ZFAN5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZFAN5_HUMAN
• UniProt AC: O76080
• Protein Name: AN1-type zinc finger protein 5
• Gene Name: ZFAND5
• Organism: Homo sapiens (Human).
• Sequence Length: 213
• Subcellular Localization: Cytoplasm.
• Protein Description: Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a potent inhibitory factor for osteoclast differentiation..
• Protein Sequence: MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADTSLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSTSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI

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
5	Phosphorylation	---MAQETNQTPGPM ---CCCCCCCCCCCE	22.13	24043423
8	Phosphorylation	MAQETNQTPGPMLCS CCCCCCCCCCCEECC	32.08	25159151
15	Phosphorylation	TPGPMLCSTGCGFYG CCCCEECCCCCCCCC	24.71	24043423
16	Phosphorylation	PGPMLCSTGCGFYGN CCCEECCCCCCCCCC	35.18	24043423
21	Phosphorylation	CSTGCGFYGNPRTNG CCCCCCCCCCCCCCC	10.98	24043423
35	Ubiquitination	GMCSVCYKEHLQRQQ CCCHHHHHHHHHHHH	33.27	-
44	Phosphorylation	HLQRQQNSGRMSPMG HHHHHHHCCCCCCCC	24.36	23401153
48	Phosphorylation	QQNSGRMSPMGTASG HHHCCCCCCCCCCCC	15.46	29255136
52	Phosphorylation	GRMSPMGTASGSNSP CCCCCCCCCCCCCCC	16.05	29255136
54	Phosphorylation	MSPMGTASGSNSPTS CCCCCCCCCCCCCCC	42.46	29255136
56	Phosphorylation	PMGTASGSNSPTSDS CCCCCCCCCCCCCCC	31.47	29255136
58	Phosphorylation	GTASGSNSPTSDSAS CCCCCCCCCCCCCHH	31.11	29255136
60	Phosphorylation	ASGSNSPTSDSASVQ CCCCCCCCCCCHHHH	45.01	29255136
61	Phosphorylation	SGSNSPTSDSASVQR CCCCCCCCCCHHHHC	32.71	29255136
63	Phosphorylation	SNSPTSDSASVQRAD CCCCCCCCHHHHCCC	23.39	29255136
65	Phosphorylation	SPTSDSASVQRADTS CCCCCCHHHHCCCCC	23.80	23927012
71	Phosphorylation	ASVQRADTSLNNCEG HHHHCCCCCCCCCCC	33.84	25627689
72	Phosphorylation	SVQRADTSLNNCEGA HHHCCCCCCCCCCCC	29.64	25262027
86	Ubiquitination	AAGSTSEKSRNVPVA CCCCCCHHHCCCCEE	55.25	21906983
98	Phosphorylation	PVAALPVTQQMTEMS CEEEEECCHHHHHCC	15.90	20058876
102	Phosphorylation	LPVTQQMTEMSISRE EECCHHHHHCCCCCC	24.97	27251275
105	Phosphorylation	TQQMTEMSISREDKI CHHHHHCCCCCCCCC	15.92	27251275
107	Phosphorylation	QMTEMSISREDKITT HHHHCCCCCCCCCCC	23.47	27251275
113	Phosphorylation	ISREDKITTPKTEVS CCCCCCCCCCCCCCC	42.67	28348404
114	Phosphorylation	SREDKITTPKTEVSE CCCCCCCCCCCCCCC	26.68	28348404
117	Phosphorylation	DKITTPKTEVSEPVV CCCCCCCCCCCCCEE	42.71	28348404
120	Phosphorylation	TTPKTEVSEPVVTQP CCCCCCCCCCEECCC	29.92	28348404
125	Phosphorylation	EVSEPVVTQPSPSVS CCCCCEECCCCCCCC	34.69	22199227
128	Phosphorylation	EPVVTQPSPSVSQPS CCEECCCCCCCCCCC	21.71	21815630
130	Phosphorylation	VVTQPSPSVSQPSTS EECCCCCCCCCCCCC	38.44	30576142
139	Phosphorylation	SQPSTSQSEEKAPEL CCCCCCCCHHHCCCC	47.71	28464451
148	Ubiquitination	EKAPELPKPKKNRCF HHCCCCCCCCCCCEE	80.32	21906983
180	Phosphorylation	LFCGLHRYSDKHNCP EEHHCCCCCCCCCCC	15.52	-
181	Phosphorylation	FCGLHRYSDKHNCPY EHHCCCCCCCCCCCC	39.89	-
183	Acetylation	GLHRYSDKHNCPYDY HCCCCCCCCCCCCCH	30.67	27452117
183	Ubiquitination	GLHRYSDKHNCPYDY HCCCCCCCCCCCCCH	30.67	-
188	Phosphorylation	SDKHNCPYDYKAEAA CCCCCCCCCHHHHHH	33.82	-
190	Phosphorylation	KHNCPYDYKAEAAAK CCCCCCCHHHHHHHH	13.27	-
191	Ubiquitination	HNCPYDYKAEAAAKI CCCCCCHHHHHHHHH	36.53	-
197	Acetylation	YKAEAAAKIRKENPV HHHHHHHHHHHHCCE	38.01	25953088
197	Ubiquitination	YKAEAAAKIRKENPV HHHHHHHHHHHHCCE	38.01	-
200	Ubiquitination	EAAAKIRKENPVVVA HHHHHHHHHCCEEEE	66.37	-
209	Ubiquitination	NPVVVAEKIQRI--- CCEEEEEECCCC---	34.11	-
209	Acetylation	NPVVVAEKIQRI--- CCEEEEEECCCC---	34.11	23954790

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
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZFAN5_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 ZFAN5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NEMO_HUMAN	IKBKG	physical	14754897
TRAF6_HUMAN	TRAF6	physical	14754897
PSMD6_HUMAN	PSMD6	physical	16424905
UBC_HUMAN	UBC	physical	21923101
SQSTM_HUMAN	SQSTM1	physical	21923101
A4_HUMAN	APP	physical	21832049
CETN1_HUMAN	CETN1	physical	28514442

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.
PubMed: 19690332

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.
PubMed: 19413330

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.
PubMed: 18669648