dbPTM

UHRF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UHRF1_HUMAN
UniProt AC	Q96T88
Protein Name	E3 ubiquitin-protein ligase UHRF1
Gene Name	UHRF1
Organism	Homo sapiens (Human).
Sequence Length	793
Subcellular Localization	Nucleus . Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.
Protein Description	Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair..
Protein Sequence	MWIQVRTMDGRQTHTVDSLSRLTKVEELRRKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYEVRLNDTIQLLVRQSLVLPHSTKERDSELSDTDSGCCLGQSESDKSSTHGEAAAETDSRPADEDMWDETELGLYKVNEYVDARDTNMGAWFEAQVVRVTRKAPSRDEPCSSTSRPALEEDVIYHVKYDDYPENGVVQMNSRDVRARARTIIKWQDLEVGQVVMLNYNPDNPKERGFWYDAEISRKRETRTARELYANVVLGDDSLNDCRIIFVDEVFKIERPGEGSPMVDNPMRRKSGPSCKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECDMAFHIYCLDPPLSSVPSEDEWYCPECRNDASEVVLAGERLRESKKKAKMASATSSSQRDWGKGMACVGRTKECTIVPSNHYGPIPGIPVGTMWRFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDHGNFFTYTGSGGRDLSGNKRTAEQSCDQKLTNTNRALALNCFAPINDQEGAEAKDWRSGKPVRVVRNVKGGKNSKYAPAEGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDDEPGPWTKEGKDRIKKLGLTMQYPEGYLEALANREREKENSKREEEEQQEGGFASPRTGKGKWKRKSAGGGPSRAGSPRRTSKKTKVEPYSLTAQQSSLIREDKSNAKLWNEVLASLKDRPASGSPFQLFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFRAQVFSCPACRYDLGRSYAMQVNQPLQTVLNQLFPGYGNGR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	RTMDGRQTHTVDSLS EECCCCCEEEHHHHH	20.39	20068231
15	Phosphorylation	MDGRQTHTVDSLSRL CCCCCEEEHHHHHHH	29.42	20068231
18	Phosphorylation	RQTHTVDSLSRLTKV CCEEEHHHHHHHHHH	24.73	20068231
20	Phosphorylation	THTVDSLSRLTKVEE EEEHHHHHHHHHHHH	29.24	20068231
24	Sumoylation	DSLSRLTKVEELRRK HHHHHHHHHHHHHHH	52.84	-
24	Ubiquitination	DSLSRLTKVEELRRK HHHHHHHHHHHHHHH	52.84	-
31	Ubiquitination	KVEELRRKIQELFHV HHHHHHHHHHHHHCC	42.16	-
50	Ubiquitination	QRLFYRGKQMEDGHT HHHEECCEECCCCCE	37.16	21890473
50	Ubiquitination	QRLFYRGKQMEDGHT HHHEECCEECCCCCE	37.16	21906983
63	Ubiquitination	HTLFDYEVRLNDTIQ CEEEEEEEECHHHHH	7.40	21890473
63	Ubiquitination	HTLFDYEVRLNDTIQ CEEEEEEEECHHHHH	7.40	21890473
63	Ubiquitination	HTLFDYEVRLNDTIQ CEEEEEEEECHHHHH	7.40	21890473
68	Phosphorylation	YEVRLNDTIQLLVRQ EEEECHHHHHHHHHC	15.00	25159151
76	Phosphorylation	IQLLVRQSLVLPHST HHHHHHCHHCCCCCC	15.19	25159151
82	Phosphorylation	QSLVLPHSTKERDSE CHHCCCCCCCCCCCC	38.95	24732914
83	Phosphorylation	SLVLPHSTKERDSEL HHCCCCCCCCCCCCC	33.61	24732914
84	Ubiquitination	LVLPHSTKERDSELS HCCCCCCCCCCCCCC	54.49	21906983
88	Phosphorylation	HSTKERDSELSDTDS CCCCCCCCCCCCCCC	46.81	22167270
89	Phosphorylation	STKERDSELSDTDSG CCCCCCCCCCCCCCC	57.49	24719451
91	Phosphorylation	KERDSELSDTDSGCC CCCCCCCCCCCCCCC	34.12	22167270
93	Phosphorylation	RDSELSDTDSGCCLG CCCCCCCCCCCCCCC	28.79	22167270
95	Phosphorylation	SELSDTDSGCCLGQS CCCCCCCCCCCCCCC	35.50	22167270
102	Phosphorylation	SGCCLGQSESDKSST CCCCCCCCCCCCCCC	36.95	22167270
104	Phosphorylation	CCLGQSESDKSSTHG CCCCCCCCCCCCCCC	56.43	24732914
107	Phosphorylation	GQSESDKSSTHGEAA CCCCCCCCCCCCCHH	45.52	28450419
108	Phosphorylation	QSESDKSSTHGEAAA CCCCCCCCCCCCHHH	30.11	28450419
109	Phosphorylation	SESDKSSTHGEAAAE CCCCCCCCCCCHHHH	40.78	28450419
117	Phosphorylation	HGEAAAETDSRPADE CCCHHHHCCCCCCCC	34.25	28450419
119	Phosphorylation	EAAAETDSRPADEDM CHHHHCCCCCCCCCC	47.81	25849741
130	Phosphorylation	DEDMWDETELGLYKV CCCCCCHHHHCEEEH	33.75	28111955
136	Ubiquitination	ETELGLYKVNEYVDA HHHHCEEEHHHCCCC	43.56	21906983
140	Phosphorylation	GLYKVNEYVDARDTN CEEEHHHCCCCCCCC	9.83	28796482
162	Acetylation	QVVRVTRKAPSRDEP EEEEEEECCCCCCCC	56.11	26051181
165	Phosphorylation	RVTRKAPSRDEPCSS EEEECCCCCCCCCCC	58.17	25159151
171	Phosphorylation	PSRDEPCSSTSRPAL CCCCCCCCCCCCCCC	47.57	30576142
172	Phosphorylation	SRDEPCSSTSRPALE CCCCCCCCCCCCCCC	36.80	30576142
173	Phosphorylation	RDEPCSSTSRPALEE CCCCCCCCCCCCCCC	16.68	25159151
174	Phosphorylation	DEPCSSTSRPALEED CCCCCCCCCCCCCCC	37.91	25159151
178	Phosphorylation	SSTSRPALEEDVIYH CCCCCCCCCCCEEEE	9.08	24719451
233	Ubiquitination	NYNPDNPKERGFWYD ECCCCCHHHCCCEEE	67.32	21906983
256	Phosphorylation	TRTARELYANVVLGD CHHHHHHHHHEECCC	7.44	28152594
265	Phosphorylation	NVVLGDDSLNDCRII HEECCCCCCCCCEEE	33.54	21712546
279	Sumoylation	IFVDEVFKIERPGEG EEEEEEEECCCCCCC	49.16	28112733
287	Phosphorylation	IERPGEGSPMVDNPM CCCCCCCCCCCCCCC	12.91	29255136
298	Phosphorylation	DNPMRRKSGPSCKHC CCCCCCCCCCCCCCC	54.87	22837395
300	Phosphorylation	PMRRKSGPSCKHCKD CCCCCCCCCCCCCHH	43.58	27251275
303	Ubiquitination	RKSGPSCKHCKDDVN CCCCCCCCCCHHHHH	57.27	-
306	Ubiquitination	GPSCKHCKDDVNRLC CCCCCCCHHHHHHHH	57.60	-
368	Phosphorylation	PECRNDASEVVLAGE CCCCCCHHHHHHHHH	33.51	25159151
385	Sumoylation	RESKKKAKMASATSS HHHHHHHHHHHCCCC	43.83	-
385	Acetylation	RESKKKAKMASATSS HHHHHHHHHHHCCCC	43.83	25953088
385	Sumoylation	RESKKKAKMASATSS HHHHHHHHHHHCCCC	43.83	25218447
385	Ubiquitination	RESKKKAKMASATSS HHHHHHHHHHHCCCC	43.83	21906983
390	Phosphorylation	KAKMASATSSSQRDW HHHHHHCCCCCCCCC	27.01	26074081
391	Phosphorylation	AKMASATSSSQRDWG HHHHHCCCCCCCCCC	27.92	26074081
392	Phosphorylation	KMASATSSSQRDWGK HHHHCCCCCCCCCCC	26.57	25159151
393	Phosphorylation	MASATSSSQRDWGKG HHHCCCCCCCCCCCC	29.06	25159151
399	Sumoylation	SSQRDWGKGMACVGR CCCCCCCCCCEECCC	41.06	-
399	Acetylation	SSQRDWGKGMACVGR CCCCCCCCCCEECCC	41.06	19608861
399	Ubiquitination	SSQRDWGKGMACVGR CCCCCCCCCCEECCC	41.06	19608861
408	Acetylation	MACVGRTKECTIVPS CEECCCCCEEEEECC	49.81	26051181
408	Ubiquitination	MACVGRTKECTIVPS CEECCCCCEEEEECC	49.81	-
411	Phosphorylation	VGRTKECTIVPSNHY CCCCCEEEEECCCCC	26.54	20068231
415	Phosphorylation	KECTIVPSNHYGPIP CEEEEECCCCCCCCC	25.91	20068231
418	Phosphorylation	TIVPSNHYGPIPGIP EEECCCCCCCCCCCC	28.93	20068231
428	Phosphorylation	IPGIPVGTMWRFRVQ CCCCCCCCEEEEEEE	17.50	20068231
431 (in isoform 2)	Phosphorylation	-	9.93	27642862
437	Phosphorylation	WRFRVQVSESGVHRP EEEEEEECCCCCCCC	14.68	22210691
439	Phosphorylation	FRVQVSESGVHRPHV EEEEECCCCCCCCEE	38.31	22210691
492	Phosphorylation	DLSGNKRTAEQSCDQ CCCCCHHHHHHHHHH	35.83	-
496	Phosphorylation	NKRTAEQSCDQKLTN CHHHHHHHHHHHCCC	15.92	-
500	Sumoylation	AEQSCDQKLTNTNRA HHHHHHHHCCCHHHH	43.99	-
500	Acetylation	AEQSCDQKLTNTNRA HHHHHHHHCCCHHHH	43.99	26051181
500	Ubiquitination	AEQSCDQKLTNTNRA HHHHHHHHCCCHHHH	43.99	-
512	Glutathionylation	NRALALNCFAPINDQ HHHHHEEEECCCCCC	2.98	22555962
525	Sumoylation	DQEGAEAKDWRSGKP CCCCHHCCCCCCCCC	49.70	-
525	Acetylation	DQEGAEAKDWRSGKP CCCCHHCCCCCCCCC	49.70	26051181
525	Ubiquitination	DQEGAEAKDWRSGKP CCCCHHCCCCCCCCC	49.70	-
531	Sumoylation	AKDWRSGKPVRVVRN CCCCCCCCCEEEEEE	41.40	-
546	Sumoylation	VKGGKNSKYAPAEGN CCCCCCCCCCCCCCC	55.62	-
546	Acetylation	VKGGKNSKYAPAEGN CCCCCCCCCCCCCCC	55.62	19608861
546	Sumoylation	VKGGKNSKYAPAEGN CCCCCCCCCCCCCCC	55.62	25218447
546	Ubiquitination	VKGGKNSKYAPAEGN CCCCCCCCCCCCCCC	55.62	19608861
559	Phosphorylation	GNRYDGIYKVVKYWP CCCCCCEEEEEECCC	11.85	-
560	Ubiquitination	NRYDGIYKVVKYWPE CCCCCEEEEEECCCC	38.33	21890473
563	Sumoylation	DGIYKVVKYWPEKGK CCEEEEEECCCCCCC	44.58	-
563	Acetylation	DGIYKVVKYWPEKGK CCEEEEEECCCCCCC	44.58	25953088
563	Ubiquitination	DGIYKVVKYWPEKGK CCEEEEEECCCCCCC	44.58	21906983
568	Ubiquitination	VVKYWPEKGKSGFLV EEECCCCCCCCCEEE	68.51	-
570	Ubiquitination	KYWPEKGKSGFLVWR ECCCCCCCCCEEEEE	59.48	21890473
570	Sumoylation	KYWPEKGKSGFLVWR ECCCCCCCCCEEEEE	59.48	-
570	Ubiquitination	KYWPEKGKSGFLVWR ECCCCCCCCCEEEEE	59.48	21890473
583	Ubiquitination	WRYLLRRDDDEPGPW EEEEECCCCCCCCCC	62.37	21890473
583	Ubiquitination	WRYLLRRDDDEPGPW EEEEECCCCCCCCCC	62.37	21890473
583	Ubiquitination	WRYLLRRDDDEPGPW EEEEECCCCCCCCCC	62.37	21890473
592	Ubiquitination	DEPGPWTKEGKDRIK CCCCCCCCCCHHHHH	61.68	21906983
599	Ubiquitination	KEGKDRIKKLGLTMQ CCCHHHHHHHCCEEE	42.72	-
600	Ubiquitination	EGKDRIKKLGLTMQY CCHHHHHHHCCEEEC	45.47	21890473
600	Sumoylation	EGKDRIKKLGLTMQY CCHHHHHHHCCEEEC	45.47	-
600	Ubiquitination	EGKDRIKKLGLTMQY CCHHHHHHHCCEEEC	45.47	21906983
613	Ubiquitination	QYPEGYLEALANRER ECCHHHHHHHHHHHH	32.90	21890473
613	Ubiquitination	QYPEGYLEALANRER ECCHHHHHHHHHHHH	32.90	21890473
613	Ubiquitination	QYPEGYLEALANRER ECCHHHHHHHHHHHH	32.90	21890473
622	Ubiquitination	LANREREKENSKREE HHHHHHHHHHHHHHH	69.30	-
625	Phosphorylation	REREKENSKREEEEQ HHHHHHHHHHHHHHH	33.89	29214152
626	Sumoylation	EREKENSKREEEEQQ HHHHHHHHHHHHHHH	75.34	-
626	Acetylation	EREKENSKREEEEQQ HHHHHHHHHHHHHHH	75.34	26051181
626	Ubiquitination	EREKENSKREEEEQQ HHHHHHHHHHHHHHH	75.34	21906983
639	Phosphorylation	QQEGGFASPRTGKGK HHCCCCCCCCCCCCC	16.80	29255136
650	Methylation	GKGKWKRKSAGGGPS CCCCCCCCCCCCCCC	40.71	116253595
651	Phosphorylation	KGKWKRKSAGGGPSR CCCCCCCCCCCCCCC	35.86	21406692
652	Phosphorylation	GKWKRKSAGGGPSRA CCCCCCCCCCCCCCC	24.56	24719451
652 (in isoform 2)	Phosphorylation	-	24.56	-
657	Phosphorylation	KSAGGGPSRAGSPRR CCCCCCCCCCCCCCC	37.73	28102081
658	Methylation	SAGGGPSRAGSPRRT CCCCCCCCCCCCCCC	46.21	115919521
661	Phosphorylation	GGPSRAGSPRRTSKK CCCCCCCCCCCCCCC	17.78	28985074
665	Phosphorylation	RAGSPRRTSKKTKVE CCCCCCCCCCCCCCC	46.29	26074081
666	Phosphorylation	AGSPRRTSKKTKVEP CCCCCCCCCCCCCCC	30.28	26074081
670	Sumoylation	RRTSKKTKVEPYSLT CCCCCCCCCCCCCCC	54.18	-
670	Acetylation	RRTSKKTKVEPYSLT CCCCCCCCCCCCCCC	54.18	26051181
670	Sumoylation	RRTSKKTKVEPYSLT CCCCCCCCCCCCCCC	54.18	28112733
670	Ubiquitination	RRTSKKTKVEPYSLT CCCCCCCCCCCCCCC	54.18	21906983
674	Phosphorylation	KKTKVEPYSLTAQQS CCCCCCCCCCCHHHH	11.65	28152594
674 (in isoform 2)	Phosphorylation	-	11.65	-
675	Phosphorylation	KTKVEPYSLTAQQSS CCCCCCCCCCHHHHH	29.93	28152594
677	Phosphorylation	KVEPYSLTAQQSSLI CCCCCCCCHHHHHHH	19.24	28152594
682	Phosphorylation	SLTAQQSSLIREDKS CCCHHHHHHHHCCCH	24.39	24719451
692	Ubiquitination	REDKSNAKLWNEVLA HCCCHHHHHHHHHHH	59.28	21890473
692	Sumoylation	REDKSNAKLWNEVLA HCCCHHHHHHHHHHH	59.28	-
692	Ubiquitination	REDKSNAKLWNEVLA HCCCHHHHHHHHHHH	59.28	21906983
700	Phosphorylation	LWNEVLASLKDRPAS HHHHHHHHCCCCCCC	31.61	20068231
702	Ubiquitination	NEVLASLKDRPASGS HHHHHHCCCCCCCCC	49.55	-
705	Ubiquitination	LASLKDRPASGSPFQ HHHCCCCCCCCCCHH	40.69	21890473
705	Ubiquitination	LASLKDRPASGSPFQ HHHCCCCCCCCCCHH	40.69	21890473
705	Ubiquitination	LASLKDRPASGSPFQ HHHCCCCCCCCCCHH	40.69	21890473
707	Phosphorylation	SLKDRPASGSPFQLF HCCCCCCCCCCHHHH	42.35	30266825
709	Phosphorylation	KDRPASGSPFQLFLS CCCCCCCCCHHHHHH	21.75	30266825
716	Phosphorylation	SPFQLFLSKVEETFQ CCHHHHHHCHHHHHH	27.59	24732914
722	Phosphorylation	LSKVEETFQCICCQE HHCHHHHHHHEECCC	6.71	27251275
751	Phosphorylation	CKDCLDRSFRAQVFS CHHHHCHHHHHHEEE	20.82	27251275
764	Phosphorylation	FSCPACRYDLGRSYA EECCCCCCCCCCCHH	18.53	27251275

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
95	S	Phosphorylation	Kinase	CSNK1D	P48730	GPS
298	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
298	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
298	S	Phosphorylation	Kinase	PKA	-	Uniprot
311	S	Phosphorylation	Kinase	PIM1	P11309	PSP
639	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
661	S	Phosphorylation	Kinase	CDK2	P24941	PSP
674	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:23297342

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
298	S	Phosphorylation	15178447
Phosphorylation at Ser-298 of the linker region decreases the binding to H3K9me3.
639	S	Phosphorylation	17081983
Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.
639	S	Phosphorylation	17081983
Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents interaction with USP7 and subsequent deubiquitination.
639	S	ubiquitylation	17081983
Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.
639	S	ubiquitylation	17081983
Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents interaction with USP7 and subsequent deubiquitination.

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 UHRF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DNMT1_HUMAN	DNMT1	physical	17934516
HDAC1_HUMAN	HDAC1	physical	17934516
DNM3A_HUMAN	DNMT3A	physical	19798101
DNM3B_HUMAN	DNMT3B	physical	19798101
KAT5_HUMAN	KAT5	physical	19800870
DNMT1_HUMAN	DNMT1	physical	19800870
HDAC1_HUMAN	HDAC1	physical	19800870
EHMT2_HUMAN	EHMT2	physical	19056828
HDAC1_HUMAN	HDAC1	physical	15361834
URFB1_HUMAN	UHRF1BP1	physical	15361834
UBP7_HUMAN	USP7	physical	21745816
DNMT1_HUMAN	DNMT1	physical	21745816
UBP7_HUMAN	USP7	physical	21268065
DNMT1_HUMAN	DNMT1	physical	21268065
DNMT1_HUMAN	DNMT1	physical	21045206
H31_HUMAN	HIST1H3A	physical	22064703
TIF1B_HUMAN	TRIM28	physical	22055183
UBP7_HUMAN	USP7	physical	22411829
UBP11_HUMAN	USP11	physical	22411829
UHRF2_HUMAN	UHRF2	physical	22411829
HDAC1_HUMAN	HDAC1	physical	22411829
SUZ12_HUMAN	SUZ12	physical	22330138
EZH2_HUMAN	EZH2	physical	22330138
SUV91_HUMAN	SUV39H1	physical	22330138
H32_HUMAN	HIST2H3C	physical	22837395
PML_HUMAN	PML	physical	22945642
H32_HUMAN	HIST2H3C	physical	21489993
H31T_HUMAN	HIST3H3	physical	22100450
RB_HUMAN	RB1	physical	16007129
H32_HUMAN	HIST2H3C	physical	23022729
DNMT1_HUMAN	DNMT1	physical	20613874
ZPR1_HUMAN	ZPR1	physical	22939629
H31T_HUMAN	HIST3H3	physical	23161542
UHRF1_HUMAN	UHRF1	physical	23161542
UBP7_HUMAN	USP7	physical	23297342
FBW1A_HUMAN	BTRC	physical	23297342
CUL1_HUMAN	CUL1	physical	23297342
3MG_HUMAN	MPG	physical	23537643
KAT5_HUMAN	KAT5	physical	23677994
H31T_HUMAN	HIST3H3	physical	23752590
UBP7_HUMAN	USP7	physical	24013172
DNMT1_HUMAN	DNMT1	physical	24368767
DNMT1_HUMAN	DNMT1	physical	24782312
UHRF1_HUMAN	UHRF1	physical	24782312
H31_HUMAN	HIST1H3A	physical	17967883
UHRF1_HUMAN	UHRF1	physical	17967883
H31T_HUMAN	HIST3H3	physical	24813945
MBD4_HUMAN	MBD4	physical	25358258
MUS81_HUMAN	MUS81	physical	25818288
ERCC1_HUMAN	ERCC1	physical	25818288
XPF_HUMAN	ERCC4	physical	25818288
EME1_HUMAN	EME1	physical	25818288
TOP2A_HUMAN	TOP2A	physical	25451918
H31T_HUMAN	HIST3H3	physical	26065575
FBW1A_HUMAN	BTRC	physical	26768845
FBW1B_HUMAN	FBXW11	physical	26768845
UBP7_HUMAN	USP7	physical	26299963
UHRF1_HUMAN	UHRF1	physical	26299963
UB2D3_HUMAN	UBE2D3	physical	26299963
UBP7_HUMAN	USP7	physical	26046769
P53_HUMAN	TP53	physical	26102039
ANM5_HUMAN	PRMT5	physical	26597461
HS90A_HUMAN	HSP90AA1	physical	27489107
DNLI1_HUMAN	LIG1	physical	28803780
UBP7_HUMAN	USP7	physical	28803780
XRCC5_HUMAN	XRCC5	physical	28803780
MCM3_HUMAN	MCM3	physical	28803780
MSH2_HUMAN	MSH2	physical	28803780
SMCA5_HUMAN	SMARCA5	physical	28803780
MSH6_HUMAN	MSH6	physical	28803780
PRP8_HUMAN	PRPF8	physical	28803780
RSF1_HUMAN	RSF1	physical	28803780
CBX3_HUMAN	CBX3	physical	28803780
H2AY_HUMAN	H2AFY	physical	28803780
DNMT1_HUMAN	DNMT1	physical	28803780

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 UHRF1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399 AND LYS-546, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-76; SER-91; SER-287;SER-639 AND SER-707, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND MASSSPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND MASSSPECTROMETRY.	16964243 [Abstract]
"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-287 AND SER-639, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Phosphorylation of ICBP90 by protein kinase A enhances topoisomeraseIIalpha expression."; Trotzier M.-A., Bronner C., Bathami K., Mathieu E., Abbady A.-Q.,Jeanblanc M., Muller C.D., Rochette-Egly C., Mousli M.; Biochem. Biophys. Res. Commun. 319:590-595(2004). Cited for: PHOSPHORYLATION, PHOSPHORYLATION AT SER-298, AND MUTAGENESIS OFSER-298; SER-651 AND SER-666.	15178447 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-385, AND MASSSPECTROMETRY.	17370265 [Abstract]

show

show

show

show

show