dbPTM

ZBT38_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZBT38_HUMAN
UniProt AC	Q8NAP3
Protein Name	Zinc finger and BTB domain-containing protein 38
Gene Name	ZBTB38 {ECO:0000312\|HGNC:HGNC:26636}
Organism	Homo sapiens (Human).
Sequence Length	1195
Subcellular Localization	Nucleus . Chromosome . Localizes to chromocenters.
Protein Description	Transcriptional regulator with bimodal DNA-binding specificity. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to E-box elements (5'-CACGTG-3'). Can also bind specifically to a single methyl-CpG pair. Represses transcription in a methyl-CpG-dependent manner. [PubMed: 16354688 Plays an important role in regulating DNA replication and common fragile sites (CFS) stability in a RBBP6- and MCM10-dependent manner; represses expression of MCM10 which plays an important role in DNA-replication]
Protein Sequence	MTVMSLSRDLKDDFHSDTVLSILNEQRIRGILCDVTIIVEDTKFKAHSNVLAASSLYFKNIFWSHTICISSHVLELDDLKAEVFTEILNYIYSSTVVVKRQETVTDLAAAGKKLGISFLEDLTDRNFSNSPGPYVFCITEKGVVKEEKNEKRHEEPAITNGPRITNAFSIIETENSNNMFSPLDLRASFKKVSDSMRTASLCLERTDVCHEAEPVRTLAEHSYAVSSVAEAYRSQPVREHDGSSPGNTGKENCEALAAKPKTCRKPKTFSIPQDSDSATENIPPPPVSNLEVNQERSPQPAAVLTRSKSPNNEGDVHFSREDENQSSDVPGPPAAEVPPLVYNCSCCSKAFDSSTLLSAHMQLHKPTQEPLVCKYCNKQFTTLNRLDRHEQICMRSSHMPIPGGNQRFLENYPTIGQNGGSFTGPEPLLSENRIGEFSSTGSTLPDTDHMVKFVNGQMLYSCVVCKRSYVTLSSLRRHANVHSWRRTYPCHYCNKVFALAEYRTRHEIWHTGERRYQCIFCLETFMTYYILKNHQKSFHAIDHRLSISKKTANGGLKPSVYPYKLYRLLPMKCKRAPYKSYRNSSYENARENSQMNESAPGTYVVQNPHSSELPTLNFQDTVNTLTNSPAIPLETSACQDIPTSANVQNAEGTKWGEEALKMDLDNNFYSTEVSVSSTENAVSSDLRAGDVPVLSLSNSSENAASVISYSGSAPSVIVHSSQFSSVIMHSNAIAAMTSSNHRAFSDPAVSQSLKDDSKPEPDKVGRFASRPKSIKEKKKTTSHTRGEIPEESNYVADPGGSLSKTTNIAEETSKIETYIAKPALPGTSTNSNVAPLCQITVKIGNEAIVKRHILGSKLFYKRGRRPKYQMQEEPLPQGNDPEPSGDSPLGLCQSECMEMSEVFDDASDQDSTDKPWRPYYNYKPKKKSRQLKKMRKVNWRKEHGNRSPSHKCKYPAELDCAVGKAPQDKPFEEEETKEMPKLQCELCDGDKAVGAGNQGRPHRHLTSRPYACELCAKQFQSPSTLKMHMRCHTGEKPYQCKTCGRCFSVQGNLQKHERIHLGLKEFVCQYCNKAFTLNETLKIHERIHTGEKRYHCQFCFQRFLYLSTKRNHEQRHIREHNGKGYACFQCPKICKTAAALGMHQKKHLFKSPSQQEKIGDVCHENSNPLENQHFIGSEDNDQKDNIQTGVENVVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Phosphorylation	RGILCDVTIIVEDTK CCEECEEEEEECCCC	7.55	21955146
42	Phosphorylation	VTIIVEDTKFKAHSN EEEEECCCCCCCCCC	25.52	21955146
43	Sumoylation	TIIVEDTKFKAHSNV EEEECCCCCCCCCCH	58.13	-
43	Ubiquitination	TIIVEDTKFKAHSNV EEEECCCCCCCCCCH	58.13	-
43	Sumoylation	TIIVEDTKFKAHSNV EEEECCCCCCCCCCH	58.13	28112733
85	Phosphorylation	DLKAEVFTEILNYIY HHHHHHHHHHHHHHH	27.56	27762562
90	Phosphorylation	VFTEILNYIYSSTVV HHHHHHHHHHCCEEE	9.59	27067055
92	Phosphorylation	TEILNYIYSSTVVVK HHHHHHHHCCEEEEE	6.04	27762562
93	Phosphorylation	EILNYIYSSTVVVKR HHHHHHHCCEEEEEE	15.24	27067055
112	Ubiquitination	TDLAAAGKKLGISFL HHHHHHHHHHCCCHH	39.85	21906983
113	Ubiquitination	DLAAAGKKLGISFLE HHHHHHHHHCCCHHH	51.53	-
128	Phosphorylation	DLTDRNFSNSPGPYV HHCCCCCCCCCCCEE	39.69	30266825
130	Phosphorylation	TDRNFSNSPGPYVFC CCCCCCCCCCCEEEE	30.00	25463755
134	Phosphorylation	FSNSPGPYVFCITEK CCCCCCCEEEEEECC	16.45	21712546
145	Sumoylation	ITEKGVVKEEKNEKR EECCCCCCHHHCCCC	58.72	-
145	Sumoylation	ITEKGVVKEEKNEKR EECCCCCCHHHCCCC	58.72	25218447
148	Sumoylation	KGVVKEEKNEKRHEE CCCCCHHHCCCCCCC	72.06	28112733
151	Sumoylation	VKEEKNEKRHEEPAI CCHHHCCCCCCCCCC	69.33	28112733
165	Phosphorylation	ITNGPRITNAFSIIE CCCCCCCCCEEEEEE	23.05	-
169	Phosphorylation	PRITNAFSIIETENS CCCCCEEEEEECCCC	21.90	-
173	Phosphorylation	NAFSIIETENSNNMF CEEEEEECCCCCCCC	30.02	-
181	Phosphorylation	ENSNNMFSPLDLRAS CCCCCCCCCHHHHHH	17.49	22817900
188	Phosphorylation	SPLDLRASFKKVSDS CCHHHHHHHHHHHHH	31.03	24719451
193	Phosphorylation	RASFKKVSDSMRTAS HHHHHHHHHHHHHHH	32.61	21601212
195	Phosphorylation	SFKKVSDSMRTASLC HHHHHHHHHHHHHHH	11.58	23312004
198	Phosphorylation	KVSDSMRTASLCLER HHHHHHHHHHHHHHC	16.38	23312004
200	Phosphorylation	SDSMRTASLCLERTD HHHHHHHHHHHHCCC	20.99	29116813
223	Phosphorylation	RTLAEHSYAVSSVAE HHHHHHHHHHHHHHH	16.96	28555341
234	Phosphorylation	SVAEAYRSQPVREHD HHHHHHHCCCCCCCC	26.59	23403867
243	Phosphorylation	PVREHDGSSPGNTGK CCCCCCCCCCCCCCH	39.14	23401153
244	Phosphorylation	VREHDGSSPGNTGKE CCCCCCCCCCCCCHH	42.21	30266825
248	Phosphorylation	DGSSPGNTGKENCEA CCCCCCCCCHHHHHH	56.39	30266825
259	Sumoylation	NCEALAAKPKTCRKP HHHHHHCCCCCCCCC	41.25	28112733
268	Phosphorylation	KTCRKPKTFSIPQDS CCCCCCCCCCCCCCC	31.01	25002506
270	Phosphorylation	CRKPKTFSIPQDSDS CCCCCCCCCCCCCCC	38.29	25002506
275	Phosphorylation	TFSIPQDSDSATENI CCCCCCCCCCCCCCC	28.37	25002506
277	Phosphorylation	SIPQDSDSATENIPP CCCCCCCCCCCCCCC	40.83	25002506
279	Phosphorylation	PQDSDSATENIPPPP CCCCCCCCCCCCCCC	33.25	25002506
288	Phosphorylation	NIPPPPVSNLEVNQE CCCCCCCCCCEECCC	41.28	25002506
297	Phosphorylation	LEVNQERSPQPAAVL CEECCCCCCCCCEEE	27.43	30266825
305	Phosphorylation	PQPAAVLTRSKSPNN CCCCEEEECCCCCCC	26.71	25002506
307	Phosphorylation	PAAVLTRSKSPNNEG CCEEEECCCCCCCCC	32.05	25463755
309	Phosphorylation	AVLTRSKSPNNEGDV EEEECCCCCCCCCCC	33.82	25463755
319	O-linked_Glycosylation	NEGDVHFSREDENQS CCCCCCCCCCCCCCC	21.63	30379171
319	Phosphorylation	NEGDVHFSREDENQS CCCCCCCCCCCCCCC	21.63	23927012
326	Phosphorylation	SREDENQSSDVPGPP CCCCCCCCCCCCCCC	39.84	25002506
327	Phosphorylation	REDENQSSDVPGPPA CCCCCCCCCCCCCCH	32.63	25002506
342	Phosphorylation	AEVPPLVYNCSCCSK HHCCCEEEECCCCCC	20.38	25002506
345	Phosphorylation	PPLVYNCSCCSKAFD CCEEEECCCCCCCCC	17.96	25002506
348	Phosphorylation	VYNCSCCSKAFDSST EEECCCCCCCCCHHH	31.20	25002506
396	Phosphorylation	HEQICMRSSHMPIPG HCHHHHHCCCCCCCC	9.56	28555341
397	Phosphorylation	EQICMRSSHMPIPGG CHHHHHCCCCCCCCC	17.28	28555341
421	Phosphorylation	TIGQNGGSFTGPEPL CCCCCCCCCCCCCCC	22.49	28555341
468	Phosphorylation	SCVVCKRSYVTLSSL EEEEECCCEEEHHHH	14.95	20860994
471	Phosphorylation	VCKRSYVTLSSLRRH EECCCEEEHHHHHHH	16.82	20860994
473	Phosphorylation	KRSYVTLSSLRRHAN CCCEEEHHHHHHHCC	20.26	22817900
474	Phosphorylation	RSYVTLSSLRRHANV CCEEEHHHHHHHCCC	29.07	25954137
546	Phosphorylation	HAIDHRLSISKKTAN HHHCCCEECCCCCCC	25.44	29496963
548	Phosphorylation	IDHRLSISKKTANGG HCCCEECCCCCCCCC	25.40	26699800
550	Sumoylation	HRLSISKKTANGGLK CCEECCCCCCCCCCC	46.19	28112733
557	Sumoylation	KTANGGLKPSVYPYK CCCCCCCCCCCCCHH	38.22	-
557	Sumoylation	KTANGGLKPSVYPYK CCCCCCCCCCCCCHH	38.22	28112733
584	Phosphorylation	PYKSYRNSSYENARE CCHHHCCCCHHHHHH	25.87	28555341
745	Phosphorylation	SSNHRAFSDPAVSQS CCCCCCCCCHHHHHH	41.52	28555341
754	Sumoylation	PAVSQSLKDDSKPEP HHHHHHCCCCCCCCC	65.81	28112733
758	Sumoylation	QSLKDDSKPEPDKVG HHCCCCCCCCCCCCH	61.47	-
758	Sumoylation	QSLKDDSKPEPDKVG HHCCCCCCCCCCCCH	61.47	28112733
763	Sumoylation	DSKPEPDKVGRFASR CCCCCCCCCHHHCCC	58.25	28112733
769	Phosphorylation	DKVGRFASRPKSIKE CCCHHHCCCCCCHHH	46.53	24719451
773	Phosphorylation	RFASRPKSIKEKKKT HHCCCCCCHHHHCCC	41.39	24719451
781	Phosphorylation	IKEKKKTTSHTRGEI HHHHCCCCCCCCCCC	27.65	28555341
782	Phosphorylation	KEKKKTTSHTRGEIP HHHCCCCCCCCCCCC	28.26	30576142
784	Phosphorylation	KKKTTSHTRGEIPEE HCCCCCCCCCCCCCH	39.89	-
792	Phosphorylation	RGEIPEESNYVADPG CCCCCCHHCCCCCCC	31.62	-
801	Phosphorylation	YVADPGGSLSKTTNI CCCCCCCCCCCCCCH	35.07	30108239
803	Phosphorylation	ADPGGSLSKTTNIAE CCCCCCCCCCCCHHH	29.65	30108239
804	Ubiquitination	DPGGSLSKTTNIAEE CCCCCCCCCCCHHHH	65.74	2190698
804	Sumoylation	DPGGSLSKTTNIAEE CCCCCCCCCCCHHHH	65.74	28112733
812	Phosphorylation	TTNIAEETSKIETYI CCCHHHHHCCCEEEE	27.16	30576142
813	Phosphorylation	TNIAEETSKIETYIA CCHHHHHCCCEEEEC	34.61	30576142
814	Sumoylation	NIAEETSKIETYIAK CHHHHHCCCEEEECC	52.56	-
814	Sumoylation	NIAEETSKIETYIAK CHHHHHCCCEEEECC	52.56	28112733
814	Ubiquitination	NIAEETSKIETYIAK CHHHHHCCCEEEECC	52.56	-
821	Ubiquitination	KIETYIAKPALPGTS CCEEEECCCCCCCCC	22.67	-
821	Sumoylation	KIETYIAKPALPGTS CCEEEECCCCCCCCC	22.67	28112733
842	Sumoylation	PLCQITVKIGNEAIV CCEEEEEEECCCHHH	35.92	28112733
850	Acetylation	IGNEAIVKRHILGSK ECCCHHHHHHHHCCH	31.95	18585939
850	Ubiquitination	IGNEAIVKRHILGSK ECCCHHHHHHHHCCH	31.95	-
850	Sumoylation	IGNEAIVKRHILGSK ECCCHHHHHHHHCCH	31.95	28112733
857	Acetylation	KRHILGSKLFYKRGR HHHHHCCHHHHCCCC	40.60	18585947
857	Sumoylation	KRHILGSKLFYKRGR HHHHHCCHHHHCCCC	40.60	28112733
923	Acetylation	WRPYYNYKPKKKSRQ CCCCCCCCCCHHHHH	46.88	9854545
923	Sumoylation	WRPYYNYKPKKKSRQ CCCCCCCCCCHHHHH	46.88	28112733
947	Phosphorylation	RKEHGNRSPSHKCKY HHHCCCCCCCCCCCC	34.45	29514088
949	Phosphorylation	EHGNRSPSHKCKYPA HCCCCCCCCCCCCCH	36.50	29514088
964	Ubiquitination	ELDCAVGKAPQDKPF HCCCCCCCCCCCCCC	50.74	-
964	Sumoylation	ELDCAVGKAPQDKPF HCCCCCCCCCCCCCC	50.74	28112733
969	Sumoylation	VGKAPQDKPFEEEET CCCCCCCCCCCHHHH	46.49	28112733
977	Sumoylation	PFEEEETKEMPKLQC CCCHHHHHCCCCCEE	56.12	-
977	Sumoylation	PFEEEETKEMPKLQC CCCHHHHHCCCCCEE	56.12	28112733
981	Sumoylation	EETKEMPKLQCELCD HHHHCCCCCEEEECC	50.29	28112733
991	Sumoylation	CELCDGDKAVGAGNQ EEECCCCCCCCCCCC	50.96	28112733
1017	Sumoylation	YACELCAKQFQSPST HHHHHHHHHCCCCCC	51.12	28112733
1021	Phosphorylation	LCAKQFQSPSTLKMH HHHHHCCCCCCEEEE	23.31	22199227
1023	Phosphorylation	AKQFQSPSTLKMHMR HHHCCCCCCEEEEEE	52.17	22199227
1026	Sumoylation	FQSPSTLKMHMRCHT CCCCCCEEEEEECCC	27.18	28112733
1082	Methylation	FTLNETLKIHERIHT EECCCCEEECCCHHC	49.81	23644510
1107	Phosphorylation	FQRFLYLSTKRNHEQ HHHHHHHHCCCCHHH	20.51	28555341
1109	Sumoylation	RFLYLSTKRNHEQRH HHHHHHCCCCHHHHH	48.07	28112733
1132	Sumoylation	YACFQCPKICKTAAA EECCCCHHHHHHHHH	69.25	28112733
1135	Sumoylation	FQCPKICKTAAALGM CCCHHHHHHHHHCCC	44.67	-
1135	Sumoylation	FQCPKICKTAAALGM CCCHHHHHHHHHCCC	44.67	28112733
1145	Ubiquitination	AALGMHQKKHLFKSP HHCCCHHHHHHCCCH	27.73	-
1150	Ubiquitination	HQKKHLFKSPSQQEK HHHHHHCCCHHHHHH	68.75	-
1150	Sumoylation	HQKKHLFKSPSQQEK HHHHHHCCCHHHHHH	68.75	28112733
1151	Phosphorylation	QKKHLFKSPSQQEKI HHHHHCCCHHHHHHH	23.58	23403867
1153	Phosphorylation	KHLFKSPSQQEKIGD HHHCCCHHHHHHHHH	52.14	23403867
1157	Ubiquitination	KSPSQQEKIGDVCHE CCHHHHHHHHHHCCC	47.88	-
1166	Phosphorylation	GDVCHENSNPLENQH HHHCCCCCCCCCCCC	36.52	30108239
1177	Phosphorylation	ENQHFIGSEDNDQKD CCCCCCCCCCCCCCC	36.64	30108239
1183	Sumoylation	GSEDNDQKDNIQTGV CCCCCCCCCCCCCCC	56.45	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
-	K	Ubiquitination	E3 ubiquitin ligase	RBBP6	Q7Z6E9	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	ICP0	P08393	PMID:32416261

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZBT38_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 ZBT38_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
RL26L_HUMAN	RPL26L1	physical	26186194
YTDC2_HUMAN	YTHDC2	physical	26186194
POP1_HUMAN	POP1	physical	26186194
DDX24_HUMAN	DDX24	physical	26186194
IPO7_HUMAN	IPO7	physical	26186194
SRPK1_HUMAN	SRPK1	physical	26186194
PTCD3_HUMAN	PTCD3	physical	26186194
STAU1_HUMAN	STAU1	physical	26186194
IF2P_HUMAN	EIF5B	physical	26186194
MBB1A_HUMAN	MYBBP1A	physical	26186194
TCOF_HUMAN	TCOF1	physical	26186194
TRI26_HUMAN	TRIM26	physical	26186194
RSBNL_HUMAN	RSBN1L	physical	26186194
RSBN1_HUMAN	RSBN1	physical	26186194
SIR1_HUMAN	SIRT1	physical	26186194
NO40_HUMAN	ZCCHC17	physical	26186194
NOC2L_HUMAN	NOC2L	physical	26186194
RT05_HUMAN	MRPS5	physical	26186194
RT35_HUMAN	MRPS35	physical	26186194
ELAV2_HUMAN	ELAVL2	physical	26186194
DDX18_HUMAN	DDX18	physical	26186194
RL15_HUMAN	RPL15	physical	26186194
DHX36_HUMAN	DHX36	physical	26186194
SPT2_HUMAN	SPTY2D1	physical	26186194
SDA1_HUMAN	SDAD1	physical	26186194
LLR1_HUMAN	LRR1	physical	26186194
H2A2B_HUMAN	HIST2H2AB	physical	26186194
ZN689_HUMAN	ZNF689	physical	26186194
SIR1_HUMAN	SIRT1	physical	28514442
LLR1_HUMAN	LRR1	physical	28514442
TRI26_HUMAN	TRIM26	physical	28514442
IPO7_HUMAN	IPO7	physical	28514442
NO40_HUMAN	ZCCHC17	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
RT35_HUMAN	MRPS35	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
YTDC2_HUMAN	YTHDC2	physical	28514442
ZN689_HUMAN	ZNF689	physical	28514442
SDA1_HUMAN	SDAD1	physical	28514442
IF2P_HUMAN	EIF5B	physical	28514442
DHX36_HUMAN	DHX36	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
RBBP6_HUMAN	RBBP6	physical	24726359

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 ZBT38_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-181, AND MASSSPECTROMETRY.	19690332 [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, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-309, ANDMASS SPECTROMETRY.	17081983 [Abstract]