dbPTM

ZN101_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN101_HUMAN
UniProt AC	Q8IZC7
Protein Name	Zinc finger protein 101
Gene Name	ZNF101
Organism	Homo sapiens (Human).
Sequence Length	436
Subcellular Localization	Nucleus .
Protein Description	May be involved in transcriptional regulation..
Protein Sequence	MDSVAFEDVAVNFTQEEWALLSPSQKNLYRDVTLETFRNLASVGIQWKDQDIENLYQNLGIKLRSLVERLCGRKEGNEHRETFSQIPDCHLNKKSQTGVKPCKCSVCGKVFLRHSFLDRHMRAHAGHKRSECGGEWRETPRKQKQHGKASISPSSGARRTVTPTRKRPYECKVCGKAFNSPNLFQIHQRTHTGKRSYKCREIVRAFTVSSFFRKHGKMHTGEKRYECKYCGKPIDYPSLFQIHVRTHTGEKPYKCKQCGKAFISAGYLRTHEIRSHALEKSHQCQECGKKLSCSSSLHRHERTHSGGKLYECQKCAKVFRCPTSLQAHERAHTGERPYECNKCGKTFNYPSCFRRHKKTHSGEKPYECTRCGKAFGWCSSLRRHEMTHTGEKPFDCKQCGKVFTFSNYLRLHERTHLAGRSQCFGRRQGDHLSPGV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	EDVAVNFTQEEWALL CCEEECCCHHHHHHC	29.84	-
62	Ubiquitination	LYQNLGIKLRSLVER HHHHHCHHHHHHHHH	35.73	29967540
93	Ubiquitination	IPDCHLNKKSQTGVK CCCCCCCCCCCCCCC	61.23	29967540
103	Acetylation	QTGVKPCKCSVCGKV CCCCCCCEECCCCEE	37.76	7663053
115	Phosphorylation	GKVFLRHSFLDRHMR CEEEHHHHHHHHHHH	22.52	27067055
139	Phosphorylation	CGGEWRETPRKQKQH CCCCCCCCCCHHHHC	21.59	-
150	Phosphorylation	QKQHGKASISPSSGA HHHCCCCCCCCCCCC	27.38	26552605
152	Phosphorylation	QHGKASISPSSGARR HCCCCCCCCCCCCCC	19.08	25849741
154	Phosphorylation	GKASISPSSGARRTV CCCCCCCCCCCCCCC	34.31	26552605
155	Phosphorylation	KASISPSSGARRTVT CCCCCCCCCCCCCCC	39.60	26552605
160	Phosphorylation	PSSGARRTVTPTRKR CCCCCCCCCCCCCCC	24.15	26552605
162	Phosphorylation	SGARRTVTPTRKRPY CCCCCCCCCCCCCCE	20.52	26552605
164	Phosphorylation	ARRTVTPTRKRPYEC CCCCCCCCCCCCEEE	39.18	26552605
170	Ubiquitination	PTRKRPYECKVCGKA CCCCCCEEEEECCCC	30.46	29967540
180	Phosphorylation	VCGKAFNSPNLFQIH ECCCCCCCCCCEEEE	14.54	25159151
188	Ubiquitination	PNLFQIHQRTHTGKR CCCEEEECCCCCCCC	54.30	29967540
210	Phosphorylation	VRAFTVSSFFRKHGK HHHHCHHHHHHHHCC	24.86	24719451
246	Phosphorylation	LFQIHVRTHTGEKPY CEEEEEECCCCCCCE	23.77	28348404
248	Phosphorylation	QIHVRTHTGEKPYKC EEEEECCCCCCCEEC	46.56	26270265
251	Ubiquitination	VRTHTGEKPYKCKQC EECCCCCCCEECCCC	55.80	-
253	Phosphorylation	THTGEKPYKCKQCGK CCCCCCCEECCCCCC	39.83	-
264	Phosphorylation	QCGKAFISAGYLRTH CCCCEEHHHHHCHHH	14.80	26552605
267	Phosphorylation	KAFISAGYLRTHEIR CEEHHHHHCHHHHHH	7.85	26552605
290	Ubiquitination	QCQECGKKLSCSSSL CHHHHCCEECCCHHC	30.80	29967540
308	Ubiquitination	ERTHSGGKLYECQKC CCCCCCCCEEEECHH	51.96	29967540
314	Ubiquitination	GKLYECQKCAKVFRC CCEEEECHHHEEEEC	48.06	-
433	Phosphorylation	RRQGDHLSPGV---- CCCCCCCCCCC----	19.05	21857030

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 ZN101_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN101_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 ZN101_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
K1C40_HUMAN	KRT40	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR101_HUMAN	KRTAP10-1	physical	25416956
KR103_HUMAN	KRTAP10-3	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 ZN101_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-433, AND MASSSPECTROMETRY.	17081983 [Abstract]