ZN628_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN628_HUMAN
• UniProt AC: Q5EBL2
• Protein Name: Zinc finger protein 628
• Gene Name: ZNF628
• Organism: Homo sapiens (Human).
• Sequence Length: 1059
• Subcellular Localization: Nucleus.
• Protein Description: Transcription activator. Binds DNA on GT-box consensus sequence 5'-TTGGTT-3' (By similarity)..
• Protein Sequence: MSGVMVGSHADMAPASTAEGAGEKPGPAAPAPAAQYECGECGKSFRWSSRLLHHQRTHTGERPYKCPDCPKAFKGSSALLYHQRGHTGERPYQCPDCPKAFKRSSLLQIHRSVHTGLRAFICGQCGLAFKWSSHYQYHLRQHTGERPYPCPDCPKAFKNSSSLRRHRHVHTGERPYTCGVCGKSFTQSTNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHQRTHGAAPAPGTASAAPPPQSREPGKVFVCDAYLQRHLQPHSPPAPPAPPPPPPPVVPELFLAAAETTVELVYRCDGCEQGFSSEELLLEHQPCPGPDAAPQPQEAPAEAPKADQPPSPLPQPPPPAAAPAPGFACLPCGKSFRTVAGLSRHQHSHGAAGGQAFRCGSCDGSFPQLASLLAHQQCHVEEAAAGRPPPQAEAAEVTCPQEPLAPAAPVPPPPPSAPASAERPYKCAECGKSFKGSSGLRYHLRDHTGERPYQCGECGKAFKRSSLLAIHQRVHTGLRAFTCGQCGLTFKWSSHYQYHLRLHSGERPYACGECGKAFRNTSCLRRHRHVHTGERPHACGVCGKSFAQTSNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHQRTHSAERPFTCPICGRGFVMAAYLQRHLRTHAPANTPPSTTAPAAGPQPPAPLAAARAPPATQDVHVLPHLQATLSLEVAGGTAQAPSLGPAAPNSQTFLLVQTAQGLQLIPSSVQPPTPPPPPAPPKLILLPSSSAGAGGGRARQGPRAVGKAGQGAGVVWLPGPGGLGVQGAASAGASGTGQSLIVLQNVGGGEAGPQEMSGVQLQPLRPAPEVTTVQLQPAQEVTTVQLQPAQEVTTVQLQPAQEVTTVQLQPVAGQLSNSSGGAVATEAPNLLVVQSGAAEELLTGPGPGEAGDGEASTGVVQDVLFETLQTDEGLQSVLVLSGADGEQTRLCVQEVETLPPGLTEPPATGPPGQKLLIIRSAPATELLDSSNTGGGTATLQLLAPPPSGPASGPAGLPGAPASQMVQVVPAGAGPGVMTPQGLPSIQIVQTLPAVQLVHTF

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
2	Phosphorylation	------MSGVMVGSH ------CCCCCCCCC	18.74	22210691
8	Phosphorylation	MSGVMVGSHADMAPA CCCCCCCCCCCCCCC	5.09	22210691
16	Phosphorylation	HADMAPASTAEGAGE CCCCCCCCCCCCCCC	36.10	22210691
17	Phosphorylation	ADMAPASTAEGAGEK CCCCCCCCCCCCCCC	17.93	22210691
59	Phosphorylation	LHHQRTHTGERPYKC HCCCCCCCCCCCCCC	28.74	27134283
64	Phosphorylation	THTGERPYKCPDCPK CCCCCCCCCCCCCCC	71.47	27134283
87	Phosphorylation	LYHQRGHTGERPYQC EEECCCCCCCCCCCC	21.17	21857030
105	Phosphorylation	PKAFKRSSLLQIHRS CHHHCCCHHHHHHHH	2.69	28555341
143	Phosphorylation	QYHLRQHTGERPYPC HHHHHHHCCCCCCCC	32.87	28555341
160	Phosphorylation	CPKAFKNSSSLRRHR CCHHHCCCHHHCCCC	34.02	26699800
161	Phosphorylation	PKAFKNSSSLRRHRH CHHHCCCHHHCCCCC	36.16	26699800
171	Phosphorylation	RRHRHVHTGERPYTC CCCCCCCCCCCCCCC	25.20	-
184	Phosphorylation	TCGVCGKSFTQSTNL CCCCCCCCCCCCCCC	19.06	23403867
186	Phosphorylation	GVCGKSFTQSTNLRQ CCCCCCCCCCCCCCC	38.17	23403867
199	Phosphorylation	RQHQRVHTGERPFRC CCCCCCCCCCCCCCC	19.41	23186163
234	Phosphorylation	GAAPAPGTASAAPPP CCCCCCCCCCCCCCC	18.03	29978859
236	Phosphorylation	APAPGTASAAPPPQS CCCCCCCCCCCCCCC	34.53	29978859
243	Phosphorylation	SAAPPPQSREPGKVF CCCCCCCCCCCCCEE	33.72	29978859
264	Phosphorylation	QRHLQPHSPPAPPAP HHHCCCCCCCCCCCC	31.21	29523821
340	Phosphorylation	PKADQPPSPLPQPPP CCCCCCCCCCCCCCC	71.47	25850435
495	Phosphorylation	GKAFKRSSLLAIHQR HHHHHHHHHHHHHHH	2.61	28555341
533	Phosphorylation	QYHLRLHSGERPYAC EEEEEEECCCCCCCC	19.44	-
561	Phosphorylation	RRHRHVHTGERPHAC HHCCCCCCCCCCCCC	18.35	-
589	Phosphorylation	RQHQRVHTGERPFRC HHHCCCCCCCCCCCC	19.41	23186163
747	Phosphorylation	PKLILLPSSSAGAGG CCEEEEECCCCCCCC	27.05	27251275
748	Phosphorylation	KLILLPSSSAGAGGG CEEEEECCCCCCCCC	17.11	27251275
749	Phosphorylation	LILLPSSSAGAGGGR EEEEECCCCCCCCCC	37.86	27251275

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

Oops, there are no upstream regulatory protein records of ZN628_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN628_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 ZN628_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ZN628_HUMAN !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.