ZN175_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN175_HUMAN
• UniProt AC: Q9Y473
• Protein Name: Zinc finger protein 175
• Gene Name: ZNF175
• Organism: Homo sapiens (Human).
• Sequence Length: 711
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Down-regulates the expression of several chemokine receptors. Interferes with HIV-1 replication by suppressing Tat-induced viral LTR promoter activity..
• Protein Sequence: MPADVNLSQKPQVLGPEKQDGSCEASVSFEDVTVDFSREEWQQLDPAQRCLYRDVMLELYSHLFAVGYHIPNPEVIFRMLKEKEPRVEEAEVSHQRCQEREFGLEIPQKEISKKASFQKDMVGEFTRDGSWCSILEELRLDADRTKKDEQNQIQPMSHSAFFNKKTLNTESNCEYKDPGKMIRTRPHLASSQKQPQKCCLFTESLKLNLEVNGQNESNDTEQLDDVVGSGQLFSHSSSDACSKNIHTGETFCKGNQCRKVCGHKQSLKQHQIHTQKKPDGCSECGGSFTQKSHLFAQQRIHSVGNLHECGKCGKAFMPQLKLSVYLTDHTGDIPCICKECGKVFIQRSELLTHQKTHTRKKPYKCHDCGKAFFQMLSLFRHQRTHSREKLYECSECGKGFSQNSTLIIHQKIHTGERQYACSECGKAFTQKSTLSLHQRIHSGQKSYVCIECGQAFIQKAHLIVHQRSHTGEKPYQCHNCGKSFISKSQLDIHHRIHTGEKPYECSDCGKTFTQKSHLNIHQKIHTGERHHVCSECGKAFNQKSILSMHQRIHTGEKPYKCSECGKAFTSKSQFKEHQRIHTGEKPYVCTECGKAFNGRSNFHKHQITHTRERPFVCYKCGKAFVQKSELITHQRTHMGEKPYECLDCGKSFSKKPQLKVHQRIHTGERPYVCSECGKAFNNRSNFNKHQTTHTRDKSYKCSYSVKGFTKQ

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
112	Phosphorylation	EIPQKEISKKASFQK CCCHHHHHHHHCCCC	29.24	-
130	Phosphorylation	GEFTRDGSWCSILEE EEECCCCCCHHHHHH	29.24	-
175	Phosphorylation	NTESNCEYKDPGKMI CCCCCCCCCCCCCEE	23.92	22817900
253	Ubiquitination	HTGETFCKGNQCRKV CCCCCCCCCCHHHHH	57.62	29967540
274	Phosphorylation	LKQHQIHTQKKPDGC HHHHCCCCCCCCCCC	43.65	30622161
302	Phosphorylation	FAQQRIHSVGNLHEC HHHHHHHCCCCHHHC	29.37	-
348	O-linked_Glycosylation	GKVFIQRSELLTHQK CCEEEEHHHHHHCCC	19.07	30379171
377	Phosphorylation	KAFFQMLSLFRHQRT HHHHHHHHHHHHCCC	21.81	24719451
498	Phosphorylation	DIHHRIHTGEKPYEC EECCCCCCCCCCEEC	44.67	27282143
501	Ubiquitination	HRIHTGEKPYECSDC CCCCCCCCCEECCCC	55.00	-
523	Ubiquitination	SHLNIHQKIHTGERH HHCCHHHHCCCCCCC	23.46	29967540
554	Phosphorylation	SMHQRIHTGEKPYKC HHHHHHHCCCCCEEC	44.67	29496963
562	Phosphorylation	GEKPYKCSECGKAFT CCCCEECCCCCCCCC	31.59	-
569	Phosphorylation	SECGKAFTSKSQFKE CCCCCCCCCHHHHHH	39.85	-
570	Phosphorylation	ECGKAFTSKSQFKEH CCCCCCCCHHHHHHH	24.69	-
572	Phosphorylation	GKAFTSKSQFKEHQR CCCCCCHHHHHHHCC	40.39	-
582	Phosphorylation	KEHQRIHTGEKPYVC HHHCCCCCCCCCEEE	44.67	28111955
585	Sumoylation	QRIHTGEKPYVCTEC CCCCCCCCCEEECCC	42.89	-
585	Sumoylation	QRIHTGEKPYVCTEC CCCCCCCCCEEECCC	42.89	-
594	Ubiquitination	YVCTECGKAFNGRSN EEECCCCCCCCCCCC	62.56	-
651	Phosphorylation	ECLDCGKSFSKKPQL EEECCCCCCCCCCCC	21.75	24719451
698	Phosphorylation	TTHTRDKSYKCSYSV CCCCCCCCCEEEEEE	33.83	23532336

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

Oops, there are no upstream regulatory protein records of ZN175_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN175_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 ZN175_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LZTR1_HUMAN	LZTR1	physical	20211142
PPIP1_HUMAN	PSTPIP1	physical	25416956
ZN264_HUMAN	ZNF264	physical	25416956
ZN250_HUMAN	ZNF250	physical	25416956
KR107_HUMAN	KRTAP10-7	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.