dbPTM

Z280C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	Z280C_HUMAN
UniProt AC	Q8ND82
Protein Name	Zinc finger protein 280C
Gene Name	ZNF280C
Organism	Homo sapiens (Human).
Sequence Length	737
Subcellular Localization	Nucleus .
Protein Description	May function as a transcription factor..
Protein Sequence	MDDDKPFQPKNISKMAELFMECEEEELEPWQKKVEETQDEDDDELIFVGEISSSKPAISNILNRGHSSSSSKGIKSEPHSPGIPEIFRTASQRCRDPPSNPVAASPRFHLVSKSSQSSVTVENASKPDFTKNSQVGSDNSSILLFDSTQESLPPSQDIPAIFREGMKNTSYVLKHPSTSKVNSVTPKKPKTSEDVPQINPSTSLPLIGSPPVTSSQVMLSKGTNTSSPYDAGADYLRACPKCNVQFNLLDPLKYHMKHCCPDMITKFLGVIVKSERPCDEDKTDSETGKLIMLVNEFYYGRHEGVTEKEPKTYTTFKCFSCSKVLKNNIRFMNHMKHHLELEKQNNESWENHTTCQHCYRQYPTPFQLQCHIESTHTPHEFSTICKICELSFETEHILLQHMKDTHKPGEMPYVCQVCQFRSSTFSDVEAHFRAAHENTKNLLCPFCLKVSKMATPYMNHYMKHQKKGVHRCPKCRLQFLTSKEKAEHKAQHRTFIKPKELEGLPPGAKVTIRASLGPLQSKLPTAPFGCAPGTSFLQVTPPTSQNTTARNPRKSNASRSKTSKLHATTSTASKVNTSKPRGRIAKSKAKPSYKQKRQRNRKNKMSLALKNIRCRRGIHKCIECHSKIKDFASHFSIYIHCSFCKYNTNCNKAFVNHMMSSHSNHPGKRFCIFKKHSGTLRGITLVCLKCDFLADSSGLDRMAKHLSQRKTHTCQVIIENVSKSTSTSEPTTGCSLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Sumoylation	---MDDDKPFQPKNI ---CCCCCCCCCCHH	55.51	-
5	Sumoylation	---MDDDKPFQPKNI ---CCCCCCCCCCHH	55.51	28112733
10	Sumoylation	DDKPFQPKNISKMAE CCCCCCCCHHHHHHH	57.01	28112733
14	Sumoylation	FQPKNISKMAELFME CCCCHHHHHHHHHHH	38.03	28112733
14	Ubiquitination	FQPKNISKMAELFME CCCCHHHHHHHHHHH	38.03	-
22	Glutathionylation	MAELFMECEEEELEP HHHHHHHHCHHHCHH	5.53	22555962
32	Ubiquitination	EELEPWQKKVEETQD HHCHHHHHHHHHCCC	55.72	21963094
33	Sumoylation	ELEPWQKKVEETQDE HCHHHHHHHHHCCCC	39.52	28112733
33	Ubiquitination	ELEPWQKKVEETQDE HCHHHHHHHHHCCCC	39.52	-
55	Sumoylation	VGEISSSKPAISNIL EEEECCCCCHHHHHH	40.18	28112733
67	Phosphorylation	NILNRGHSSSSSKGI HHHHCCCCCCCCCCC	34.44	20363803
68	Phosphorylation	ILNRGHSSSSSKGIK HHHCCCCCCCCCCCC	28.68	20363803
69	Phosphorylation	LNRGHSSSSSKGIKS HHCCCCCCCCCCCCC	41.46	20363803
70	Phosphorylation	NRGHSSSSSKGIKSE HCCCCCCCCCCCCCC	37.71	25852190
71	Phosphorylation	RGHSSSSSKGIKSEP CCCCCCCCCCCCCCC	36.53	25852190
72	Sumoylation	GHSSSSSKGIKSEPH CCCCCCCCCCCCCCC	67.61	-
72	Ubiquitination	GHSSSSSKGIKSEPH CCCCCCCCCCCCCCC	67.61	29967540
75	Sumoylation	SSSSKGIKSEPHSPG CCCCCCCCCCCCCCC	58.39	-
75	Acetylation	SSSSKGIKSEPHSPG CCCCCCCCCCCCCCC	58.39	26051181
75	Neddylation	SSSSKGIKSEPHSPG CCCCCCCCCCCCCCC	58.39	32015554
75	Sumoylation	SSSSKGIKSEPHSPG CCCCCCCCCCCCCCC	58.39	28112733
76	Phosphorylation	SSSKGIKSEPHSPGI CCCCCCCCCCCCCCH	55.21	25159151
80	Phosphorylation	GIKSEPHSPGIPEIF CCCCCCCCCCHHHHH	35.22	23927012
99	Phosphorylation	QRCRDPPSNPVAASP HHCCCCCCCCCCCCC	60.19	24732914
105	Phosphorylation	PSNPVAASPRFHLVS CCCCCCCCCCEEEEE	13.58	30266825
107	Methylation	NPVAASPRFHLVSKS CCCCCCCCEEEEECC	29.17	115920433
112	Phosphorylation	SPRFHLVSKSSQSSV CCCEEEEECCCCCCE	32.93	26714015
113	Sumoylation	PRFHLVSKSSQSSVT CCEEEEECCCCCCEE	46.80	28112733
114	Phosphorylation	RFHLVSKSSQSSVTV CEEEEECCCCCCEEE	26.55	29978859
115	Phosphorylation	FHLVSKSSQSSVTVE EEEEECCCCCCEEEE	37.51	17525332
117	Phosphorylation	LVSKSSQSSVTVENA EEECCCCCCEEEECC	28.82	25159151
118	Phosphorylation	VSKSSQSSVTVENAS EECCCCCCEEEECCC	17.73	17525332
120	Phosphorylation	KSSQSSVTVENASKP CCCCCCEEEECCCCC	24.85	29978859
126	Sumoylation	VTVENASKPDFTKNS EEEECCCCCCCCCCC	46.31	-
126	Acetylation	VTVENASKPDFTKNS EEEECCCCCCCCCCC	46.31	26051181
126	Sumoylation	VTVENASKPDFTKNS EEEECCCCCCCCCCC	46.31	28112733
126	Ubiquitination	VTVENASKPDFTKNS EEEECCCCCCCCCCC	46.31	29967540
130	Phosphorylation	NASKPDFTKNSQVGS CCCCCCCCCCCCCCC	36.37	-
133	Phosphorylation	KPDFTKNSQVGSDNS CCCCCCCCCCCCCCC	28.00	-
155	Phosphorylation	TQESLPPSQDIPAIF CCCCCCCCCCHHHHH	38.25	22817900
167	Sumoylation	AIFREGMKNTSYVLK HHHHHCCCCCEEECC	68.85	-
167	Sumoylation	AIFREGMKNTSYVLK HHHHHCCCCCEEECC	68.85	28112733
169	Phosphorylation	FREGMKNTSYVLKHP HHHCCCCCEEECCCC	18.86	26714015
170	Phosphorylation	REGMKNTSYVLKHPS HHCCCCCEEECCCCC	23.72	21712546
174	Methylation	KNTSYVLKHPSTSKV CCCEEECCCCCCCCC	43.35	115978253
174	Sumoylation	KNTSYVLKHPSTSKV CCCEEECCCCCCCCC	43.35	28112733
174	Ubiquitination	KNTSYVLKHPSTSKV CCCEEECCCCCCCCC	43.35	27667366
177	Phosphorylation	SYVLKHPSTSKVNSV EEECCCCCCCCCCCC	45.06	26714015
178	Phosphorylation	YVLKHPSTSKVNSVT EECCCCCCCCCCCCC	36.70	26714015
179	Phosphorylation	VLKHPSTSKVNSVTP ECCCCCCCCCCCCCC	38.66	26714015
180	Sumoylation	LKHPSTSKVNSVTPK CCCCCCCCCCCCCCC	45.59	28112733
180	Ubiquitination	LKHPSTSKVNSVTPK CCCCCCCCCCCCCCC	45.59	29967540
183	Phosphorylation	PSTSKVNSVTPKKPK CCCCCCCCCCCCCCC	30.29	29396449
185	Phosphorylation	TSKVNSVTPKKPKTS CCCCCCCCCCCCCCC	29.25	30576142
187	Acetylation	KVNSVTPKKPKTSED CCCCCCCCCCCCCCC	72.79	30592707
187	Sumoylation	KVNSVTPKKPKTSED CCCCCCCCCCCCCCC	72.79	28112733
201	Phosphorylation	DVPQINPSTSLPLIG CCCCCCCCCCCCCCC	26.58	22199227
202	Phosphorylation	VPQINPSTSLPLIGS CCCCCCCCCCCCCCC	35.22	22199227
203	Phosphorylation	PQINPSTSLPLIGSP CCCCCCCCCCCCCCC	32.12	22199227
209	Phosphorylation	TSLPLIGSPPVTSSQ CCCCCCCCCCCCCCC	21.02	22199227
213	Phosphorylation	LIGSPPVTSSQVMLS CCCCCCCCCCCEEEC	28.56	22199227
214	Phosphorylation	IGSPPVTSSQVMLSK CCCCCCCCCCEEECC	21.00	22199227
215	Phosphorylation	GSPPVTSSQVMLSKG CCCCCCCCCEEECCC	19.89	22199227
220	Phosphorylation	TSSQVMLSKGTNTSS CCCCEEECCCCCCCC	15.79	-
223	Phosphorylation	QVMLSKGTNTSSPYD CEEECCCCCCCCCCC	38.77	25159151
225	Phosphorylation	MLSKGTNTSSPYDAG EECCCCCCCCCCCCC	30.35	25159151
226	Phosphorylation	LSKGTNTSSPYDAGA ECCCCCCCCCCCCCH	31.24	25159151
227	Phosphorylation	SKGTNTSSPYDAGAD CCCCCCCCCCCCCHH	25.99	23401153
229	Phosphorylation	GTNTSSPYDAGADYL CCCCCCCCCCCHHHH	22.00	22115753
235	Phosphorylation	PYDAGADYLRACPKC CCCCCHHHHHHCCCC	9.50	24732914
241	Sumoylation	DYLRACPKCNVQFNL HHHHHCCCCCCEEEC	38.02	-
241	Sumoylation	DYLRACPKCNVQFNL HHHHHCCCCCCEEEC	38.02	-
241	Ubiquitination	DYLRACPKCNVQFNL HHHHHCCCCCCEEEC	38.02	-
253	Acetylation	FNLLDPLKYHMKHCC EECCCHHHHHHHHHC	38.20	25953088
273	Sumoylation	KFLGVIVKSERPCDE HHHHHHHCCCCCCCC	35.16	-
273	Sumoylation	KFLGVIVKSERPCDE HHHHHHHCCCCCCCC	35.16	28112733
282	Acetylation	ERPCDEDKTDSETGK CCCCCCCCCCCCCCC	52.78	26051181
283	Phosphorylation	RPCDEDKTDSETGKL CCCCCCCCCCCCCCE	58.01	28985074
285	Phosphorylation	CDEDKTDSETGKLIM CCCCCCCCCCCCEEE	42.14	30576142
287	Phosphorylation	EDKTDSETGKLIMLV CCCCCCCCCCEEEEE	43.50	30576142
323	Acetylation	FKCFSCSKVLKNNIR EEEEECHHHHHHHHH	56.78	25953088
326	Ubiquitination	FSCSKVLKNNIRFMN EECHHHHHHHHHHHH	51.43	29967540
348	Phosphorylation	LEKQNNESWENHTTC HHHHCCCCCCCCCCH	41.64	26714015
426	Phosphorylation	QFRSSTFSDVEAHFR ECCCCCHHHHHHHHH	40.61	-
455	Phosphorylation	LKVSKMATPYMNHYM HHHHHHCCHHHHHHH	16.08	-
481	Phosphorylation	KCRLQFLTSKEKAEH HHHHEECCCHHHHHH	38.76	29083192
482	Phosphorylation	CRLQFLTSKEKAEHK HHHEECCCHHHHHHH	40.75	29083192
509	Ubiquitination	EGLPPGAKVTIRASL CCCCCCCEEEEEEEC	45.91	29967540
511	Phosphorylation	LPPGAKVTIRASLGP CCCCCEEEEEEECCC	12.21	24719451
515	Phosphorylation	AKVTIRASLGPLQSK CEEEEEEECCCHHHC	24.82	25159151
521	Phosphorylation	ASLGPLQSKLPTAPF EECCCHHHCCCCCCC	43.79	-
522	Sumoylation	SLGPLQSKLPTAPFG ECCCHHHCCCCCCCC	45.59	28112733
525	Phosphorylation	PLQSKLPTAPFGCAP CHHHCCCCCCCCCCC	58.35	24732914
534	Phosphorylation	PFGCAPGTSFLQVTP CCCCCCCCCEEEECC	18.42	24732914
535	Phosphorylation	FGCAPGTSFLQVTPP CCCCCCCCEEEECCC	29.85	24732914
540	Phosphorylation	GTSFLQVTPPTSQNT CCCEEEECCCCCCCC	15.58	25159151
543	Phosphorylation	FLQVTPPTSQNTTAR EEEECCCCCCCCCCC	44.11	25022875
544	Phosphorylation	LQVTPPTSQNTTARN EEECCCCCCCCCCCC	27.49	25022875
547	Phosphorylation	TPPTSQNTTARNPRK CCCCCCCCCCCCCCC	17.75	24732914
548	Phosphorylation	PPTSQNTTARNPRKS CCCCCCCCCCCCCCC	31.04	24732914
555	Phosphorylation	TARNPRKSNASRSKT CCCCCCCCCCCCCCC	38.62	-
560	Phosphorylation	RKSNASRSKTSKLHA CCCCCCCCCCCCCEE	37.48	-
561	Ubiquitination	KSNASRSKTSKLHAT CCCCCCCCCCCCEEE	56.56	21890473
564	Acetylation	ASRSKTSKLHATTST CCCCCCCCCEEECCC	49.91	25953088
564	Sumoylation	ASRSKTSKLHATTST CCCCCCCCCEEECCC	49.91	28112733
564	Ubiquitination	ASRSKTSKLHATTST CCCCCCCCCEEECCC	49.91	29967540
568	Phosphorylation	KTSKLHATTSTASKV CCCCCEEECCCCCCC	15.55	-
574	Sumoylation	ATTSTASKVNTSKPR EECCCCCCCCCCCCC	36.72	28112733
574	Ubiquitination	ATTSTASKVNTSKPR EECCCCCCCCCCCCC	36.72	29967540
604	Sumoylation	RQRNRKNKMSLALKN HHHHHHHHHHHHHHH	32.66	-
604	Sumoylation	RQRNRKNKMSLALKN HHHHHHHHHHHHHHH	32.66	-
606	Phosphorylation	RNRKNKMSLALKNIR HHHHHHHHHHHHHHH	16.46	25159151
610	Ubiquitination	NKMSLALKNIRCRRG HHHHHHHHHHHHCCC	44.73	21890473
620	Ubiquitination	RCRRGIHKCIECHSK HHCCCHHHHHHCHHH	34.68	29967540
640	Ubiquitination	SHFSIYIHCSFCKYN HHCEEEEEECCCCCC	5.56	21963094
689	Ubiquitination	GITLVCLKCDFLADS EEEEEEECCCHHHCC	26.99	21963094
697	Phosphorylation	CDFLADSSGLDRMAK CCHHHCCCCHHHHHH	43.87	26714015
711	Phosphorylation	KHLSQRKTHTCQVII HHHHHCCCCEEEEEE	25.30	20068231
713	Phosphorylation	LSQRKTHTCQVIIEN HHHCCCCEEEEEEEE	15.18	20068231
722	Phosphorylation	QVIIENVSKSTSTSE EEEEEEECCCCCCCC	32.25	28258704
723	Ubiquitination	VIIENVSKSTSTSEP EEEEEECCCCCCCCC	54.17	32015554
724	Phosphorylation	IIENVSKSTSTSEPT EEEEECCCCCCCCCC	21.78	28258704
725	Phosphorylation	IENVSKSTSTSEPTT EEEECCCCCCCCCCC	39.50	28258704
726	Phosphorylation	ENVSKSTSTSEPTTG EEECCCCCCCCCCCC	36.71	25627689
727	Phosphorylation	NVSKSTSTSEPTTGC EECCCCCCCCCCCCC	36.88	18491316
728	Phosphorylation	VSKSTSTSEPTTGCS ECCCCCCCCCCCCCC	41.15	18491316
737	Ubiquitination	PTTGCSLK------- CCCCCCCC-------	41.84	32015554

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 Z280C_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of Z280C_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 Z280C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of Z280C_HUMAN !!

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 Z280C_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-227, AND MASSSPECTROMETRY.	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-226 AND THR-540, ANDMASS 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-76; SER-80 AND THR-540,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.	18220336 [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-115 AND SER-118, ANDMASS SPECTROMETRY.	17525332 [Abstract]