UB2R2_HUMAN - dbPTM
UB2R2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UB2R2_HUMAN
UniProt AC Q712K3
Protein Name Ubiquitin-conjugating enzyme E2 R2
Gene Name UBE2R2
Organism Homo sapiens (Human).
Sequence Length 238
Subcellular Localization
Protein Description Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin..
Protein Sequence MAQQQMTSSQKALMLELKSLQEEPVEGFRITLVDESDLYNWEVAIFGPPNTLYEGGYFKAHIKFPIDYPYSPPTFRFLTKMWHPNIYENGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMFRKWRDSKGKDKEYAEIIRKQVSATKAEAEKDGVKVPTTLAEYCIKTKVPSNDNSSDLLYDDLYDDDIDDEDEEEEDADCYDDDDSGNEES
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
2Acetylation------MAQQQMTSS
------CCHHHCHHH		18.85-
7Phosphorylation-MAQQQMTSSQKALM
-CCHHHCHHHHHHHH		22.3823401153
8PhosphorylationMAQQQMTSSQKALML
CCHHHCHHHHHHHHH		25.9823401153
9PhosphorylationAQQQMTSSQKALMLE
CHHHCHHHHHHHHHH		26.9124043423
11UbiquitinationQQMTSSQKALMLELK
HHCHHHHHHHHHHHH		45.4923000965
14SulfoxidationTSSQKALMLELKSLQ
HHHHHHHHHHHHHHC		3.0621406390
18UbiquitinationKALMLELKSLQEEPV
HHHHHHHHHHCCCCC		39.481890473
59UbiquitinationLYEGGYFKAHIKFPI
EEECCEEEEEEECCC		30.4823000965
63UbiquitinationGYFKAHIKFPIDYPY
CEEEEEEECCCCCCC		34.9123000965
63AcetylationGYFKAHIKFPIDYPY
CEEEEEEECCCCCCC		34.9125953088
80UbiquitinationPTFRFLTKMWHPNIY
CCHHHHHHHCCCCCC		41.9821963094
99UbiquitinationVCISILHPPVDDPQS
EEEEEECCCCCCCCC		27.4522817900
104UbiquitinationLHPPVDDPQSGELPS
ECCCCCCCCCCCCCC		26.2722817900
108UbiquitinationVDDPQSGELPSERWN
CCCCCCCCCCCCCCC		63.8627667366
111PhosphorylationPQSGELPSERWNPTQ
CCCCCCCCCCCCCCH		53.0424719451
119UbiquitinationERWNPTQNVRTILLS
CCCCCCHHHHHHHHH		27.9323000965
121UbiquitinationWNPTQNVRTILLSVI
CCCCHHHHHHHHHHH		24.4923000965
128UbiquitinationRTILLSVISLLNEPN
HHHHHHHHHHHCCCC		1.8422817900
130UbiquitinationILLSVISLLNEPNTF
HHHHHHHHHCCCCCC		4.0124816145
133UbiquitinationSVISLLNEPNTFSPA
HHHHHHCCCCCCCCC		39.6422817900
137UbiquitinationLLNEPNTFSPANVDA
HHCCCCCCCCCCCCH		11.9327667366
138UbiquitinationLNEPNTFSPANVDAS
HCCCCCCCCCCCCHH		22.5122817900
144UbiquitinationFSPANVDASVMFRKW
CCCCCCCHHHHHHHH		10.3522817900
148UbiquitinationNVDASVMFRKWRDSK
CCCHHHHHHHHHCCC		7.3323000965
149UbiquitinationVDASVMFRKWRDSKG
CCHHHHHHHHHCCCC		21.3822817900
150UbiquitinationDASVMFRKWRDSKGK
CHHHHHHHHHCCCCC		35.0023000965
153UbiquitinationVMFRKWRDSKGKDKE
HHHHHHHCCCCCCHH		54.2927667366
157AcetylationKWRDSKGKDKEYAEI
HHHCCCCCCHHHHHH		70.1725953088
157UbiquitinationKWRDSKGKDKEYAEI
HHHCCCCCCHHHHHH		70.17-
159UbiquitinationRDSKGKDKEYAEIIR
HCCCCCCHHHHHHHH		56.9933845483
164UbiquitinationKDKEYAEIIRKQVSA
CCHHHHHHHHHHHHH		2.5523000965
166UbiquitinationKEYAEIIRKQVSATK
HHHHHHHHHHHHHCH		29.0823000965
166MethylationKEYAEIIRKQVSATK
HHHHHHHHHHHHHCH		29.08115919293
167UbiquitinationEYAEIIRKQVSATKA
HHHHHHHHHHHHCHH		44.6421906983
173UbiquitinationRKQVSATKAEAEKDG
HHHHHHCHHHHHHCC		43.9022817900
178UbiquitinationATKAEAEKDGVKVPT
HCHHHHHHCCCCCCC		67.8233845483
182UbiquitinationEAEKDGVKVPTTLAE
HHHHCCCCCCCHHHH		48.2932015554
185PhosphorylationKDGVKVPTTLAEYCI
HCCCCCCCHHHHHHH		37.1129978859
186O-linked_GlycosylationDGVKVPTTLAEYCIK
CCCCCCCHHHHHHHH		20.2128657654
186PhosphorylationDGVKVPTTLAEYCIK
CCCCCCCHHHHHHHH		20.2129978859
190PhosphorylationVPTTLAEYCIKTKVP
CCCHHHHHHHHCCCC		8.2228796482
193UbiquitinationTLAEYCIKTKVPSND
HHHHHHHHCCCCCCC		38.4423000965
194PhosphorylationLAEYCIKTKVPSNDN
HHHHHHHCCCCCCCC		19.8426074081
195UbiquitinationAEYCIKTKVPSNDNS
HHHHHHCCCCCCCCC		47.3423000965
198PhosphorylationCIKTKVPSNDNSSDL
HHHCCCCCCCCCCCC		60.8626074081
202PhosphorylationKVPSNDNSSDLLYDD
CCCCCCCCCCCCCHH		28.2626074081
203PhosphorylationVPSNDNSSDLLYDDL
CCCCCCCCCCCCHHH		38.2326074081
207PhosphorylationDNSSDLLYDDLYDDD
CCCCCCCCHHHCCCC		18.08-
211PhosphorylationDLLYDDLYDDDIDDE
CCCCHHHCCCCCCCC		25.0728348404
228PhosphorylationEEEDADCYDDDDSGN
HHHCCCCCCCCCCCC		23.9728348404
233PhosphorylationDCYDDDDSGNEES--
CCCCCCCCCCCCC--		50.9812037680
238PhosphorylationDDSGNEES-------
CCCCCCCC-------		39.0718669648
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
233SPhosphorylationKinaseCSNK2A1P68400
GPS
233SPhosphorylationKinaseCK2-FAMILY-GPS
233SPhosphorylationKinaseCK2-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UB2R2_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 UB2R2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBW1A_HUMANBTRCphysical
12037680
R113B_HUMANRNF113Bphysical
19549727
ARI2_HUMANARIH2physical
19549727
CBLC_HUMANCBLCphysical
19549727
DTX3L_HUMANDTX3Lphysical
19549727
DZIP3_HUMANDZIP3physical
19549727
INF2_HUMANINF2physical
21900206
PLPL2_HUMANPNPLA2physical
21900206
GDIR1_HUMANARHGDIAphysical
21900206
FBXW5_HUMANFBXW5physical
21900206
TLS1_HUMANC9orf78physical
22863883
NUBP2_HUMANNUBP2physical
22863883
RD23A_HUMANRAD23Aphysical
22863883
1433S_HUMANSFNphysical
22863883
UBR7_HUMANUBR7physical
22863883
WDR4_HUMANWDR4physical
22863883
1433E_HUMANYWHAEphysical
22863883
1433G_HUMANYWHAGphysical
22863883
1433F_HUMANYWHAHphysical
22863883
UBC_HUMANUBCphysical
21900206
UB2R2_HUMANUBE2R2physical
20061386
UB2D2_HUMANUBE2D2physical
26344197
UBC_HUMANUBCphysical
27044868
CTNB1_HUMANCTNNB1physical
27044868
RBX1_HUMANRBX1physical
27044868
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 UB2R2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzymeUBC3B induces its interaction with beta-TrCP and enhances beta-catenindegradation.";
Semplici F., Meggio F., Pinna L.A., Oliviero S.;
Oncogene 21:3978-3987(2002).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, INTERACTIONWITH BTRC, PHOSPHORYLATION AT SER-233, AND MUTAGENESIS OF CYS-93;LEU-97 AND SER-233.

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