCCCC	20.29	23403867
690	Phosphorylation	TTANQRFSSPAPSSD EECCCCCCCCCCCCC	37.29	28450419
691	Phosphorylation	TANQRFSSPAPSSDG ECCCCCCCCCCCCCC	23.52	29255136
695	Phosphorylation	RFSSPAPSSDGKVSP CCCCCCCCCCCCCCC	43.07	20068231
696	Phosphorylation	FSSPAPSSDGKVSPG CCCCCCCCCCCCCCC	49.69	20068231
701	Phosphorylation	PSSDGKVSPGTLSIG CCCCCCCCCCEEEEC	22.54	20068231
704	Phosphorylation	DGKVSPGTLSIGSAL CCCCCCCEEEECCCE	22.25	20068231
706	Phosphorylation	KVSPGTLSIGSALTV CCCCCEEEECCCEEC	25.41	27080861
709	Phosphorylation	PGTLSIGSALTVPSF CCEEEECCCEECCCC	20.59	27080861
712	Phosphorylation	LSIGSALTVPSFPAN EEECCCEECCCCCCC	30.04	20068231
715	Phosphorylation	GSALTVPSFPANSTA CCCEECCCCCCCCCE	39.25	20068231
720	Phosphorylation	VPSFPANSTAMVDLT CCCCCCCCCEEEECC	21.46	27080861
721	Phosphorylation	PSFPANSTAMVDLTN CCCCCCCCEEEECCH	20.69	27080861
727	Phosphorylation	STAMVDLTNSLRAFM CCEEEECCHHHHHHH	20.49	27080861
729	Phosphorylation	AMVDLTNSLRAFMDV EEEECCHHHHHHHCC	17.63	27080861
751	Ubiquitination	MLDEKLIKFLALQRI ECCHHHHHHHHHHHH	44.77	21890473
751	Ubiquitination	MLDEKLIKFLALQRI ECCHHHHHHHHHHHH	44.77	21890473
751 (in isoform 1)	Ubiquitination	-	44.77	21890473
751 (in isoform 3)	Ubiquitination	-	44.77	21890473
769	Phosphorylation	FPSRVQPSPGSVGTH CCCCCCCCCCCCCCC	25.46	26055452
772	Phosphorylation	RVQPSPGSVGTHQLA CCCCCCCCCCCCCCC	22.28	20068231
775	Phosphorylation	PSPGSVGTHQLASGG CCCCCCCCCCCCCCC	12.32	27732954
780	Phosphorylation	VGTHQLASGGHHIEV CCCCCCCCCCCCEEE	54.63	26055452
877	Phosphorylation	SCDFSEKTPPTPPSS CCCCCCCCCCCCCHH	30.37	26657352
880	Phosphorylation	FSEKTPPTPPSSIVA CCCCCCCCCCHHHHH	49.38	25159151
883	Phosphorylation	KTPPTPPSSIVAKVQ CCCCCCCHHHHHHHH	33.62	30266825
884	Phosphorylation	TPPTPPSSIVAKVQS CCCCCCHHHHHHHHH	27.19	30266825
900	Sumoylation	IRRRRHQKQDEEPSE HHHHHHHCCCCCCHH	54.30	28112733
906	Phosphorylation	QKQDEEPSEEAAMMS HCCCCCCHHHHHHHH	51.88	24043423
913	Phosphorylation	SEEAAMMSSQAQGPQ HHHHHHHHHHCCCCC	13.25	24043423
914	Phosphorylation	EEAAMMSSQAQGPQR HHHHHHHHHCCCCCC	16.19	24043423
973	Sumoylation	EFATKQPKGDASLLQ HHHCCCCCCCHHHHC	67.91	28112733
973	Ubiquitination	EFATKQPKGDASLLQ HHHCCCCCCCHHHHC	67.91	-
977	Phosphorylation	KQPKGDASLLQDGVL CCCCCCHHHHCCCHH	34.06	23663014
987	Sumoylation	QDGVLAEKLSLKPHQ CCCHHHHHCCCCCCC	37.46	28112733
987	Ubiquitination	QDGVLAEKLSLKPHQ CCCHHHHHCCCCCCC	37.46	-
989	Phosphorylation	GVLAEKLSLKPHQGP CHHHHHCCCCCCCCC	45.47	25159151
991	Sumoylation	LAEKLSLKPHQGPVL HHHHCCCCCCCCCCC	36.76	28112733
991	Ubiquitination	LAEKLSLKPHQGPVL HHHHCCCCCCCCCCC	36.76	-
1000	Phosphorylation	HQGPVLRSNSVP--- CCCCCCCCCCCC---	29.33	29514088
1002	Phosphorylation	GPVLRSNSVP----- CCCCCCCCCC-----	36.69	29514088

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 PHF12_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PHF12_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 PHF12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIN3A_HUMAN	SIN3A	physical	11390640
HDAC1_HUMAN	HDAC1	physical	11390640
HDAC1_HUMAN	HDAC1	physical	26496610
HDAC2_HUMAN	HDAC2	physical	26496610
KDM5A_HUMAN	KDM5A	physical	26496610
RBBP7_HUMAN	RBBP7	physical	26496610
S10A4_HUMAN	S100A4	physical	26496610
MO4L2_HUMAN	MORF4L2	physical	26496610
MO4L1_HUMAN	MORF4L1	physical	26496610
SIN3B_HUMAN	SIN3B	physical	26496610
EMSY_HUMAN	C11orf30	physical	26496610
GATD1_HUMAN	GATAD1	physical	26496610
SPICE_HUMAN	SPICE1	physical	26496610
ZN281_HUMAN	ZNF281	physical	26841866
MO4L1_HUMAN	MORF4L1	physical	26841866
SIN3B_HUMAN	SIN3B	physical	26841866
KDM5A_HUMAN	KDM5A	physical	26841866
ZN131_HUMAN	ZNF131	physical	26841866
HDAC1_HUMAN	HDAC1	physical	26841866
MO4L2_HUMAN	MORF4L2	physical	26841866
RBBP7_HUMAN	RBBP7	physical	26841866
EMSY_HUMAN	C11orf30	physical	26841866
QSER1_HUMAN	QSER1	physical	26841866
CHD9_HUMAN	CHD9	physical	26841866
GATD1_HUMAN	GATAD1	physical	26841866
HDAC2_HUMAN	HDAC2	physical	26841866
PHF12_HUMAN	PHF12	physical	26841866
TBA4A_HUMAN	TUBA4A	physical	26841866
ZN143_HUMAN	ZNF143	physical	26841866
DPM1_HUMAN	DPM1	physical	26841866
ZN335_HUMAN	ZNF335	physical	26841866
RFOX2_HUMAN	RBFOX2	physical	26841866
RFOX1_HUMAN	RBFOX1	physical	26841866
H2AY_HUMAN	H2AFY	physical	26841866
BAG2_HUMAN	BAG2	physical	26841866
HSPB1_HUMAN	HSPB1	physical	26841866
NF2L1_HUMAN	NFE2L1	physical	26841866
TBB8_HUMAN	TUBB8	physical	26841866
DNJA3_HUMAN	DNAJA3	physical	26841866
SENP1_HUMAN	SENP1	physical	26841866
ABCF2_HUMAN	ABCF2	physical	26841866
GPTC8_HUMAN	GPATCH8	physical	26841866
ABCG2_HUMAN	ABCG2	physical	26841866

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 PHF12_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-131; SER-133 ANDTHR-671, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-131; SER-133 ANDTHR-671, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-131; SER-133; SER-134AND THR-671, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-880, AND MASSSPECTROMETRY.	15302935 [Abstract]