dbPTM

ZCHC7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZCHC7_HUMAN
UniProt AC	Q8N3Z6
Protein Name	Zinc finger CCHC domain-containing protein 7
Gene Name	ZCCHC7
Organism	Homo sapiens (Human).
Sequence Length	543
Subcellular Localization	Nucleus, nucleolus .
Protein Description
Protein Sequence	MMFGGYETIEAYEDDLYRDESSSELSVDSEVEFQLYSQIHYAQDLDDVIREEEHEEKNSGNSESSSSKPNQKKLIVLSDSEVIQLSDGSEVITLSDEDSIYRCKGKNVRVQAQENAHGLSSSLQSNELVDKKCKSDIEKPKSEERSGVIREVMIIEVSSSEEEESTISEGDNVESWMLLGCEVDDKDDDILLNLVGCENSVTEGEDGINWSISDKDIEAQIANNRTPGRWTQRYYSANKNIICRNCDKRGHLSKNCPLPRKVRRCFLCSRRGHLLYSCPAPLCEYCPVPKMLDHSCLFRHSWDKQCDRCHMLGHYTDACTEIWRQYHLTTKPGPPKKPKTPSRPSALAYCYHCAQKGHYGHECPEREVYDPSPVSPFICYYDDKYEIQEREKRLKQKIKVLKKNGVIPEPSKLPYIKAANENPHHDIRKGRASWKSNRWPQENKETQKEMKNKNRNWEKHRKADRHREVDEDFPRGPKTYSSPGSFKTQKPSKPFHRSSHYHTSREDKSPKEGKRGKQKKKERCWEDDDNDNLFLIKQRKKKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MMFGGYETIEAYE --CCCCCCCHHHHHH	15.41	23663014
8	Phosphorylation	MMFGGYETIEAYEDD CCCCCCCHHHHHHHC	18.68	23663014
12	Phosphorylation	GYETIEAYEDDLYRD CCCHHHHHHHCCCCC	13.70	23663014
17	Phosphorylation	EAYEDDLYRDESSSE HHHHHCCCCCCCCCC	24.02	23663014
64	Phosphorylation	KNSGNSESSSSKPNQ HHCCCCCCCCCCCCC	35.03	-
65	Phosphorylation	NSGNSESSSSKPNQK HCCCCCCCCCCCCCC	34.28	28985074
66	Phosphorylation	SGNSESSSSKPNQKK CCCCCCCCCCCCCCE	52.22	-
67	Phosphorylation	GNSESSSSKPNQKKL CCCCCCCCCCCCCEE	54.82	-
78	Phosphorylation	QKKLIVLSDSEVIQL CCEEEEECCCCEEEC	28.35	26074081
80	Phosphorylation	KLIVLSDSEVIQLSD EEEEECCCCEEECCC	30.32	26074081
120	Phosphorylation	QENAHGLSSSLQSNE EHHHCCCCHHHHHCH	23.60	30108239
121	Phosphorylation	ENAHGLSSSLQSNEL HHHCCCCHHHHHCHH	39.86	29743597
122	Phosphorylation	NAHGLSSSLQSNELV HHCCCCHHHHHCHHH	27.35	29743597
125	Phosphorylation	GLSSSLQSNELVDKK CCCHHHHHCHHHHHH	37.25	29743597
130 (in isoform 2)	Ubiquitination	-	58.27	21906983
131	Ubiquitination	QSNELVDKKCKSDIE HHCHHHHHHCHHHCC	53.22	2190698
131 (in isoform 1)	Ubiquitination	-	53.22	21906983
131	Sumoylation	QSNELVDKKCKSDIE HHCHHHHHHCHHHCC	53.22	28112733
131	Acetylation	QSNELVDKKCKSDIE HHCHHHHHHCHHHCC	53.22	26051181
132	Ubiquitination	SNELVDKKCKSDIEK HCHHHHHHCHHHCCC	42.29	-
139	Sumoylation	KCKSDIEKPKSEERS HCHHHCCCCCCHHCC	59.07	28112733
141	Sumoylation	KSDIEKPKSEERSGV HHHCCCCCCHHCCCC	79.96	28112733
141	Sumoylation	KSDIEKPKSEERSGV HHHCCCCCCHHCCCC	79.96	-
142	Phosphorylation	SDIEKPKSEERSGVI HHCCCCCCHHCCCCE	53.90	25159151
159	Phosphorylation	VMIIEVSSSEEEEST EEEEEECCCCCCCCC	47.12	22210691
166	Phosphorylation	SSEEEESTISEGDNV CCCCCCCCCCCCCCC	31.63	22210691
226	Phosphorylation	AQIANNRTPGRWTQR HHHHCCCCCCHHHHH	32.02	25159151
231	Phosphorylation	NRTPGRWTQRYYSAN CCCCCHHHHHHHCCC	11.21	28555341
236	Phosphorylation	RWTQRYYSANKNIIC HHHHHHHCCCCCEEE	19.21	29214152
239	Acetylation	QRYYSANKNIICRNC HHHHCCCCCEEECCC	49.60	26051181
239	Sumoylation	QRYYSANKNIICRNC HHHHCCCCCEEECCC	49.60	28112733
239	Ubiquitination	QRYYSANKNIICRNC HHHHCCCCCEEECCC	49.60	-
239	Sumoylation	QRYYSANKNIICRNC HHHHCCCCCEEECCC	49.60	-
254	Sumoylation	DKRGHLSKNCPLPRK CCCCCCCCCCCCCHH	69.77	28112733
276	Phosphorylation	SRRGHLLYSCPAPLC CCCCEEEECCCCCCC	18.00	22210691
277	Phosphorylation	RRGHLLYSCPAPLCE CCCEEEECCCCCCCC	17.37	22210691
295	Phosphorylation	VPKMLDHSCLFRHSW CCCCCCCCHHHCCCH	16.51	22210691
326	Phosphorylation	CTEIWRQYHLTTKPG HHHHHHHHCCCCCCC	7.10	20068231
329	Phosphorylation	IWRQYHLTTKPGPPK HHHHHCCCCCCCCCC	21.33	20068231
330	Phosphorylation	WRQYHLTTKPGPPKK HHHHCCCCCCCCCCC	41.42	20068231
331	Sumoylation	RQYHLTTKPGPPKKP HHHCCCCCCCCCCCC	42.62	-
331	Sumoylation	RQYHLTTKPGPPKKP HHHCCCCCCCCCCCC	42.62	-
339	Sumoylation	PGPPKKPKTPSRPSA CCCCCCCCCCCCHHH	80.22	28112733
340	Phosphorylation	GPPKKPKTPSRPSAL CCCCCCCCCCCHHHH	34.72	25159151
342	Phosphorylation	PKKPKTPSRPSALAY CCCCCCCCCHHHHHH	63.15	30576142
345	Phosphorylation	PKTPSRPSALAYCYH CCCCCCHHHHHHHHH	34.50	28555341
384	Ubiquitination	FICYYDDKYEIQERE EEEECCCHHHHHHHH	41.72	-
403	Methylation	QKIKVLKKNGVIPEP HHHHHHHHCCCCCCC	55.56	-
403	Trimethylation	QKIKVLKKNGVIPEP HHHHHHHHCCCCCCC	55.56	-
412	Sumoylation	GVIPEPSKLPYIKAA CCCCCCCCCCCEECC	65.28	28112733
412	Sumoylation	GVIPEPSKLPYIKAA CCCCCCCCCCCEECC	65.28	-
412	Methylation	GVIPEPSKLPYIKAA CCCCCCCCCCCEECC	65.28	-
417	Sumoylation	PSKLPYIKAANENPH CCCCCCEECCCCCCC	35.29	-
417	Ubiquitination	PSKLPYIKAANENPH CCCCCCEECCCCCCC	35.29	-
417	Sumoylation	PSKLPYIKAANENPH CCCCCCEECCCCCCC	35.29	28112733
433	Phosphorylation	DIRKGRASWKSNRWP CHHHCCHHHHHCCCC	33.41	24719451
435	Sumoylation	RKGRASWKSNRWPQE HHCCHHHHHCCCCCC	35.04	28112733
435	Sumoylation	RKGRASWKSNRWPQE HHCCHHHHHCCCCCC	35.04	-
444	Sumoylation	NRWPQENKETQKEMK CCCCCCCHHHHHHHH	62.48	-
444	Sumoylation	NRWPQENKETQKEMK CCCCCCCHHHHHHHH	62.48	-
478	Sumoylation	EDFPRGPKTYSSPGS CCCCCCCCCCCCCCC	64.02	28112733
479	Phosphorylation	DFPRGPKTYSSPGSF CCCCCCCCCCCCCCC	31.59	29396449
480	Phosphorylation	FPRGPKTYSSPGSFK CCCCCCCCCCCCCCC	17.18	30108239
481	Phosphorylation	PRGPKTYSSPGSFKT CCCCCCCCCCCCCCC	34.98	30266825
482	Phosphorylation	RGPKTYSSPGSFKTQ CCCCCCCCCCCCCCC	23.90	30266825
485	Phosphorylation	KTYSSPGSFKTQKPS CCCCCCCCCCCCCCC	27.27	30266825
487	Sumoylation	YSSPGSFKTQKPSKP CCCCCCCCCCCCCCC	52.31	-
487	Sumoylation	YSSPGSFKTQKPSKP CCCCCCCCCCCCCCC	52.31	28112733
490	Sumoylation	PGSFKTQKPSKPFHR CCCCCCCCCCCCCCC	57.39	-
490	Sumoylation	PGSFKTQKPSKPFHR CCCCCCCCCCCCCCC	57.39	28112733
493	Sumoylation	FKTQKPSKPFHRSSH CCCCCCCCCCCCCCC	61.30	-
493	Sumoylation	FKTQKPSKPFHRSSH CCCCCCCCCCCCCCC	61.30	28112733
537	Sumoylation	NDNLFLIKQRKKKS- CCCEEEEEECCCCC-	46.31	-
537	Ubiquitination	NDNLFLIKQRKKKS- CCCEEEEEECCCCC-	46.31	-
537	Sumoylation	NDNLFLIKQRKKKS- CCCEEEEEECCCCC-	46.31	28112733

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 ZCHC7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZCHC7_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 ZCHC7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAPD5_HUMAN	PAPD5	physical	21878619
PAPD7_HUMAN	PAPD7	physical	21878619
PDLI7_HUMAN	PDLIM7	physical	26186194
VIGLN_HUMAN	HDLBP	physical	26186194
SENP5_HUMAN	SENP5	physical	26186194
IF2B_HUMAN	EIF2S2	physical	26186194
HDGR2_HUMAN	HDGFRP2	physical	26186194
BCD1_HUMAN	ZNHIT6	physical	26186194
TASOR_HUMAN	FAM208A	physical	26186194
PDLI7_HUMAN	PDLIM7	physical	28514442
HDGR2_HUMAN	HDGFRP2	physical	28514442
SENP5_HUMAN	SENP5	physical	28514442
ZKSC1_HUMAN	ZKSCAN1	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.

Regulatory Network of ZCHC7_HUMAN

Related Literatures of Post-Translational Modification

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-482, 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-482, AND MASSSPECTROMETRY.	18669648 [Abstract]