dbPTM

ZN160_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN160_HUMAN
UniProt AC	Q9HCG1
Protein Name	Zinc finger protein 160
Gene Name	ZNF160
Organism	Homo sapiens (Human).
Sequence Length	818
Subcellular Localization	Nucleus .
Protein Description	May be involved in transcriptional regulation..
Protein Sequence	MALTQVRLTFRDVAIEFSQEEWKCLDPAQRILYRDVMLENYWNLVSLGLCHFDMNIISMLEEGKEPWTVKSCVKIARKPRTPECVKGVVTDIPPKCTIKDLLPKEKSSTEAVFHTVVLERHESPDIEDFSFKEPQKNVHDFECQWRDDTGNYKGVLMAQKEGKRDQRDRRDIENKLMNNQLGVSFHSHLPELQLFQGEGKMYECNQVEKSTNNGSSVSPLQQIPSSVQTHRSKKYHELNHFSLLTQRRKANSCGKPYKCNECGKAFTQNSNLTSHRRIHSGEKPYKCSECGKTFTVRSNLTIHQVIHTGEKPYKCHECGKVFRHNSYLATHRRIHTGEKPYKCNECGKAFRGHSNLTTHQLIHTGEKPFKCNECGKLFTQNSHLISHWRIHTGEKPYKCNECGKAFSVRSSLAIHQTIHTGEKPYKCNECGKVFRYNSYLGRHRRVHTGEKPYKCNECGKAFSMHSNLATHQVIHTGTKPFKCNECSKVFTQNSQLANHRRIHTGEKPYKCNECGKAFSVRSSLTTHQAIHSGEKPYKCIECGKSFTQKSHLRSHRGIHSGEKPYKCNECGKVFAQTSQLARHWRVHTGEKPYKCNDCGRAFSDRSSLTFHQAIHTGEKPYKCHECGKVFRHNSYLATHRRIHTGEKPYKCNECGKAFSMHSNLTTHKVIHTGEKPYKCNQCGKVFTQNSHLANHQRTHTGEKPYRCNECGKAFSVRSSLTTHQAIHTGKKPYKCNECGKVFTQNAHLANHRRIHTGEKPYRCTECGKAFRVRSSLTTHMAIHTGEKRYKCNECGKVFRQSSNLASHHRMHTGEKPYK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	RDVAIEFSQEEWKCL HHHHHCCCHHHHCCC	24.72	27251275
23	Ubiquitination	EFSQEEWKCLDPAQR CCCHHHHCCCCHHHH	28.35	-
41	Phosphorylation	RDVMLENYWNLVSLG HHHHHHHHHHHHHHC	6.06	28857561
46	Phosphorylation	ENYWNLVSLGLCHFD HHHHHHHHHCCCCCC	21.64	28857561
58	Phosphorylation	HFDMNIISMLEEGKE CCCCCHHHHHHCCCC	17.33	29978859
68	Phosphorylation	EEGKEPWTVKSCVKI HCCCCCCCHHHHHHH	28.86	28857561
97	Phosphorylation	TDIPPKCTIKDLLPK CCCCCCCCHHHHCCC	36.87	21130716
123	Phosphorylation	VVLERHESPDIEDFS EEEECCCCCCCCCCC	23.03	25849741
130	Phosphorylation	SPDIEDFSFKEPQKN CCCCCCCCCCCCCCC	47.97	24719451
132	Ubiquitination	DIEDFSFKEPQKNVH CCCCCCCCCCCCCCC	68.25	-
136	Ubiquitination	FSFKEPQKNVHDFEC CCCCCCCCCCCCEEE	72.20	-
210	Phosphorylation	ECNQVEKSTNNGSSV EECCEEECCCCCCCC	23.90	-
216	Phosphorylation	KSTNNGSSVSPLQQI ECCCCCCCCCCHHHC	28.19	-
218	Phosphorylation	TNNGSSVSPLQQIPS CCCCCCCCCHHHCCC	23.11	25849741
258	Sumoylation	NSCGKPYKCNECGKA HCCCCCEECCCCCCC	38.83	-
258	Sumoylation	NSCGKPYKCNECGKA HCCCCCEECCCCCCC	38.83	-
267	Phosphorylation	NECGKAFTQNSNLTS CCCCCCCCCCCCCCC	31.53	-
280	Phosphorylation	TSHRRIHSGEKPYKC CCCCCCCCCCCCEEC	46.40	29496963
285	Phosphorylation	IHSGEKPYKCSECGK CCCCCCCEECCCCCC	35.38	-
293	Phosphorylation	KCSECGKTFTVRSNL ECCCCCCEEEEECCC	15.15	-
295	Phosphorylation	SECGKTFTVRSNLTI CCCCCEEEEECCCEE	21.90	-
308	Phosphorylation	TIHQVIHTGEKPYKC EEEEEEECCCCCEEE	35.59	29496963
314	Acetylation	HTGEKPYKCHECGKV ECCCCCEEECCCCCC	37.33	30593595
326	Phosphorylation	GKVFRHNSYLATHRR CCCCCCCCCHHCCCC	18.52	23312004
327	Phosphorylation	KVFRHNSYLATHRRI CCCCCCCCHHCCCCE	12.98	23312004
330	Phosphorylation	RHNSYLATHRRIHTG CCCCCHHCCCCEECC	17.20	23312004
336	Phosphorylation	ATHRRIHTGEKPYKC HCCCCEECCCCCEEC	44.67	29496963
341	Phosphorylation	IHTGEKPYKCNECGK EECCCCCEECCCCCC	38.96	18767875
342	Sumoylation	HTGEKPYKCNECGKA ECCCCCEECCCCCCC	38.83	-
342	Sumoylation	HTGEKPYKCNECGKA ECCCCCEECCCCCCC	38.83	-
364	Phosphorylation	TTHQLIHTGEKPFKC CHHHEEECCCCCEEC	39.79	18669648
392	Phosphorylation	ISHWRIHTGEKPYKC HCCEEEECCCCCEEC	44.67	29496963
397	Phosphorylation	IHTGEKPYKCNECGK EECCCCCEECCCCCC	38.96	18767875
398	Sumoylation	HTGEKPYKCNECGKA ECCCCCEECCCCCCE	38.83	-
398	Sumoylation	HTGEKPYKCNECGKA ECCCCCEECCCCCCE	38.83	-
420	Phosphorylation	AIHQTIHTGEKPYKC EEECEEECCCCCEEC	43.09	29496963
423	Sumoylation	QTIHTGEKPYKCNEC CEEECCCCCEECCCC	55.80	-
423	Sumoylation	QTIHTGEKPYKCNEC CEEECCCCCEECCCC	55.80	-
425	Phosphorylation	IHTGEKPYKCNECGK EECCCCCEECCCCCC	38.96	18767875
426	Sumoylation	HTGEKPYKCNECGKV ECCCCCEECCCCCCE	38.83	-
426	Sumoylation	HTGEKPYKCNECGKV ECCCCCEECCCCCCE	38.83	-
448	Phosphorylation	GRHRRVHTGEKPYKC CCCCCCCCCCCCEEC	44.15	29496963
451	Sumoylation	RRVHTGEKPYKCNEC CCCCCCCCCEECCCC	55.80	-
451	Ubiquitination	RRVHTGEKPYKCNEC CCCCCCCCCEECCCC	55.80	-
451	Sumoylation	RRVHTGEKPYKCNEC CCCCCCCCCEECCCC	55.80	-
454	Sumoylation	HTGEKPYKCNECGKA CCCCCCEECCCCCCE	38.83	-
454	Sumoylation	HTGEKPYKCNECGKA CCCCCCEECCCCCCE	38.83	-
504	Phosphorylation	ANHRRIHTGEKPYKC CCCCCCCCCCCCEEC	44.67	29496963
509	Phosphorylation	IHTGEKPYKCNECGK CCCCCCCEECCCCCC	38.96	18767875
510	Sumoylation	HTGEKPYKCNECGKA CCCCCCEECCCCCCE	38.83	-
510	Sumoylation	HTGEKPYKCNECGKA CCCCCCEECCCCCCE	38.83	-
532	Phosphorylation	TTHQAIHSGEKPYKC CCCCHHHCCCCCEEE	42.40	29496963
549	Ubiquitination	CGKSFTQKSHLRSHR CCCCCCCHHHHHHCC	36.46	-
560	Phosphorylation	RSHRGIHSGEKPYKC HHCCCCCCCCCCEEC	46.88	29496963
563	Acetylation	RGIHSGEKPYKCNEC CCCCCCCCCEECCCC	58.11	20167786
566	Sumoylation	HSGEKPYKCNECGKV CCCCCCEECCCCHHE	38.83	-
566	Sumoylation	HSGEKPYKCNECGKV CCCCCCEECCCCHHE	38.83	-
577	Phosphorylation	CGKVFAQTSQLARHW CHHEHHHHHHHHHHC	18.27	25690035
578	Phosphorylation	GKVFAQTSQLARHWR HHEHHHHHHHHHHCE	15.89	25690035
588	Phosphorylation	ARHWRVHTGEKPYKC HHHCEEECCCCCEEC	44.15	29496963
591	Sumoylation	WRVHTGEKPYKCNDC CEEECCCCCEECCCC	55.80	-
591	Acetylation	WRVHTGEKPYKCNDC CEEECCCCCEECCCC	55.80	20167786
591	Ubiquitination	WRVHTGEKPYKCNDC CEEECCCCCEECCCC	55.80	-
591	Sumoylation	WRVHTGEKPYKCNDC CEEECCCCCEECCCC	55.80	-
594	Acetylation	HTGEKPYKCNDCGRA ECCCCCEECCCCCCC	34.78	20167786
616	Phosphorylation	TFHQAIHTGEKPYKC EEHHHHHCCCCCEEE	40.71	29496963
619	Sumoylation	QAIHTGEKPYKCHEC HHHHCCCCCEEECCC	55.80	-
619	Ubiquitination	QAIHTGEKPYKCHEC HHHHCCCCCEEECCC	55.80	-
619	Sumoylation	QAIHTGEKPYKCHEC HHHHCCCCCEEECCC	55.80	-
634	Phosphorylation	GKVFRHNSYLATHRR CCCCCCCCCHHCCCC	18.52	23312004
635	Phosphorylation	KVFRHNSYLATHRRI CCCCCCCCHHCCCCE	12.98	23312004
638	Phosphorylation	RHNSYLATHRRIHTG CCCCCHHCCCCEECC	17.20	23312004
644	Phosphorylation	ATHRRIHTGEKPYKC HCCCCEECCCCCEEC	44.67	29496963
649	Phosphorylation	IHTGEKPYKCNECGK EECCCCCEECCCCCC	38.96	18767875
650	Sumoylation	HTGEKPYKCNECGKA ECCCCCEECCCCCCE	38.83	-
650	Sumoylation	HTGEKPYKCNECGKA ECCCCCEECCCCCCE	38.83	-
666	Phosphorylation	SMHSNLTTHKVIHTG ECCCCCCCCEEEECC	23.90	-
672	Phosphorylation	TTHKVIHTGEKPYKC CCCEEEECCCCCEEC	35.59	29496963
678	Acetylation	HTGEKPYKCNQCGKV ECCCCCEECCCCCCE	34.92	30593601
698	Phosphorylation	HLANHQRTHTGEKPY HHHCCCCCCCCCCCE	19.74	-
700	Phosphorylation	ANHQRTHTGEKPYRC HCCCCCCCCCCCEEC	46.56	24719451
703	Acetylation	QRTHTGEKPYRCNEC CCCCCCCCCEECCCC	49.01	30593589
728	Phosphorylation	TTHQAIHTGKKPYKC CCCCHHHCCCCCEEC	44.58	28555341
734	Sumoylation	HTGKKPYKCNECGKV HCCCCCEECCCCCCE	38.83	-
734	Sumoylation	HTGKKPYKCNECGKV HCCCCCEECCCCCCE	38.83	-
756	Phosphorylation	ANHRRIHTGEKPYRC CCCCCCCCCCCCEEC	44.67	29496963
759	Ubiquitination	RRIHTGEKPYRCTEC CCCCCCCCCEECCCC	49.01	-
759	Sumoylation	RRIHTGEKPYRCTEC CCCCCCCCCEECCCC	49.01	-
759	Sumoylation	RRIHTGEKPYRCTEC CCCCCCCCCEECCCC	49.01	-
768	Ubiquitination	YRCTECGKAFRVRSS EECCCCCCEEEEECC	56.88	-
784	Phosphorylation	TTHMAIHTGEKRYKC HCEEEEECCCCEEEE	40.71	28555341
789	Phosphorylation	IHTGEKRYKCNECGK EECCCCEEEECCCHH	30.84	-
802	Phosphorylation	GKVFRQSSNLASHHR HHHHHHCCCHHHHCC	27.76	-

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 ZN160_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN160_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 ZN160_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ZN160_HUMAN !!

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 ZN160_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-588, AND MASSSPECTROMETRY.	17924679 [Abstract]