dbPTM

ZN169_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN169_HUMAN
UniProt AC	Q14929
Protein Name	Zinc finger protein 169
Gene Name	ZNF169
Organism	Homo sapiens (Human).
Sequence Length	603
Subcellular Localization	Nucleus .
Protein Description	May be involved in transcriptional regulation..
Protein Sequence	MSPGLLTTRKEALMAFRDVAVAFTQKEWKLLSSAQRTLYREVMLENYSHLVSLGIAFSKPKLIEQLEQGDEPWREENEHLLDLCPEPRTEFQPSFPHLVAFSSSQLLRQYALSGHPTQIFPSSSAGGDFQLEAPRCSSEKGESGETEGPDSSLRKRPSRISRTFFSPHQGDPVEWVEGNREGGTDLRLAQRMSLGGSDTMLKGADTSESGAVIRGNYRLGLSKKSSLFSHQKHHVCPECGRGFCQRSDLIKHQRTHTGEKPYLCPECGRRFSQKASLSIHQRKHSGEKPYVCRECGRHFRYTSSLTNHKRIHSGERPFVCQECGRGFRQKIALLLHQRTHLEEKPFVCPECGRGFCQKASLLQHQSSHTGERPFLCLECGRSFRQQSLLLSHQVTHSGEKPYVCAECGHSFRQKVTLIRHQRTHTGEKPYLCPQCGRGFSQKVTLIGHQRTHTGEKPYLCPDCGRGFGQKVTLIRHQRTHTGEKPYLCPKCGRAFGFKSLLTRHQRTHSEEELYVDRVCGQGLGQKSHLISDQRTHSGEKPCICDECGRGFGFKSALIRHQRTHSGEKPYVCRECGRGFSQKSHLHRHRRTKSGHQLLPQEVF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Phosphorylation	RDVAVAFTQKEWKLL HHHHHHHHHHHHHHH	29.06	19664995
58	Phosphorylation	VSLGIAFSKPKLIEQ HHHHHCCCCHHHHHH	38.74	24719451
145	Phosphorylation	SEKGESGETEGPDSS CCCCCCCCCCCCCCH	53.62	17081983
158	Phosphorylation	SSLRKRPSRISRTFF CHHHCCCCCEECCCC	46.40	22817900
166	Phosphorylation	RISRTFFSPHQGDPV CEECCCCCCCCCCCE	19.79	24719451
197	Phosphorylation	QRMSLGGSDTMLKGA HHHHCCCCCCCCCCC	28.27	23312004
199	Phosphorylation	MSLGGSDTMLKGADT HHCCCCCCCCCCCCC	26.54	23312004
217	Phosphorylation	GAVIRGNYRLGLSKK CCEEECCEEECCCCC	15.27	29759185
255	Phosphorylation	DLIKHQRTHTGEKPY HHHHCCCCCCCCCCE	19.74	-
257	Phosphorylation	IKHQRTHTGEKPYLC HHCCCCCCCCCCEEC	46.56	-
262	Phosphorylation	THTGEKPYLCPECGR CCCCCCCEECCCCCC	31.81	-
416	Phosphorylation	HSFRQKVTLIRHQRT CCHHHHHEEEEECCC	24.41	-
423	Phosphorylation	TLIRHQRTHTGEKPY EEEEECCCCCCCCCE	19.74	-
425	Phosphorylation	IRHQRTHTGEKPYLC EEECCCCCCCCCEEC	46.56	-
451	Phosphorylation	TLIGHQRTHTGEKPY EEEEECCCCCCCCCE	19.74	-
453	Phosphorylation	IGHQRTHTGEKPYLC EEECCCCCCCCCEEC	46.56	-
472	Phosphorylation	RGFGQKVTLIRHQRT CCCCCEEEEEEEECC	24.41	-
479	Phosphorylation	TLIRHQRTHTGEKPY EEEEEECCCCCCCCE	19.74	-
481	Phosphorylation	IRHQRTHTGEKPYLC EEEECCCCCCCCEEC	46.56	-
499	Phosphorylation	GRAFGFKSLLTRHQR CCCCCHHHHHHHHCC	26.75	24719451
568	Sumoylation	QRTHSGEKPYVCREC CCCCCCCCCEEECCC	45.21	-
568	Sumoylation	QRTHSGEKPYVCREC CCCCCCCCCEEECCC	45.21	-
593	Phosphorylation	HRHRRTKSGHQLLPQ HHCCCCCCCCCCCCC	40.68	28555341

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 ZN169_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN169_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 ZN169_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KR107_HUMAN	KRTAP10-7	physical	25416956
PEO1_HUMAN	C10orf2	physical	28514442
RBAK_HUMAN	RBAK	physical	28514442
SOGA1_HUMAN	SOGA1	physical	28514442
ZY11A_HUMAN	ZYG11A	physical	28514442
ZNF92_HUMAN	ZNF92	physical	28514442
SORL_HUMAN	SORL1	physical	28514442
ZN689_HUMAN	ZNF689	physical	28514442
ZBT10_HUMAN	ZBTB10	physical	28514442
ZN445_HUMAN	ZNF445	physical	28514442
TRI41_HUMAN	TRIM41	physical	28514442
TRI26_HUMAN	TRIM26	physical	28514442
LRP1B_HUMAN	LRP1B	physical	28514442
LTBP4_HUMAN	LTBP4	physical	28514442
ZN121_HUMAN	ZNF121	physical	28514442
ZN316_HUMAN	ZNF316	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
HIC2_HUMAN	HIC2	physical	28514442
Z324A_HUMAN	ZNF324	physical	28514442
RT35_HUMAN	MRPS35	physical	28514442
ZNF45_HUMAN	ZNF45	physical	28514442
SART3_HUMAN	SART3	physical	28514442
CENPB_HUMAN	CENPB	physical	28514442
CLH2_HUMAN	CLTCL1	physical	28514442
ZKSC8_HUMAN	ZKSCAN8	physical	28514442
RT09_HUMAN	MRPS9	physical	28514442
ZSC25_HUMAN	ZSCAN25	physical	28514442
ZN865_HUMAN	ZNF865	physical	28514442
RT33_HUMAN	MRPS33	physical	28514442
ZN184_HUMAN	ZNF184	physical	28514442
ZBT24_HUMAN	ZBTB24	physical	28514442
HNRPR_HUMAN	HNRNPR	physical	28514442
HNRPQ_HUMAN	SYNCRIP	physical	28514442
ZN629_HUMAN	ZNF629	physical	28514442
STAU2_HUMAN	STAU2	physical	28514442
NAT10_HUMAN	NAT10	physical	28514442
ZFR_HUMAN	ZFR	physical	28514442
PATZ1_HUMAN	PATZ1	physical	28514442
HASP_HUMAN	GSG2	physical	28514442
RT11_HUMAN	MRPS11	physical	28514442
TPD52_HUMAN	TPD52	physical	28514442
STRBP_HUMAN	STRBP	physical	28514442
RS3_HUMAN	RPS3	physical	28514442
RS15_HUMAN	RPS15	physical	28514442

Drug and Disease Associations

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

Regulatory Network of ZN169_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-158, AND MASSSPECTROMETRY.	17081983 [Abstract]