NO40_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NO40_HUMAN
• UniProt AC: Q9NP64
• Protein Name: Nucleolar protein of 40 kDa
• Gene Name: ZCCHC17
• Organism: Homo sapiens (Human).
• Sequence Length: 241
• Subcellular Localization: Nucleus, nucleolus .
• Protein Sequence: MNSGRPETMENLPALYTIFQGEVAMVTDYGAFIKIPGCRKQGLVHRTHMSSCRVDKPSEIVDVGDKVWVKLIGREMKNDRIKVSLSMKVVNQGTGKDLDPNNVIIEQEERRRRSFQDYTGQKITLEAVLNTTCKKCGCKGHFAKDCFMQPGGTKYSLIPDEEEEKEEAKSAEFEKPDPTRNPSRKRKKEKKKKKHRDRKSSDSDSSDSESDTGKRARHTSKDSKAAKKKKKKKKHKKKHKE

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
56	Ubiquitination	MSSCRVDKPSEIVDV CCCCCCCCCHHEEEC	47.81	-
84	Phosphorylation	KNDRIKVSLSMKVVN CCCCEEEEEEEEEEE	15.10	-
86	Phosphorylation	DRIKVSLSMKVVNQG CCEEEEEEEEEEECC	14.73	22210691
96	Acetylation	VVNQGTGKDLDPNNV EEECCCCCCCCCCCE	55.76	26051181
96	Ubiquitination	VVNQGTGKDLDPNNV EEECCCCCCCCCCCE	55.76	-
114	Phosphorylation	QEERRRRSFQDYTGQ CHHHHHHHCHHHCCC	26.00	25159151
118	Phosphorylation	RRRSFQDYTGQKITL HHHHCHHHCCCEEEH	11.29	29396449
119	Phosphorylation	RRSFQDYTGQKITLE HHHCHHHCCCEEEHH	41.23	23186163
120	Acetylation	RSFQDYTGQKITLEA HHCHHHCCCEEEHHH	22.13	19608861
131	Phosphorylation	TLEAVLNTTCKKCGC EHHHHHCCCHHHCCC	29.43	28555341
132	Phosphorylation	LEAVLNTTCKKCGCK HHHHHCCCHHHCCCC	22.66	25627689
136	Acetylation	LNTTCKKCGCKGHFA HCCCHHHCCCCCEEE	4.77	-
136	Acetylation	LNTTCKKCGCKGHFA HCCCHHHCCCCCEEE	4.77	19608861
144	Acetylation	GCKGHFAKDCFMQPG CCCCEEECCCEECCC	54.83	23749302
148	Sulfoxidation	HFAKDCFMQPGGTKY EEECCCEECCCCCEE	6.21	21406390
153	Phosphorylation	CFMQPGGTKYSLIPD CEECCCCCEEEECCC	32.49	28555341
155	Phosphorylation	MQPGGTKYSLIPDEE ECCCCCEEEECCCHH	14.46	23403867
156	Phosphorylation	QPGGTKYSLIPDEEE CCCCCEEEECCCHHH	22.75	21815630
170	Phosphorylation	EEKEEAKSAEFEKPD HHHHHHHHCCCCCCC	39.83	29255136
179	Phosphorylation	EFEKPDPTRNPSRKR CCCCCCCCCCHHHHH	50.92	23401153
183	Phosphorylation	PDPTRNPSRKRKKEK CCCCCCHHHHHHHHH	54.72	14702039
200	Phosphorylation	KKHRDRKSSDSDSSD HHHCCCCCCCCCCCC	40.03	28985074
201	Phosphorylation	KHRDRKSSDSDSSDS HHCCCCCCCCCCCCC	44.14	-
203	Phosphorylation	RDRKSSDSDSSDSES CCCCCCCCCCCCCCC	41.14	-
205	Phosphorylation	RKSSDSDSSDSESDT CCCCCCCCCCCCCHH	39.74	28985074
206	Phosphorylation	KSSDSDSSDSESDTG CCCCCCCCCCCCHHH	50.58	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NO40_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NO40_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NO40_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
JMJD6_HUMAN	JMJD6	physical	23455924
KDM1A_HUMAN	KDM1A	physical	23455924
SUV91_HUMAN	SUV39H1	physical	23455924
JMJD6_HUMAN	JMJD6	physical	28514442
SHOT1_HUMAN	KIAA1598	physical	28514442
PININ_HUMAN	PNN	physical	28514442
CSK22_HUMAN	CSNK2A2	physical	28514442
SSFA2_HUMAN	SSFA2	physical	28514442
CAPON_HUMAN	NOS1AP	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
NKAP_HUMAN	NKAP	physical	28514442
RNPS1_HUMAN	RNPS1	physical	28514442
FRIL_HUMAN	FTL	physical	28514442
BPIB1_HUMAN	BPIFB1	physical	28514442
IGJ_HUMAN	IGJ	physical	28514442
SRRM2_HUMAN	SRRM2	physical	28514442
ZC3HE_HUMAN	ZC3H14	physical	28514442
POF1B_HUMAN	POF1B	physical	28514442

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-144, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-114, AND MASSSPECTROMETRY.
PubMed: 18669648