dbPTM

AATF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AATF_HUMAN
UniProt AC	Q9NY61
Protein Name	Protein AATF
Gene Name	AATF
Organism	Homo sapiens (Human).
Sequence Length	560
Subcellular Localization	Nucleus, nucleolus .
Protein Description	May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date..
Protein Sequence	MAGPQPLALQLEQLLNPRPSEADPEADPEEATAARVIDRFDEGEDGEGDFLVVGSIRKLASASLLDTDKRYCGKTTSRKAWNEDHWEQTLPGSSDEEISDEEGSGDEDSEGLGLEEYDEDDLGAAEEQECGDHRESKKSRSHSAKTPGFSVQSISDFEKFTKGMDDLGSSEEEEDEESGMEEGDDAEDSQGESEEDRAGDRNSEDDGVVMTFSSVKVSEEVEKGRAVKNQIALWDQLLEGRIKLQKALLTTNQLPQPDVFPLFKDKGGPEFSSALKNSHKALKALLRSLVGLQEELLFQYPDTRYLVDGTKPNAGSEEISSEDDELVEEKKQQRRRVPAKRKLEMEDYPSFMAKRFADFTVYRNRTLQKWHDKTKLASGKLGKGFGAFERSILTQIDHILMDKERLLRRTQTKRSVYRVLGKPEPAAQPVPESLPGEPEILPQAPANAHLKDLDEEIFDDDDFYHQLLRELIERKTSSLDPNDQVAMGRQWLAIQKLRSKIHKKVDRKASKGRKLRFHVLSKLLSFMAPIDHTTMNDDARTELYRSLFGQLHPPDEGHGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGPQPLAL ------CCCCCCCHH	38.07	19413330
20	Phosphorylation	QLLNPRPSEADPEAD HHHCCCCCCCCCCCC	46.85	30814471
55	Phosphorylation	GDFLVVGSIRKLASA CCEEEECHHHHHHHH	13.96	24732914
58	Sumoylation	LVVGSIRKLASASLL EEECHHHHHHHHHHC	46.89	-
58	Sumoylation	LVVGSIRKLASASLL EEECHHHHHHHHHHC	46.89	-
58	Ubiquitination	LVVGSIRKLASASLL EEECHHHHHHHHHHC	46.89	29967540
61	Phosphorylation	GSIRKLASASLLDTD CHHHHHHHHHHCCCC	28.91	29255136
63	Phosphorylation	IRKLASASLLDTDKR HHHHHHHHHCCCCCC	27.28	29255136
67	Phosphorylation	ASASLLDTDKRYCGK HHHHHCCCCCCCCCC	43.31	29255136
69	Acetylation	ASLLDTDKRYCGKTT HHHCCCCCCCCCCCC	47.57	25953088
69	Ubiquitination	ASLLDTDKRYCGKTT HHHCCCCCCCCCCCC	47.57	21906983
71	Phosphorylation	LLDTDKRYCGKTTSR HCCCCCCCCCCCCCC	15.99	27762562
74	Ubiquitination	TDKRYCGKTTSRKAW CCCCCCCCCCCCCCC	45.10	22817900
74	Acetylation	TDKRYCGKTTSRKAW CCCCCCCCCCCCCCC	45.10	26051181
75	Phosphorylation	DKRYCGKTTSRKAWN CCCCCCCCCCCCCCC	18.45	27762562
76	Phosphorylation	KRYCGKTTSRKAWNE CCCCCCCCCCCCCCC	29.98	27762562
89	Phosphorylation	NEDHWEQTLPGSSDE CCCHHHHCCCCCCCC	24.33	17081983
93	Phosphorylation	WEQTLPGSSDEEISD HHHCCCCCCCCCCCC	32.45	17081983
94	Phosphorylation	EQTLPGSSDEEISDE HHCCCCCCCCCCCCC	55.76	17081983
99	Phosphorylation	GSSDEEISDEEGSGD CCCCCCCCCCCCCCC	42.10	17081983
104	Phosphorylation	EISDEEGSGDEDSEG CCCCCCCCCCCCCCC	46.48	17081983
109	Phosphorylation	EGSGDEDSEGLGLEE CCCCCCCCCCCCCCC	31.36	17081983
117	Phosphorylation	EGLGLEEYDEDDLGA CCCCCCCCCCCCCCH	18.43	22817900
141	Phosphorylation	RESKKSRSHSAKTPG CCHHHHHCCCCCCCC	28.96	17157788
143	Phosphorylation	SKKSRSHSAKTPGFS HHHHHCCCCCCCCCC	32.48	28555341
145	Acetylation	KSRSHSAKTPGFSVQ HHHCCCCCCCCCCEE	59.26	25953088
145	Ubiquitination	KSRSHSAKTPGFSVQ HHHCCCCCCCCCCEE	59.26	29967540
146	Phosphorylation	SRSHSAKTPGFSVQS HHCCCCCCCCCCEEC	28.49	27050516
150	Phosphorylation	SAKTPGFSVQSISDF CCCCCCCCEECHHHH	25.76	30108239
153	Phosphorylation	TPGFSVQSISDFEKF CCCCCEECHHHHHHH	23.15	25159151
155	Phosphorylation	GFSVQSISDFEKFTK CCCEECHHHHHHHHC	41.30	25159151
159	Ubiquitination	QSISDFEKFTKGMDD ECHHHHHHHHCCCCC	59.32	21963094
162	Ubiquitination	SDFEKFTKGMDDLGS HHHHHHHCCCCCCCC	56.20	22817900
189	Phosphorylation	EGDDAEDSQGESEED CCCCCCCCCCCCHHH	31.43	22817900
203	Phosphorylation	DRAGDRNSEDDGVVM HCCCCCCCCCCCEEE	43.21	29255136
211	Phosphorylation	EDDGVVMTFSSVKVS CCCCEEEEEECEEEC	14.57	24732914
213	Phosphorylation	DGVVMTFSSVKVSEE CCEEEEEECEEECHH	25.67	24732914
214	Phosphorylation	GVVMTFSSVKVSEEV CEEEEEECEEECHHH	23.05	24732914
218	Phosphorylation	TFSSVKVSEEVEKGR EEECEEECHHHHHCH	23.48	113136019
223	Sumoylation	KVSEEVEKGRAVKNQ EECHHHHHCHHHHHH	59.89	-
223	Ubiquitination	KVSEEVEKGRAVKNQ EECHHHHHCHHHHHH	59.89	22817900
223	Sumoylation	KVSEEVEKGRAVKNQ EECHHHHHCHHHHHH	59.89	-
223	Acetylation	KVSEEVEKGRAVKNQ EECHHHHHCHHHHHH	59.89	26051181
228	Ubiquitination	VEKGRAVKNQIALWD HHHCHHHHHHHHHHH	41.99	21906983
243	Ubiquitination	QLLEGRIKLQKALLT HHHHCHHHHHHHHHH	43.43	22817900
246	Ubiquitination	EGRIKLQKALLTTNQ HCHHHHHHHHHHCCC	51.98	21963094
251	Phosphorylation	LQKALLTTNQLPQPD HHHHHHHCCCCCCCC	22.42	110759379
264	Ubiquitination	PDVFPLFKDKGGPEF CCCCHHHCCCCCHHH	67.24	21906983
266	Ubiquitination	VFPLFKDKGGPEFSS CCHHHCCCCCHHHHH	67.37	21906983
272	Phosphorylation	DKGGPEFSSALKNSH CCCCHHHHHHHHHHH	17.03	30266825
273	Phosphorylation	KGGPEFSSALKNSHK CCCHHHHHHHHHHHH	42.83	30266825
276	Ubiquitination	PEFSSALKNSHKALK HHHHHHHHHHHHHHH	57.00	27667366
276	Methylation	PEFSSALKNSHKALK HHHHHHHHHHHHHHH	57.00	-
280	Ubiquitination	SALKNSHKALKALLR HHHHHHHHHHHHHHH	56.06	-
283	Ubiquitination	KNSHKALKALLRSLV HHHHHHHHHHHHHHH	41.68	27667366
283	Acetylation	KNSHKALKALLRSLV HHHHHHHHHHHHHHH	41.68	25953088
288	Phosphorylation	ALKALLRSLVGLQEE HHHHHHHHHHCCCHH	27.63	50558303
305	Phosphorylation	FQYPDTRYLVDGTKP HHCCCCEEEECCCCC	17.11	29255136
310	Phosphorylation	TRYLVDGTKPNAGSE CEEEECCCCCCCCCC	38.57	29255136
316	Phosphorylation	GTKPNAGSEEISSED CCCCCCCCCCCCCCC	29.64	29255136
320	Phosphorylation	NAGSEEISSEDDELV CCCCCCCCCCCHHHH	30.84	29255136
321	Phosphorylation	AGSEEISSEDDELVE CCCCCCCCCCHHHHH	51.19	29255136
340	Ubiquitination	QRRRVPAKRKLEMED HHCCCCCHHHCHHHC	43.95	22817900
342	Sumoylation	RRVPAKRKLEMEDYP CCCCCHHHCHHHCCH	48.36	-
342	Sumoylation	RRVPAKRKLEMEDYP CCCCCHHHCHHHCCH	48.36	-
342	Ubiquitination	RRVPAKRKLEMEDYP CCCCCHHHCHHHCCH	48.36	21906983
354	Ubiquitination	DYPSFMAKRFADFTV CCHHHHHHHHHCEEE	35.94	21906983
366	Phosphorylation	FTVYRNRTLQKWHDK EEEEECCCHHHHHCC	36.77	54273399
369	Acetylation	YRNRTLQKWHDKTKL EECCCHHHHHCCCCC	50.00	7704545
369	Ubiquitination	YRNRTLQKWHDKTKL EECCCHHHHHCCCCC	50.00	27667366
380	Ubiquitination	KTKLASGKLGKGFGA CCCCCCCCCCCCCCH	52.12	23000965
380	Acetylation	KTKLASGKLGKGFGA CCCCCCCCCCCCCCH	52.12	23749302
383	Acetylation	LASGKLGKGFGAFER CCCCCCCCCCCHHHH	62.60	26051181
383	Ubiquitination	LASGKLGKGFGAFER CCCCCCCCCCCHHHH	62.60	23000965
391	Phosphorylation	GFGAFERSILTQIDH CCCHHHHHHHHHHHH	18.10	20068231
394	Phosphorylation	AFERSILTQIDHILM HHHHHHHHHHHHHHH	23.08	20068231
403	Acetylation	IDHILMDKERLLRRT HHHHHHCHHHHHHHH	30.67	26051181
403	Ubiquitination	IDHILMDKERLLRRT HHHHHHCHHHHHHHH	30.67	21890473
410	Phosphorylation	KERLLRRTQTKRSVY HHHHHHHHHCHHHHH	33.87	20068231
412	Phosphorylation	RLLRRTQTKRSVYRV HHHHHHHCHHHHHHH	28.01	20068231
415	Phosphorylation	RRTQTKRSVYRVLGK HHHHCHHHHHHHHCC	25.67	24719451
422	Ubiquitination	SVYRVLGKPEPAAQP HHHHHHCCCCCCCCC	41.89	21906983
422	Sumoylation	SVYRVLGKPEPAAQP HHHHHHCCCCCCCCC	41.89	-
422	Sumoylation	SVYRVLGKPEPAAQP HHHHHHCCCCCCCCC	41.89	-
422	Acetylation	SVYRVLGKPEPAAQP HHHHHHCCCCCCCCC	41.89	26051181
433	Phosphorylation	AAQPVPESLPGEPEI CCCCCCCCCCCCCCC	33.52	27050516
451	Ubiquitination	APANAHLKDLDEEIF CCCCCCCCCCCHHHC	46.51	29967540
475	Ubiquitination	LRELIERKTSSLDPN HHHHHHHHCCCCCCC	39.71	21906983
475	Sumoylation	LRELIERKTSSLDPN HHHHHHHHCCCCCCC	39.71	-
475	Sumoylation	LRELIERKTSSLDPN HHHHHHHHCCCCCCC	39.71	-
476	Phosphorylation	RELIERKTSSLDPND HHHHHHHCCCCCCCC	29.75	30108239
477	Phosphorylation	ELIERKTSSLDPNDQ HHHHHHCCCCCCCCH	31.75	30108239
478	Phosphorylation	LIERKTSSLDPNDQV HHHHHCCCCCCCCHH	41.86	21815630
487	Sulfoxidation	DPNDQVAMGRQWLAI CCCCHHHHHHHHHHH	4.83	21406390
496	Ubiquitination	RQWLAIQKLRSKIHK HHHHHHHHHHHHHHH	39.49	22817900
500	Ubiquitination	AIQKLRSKIHKKVDR HHHHHHHHHHHHHHH	42.25	22817900
510	Phosphorylation	KKVDRKASKGRKLRF HHHHHHCHHCCHHHH	38.38	22817900
522	Ubiquitination	LRFHVLSKLLSFMAP HHHHHHHHHHHHHCC	49.65	21963094

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
143	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
189	S	Phosphorylation	Kinase	ATM	Q13315	PSP
366	T	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
477	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
510	S	Phosphorylation	Kinase	CHEK2	O96017	GPS

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RB_HUMAN	RB1	physical	12450794
TAU_HUMAN	MAPT	physical	14697667
TS101_RAT	Tsg101	physical	14761944
PAWR_HUMAN	PAWR	physical	14627703
RBL2_HUMAN	RBL2	physical	12450794
RBL1_HUMAN	RBL1	physical	12450794
RB_HUMAN	RB1	physical	10783144
PHS2_HUMAN	PCBD2	physical	20211142
MAGD1_HUMAN	MAGED1	physical	17488777
CHK2_HUMAN	CHEK2	physical	17157788
TF65_HUMAN	RELA	physical	17157788
MDM2_HUMAN	MDM2	physical	17468107
CBPD_HUMAN	CPD	physical	21988832
EFNB3_HUMAN	EFNB3	physical	21988832
SMAD3_HUMAN	SMAD3	physical	21988832
NED4L_HUMAN	NEDD4L	physical	21988832
ZN468_HUMAN	ZNF468	physical	21988832
HIPK2_HUMAN	HIPK2	physical	25210797
ANDR_HUMAN	AR	physical	23146908
DAPK3_HUMAN	DAPK3	physical	23146908
TS101_HUMAN	TSG101	physical	23146908
BRX1_HUMAN	BRIX1	physical	26344197
DDX52_HUMAN	DDX52	physical	26344197
PUM3_HUMAN	KIAA0020	physical	26344197
KRI1_HUMAN	KRI1	physical	26344197
MPP10_HUMAN	MPHOSPH10	physical	26344197
NOC2L_HUMAN	NOC2L	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
RPF2_HUMAN	RPF2	physical	26344197

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 AATF_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, AND MASSSPECTROMETRY.	19413330 [Abstract]
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-316; SER-320 ANDSER-321, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-316; SER-320 AND SER-321, AND MASSSPECTROMETRY.	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-316; SER-320 ANDSER-321, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASSSPECTROMETRY.	19007248 [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-203; SER-316; SER-320AND SER-321, AND MASS SPECTROMETRY.	16565220 [Abstract]
"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-203; SER-320 ANDSER-321, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Che-1 affects cell growth by interfering with the recruitment ofHDAC1 by Rb."; Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M.,Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S.,Floridi A., Passananti C., Fanciulli M.; Cancer Cell 2:387-399(2002). Cited for: FUNCTION, PHOSPHORYLATION AT THE G1/S TRANSITION, AND INTERACTION WITHRB1; RBL1 AND RBL2.	12450794 [Abstract]