dbPTM

ZN148_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN148_HUMAN
UniProt AC	Q9UQR1
Protein Name	Zinc finger protein 148
Gene Name	ZNF148
Organism	Homo sapiens (Human).
Sequence Length	794
Subcellular Localization	Nucleus.
Protein Description	Involved in transcriptional regulation. Represses the transcription of a number of genes including gastrin, stromelysin and enolase. Binds to the G-rich box in the enhancer region of these genes..
Protein Sequence	MNIDDKLEGLFLKCGGIDEMQSSRTMVVMGGVSGQSTVSGELQDSVLQDRSMPHQEILAADEVLQESEMRQQDMISHDELMVHEETVKNDEEQMETHERLPQGLQYALNVPISVKQEITFTDVSEQLMRDKKQIREPVDLQKKKKRKQRSPAKILTINEDGSLGLKTPKSHVCEHCNAAFRTNYHLQRHVFIHTGEKPFQCSQCDMRFIQKYLLQRHEKIHTGEKPFRCDECGMRFIQKYHMERHKRTHSGEKPYQCEYCLQYFSRTDRVLKHKRMCHENHDKKLNRCAIKGGLLTSEEDSGFSTSPKDNSLPKKKRQKTEKKSSGMDKESALDKSDLKKDKNDYLPLYSSSTKVKDEYMVAEYAVEMPHSSVGGSHLEDASGEIHPPKLVLKKINSKRSLKQPLEQNQTISPLSTYEESKVSKYAFELVDKQALLDSEGNADIDQVDNLQEGPSKPVHSSTNYDDAMQFLKKKRYLQAASNNSREYALNVGTIASQPSVTQAAVASVIDESTTASILESQALNVEIKSNHDKNVIPDEVLQTLLDHYSHKANGQHEISFSVADTEVTSSISINSSEVPEVTPSENVGSSSQASSSDKANMLQEYSKFLQQALDRTSQNDAYLNSPSLNFVTDNQTLPNQPAFSSIDKQVYATMPINSFRSGMNSPLRTTPDKSHFGLIVGDSQHSFPFSGDETNHASATSTQDFLDQVTSQKKAEAQPVHQAYQMSSFEQPFRAPYHGSRAGIATQFSTANGQVNLRGPGTSAEFSEFPLVNVNDNRAGMTSSPDATTGQTFG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Sumoylation	--MNIDDKLEGLFLK --CCHHHHHHHHHHH	44.69	28112733
22	Phosphorylation	GGIDEMQSSRTMVVM CCCCHHHCCCEEEEE	22.07	21955146
23	Phosphorylation	GIDEMQSSRTMVVMG CCCHHHCCCEEEEEC	18.19	21955146
25	Phosphorylation	DEMQSSRTMVVMGGV CHHHCCCEEEEECCC	19.10	18669648
33	Phosphorylation	MVVMGGVSGQSTVSG EEEECCCCCCCCCCH	34.10	21955146
36	Phosphorylation	MGGVSGQSTVSGELQ ECCCCCCCCCCHHHC	34.01	21955146
37	Phosphorylation	GGVSGQSTVSGELQD CCCCCCCCCCHHHCC	15.71	18669648
39	Phosphorylation	VSGQSTVSGELQDSV CCCCCCCCHHHCCHH	27.00	21955146
45	Phosphorylation	VSGELQDSVLQDRSM CCHHHCCHHHCCCCC	16.27	21955146
51	Phosphorylation	DSVLQDRSMPHQEIL CHHHCCCCCCHHHHH	44.98	30108239
88	Sumoylation	MVHEETVKNDEEQME HCCHHHCCCHHHHHH	67.13	28112733
106	Phosphorylation	RLPQGLQYALNVPIS HCCCHHHHHHCCCEE	20.35	27642862
115	Sumoylation	LNVPISVKQEITFTD HCCCEEECEEEEECC	35.11	-
115	Sumoylation	LNVPISVKQEITFTD HCCCEEECEEEEECC	35.11	28112733
119	Phosphorylation	ISVKQEITFTDVSEQ EEECEEEEECCHHHH	21.52	20860994
121	Phosphorylation	VKQEITFTDVSEQLM ECEEEEECCHHHHHH	27.17	20860994
132	Sumoylation	EQLMRDKKQIREPVD HHHHCCHHHHCCCCC	56.07	-
132	Sumoylation	EQLMRDKKQIREPVD HHHHCCHHHHCCCCC	56.07	28112733
147	Ubiquitination	LQKKKKRKQRSPAKI HHHHHHHCCCCCCCE	59.97	23000965
150	Phosphorylation	KKKRKQRSPAKILTI HHHHCCCCCCCEEEE	27.07	25849741
153	Ubiquitination	RKQRSPAKILTINED HCCCCCCCEEEECCC	41.45	23000965
156	Phosphorylation	RSPAKILTINEDGSL CCCCCEEEECCCCCC	25.81	21949786
162	Phosphorylation	LTINEDGSLGLKTPK EEECCCCCCCCCCCC	31.42	27251275
166	Ubiquitination	EDGSLGLKTPKSHVC CCCCCCCCCCCCHHH	62.07	29967540
167	Phosphorylation	DGSLGLKTPKSHVCE CCCCCCCCCCCHHHH	40.78	22199227
194	Phosphorylation	QRHVFIHTGEKPFQC CCCEEEECCCCCCCC	42.07	30576142
197	Ubiquitination	VFIHTGEKPFQCSQC EEEECCCCCCCCCHH	53.10	-
202	Phosphorylation	GEKPFQCSQCDMRFI CCCCCCCCHHCHHHH	24.06	30576142
222	Phosphorylation	QRHEKIHTGEKPFRC HHHHCCCCCCCCCCC	50.97	29496963
239	Sumoylation	CGMRFIQKYHMERHK HHHHHHHHHHHHHHC	32.10	-
239	Ubiquitination	CGMRFIQKYHMERHK HHHHHHHHHHHHHHC	32.10	29967540
239	Sumoylation	CGMRFIQKYHMERHK HHHHHHHHHHHHHHC	32.10	-
248	Phosphorylation	HMERHKRTHSGEKPY HHHHHCCCCCCCCCC	25.79	28152594
250	Phosphorylation	ERHKRTHSGEKPYQC HHHCCCCCCCCCCCC	48.29	26055452
255	Phosphorylation	THSGEKPYQCEYCLQ CCCCCCCCCCHHHHH	36.54	29214152
259	Phosphorylation	EKPYQCEYCLQYFSR CCCCCCHHHHHHHHH	13.19	-
291	Methylation	KLNRCAIKGGLLTSE HHHHHHEECCCCCCC	28.53	115978281
291	Ubiquitination	KLNRCAIKGGLLTSE HHHHHHEECCCCCCC	28.53	23000965
291	Acetylation	KLNRCAIKGGLLTSE HHHHHHEECCCCCCC	28.53	26051181
291	Sumoylation	KLNRCAIKGGLLTSE HHHHHHEECCCCCCC	28.53	28112733
296	Phosphorylation	AIKGGLLTSEEDSGF HEECCCCCCCCCCCC	38.85	23927012
297	Phosphorylation	IKGGLLTSEEDSGFS EECCCCCCCCCCCCC	38.67	25159151
301	Phosphorylation	LLTSEEDSGFSTSPK CCCCCCCCCCCCCCC	45.04	22167270
304	Phosphorylation	SEEDSGFSTSPKDNS CCCCCCCCCCCCCCC	31.34	29255136
305	Phosphorylation	EEDSGFSTSPKDNSL CCCCCCCCCCCCCCC	46.95	29255136
306	Phosphorylation	EDSGFSTSPKDNSLP CCCCCCCCCCCCCCC	28.84	29255136
308	Sumoylation	SGFSTSPKDNSLPKK CCCCCCCCCCCCCHH	70.12	28112733
311	Phosphorylation	STSPKDNSLPKKKRQ CCCCCCCCCCHHHHH	57.07	22167270
324	Phosphorylation	RQKTEKKSSGMDKES HHHHCHHCCCCCHHH	43.10	29214152
325	Phosphorylation	QKTEKKSSGMDKESA HHHCHHCCCCCHHHH	47.20	-
329	Acetylation	KKSSGMDKESALDKS HHCCCCCHHHHCCHH	44.68	25953088
331	Phosphorylation	SSGMDKESALDKSDL CCCCCHHHHCCHHHH	39.61	-
335	Acetylation	DKESALDKSDLKKDK CHHHHCCHHHHHCCC	46.87	25953088
336	Phosphorylation	KESALDKSDLKKDKN HHHHCCHHHHHCCCC	48.09	25159151
342	Ubiquitination	KSDLKKDKNDYLPLY HHHHHCCCCCCCCCC	61.67	29967540
342	Acetylation	KSDLKKDKNDYLPLY HHHHHCCCCCCCCCC	61.67	25953088
345	Phosphorylation	LKKDKNDYLPLYSSS HHCCCCCCCCCCCCC	21.44	27642862
349	Phosphorylation	KNDYLPLYSSSTKVK CCCCCCCCCCCCCCC	12.45	27642862
350	Phosphorylation	NDYLPLYSSSTKVKD CCCCCCCCCCCCCCC	26.04	25159151
351	Phosphorylation	DYLPLYSSSTKVKDE CCCCCCCCCCCCCCE	28.59	25159151
352	Phosphorylation	YLPLYSSSTKVKDEY CCCCCCCCCCCCCEE	26.72	25159151
353	Phosphorylation	LPLYSSSTKVKDEYM CCCCCCCCCCCCEEE	41.63	25627689
356	Sumoylation	YSSSTKVKDEYMVAE CCCCCCCCCEEEEEE	46.53	-
356	Sumoylation	YSSSTKVKDEYMVAE CCCCCCCCCEEEEEE	46.53	25114211
400	Phosphorylation	KKINSKRSLKQPLEQ HHCCCCCCCCCCHHC	43.59	23403867
402	Ubiquitination	INSKRSLKQPLEQNQ CCCCCCCCCCHHCCC	51.63	29967540
402	Sumoylation	INSKRSLKQPLEQNQ CCCCCCCCCCHHCCC	51.63	28112733
410	Phosphorylation	QPLEQNQTISPLSTY CCHHCCCCCCCCHHH	30.85	30266825
412	Phosphorylation	LEQNQTISPLSTYEE HHCCCCCCCCHHHCH	24.15	23927012
415	Phosphorylation	NQTISPLSTYEESKV CCCCCCCHHHCHHHH	32.12	30266825
416	Phosphorylation	QTISPLSTYEESKVS CCCCCCHHHCHHHHH	42.51	30266825
417	Phosphorylation	TISPLSTYEESKVSK CCCCCHHHCHHHHHH	17.83	30266825
420	Phosphorylation	PLSTYEESKVSKYAF CCHHHCHHHHHHHHH	26.81	23927012
421	Ubiquitination	LSTYEESKVSKYAFE CHHHCHHHHHHHHHH	54.53	29967540
421	Acetylation	LSTYEESKVSKYAFE CHHHCHHHHHHHHHH	54.53	26051181
421	Sumoylation	LSTYEESKVSKYAFE CHHHCHHHHHHHHHH	54.53	28112733
423	Phosphorylation	TYEESKVSKYAFELV HHCHHHHHHHHHHHH	24.56	23312004
424	Sumoylation	YEESKVSKYAFELVD HCHHHHHHHHHHHHH	43.52	-
424	Ubiquitination	YEESKVSKYAFELVD HCHHHHHHHHHHHHH	43.52	29967540
424	Sumoylation	YEESKVSKYAFELVD HCHHHHHHHHHHHHH	43.52	28112733
424	Acetylation	YEESKVSKYAFELVD HCHHHHHHHHHHHHH	43.52	25953088
425	Phosphorylation	EESKVSKYAFELVDK CHHHHHHHHHHHHHH	14.71	-
432	Ubiquitination	YAFELVDKQALLDSE HHHHHHHHHHHHCCC	29.95	29967540
438	Phosphorylation	DKQALLDSEGNADID HHHHHHCCCCCCCHH	47.58	25159151
456	Acetylation	NLQEGPSKPVHSSTN CCCCCCCCCCCCCCC	54.94	25953088
456	Ubiquitination	NLQEGPSKPVHSSTN CCCCCCCCCCCCCCC	54.94	29967540
472	Ubiquitination	DDAMQFLKKKRYLQA HHHHHHHHHHHHHHH	58.50	29967540
496	O-linked_Glycosylation	LNVGTIASQPSVTQA ECHHHCCCCCCHHHH	38.48	31492838
501	O-linked_Glycosylation	IASQPSVTQAAVASV CCCCCCHHHHHHHHH	19.48	31492838
533	Ubiquitination	EIKSNHDKNVIPDEV EECCCCCCCCCCHHH	45.63	29967540
533	Acetylation	EIKSNHDKNVIPDEV EECCCCCCCCCCHHH	45.63	26051181
543	Phosphorylation	IPDEVLQTLLDHYSH CCHHHHHHHHHHHCH	25.73	27251275
549	Phosphorylation	QTLLDHYSHKANGQH HHHHHHHCHHHCCCE	18.32	27251275
559	O-linked_Glycosylation	ANGQHEISFSVADTE HCCCEEEEEEECCCE	14.42	31492838
572	O-linked_Glycosylation	TEVTSSISINSSEVP CEEEEEEEECCCCCC	20.05	31492838
607	Acetylation	NMLQEYSKFLQQALD HHHHHHHHHHHHHHH	49.55	19608861
607	Ubiquitination	NMLQEYSKFLQQALD HHHHHHHHHHHHHHH	49.55	19608861
625	Phosphorylation	QNDAYLNSPSLNFVT CCCCCCCCCCCCCCC	17.17	22210691
627	Phosphorylation	DAYLNSPSLNFVTDN CCCCCCCCCCCCCCC	35.45	22210691
632	Phosphorylation	SPSLNFVTDNQTLPN CCCCCCCCCCCCCCC	25.70	28348404
636	Phosphorylation	NFVTDNQTLPNQPAF CCCCCCCCCCCCCCC	50.89	28348404
636	O-linked_Glycosylation	NFVTDNQTLPNQPAF CCCCCCCCCCCCCCC	50.89	31492838
644	O-linked_Glycosylation	LPNQPAFSSIDKQVY CCCCCCCCCCCCCCE	28.61	31492838
651	Phosphorylation	SSIDKQVYATMPINS CCCCCCCEEECCCCH	8.21	28796482
653	Phosphorylation	IDKQVYATMPINSFR CCCCCEEECCCCHHC	13.04	26074081
658	Phosphorylation	YATMPINSFRSGMNS EEECCCCHHCCCCCC	23.82	26074081
661	Phosphorylation	MPINSFRSGMNSPLR CCCCHHCCCCCCCCC	40.14	25159151
665	Phosphorylation	SFRSGMNSPLRTTPD HHCCCCCCCCCCCCC	19.20	29255136
669	Phosphorylation	GMNSPLRTTPDKSHF CCCCCCCCCCCCCCC	50.81	25159151
670	Phosphorylation	MNSPLRTTPDKSHFG CCCCCCCCCCCCCCE	24.05	23401153
683	Phosphorylation	FGLIVGDSQHSFPFS CEEEECCCCCCCCCC	24.70	26074081
686	Phosphorylation	IVGDSQHSFPFSGDE EECCCCCCCCCCCCC	27.29	26074081
702	Phosphorylation	NHASATSTQDFLDQV CCCCCCCHHHHHHHH	28.01	30576142
724	Phosphorylation	AQPVHQAYQMSSFEQ CCCHHHHHHCCCCCC	9.74	27642862
727	Phosphorylation	VHQAYQMSSFEQPFR HHHHHHCCCCCCCCC	19.15	28348404
728	Phosphorylation	HQAYQMSSFEQPFRA HHHHHCCCCCCCCCC	27.71	28348404
734	Methylation	SSFEQPFRAPYHGSR CCCCCCCCCCCCCCC	41.14	115920397
740	Phosphorylation	FRAPYHGSRAGIATQ CCCCCCCCCCEEEEE	12.97	-
749	Phosphorylation	AGIATQFSTANGQVN CEEEEEEECCCCEEE	19.45	28857561
749	O-linked_Glycosylation	AGIATQFSTANGQVN CEEEEEEECCCCEEE	19.45	31492838
750	Phosphorylation	GIATQFSTANGQVNL EEEEEEECCCCEEEE	25.98	28857561
762	Phosphorylation	VNLRGPGTSAEFSEF EEECCCCCCCCCCCC	28.09	24719451
763	Phosphorylation	NLRGPGTSAEFSEFP EECCCCCCCCCCCCC	31.54	26714015
767	Phosphorylation	PGTSAEFSEFPLVNV CCCCCCCCCCCEEEC	29.81	26074081
782	Phosphorylation	NDNRAGMTSSPDATT CCCCCCCCCCCCCCC	25.74	30266825
783	Phosphorylation	DNRAGMTSSPDATTG CCCCCCCCCCCCCCC	30.86	30266825
784	Phosphorylation	NRAGMTSSPDATTGQ CCCCCCCCCCCCCCC	20.03	26846344
788	Phosphorylation	MTSSPDATTGQTFG- CCCCCCCCCCCCCC-	38.55	30266825
789	Phosphorylation	TSSPDATTGQTFG-- CCCCCCCCCCCCC--	29.07	23663014
792	Phosphorylation	PDATTGQTFG----- CCCCCCCCCC-----	31.50	23403867

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
202	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN148_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 ZN148_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAVN1_HUMAN	PTRF	physical	10727401
P53_HUMAN	TP53	physical	11416144
HDAC3_HUMAN	HDAC3	physical	19583777
EP300_HUMAN	EP300	physical	21828133
TRRAP_HUMAN	TRRAP	physical	21828133
KAT2A_HUMAN	KAT2A	physical	21828133
ZN316_HUMAN	ZNF316	physical	22939629
TRI10_HUMAN	TRIM10	physical	25416956
GLRX3_HUMAN	GLRX3	physical	25416956
GORS2_HUMAN	GORASP2	physical	25416956
NTM2F_HUMAN	NUTM2F	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
DEUP1_HUMAN	CCDC67	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 ZN148_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-607, AND MASS SPECTROMETRY.	19608861 [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-306; SER-412 ANDSER-784, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-784, 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 THR-194; SER-250; SER-306;SER-412 AND SER-784, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-412, ANDMASS SPECTROMETRY.	15302935 [Abstract]