dbPTM

ZN512_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZN512_HUMAN
UniProt AC	Q96ME7
Protein Name	Zinc finger protein 512
Gene Name	ZNF512
Organism	Homo sapiens (Human).
Sequence Length	567
Subcellular Localization	Nucleus .
Protein Description	May be involved in transcriptional regulation..
Protein Sequence	MSSRLGAVPATSGPTTFKQQRSTRIVGAKNSRTQCSIKDNSFQYTIPHDDSLSGSSSASSCEPVSDFPASFRKSTYWMKMRRIKPAATSHVEGSGGVSAKGKRKPRQEEDEDYREFPQKKHKLYGRKQRPKTQPNPKSQARRIRKEPPVYAAGSLEEQWYLEIVDKGSVSCPTCQAVGRKTIEGLKKHMENCKQEMFTCHHCGKQLRSLAGMKYHVMANHNSLPILKAGDEIDEPSERERLRTVLKRLGKLRCMRESCSSSFTSIMGYLYHVRKCGKGAAELEKMTLKCHHCGKPYRSKAGLAYHLRSEHGPISFFPESGQPECLKEMNLESKSGGRVQRRSAKIAVYHLQELASAELAKEWPKRKVLQDLVPDDRKLKYTRPGLPTFSQEVLHKWKTDIKKYHRIQCPNQGCEAVYSSVSGLKAHLGSCTLGNFVAGKYKCLLCQKEFVSESGVKYHINSVHAEDWFVVNPTTTKSFEKLMKIKQRQQEEEKRRQQHRSRRSLRRRQQPGIELPETELSLRVGKDQRRNNEELVVSASCKEPEQEPVPAQFQKVKPPKTNHKRGRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	RLGAVPATSGPTTFK CCCCCCCCCCCCCCC	28.31	28555341
12	Phosphorylation	LGAVPATSGPTTFKQ CCCCCCCCCCCCCCC	44.90	28555341
18	Methylation	TSGPTTFKQQRSTRI CCCCCCCCCCCCEEE	43.35	90499
18	Sumoylation	TSGPTTFKQQRSTRI CCCCCCCCCCCCEEE	43.35	28112733
18	Ubiquitination	TSGPTTFKQQRSTRI CCCCCCCCCCCCEEE	43.35	-
18	Acetylation	TSGPTTFKQQRSTRI CCCCCCCCCCCCEEE	43.35	25953088
18	Sumoylation	TSGPTTFKQQRSTRI CCCCCCCCCCCCEEE	43.35	-
22	Phosphorylation	TTFKQQRSTRIVGAK CCCCCCCCEEEECCC	20.07	26074081
23	Phosphorylation	TFKQQRSTRIVGAKN CCCCCCCEEEECCCC	26.97	26074081
84	Sumoylation	WMKMRRIKPAATSHV CEEEECCCCCCCCCC	27.13	28112733
84	Sumoylation	WMKMRRIKPAATSHV CEEEECCCCCCCCCC	27.13	-
84	Acetylation	WMKMRRIKPAATSHV CEEEECCCCCCCCCC	27.13	26051181
88	Phosphorylation	RRIKPAATSHVEGSG ECCCCCCCCCCCCCC	22.82	20860994
89	Phosphorylation	RIKPAATSHVEGSGG CCCCCCCCCCCCCCC	22.32	23312004
94	Phosphorylation	ATSHVEGSGGVSAKG CCCCCCCCCCCCCCC	20.90	25159151
98	Phosphorylation	VEGSGGVSAKGKRKP CCCCCCCCCCCCCCC	27.77	25159151
100	Acetylation	GSGGVSAKGKRKPRQ CCCCCCCCCCCCCCC	58.41	25953088
102	Acetylation	GGVSAKGKRKPRQEE CCCCCCCCCCCCCCC	57.45	26051181
113	Phosphorylation	RQEEDEDYREFPQKK CCCCCCCHHHCHHHH	15.25	-
119	Acetylation	DYREFPQKKHKLYGR CHHHCHHHHHHHHCC	58.02	25953088
119	Ubiquitination	DYREFPQKKHKLYGR CHHHCHHHHHHHHCC	58.02	-
137	Ubiquitination	PKTQPNPKSQARRIR CCCCCCHHHHHHHHH	62.94	-
180	Ubiquitination	TCQAVGRKTIEGLKK CCHHHCCHHHHHHHH	48.18	-
186	Ubiquitination	RKTIEGLKKHMENCK CHHHHHHHHHHHHHH	52.03	-
213	Ubiquitination	LRSLAGMKYHVMANH HHHHHCCEEEEEECC	31.14	-
214	Phosphorylation	RSLAGMKYHVMANHN HHHHCCEEEEEECCC	7.25	-
222	Phosphorylation	HVMANHNSLPILKAG EEEECCCCCCEEECC	28.15	24719451
227	Sumoylation	HNSLPILKAGDEIDE CCCCCEEECCCCCCC	51.55	28112733
284	Ubiquitination	KGAAELEKMTLKCHH CCHHHHHHCCEEECC	50.22	-
286	O-linked_Glycosylation	AAELEKMTLKCHHCG HHHHHHCCEEECCCC	33.85	30379171
298	Phosphorylation	HCGKPYRSKAGLAYH CCCCCCCCCCCHHHH	22.48	27251275
299	Sumoylation	CGKPYRSKAGLAYHL CCCCCCCCCCHHHHH	37.16	-
299	Sumoylation	CGKPYRSKAGLAYHL CCCCCCCCCCHHHHH	37.16	-
308	Phosphorylation	GLAYHLRSEHGPISF CHHHHHHCCCCCCCC	40.06	27251275
314	Phosphorylation	RSEHGPISFFPESGQ HCCCCCCCCCCCCCC	24.78	27251275
326	Acetylation	SGQPECLKEMNLESK CCCCHHHHHCCCCCC	67.58	26051181
326	Ubiquitination	SGQPECLKEMNLESK CCCCHHHHHCCCCCC	67.58	-
332	Phosphorylation	LKEMNLESKSGGRVQ HHHCCCCCCCCCCCH	34.98	22468782
333	Sumoylation	KEMNLESKSGGRVQR HHCCCCCCCCCCCHH	43.68	-
333	Sumoylation	KEMNLESKSGGRVQR HHCCCCCCCCCCCHH	43.68	25218447
342	Phosphorylation	GGRVQRRSAKIAVYH CCCCHHHHHHHHHHH	35.78	-
344	Sumoylation	RVQRRSAKIAVYHLQ CCHHHHHHHHHHHHH	32.23	-
344	Sumoylation	RVQRRSAKIAVYHLQ CCHHHHHHHHHHHHH	32.23	-
344	Acetylation	RVQRRSAKIAVYHLQ CCHHHHHHHHHHHHH	32.23	25953088
355	Phosphorylation	YHLQELASAELAKEW HHHHHHHHHHHHHHC	34.59	22468782
366	Ubiquitination	AKEWPKRKVLQDLVP HHHCCCCHHHHHHCC	54.12	-
379	Ubiquitination	VPDDRKLKYTRPGLP CCCCCCCCCCCCCCC	47.84	-
380	Phosphorylation	PDDRKLKYTRPGLPT CCCCCCCCCCCCCCC	20.58	20860994
381	Phosphorylation	DDRKLKYTRPGLPTF CCCCCCCCCCCCCCC	28.88	20860994
387	Phosphorylation	YTRPGLPTFSQEVLH CCCCCCCCCCHHHHH	40.75	-
389	Phosphorylation	RPGLPTFSQEVLHKW CCCCCCCCHHHHHHH	28.10	20860994
395	Ubiquitination	FSQEVLHKWKTDIKK CCHHHHHHHCCCHHH	46.34	-
417	Phosphorylation	NQGCEAVYSSVSGLK CCCCHHHHHCCCCHH	11.41	28152594
418	Phosphorylation	QGCEAVYSSVSGLKA CCCHHHHHCCCCHHH	20.05	28152594
419	Phosphorylation	GCEAVYSSVSGLKAH CCHHHHHCCCCHHHH	11.56	28152594
421	O-linked_Glycosylation	EAVYSSVSGLKAHLG HHHHHCCCCHHHHCC	40.11	30379171
421	Phosphorylation	EAVYSSVSGLKAHLG HHHHHCCCCHHHHCC	40.11	28152594
439	Ubiquitination	LGNFVAGKYKCLLCQ HHHHHCCCEEEEEEE	31.62	-
476	Ubiquitination	VVNPTTTKSFEKLMK EECCCCCHHHHHHHH	51.56	-
476	Acetylation	VVNPTTTKSFEKLMK EECCCCCHHHHHHHH	51.56	26051181
503	Phosphorylation	QQHRSRRSLRRRQQP HHHHHHHHHHHHCCC	25.72	-
520	Phosphorylation	ELPETELSLRVGKDQ CCCHHHHEEEECCCC	14.11	24719451
537	Phosphorylation	NNEELVVSASCKEPE CCCEEEEEEECCCCC	13.64	25627689

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 ZN512_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZN512_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 ZN512_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZN273_HUMAN	ZNF273	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
WDR3_HUMAN	WDR3	physical	28514442
ZN346_HUMAN	ZNF346	physical	28514442
BLM_HUMAN	BLM	physical	28514442
DDX31_HUMAN	DDX31	physical	28514442
RL30_HUMAN	RPL30	physical	28514442
NEPRO_HUMAN	C3orf17	physical	28514442
NAT10_HUMAN	NAT10	physical	28514442
NO40_HUMAN	ZCCHC17	physical	28514442
NOL8_HUMAN	NOL8	physical	28514442
BUD13_HUMAN	BUD13	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
NGDN_HUMAN	NGDN	physical	28514442
STAU1_HUMAN	STAU1	physical	28514442
LENG8_HUMAN	LENG8	physical	28514442
NOL6_HUMAN	NOL6	physical	28514442
URB2_HUMAN	URB2	physical	28514442
NVL_HUMAN	NVL	physical	28514442
RRP5_HUMAN	PDCD11	physical	28514442
RL32_HUMAN	RPL32	physical	28514442
KNOP1_HUMAN	KNOP1	physical	28514442
BBX_HUMAN	BBX	physical	28514442
NPA1P_HUMAN	URB1	physical	28514442
CEBPZ_HUMAN	CEBPZ	physical	28514442
TAF1A_HUMAN	TAF1A	physical	28514442
CENPU_HUMAN	CENPU	physical	28514442
ZN121_HUMAN	ZNF121	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
DDX51_HUMAN	DDX51	physical	28514442
YTDC2_HUMAN	YTHDC2	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
REXO4_HUMAN	REXO4	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
NOC2L_HUMAN	NOC2L	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
TUT7_HUMAN	ZCCHC6	physical	28514442
MRM3_HUMAN	RNMTL1	physical	28514442
RRP7A_HUMAN	RRP7A	physical	28514442
DDX54_HUMAN	DDX54	physical	28514442
FXR1_HUMAN	FXR1	physical	28514442
ZBT24_HUMAN	ZBTB24	physical	28514442
RS3A_HUMAN	RPS3A	physical	28514442
ZN593_HUMAN	ZNF593	physical	28514442
ZN431_HUMAN	ZNF431	physical	28514442
NMNA1_HUMAN	NMNAT1	physical	28514442
RL4_HUMAN	RPL4	physical	28514442
SDA1_HUMAN	SDAD1	physical	28514442
DDX21_HUMAN	DDX21	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
RBMX2_HUMAN	RBMX2	physical	28514442
ZN668_HUMAN	ZNF668	physical	28514442
SPB1_HUMAN	FTSJ3	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
ZN771_HUMAN	ZNF771	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.

Regulatory Network of ZN512_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.	19007248 [Abstract]