UHRF2_HUMAN - dbPTM
UHRF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UHRF2_HUMAN
UniProt AC Q96PU4
Protein Name E3 ubiquitin-protein ligase UHRF2
Gene Name UHRF2
Organism Homo sapiens (Human).
Sequence Length 802
Subcellular Localization Nucleus . Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 (By similarity)..
Protein Description E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131..
Protein Sequence MWIQVRTIDGSKTCTIEDVSRKATIEELRERVWALFDVRPECQRLFYRGKQLENGYTLFDYDVGLNDIIQLLVRPDPDHLPGTSTQIEAKPCSNSPPKVKKAPRVGPSNQPSTSARARLIDPGFGIYKVNELVDARDVGLGAWFEAHIHSVTRASDGQSRGKTPLKNGSSCKRTNGNIKHKSKENTNKLDSVPSTSNSDCVAADEDVIYHIQYDEYPESGTLEMNVKDLRPRARTILKWNELNVGDVVMVNYNVESPGQRGFWFDAEITTLKTISRTKKELRVKIFLGGSEGTLNDCKIISVDEIFKIERPGAHPLSFADGKFLRRNDPECDLCGGDPEKKCHSCSCRVCGGKHEPNMQLLCDECNVAYHIYCLNPPLDKVPEEEYWYCPSCKTDSSEVVKAGERLKMSKKKAKMPSASTESRRDWGRGMACVGRTRECTIVPSNHYGPIPGIPVGSTWRFRVQVSEAGVHRPHVGGIHGRSNDGAYSLVLAGGFADEVDRGDEFTYTGSGGKNLAGNKRIGAPSADQTLTNMNRALALNCDAPLDDKIGAESRNWRAGKPVRVIRSFKGRKISKYAPEEGNRYDGIYKVVKYWPEISSSHGFLVWRYLLRRDDVEPAPWTSEGIERSRRLCLRLQYPAGYPSDKEGKKPKGQSKKQPSGTTKRPISDDDCPSASKVYKASDSAEAIEAFQLTPQQQHLIREDCQNQKLWDEVLSHLVEGPNFLKKLEQSFMCVCCQELVYQPVTTECFHNVCKDCLQRSFKAQVFSCPACRHDLGQNYIMIPNEILQTLLDLFFPGYSKGR
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 Orthologous
Protein Cluster
12AcetylationVRTIDGSKTCTIEDV
EEEECCCCEEEHHHH
53.8223954790
12UbiquitinationVRTIDGSKTCTIEDV
EEEECCCCEEEHHHH
53.8229967540
22UbiquitinationTIEDVSRKATIEELR
EHHHHHCCCCHHHHH
42.2329967540
42UbiquitinationLFDVRPECQRLFYRG
HHHCCHHHHHHHCCC
2.9421890473
83PhosphorylationDPDHLPGTSTQIEAK
CCCCCCCCCCEEEEE
27.0223312004
84PhosphorylationPDHLPGTSTQIEAKP
CCCCCCCCCEEEEEE
24.9923312004
85PhosphorylationDHLPGTSTQIEAKPC
CCCCCCCCEEEEEEC
33.1428111955
93PhosphorylationQIEAKPCSNSPPKVK
EEEEEECCCCCCCCC
49.2025159151
95PhosphorylationEAKPCSNSPPKVKKA
EEEECCCCCCCCCCC
26.7025159151
99UbiquitinationCSNSPPKVKKAPRVG
CCCCCCCCCCCCCCC
10.6921890473
108PhosphorylationKAPRVGPSNQPSTSA
CCCCCCCCCCCCCCH
42.01-
112PhosphorylationVGPSNQPSTSARARL
CCCCCCCCCCHHHHH
25.8223403867
113PhosphorylationGPSNQPSTSARARLI
CCCCCCCCCHHHHHC
32.8423403867
114PhosphorylationPSNQPSTSARARLID
CCCCCCCCHHHHHCC
21.7923403867
128UbiquitinationDPGFGIYKVNELVDA
CCCCCEEEHHHEECH
36.34-
130UbiquitinationGFGIYKVNELVDARD
CCCEEEHHHEECHHH
32.5024816145
187UbiquitinationHKSKENTNKLDSVPS
CCCCCCCCCCCCCCC
55.2524816145
238SumoylationPRARTILKWNELNVG
HHHHHHEECCCCCCC
44.09-
249UbiquitinationLNVGDVVMVNYNVES
CCCCCEEEEEECCCC
1.3021890473
290PhosphorylationVKIFLGGSEGTLNDC
EEEEECCCCCCCCCC
30.93-
292UbiquitinationIFLGGSEGTLNDCKI
EEECCCCCCCCCCEE
36.8822817900
295UbiquitinationGGSEGTLNDCKIISV
CCCCCCCCCCEEEEH
53.0921890473
307UbiquitinationISVDEIFKIERPGAH
EEHHHEEEECCCCCC
49.6829967540
309UbiquitinationVDEIFKIERPGAHPL
HHHEEEECCCCCCCC
54.1121890473
312UbiquitinationIFKIERPGAHPLSFA
EEEECCCCCCCCCCC
42.6222817900
322UbiquitinationPLSFADGKFLRRNDP
CCCCCCCCCCCCCCC
41.6023000965
322 (in isoform 1)Ubiquitination-41.6021890473
322 (in isoform 2)Ubiquitination-41.6021890473
337UbiquitinationECDLCGGDPEKKCHS
CCCCCCCCHHCCCCC
33.2124816145
349UbiquitinationCHSCSCRVCGGKHEP
CCCCCCEECCCCCCC
4.1122817900
352UbiquitinationCSCRVCGGKHEPNMQ
CCCEECCCCCCCCCE
24.0321890473
366UbiquitinationQLLCDECNVAYHIYC
EEECCCCCCEEEEEE
21.2921890473
369UbiquitinationCDECNVAYHIYCLNP
CCCCCCEEEEEECCC
5.6222817900
393UbiquitinationYWYCPSCKTDSSEVV
CEECCCCCCCHHHHH
60.7629967540
401SumoylationTDSSEVVKAGERLKM
CCHHHHHHHHHHHHC
56.71-
401UbiquitinationTDSSEVVKAGERLKM
CCHHHHHHHHHHHHC
56.71-
401SumoylationTDSSEVVKAGERLKM
CCHHHHHHHHHHHHC
56.71-
410UbiquitinationGERLKMSKKKAKMPS
HHHHHCCHHCCCCCC
55.5924816145
417PhosphorylationKKKAKMPSASTESRR
HHCCCCCCCCCHHHH
31.2127134283
422PhosphorylationMPSASTESRRDWGRG
CCCCCCHHHHHHCCC
32.4827134283
428MethylationESRRDWGRGMACVGR
HHHHHHCCCCCCCCC
27.71115919525
447PhosphorylationTIVPSNHYGPIPGIP
EEECCCCCCCCCCCC
28.93-
482 (in isoform 2)Phosphorylation-43.8122210691
487PhosphorylationGRSNDGAYSLVLAGG
CCCCCCCEEEEEECC
14.2027642862
499UbiquitinationAGGFADEVDRGDEFT
ECCCCCCCCCCCCEE
6.6422817900
502UbiquitinationFADEVDRGDEFTYTG
CCCCCCCCCCEEEEC
34.0421890473
510PhosphorylationDEFTYTGSGGKNLAG
CCEEEECCCCCCCCC
36.2521815630
516UbiquitinationGSGGKNLAGNKRIGA
CCCCCCCCCCCCCCC
28.9821890473
519UbiquitinationGKNLAGNKRIGAPSA
CCCCCCCCCCCCCCH
44.4622817900
548UbiquitinationCDAPLDDKIGAESRN
CCCCCCCCCCCCCCC
42.5832015554
548AcetylationCDAPLDDKIGAESRN
CCCCCCCCCCCCCCC
42.5826051181
572UbiquitinationIRSFKGRKISKYAPE
EEECCCCCCCCCCCC
61.0622817900
575 (in isoform 1)Ubiquitination-49.2421890473
575UbiquitinationFKGRKISKYAPEEGN
CCCCCCCCCCCCCCC
49.2422817900
584PhosphorylationAPEEGNRYDGIYKVV
CCCCCCCCCCHHHHH
23.63-
588PhosphorylationGNRYDGIYKVVKYWP
CCCCCCHHHHHHHCH
11.85-
589 (in isoform 1)Ubiquitination-38.3321890473
589UbiquitinationNRYDGIYKVVKYWPE
CCCCCHHHHHHHCHH
38.3327667366
592UbiquitinationDGIYKVVKYWPEISS
CCHHHHHHHCHHHHH
44.5833845483
637PhosphorylationRLCLRLQYPAGYPSD
HHHHHHCCCCCCCCC
10.3123403867
641PhosphorylationRLQYPAGYPSDKEGK
HHCCCCCCCCCCCCC
11.1523403867
643PhosphorylationQYPAGYPSDKEGKKP
CCCCCCCCCCCCCCC
53.4822115753
645UbiquitinationPAGYPSDKEGKKPKG
CCCCCCCCCCCCCCC
73.1033845483
654PhosphorylationGKKPKGQSKKQPSGT
CCCCCCCCCCCCCCC
50.95-
659PhosphorylationGQSKKQPSGTTKRPI
CCCCCCCCCCCCCCC
46.4026074081
661PhosphorylationSKKQPSGTTKRPISD
CCCCCCCCCCCCCCC
33.2226074081
662PhosphorylationKKQPSGTTKRPISDD
CCCCCCCCCCCCCCC
28.6926074081
663UbiquitinationKQPSGTTKRPISDDD
CCCCCCCCCCCCCCC
56.8929967540
667PhosphorylationGTTKRPISDDDCPSA
CCCCCCCCCCCCCCH
37.3629255136
673PhosphorylationISDDDCPSASKVYKA
CCCCCCCCHHHEEHH
52.0523927012
675PhosphorylationDDDCPSASKVYKASD
CCCCCCHHHEEHHCC
27.3023927012
676AcetylationDDCPSASKVYKASDS
CCCCCHHHEEHHCCC
49.6625953088
676UbiquitinationDDCPSASKVYKASDS
CCCCCHHHEEHHCCC
49.6629967540
679UbiquitinationPSASKVYKASDSAEA
CCHHHEEHHCCCHHH
44.3929967540
681PhosphorylationASKVYKASDSAEAIE
HHHEEHHCCCHHHHH
28.1327251275
683PhosphorylationKVYKASDSAEAIEAF
HEEHHCCCHHHHHHH
26.0525849741
708UbiquitinationREDCQNQKLWDEVLS
HHHHHCCHHHHHHHH
60.1229967540

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 UHRF2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UHRF2_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 UHRF2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNP_HUMANPCNPphysical
14741369
HDAC1_HUMANHDAC1physical
15361834
CDK1_HUMANCDK1physical
21952639
CDK2_HUMANCDK2physical
21952639
CDK4_HUMANCDK4physical
21952639
CDK6_HUMANCDK6physical
21952639
PCNA_HUMANPCNAphysical
21952639
RB_HUMANRB1physical
21952639
P53_HUMANTP53physical
21952639
MCL1_HUMANMCL1physical
21952639
B2CL1_HUMANBCL2L1physical
21952639
BAX_HUMANBAXphysical
21952639
CTNB1_HUMANCTNNB1physical
21952639
FYN_HUMANFYNphysical
21952639
LCK_HUMANLCKphysical
21952639
LYN_HUMANLYNphysical
21952639
BCAR1_HUMANBCAR1physical
21952639
RAD51_HUMANRAD51physical
21952639
HDAC1_HUMANHDAC1physical
21952639
TYY1_HUMANYY1physical
21952639
JAK3_HUMANJAK3physical
21952639
CD27_HUMANCD27physical
21952639
PTPRC_HUMANPTPRCphysical
21952639
SKP1_HUMANSKP1physical
21952639
CCNA2_HUMANCCNA2physical
21952639
CCND1_HUMANCCND1physical
21952639
CCNB1_HUMANCCNB1physical
21952639
CCNE1_HUMANCCNE1physical
21952639
H31_HUMANHIST1H3Aphysical
22064703
PCNP_HUMANPCNPphysical
12176013
CDK2_HUMANCDK2physical
15178429
CCNE1_HUMANCCNE1physical
15178429
UB2D1_HUMANUBE2D1physical
21952639
UB2D1_HUMANUBE2D1physical
14741369
ZN131_HUMANZNF131physical
23404503
UBC9_HUMANUBE2Iphysical
23404503
3MG_HUMANMPGphysical
23537643
E2F1_HUMANE2F1physical
23833190
UHRF2_HUMANUHRF2physical
14741369
ZN618_HUMANZNF618physical
27129234
PARP1_HUMANPARP1physical
27129234
HS71L_HUMANHSPA1Lphysical
27129234
XRCC5_HUMANXRCC5physical
27129234
UBP7_HUMANUSP7physical
27129234
XRCC6_HUMANXRCC6physical
27129234
KAT5_HUMANKAT5physical
27743347
HDAC1_HUMANHDAC1physical
27743347
H31_HUMANHIST1H3Aphysical
28004105
UBP7_HUMANUSP7physical
27114453
GUAA_HUMANGMPSphysical
27114453
RFA1_HUMANRPA1physical
27114453
DNMT1_HUMANDNMT1physical
27114453
HDAC1_HUMANHDAC1physical
27114453
CD11B_HUMANCDK11Bphysical
27114453
BCLF1_HUMANBCLAF1physical
27114453
CD11A_HUMANCDK11Aphysical
27114453
KIF4A_HUMANKIF4Aphysical
27114453
CHD3_HUMANCHD3physical
27114453
CUL4B_HUMANCUL4Bphysical
27114453
CTBP2_HUMANCTBP2physical
27114453
CDC73_HUMANCDC73physical
27114453
PCNA_HUMANPCNAphysical
27114453
CHERP_HUMANCHERPphysical
27114453
PSMD5_HUMANPSMD5physical
27114453
PUF60_HUMANPUF60physical
27114453
P66B_HUMANGATAD2Bphysical
27114453
LC7L2_HUMANLUC7L2physical
27114453
FANCI_HUMANFANCIphysical
27114453
MSH3_HUMANMSH3physical
27114453
ERCC2_HUMANERCC2physical
27114453
CNDG2_HUMANNCAPG2physical
27114453
DIDO1_HUMANDIDO1physical
27114453
MRE11_HUMANMRE11Aphysical
27114453
CNDD3_HUMANNCAPD3physical
27114453
SUZ12_HUMANSUZ12physical
27114453
CAF1B_HUMANCHAF1Bphysical
27114453
LC7L3_HUMANLUC7L3physical
27114453
RCOR1_HUMANRCOR1physical
27114453
KDM2A_HUMANKDM2Aphysical
27114453
ATR_HUMANATRphysical
27114453
FACD2_HUMANFANCD2physical
27114453
MBD3_HUMANMBD3physical
27114453
COT2_HUMANNR2F2physical
27114453
CDC16_HUMANCDC16physical
27114453
CHD8_HUMANCHD8physical
27114453
PB1_HUMANPBRM1physical
27114453
EHMT2_HUMANEHMT2physical
27114453
RB_HUMANRB1physical
27114453
EED_HUMANEEDphysical
27114453
FXL18_HUMANFBXL18physical
27114453
KDM4B_HUMANKDM4Bphysical
27114453
BRD3_HUMANBRD3physical
27114453
CHD2_HUMANCHD2physical
27114453
TLK1_HUMANTLK1physical
27114453
ZN574_HUMANZNF574physical
27114453
BTAF1_HUMANBTAF1physical
27114453
TF7L2_HUMANTCF7L2physical
27114453
TFAP4_HUMANTFAP4physical
27114453
BMI1_HUMANBMI1physical
27114453
PCNP_HUMANPCNPphysical
27114453
PIN1_HUMANPIN1physical
27114453
UB2D3_HUMANUBE2D3physical
27114453

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 UHRF2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-667, AND MASSSPECTROMETRY.

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