ZN250_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZN250_HUMAN
• UniProt AC: P15622
• Protein Name: Zinc finger protein 250
• Gene Name: ZNF250
• Organism: Homo sapiens (Human).
• Sequence Length: 560
• Subcellular Localization: Nucleus .
• Protein Description: May be involved in transcriptional regulation..
• Protein Sequence: MAAARLLPVPAGPQPLSFQAKLTFEDVAVLLSQDEWDRLCPAQRGLYRNVMMETYGNVVSLGLPGSKPDIISQLERGEDPWVLDRKGAKKSQGLWSDYSDNLKYDHTTACTQQDSLSCPWECETKGESQNTDLSPKPLISEQTVILGKTPLGRIDQENNETKQSFCLSPNSVDHREVQVLSQSMPLTPHQAVPSGERPYMCVECGKCFGRSSHLLQHQRIHTGEKPYVCSVCGKAFSQSSVLSKHRRIHTGEKPYECNECGKAFRVSSDLAQHHKIHTGEKPHECLECRKAFTQLSHLIQHQRIHTGERPYVCPLCGKAFNHSTVLRSHQRVHTGEKPHRCNECGKTFSVKRTLLQHQRIHTGEKPYTCSECGKAFSDRSVLIQHHNVHTGEKPYECSECGKTFSHRSTLMNHERIHTEEKPYACYECGKAFVQHSHLIQHQRVHTGEKPYVCGECGHAFSARRSLIQHERIHTGEKPFQCTECGKAFSLKATLIVHLRTHTGEKPYECNSCGKAFSQYSVLIQHQRIHTGEKPYECGECGRAFNQHGHLIQHQKVHRKL

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
55	Phosphorylation	RNVMMETYGNVVSLG HHHHHHHHCCEEECC	8.06	24719451
60	Phosphorylation	ETYGNVVSLGLPGSK HHHCCEEECCCCCCC	16.67	24719451
66	Phosphorylation	VSLGLPGSKPDIISQ EECCCCCCCCCHHHH	38.79	-
72	Phosphorylation	GSKPDIISQLERGED CCCCCHHHHHHCCCC	29.10	-
90	Ubiquitination	LDRKGAKKSQGLWSD ECCCCCCCCCCCCCC	47.69	-
91	Phosphorylation	DRKGAKKSQGLWSDY CCCCCCCCCCCCCCC	28.86	24043423
96	Phosphorylation	KKSQGLWSDYSDNLK CCCCCCCCCCCCCCC	31.54	24043423
98	Phosphorylation	SQGLWSDYSDNLKYD CCCCCCCCCCCCCCC	16.65	24043423
99	Phosphorylation	QGLWSDYSDNLKYDH CCCCCCCCCCCCCCC	25.64	22210691
104	Phosphorylation	DYSDNLKYDHTTACT CCCCCCCCCCCCCCC	19.00	-
125	Sumoylation	CPWECETKGESQNTD CCCEEECCCCCCCCC	38.09	28112733
128	Phosphorylation	ECETKGESQNTDLSP EEECCCCCCCCCCCC	37.08	30266825
131	Phosphorylation	TKGESQNTDLSPKPL CCCCCCCCCCCCCCC	30.58	30266825
134	Phosphorylation	ESQNTDLSPKPLISE CCCCCCCCCCCCCCC	33.42	30266825
136	Sumoylation	QNTDLSPKPLISEQT CCCCCCCCCCCCCCE	49.43	28112733
140	Phosphorylation	LSPKPLISEQTVILG CCCCCCCCCCEEEEC	31.19	30266825
143	Phosphorylation	KPLISEQTVILGKTP CCCCCCCEEEECCCC	12.88	28450419
148	Sumoylation	EQTVILGKTPLGRID CCEEEECCCCCCCCC	43.45	28112733
161	Phosphorylation	IDQENNETKQSFCLS CCCCCCCCCCEEECC	36.19	28555341
162	Sumoylation	DQENNETKQSFCLSP CCCCCCCCCEEECCC	37.45	28112733
164	Phosphorylation	ENNETKQSFCLSPNS CCCCCCCEEECCCCC	21.34	23898821
168	Phosphorylation	TKQSFCLSPNSVDHR CCCEEECCCCCCCHH	24.18	25849741
171	Phosphorylation	SFCLSPNSVDHREVQ EEECCCCCCCHHHHH	32.10	29978859
181	Phosphorylation	HREVQVLSQSMPLTP HHHHHHHHCCCCCCC	22.73	26074081
183	Phosphorylation	EVQVLSQSMPLTPHQ HHHHHHCCCCCCCCC	20.99	26074081
187	Phosphorylation	LSQSMPLTPHQAVPS HHCCCCCCCCCCCCC	16.92	26074081
194	Phosphorylation	TPHQAVPSGERPYMC CCCCCCCCCCCCEEE	46.84	26074081
199	Phosphorylation	VPSGERPYMCVECGK CCCCCCCEEEEECCC	14.90	26074081
222	Phosphorylation	LQHQRIHTGEKPYVC HHCCCCCCCCCCEEE	44.67	28111955
225	Sumoylation	QRIHTGEKPYVCSVC CCCCCCCCCEEEEEC	42.89	28112733
225	Sumoylation	QRIHTGEKPYVCSVC CCCCCCCCCEEEEEC	42.89	-
239	Phosphorylation	CGKAFSQSSVLSKHR CCCCCCCHHHHHHCC	22.63	28555341
250	Phosphorylation	SKHRRIHTGEKPYEC HHCCCCCCCCCCEEC	44.67	28152594
253	Ubiquitination	RRIHTGEKPYECNEC CCCCCCCCCEECCCC	55.00	-
255	Phosphorylation	IHTGEKPYECNECGK CCCCCCCEECCCCCC	44.15	28152594
278	Phosphorylation	AQHHKIHTGEKPHEC HHHCCCCCCCCCHHH	50.97	28555341
306	Phosphorylation	IQHQRIHTGERPYVC HHHCCCCCCCCCEEC	38.06	28555341
324	Phosphorylation	GKAFNHSTVLRSHQR CCCCCCCHHHHCCCC	18.93	24719451
347	Phosphorylation	RCNECGKTFSVKRTL CCCCCCCCEECCHHH	13.36	30576142
349	Phosphorylation	NECGKTFSVKRTLLQ CCCCCCEECCHHHHH	31.77	30576142
362	Phosphorylation	LQHQRIHTGEKPYTC HHCCCCCCCCCCEEC	44.67	26055452
390	Phosphorylation	IQHHNVHTGEKPYEC EEECCCCCCCCCEEC	42.63	28348404
398	Phosphorylation	GEKPYECSECGKTFS CCCCEECCCCCCCCC	24.79	-
421	Sumoylation	ERIHTEEKPYACYEC CCCCCCCCCCCCHHC	36.78	-
421	Sumoylation	ERIHTEEKPYACYEC CCCCCCCCCCCCHHC	36.78	28112733
446	Phosphorylation	IQHQRVHTGEKPYVC HCCCCCCCCCCCEEE	44.15	-
474	Phosphorylation	IQHERIHTGEKPFQC HCCCCCCCCCCCEEE	44.67	22817900
489	Phosphorylation	TECGKAFSLKATLIV CCCCCEEEEEEEEEE	33.54	24719451
500	Phosphorylation	TLIVHLRTHTGEKPY EEEEEECCCCCCCCE	30.10	-
502	Phosphorylation	IVHLRTHTGEKPYEC EEEECCCCCCCCEEC	46.56	-
530	Phosphorylation	IQHQRIHTGEKPYEC EECCEECCCCCCCCC	44.67	28111955

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

Oops, there are no upstream regulatory protein records of ZN250_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZN250_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 ZN250_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DPPA2_HUMAN	DPPA2	physical	16189514
KR412_HUMAN	KRTAP4-12	physical	16189514
CEP44_HUMAN	CEP44	physical	16189514
ZBT8A_HUMAN	ZBTB8A	physical	16189514
ZN250_HUMAN	ZNF250	physical	25416956
CARD9_HUMAN	CARD9	physical	25416956
GMCL1_HUMAN	GMCL1	physical	25416956
CC136_HUMAN	CCDC136	physical	25416956
GNPTA_HUMAN	GNPTAB	physical	25416956
PKHF2_HUMAN	PLEKHF2	physical	25416956
C102B_HUMAN	CCDC102B	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
TRI41_HUMAN	TRIM41	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
KASH5_HUMAN	CCDC155	physical	25416956
SYNE4_HUMAN	SYNE4	physical	25416956
F124A_HUMAN	FAM124A	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
TRFL_HUMAN	LTF	physical	26186194
TPM2_HUMAN	TPM2	physical	26186194
SPIT1_HUMAN	SPINT1	physical	26186194
TRAF1_HUMAN	TRAF1	physical	21516116
PKHF2_HUMAN	PLEKHF2	physical	21516116
TIF1B_HUMAN	TRIM28	physical	28514442
SPIT1_HUMAN	SPINT1	physical	28514442
TPM2_HUMAN	TPM2	physical	28514442
TRFL_HUMAN	LTF	physical	28514442

Drug and Disease Associations

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