dbPTM

ZZZ3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZZZ3_HUMAN
UniProt AC	Q8IYH5
Protein Name	ZZ-type zinc finger-containing protein 3
Gene Name	ZZZ3
Organism	Homo sapiens (Human).
Sequence Length	903
Subcellular Localization	Nucleus .
Protein Description	Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4..
Protein Sequence	MAASRSTRVTRSTVGLNGLDESFCGRTLRNRSIAHPEEISSNSQVRSRSPKKRPEPVPIQKGNNNGRTTDLKQQSTRESWVSPRKRGLSSSEKDNIERQAIENCERRQTEPVSPVLKRIKRCLRSEAPNSSEEDSPIKSDKESVEQRSTVVDNDADFQGTKRACRCLILDDCEKREIKKVNVSEEGPLNSAVVEEITGYLAVNGVDDSDSAVINCDDCQPDGNTKQNSIGSYVLQEKSVAENGDTDTQTSMFLDSRKEDSYIDHKVPCTDSQVQVKLEDHKIVTACLPVEHVNQLTTEPATGPFSETQSSLRDSEEEVDVVGDSSASKEQCKENTNNELDTSLESMPASGEPEPSPVLDCVSAQMMSLSEPQEHRYTLRTSPRRAAPTRGSPTKNSSPYRENGQFEENNLSPNETNATVSDNVSQSPTNPGEISQNEKGICCDSQNNGSEGVSKPPSEARLNIGHLPSAKESASQHITEEEDDDPDVYYFESDHVALKHNKDYQRLLQTIAVLEAQRSQAVQDLESLGRHQREALKNPIGFVEKLQKKADIGLPYPQRVVQLPEIVWDQYTHSLGNFEREFKNRKRHTRRVKLVFDKVGLPARPKSPLDPKKDGESLSYSMLPLSDGPEGSSSRPQMIRGRLCDDTKPETFNQLWTVEEQKKLEQLLIKYPPEEVESRRWQKIADELGNRTAKQVASRVQKYFIKLTKAGIPVPGRTPNLYIYSKKSSTSRRQHPLNKHLFKPSTFMTSHEPPVYMDEDDDRSCFHSHMNTAVEDASDDESIPIMYRNLPEYKELLQFKKLKKQKLQQMQAESGFVQHVGFKCDNCGIEPIQGVRWHCQDCPPEMSLDFCDSCSDCLHETDIHKEDHQLEPIYRSETFLDRDYCVSQGTSYNYLDPNYFPANR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAASRSTRVTRST --CCCCCCCCCCCCC	20.33	23403867
22	Phosphorylation	GLNGLDESFCGRTLR CCCCCCHHHCCCCCC	26.04	29214152
32	Phosphorylation	GRTLRNRSIAHPEEI CCCCCCCCCCCHHHH	27.89	26270265
40	Phosphorylation	IAHPEEISSNSQVRS CCCHHHHCCCCCCCC	27.09	24719451
41	Phosphorylation	AHPEEISSNSQVRSR CCHHHHCCCCCCCCC	46.27	24732914
43	Phosphorylation	PEEISSNSQVRSRSP HHHHCCCCCCCCCCC	31.81	24732914
47	Phosphorylation	SSNSQVRSRSPKKRP CCCCCCCCCCCCCCC	37.95	24732914
49	Phosphorylation	NSQVRSRSPKKRPEP CCCCCCCCCCCCCCC	42.17	24732914
79	Phosphorylation	KQQSTRESWVSPRKR HHHHHHHHCCCCCCC	29.50	29396449
82	Phosphorylation	STRESWVSPRKRGLS HHHHHCCCCCCCCCC	16.84	23401153
89	Phosphorylation	SPRKRGLSSSEKDNI CCCCCCCCHHHHHHH	34.34	23401153
90	Phosphorylation	PRKRGLSSSEKDNIE CCCCCCCHHHHHHHH	47.78	23927012
91	Phosphorylation	RKRGLSSSEKDNIER CCCCCCHHHHHHHHH	45.34	24732914
93	Acetylation	RGLSSSEKDNIERQA CCCCHHHHHHHHHHH	59.01	26051181
109	Phosphorylation	ENCERRQTEPVSPVL HHHHHHCCCCCCHHH	40.21	23927012
113	Phosphorylation	RRQTEPVSPVLKRIK HHCCCCCCHHHHHHH	21.73	29255136
117	Acetylation	EPVSPVLKRIKRCLR CCCCHHHHHHHHHHH	52.92	25953088
125	Phosphorylation	RIKRCLRSEAPNSSE HHHHHHHCCCCCCCC	25.76	23090842
130	Phosphorylation	LRSEAPNSSEEDSPI HHCCCCCCCCCCCCC	37.76	25159151
131	Phosphorylation	RSEAPNSSEEDSPIK HCCCCCCCCCCCCCC	52.20	25159151
135	Phosphorylation	PNSSEEDSPIKSDKE CCCCCCCCCCCCCHH	31.63	25159151
139	Phosphorylation	EEDSPIKSDKESVEQ CCCCCCCCCHHHHHH	55.42	30108239
143	Phosphorylation	PIKSDKESVEQRSTV CCCCCHHHHHHHHCC	36.37	30108239
161	Acetylation	DADFQGTKRACRCLI CCCHHHHHHHHEEEE	44.84	25953088
161	Ubiquitination	DADFQGTKRACRCLI CCCHHHHHHHHEEEE	44.84	29967540
207	Acetylation	LAVNGVDDSDSAVIN EEECCCCCCCCCEEE	52.52	19608861
231	Acetylation	TKQNSIGSYVLQEKS CCCCCHHHHEEEECC	15.48	19608861
244	Acetylation	KSVAENGDTDTQTSM CCCCCCCCCCCCHHH	53.65	19608861
260	Phosphorylation	LDSRKEDSYIDHKVP CCCCCCCCCCCCCCC	25.69	29214152
261	Phosphorylation	DSRKEDSYIDHKVPC CCCCCCCCCCCCCCC	23.77	29214152
265	Acetylation	EDSYIDHKVPCTDSQ CCCCCCCCCCCCCCC	44.09	26051181
276	Sumoylation	TDSQVQVKLEDHKIV CCCCEEEEECCCCEE	29.12	28112733
301	Phosphorylation	QLTTEPATGPFSETQ HCCCCCCCCCCCCCH	56.98	28348404
305	Phosphorylation	EPATGPFSETQSSLR CCCCCCCCCCHHHCC	42.75	22210691
307	Phosphorylation	ATGPFSETQSSLRDS CCCCCCCCHHHCCCC	32.33	28348404
309	Phosphorylation	GPFSETQSSLRDSEE CCCCCCHHHCCCCCC	38.47	28348404
310	Phosphorylation	PFSETQSSLRDSEEE CCCCCHHHCCCCCCC	20.01	30576142
314	Phosphorylation	TQSSLRDSEEEVDVV CHHHCCCCCCCCCCC	40.24	30576142
325	Phosphorylation	VDVVGDSSASKEQCK CCCCCCCCCCHHHHH	41.10	30576142
376	Phosphorylation	SEPQEHRYTLRTSPR CCCCCHHCCCCCCCC	16.42	27174698
377	Phosphorylation	EPQEHRYTLRTSPRR CCCCHHCCCCCCCCC	15.10	27174698
380	Phosphorylation	EHRYTLRTSPRRAAP CHHCCCCCCCCCCCC	46.31	20068231
381	Phosphorylation	HRYTLRTSPRRAAPT HHCCCCCCCCCCCCC	15.24	22617229
388	Phosphorylation	SPRRAAPTRGSPTKN CCCCCCCCCCCCCCC	42.82	30266825
391	Phosphorylation	RAAPTRGSPTKNSSP CCCCCCCCCCCCCCC	26.55	30266825
393	Phosphorylation	APTRGSPTKNSSPYR CCCCCCCCCCCCCCC	44.55	30266825
394	Acetylation	PTRGSPTKNSSPYRE CCCCCCCCCCCCCCC	59.21	-
396	Phosphorylation	RGSPTKNSSPYRENG CCCCCCCCCCCCCCC	33.96	28348404
397	Phosphorylation	GSPTKNSSPYRENGQ CCCCCCCCCCCCCCC	35.03	28348404
399	Phosphorylation	PTKNSSPYRENGQFE CCCCCCCCCCCCCCC	32.29	28348404
411	Phosphorylation	QFEENNLSPNETNAT CCCCCCCCCCCCCCC	28.01	25921289
424	Phosphorylation	ATVSDNVSQSPTNPG CCCCCCCCCCCCCCC	31.06	26074081
426	Phosphorylation	VSDNVSQSPTNPGEI CCCCCCCCCCCCCCC	26.62	26074081
428	Phosphorylation	DNVSQSPTNPGEISQ CCCCCCCCCCCCCCC	60.33	26074081
444	Phosphorylation	EKGICCDSQNNGSEG CCCCCCCCCCCCCCC	22.39	28555341
454	Acetylation	NGSEGVSKPPSEARL CCCCCCCCCCHHHHC	59.55	26051181
468	Phosphorylation	LNIGHLPSAKESASQ CCCCCCCCHHHHHHH	59.33	24719451
474	Phosphorylation	PSAKESASQHITEEE CCHHHHHHHCCCCCC	31.41	17525332
605	Ubiquitination	VGLPARPKSPLDPKK CCCCCCCCCCCCCCC	60.18	-
606	Phosphorylation	GLPARPKSPLDPKKD CCCCCCCCCCCCCCC	33.12	30266825
618	Phosphorylation	KKDGESLSYSMLPLS CCCCCCCEEEEEECC	25.17	28555341
647	Sumoylation	GRLCDDTKPETFNQL CCCCCCCCCCHHHHC	48.10	28112733
647	Ubiquitination	GRLCDDTKPETFNQL CCCCCCCCCCHHHHC	48.10	29967540
647	Acetylation	GRLCDDTKPETFNQL CCCCCCCCCCHHHHC	48.10	26051181
661	Ubiquitination	LWTVEEQKKLEQLLI CCCHHHHHHHHHHHH	63.71	29967540
661	Acetylation	LWTVEEQKKLEQLLI CCCHHHHHHHHHHHH	63.71	19813445
670	Phosphorylation	LEQLLIKYPPEEVES HHHHHHHCCHHHHHH	19.61	-
677	Phosphorylation	YPPEEVESRRWQKIA CCHHHHHHHHHHHHH	32.11	-
701	Acetylation	QVASRVQKYFIKLTK HHHHHHHHHHHHHHH	38.99	19608861
708	Sumoylation	KYFIKLTKAGIPVPG HHHHHHHHCCCCCCC	55.86	28112733
717	Phosphorylation	GIPVPGRTPNLYIYS CCCCCCCCCCEEEEE	23.57	28674419
725	Acetylation	PNLYIYSKKSSTSRR CCEEEEECCCCCCCC	39.44	19608861
738	Acetylation	RRQHPLNKHLFKPST CCCCCCCCCCCCCCC	49.74	19608861
763	Phosphorylation	MDEDDDRSCFHSHMN CCCCCCCHHHHHHHH	28.29	27251275
767	Phosphorylation	DDRSCFHSHMNTAVE CCCHHHHHHHHHHCC	12.27	27251275
771	Phosphorylation	CFHSHMNTAVEDASD HHHHHHHHHCCCCCC	25.22	27251275
777	Phosphorylation	NTAVEDASDDESIPI HHHCCCCCCCCCCCC	58.89	25849741
781	Phosphorylation	EDASDDESIPIMYRN CCCCCCCCCCCHHCC	40.43	27251275
786	Phosphorylation	DESIPIMYRNLPEYK CCCCCCHHCCCHHHH	9.32	27251275
799	Acetylation	YKELLQFKKLKKQKL HHHHHHHHHHHHHHH	44.21	25953088
822	Acetylation	FVQHVGFKCDNCGIE CCCCCCEECCCCCCC	34.45	26051181

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 ZZZ3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZZZ3_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 ZZZ3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAML3_HUMAN	MAML3	physical	20211142
PBIP1_HUMAN	PBXIP1	physical	20211142
PHS2_HUMAN	PCBD2	physical	20211142
ZN496_HUMAN	ZNF496	physical	20211142
ZN513_HUMAN	ZNF513	physical	20211142
ZBTB9_HUMAN	ZBTB9	physical	20211142
F124A_HUMAN	FAM124A	physical	25416956

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 ZZZ3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-701 AND LYS-738, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, 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-130; SER-131 ANDSER-135, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-474, AND MASSSPECTROMETRY.	17525332 [Abstract]