dbPTM

UB2R1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UB2R1_HUMAN
UniProt AC	P49427
Protein Name	Ubiquitin-conjugating enzyme E2 R1
Gene Name	CDC34
Organism	Homo sapiens (Human).
Sequence Length	236
Subcellular Localization	Cytoplasm. Nucleus. The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase.
Protein Description	Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. [PubMed: 22496338 Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgamma and ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin. Is target of human herpes virus 1 protein ICP0, leading to ICP0-dependent dynamic interaction with proteasomes]
Protein Sequence	MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEEADSCFGDDEDDSGTEES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Ubiquitination	PLVPSSQKALLLELK CCCCHHHHHHHHHHC	42.84	21906983
18	Ubiquitination	KALLLELKGLQEEPV HHHHHHHCCCCCCCC	48.47	21906983
63	Ubiquitination	GYFKARLKFPIDYPY CEEEEEEECCCCCCC	43.47	21906983
68	Phosphorylation	RLKFPIDYPYSPPAF EEECCCCCCCCCHHH	12.56	20068231
70	Phosphorylation	KFPIDYPYSPPAFRF ECCCCCCCCCHHHHH	27.81	20068231
71	Phosphorylation	FPIDYPYSPPAFRFL CCCCCCCCCHHHHHH	21.65	20068231
80	Ubiquitination	PAFRFLTKMWHPNIY HHHHHHHHHCCCCCC	41.98	-
89	Phosphorylation	WHPNIYETGDVCISI CCCCCCCCCCEEEEE	23.01	-
111	Phosphorylation	PQSGELPSERWNPTQ CCCCCCCCCCCCCCH	53.04	24719451
150	Ubiquitination	DASVMYRKWKESKGK CHHHHHHHHHHHCCC	45.17	PubMed
157	Ubiquitination	KWKESKGKDREYTDI HHHHHCCCCHHHHHH	58.30	-
162	Phosphorylation	KGKDREYTDIIRKQV CCCCHHHHHHHHHHH	18.90	-
166	Methylation	REYTDIIRKQVLGTK HHHHHHHHHHHHCCC	24.56	-
167	Ubiquitination	EYTDIIRKQVLGTKV HHHHHHHHHHHCCCC	34.06	-
182	Ubiquitination	DAERDGVKVPTTLAE CCCCCCCCCCCHHHH	48.29	-
185	Phosphorylation	RDGVKVPTTLAEYCV CCCCCCCCHHHHHHH	37.11	29978859
186	O-linked_Glycosylation	DGVKVPTTLAEYCVK CCCCCCCHHHHHHHH	20.21	28657654
186	Phosphorylation	DGVKVPTTLAEYCVK CCCCCCCHHHHHHHH	20.21	29978859
190	Phosphorylation	VPTTLAEYCVKTKAP CCCHHHHHHHHCCCC	9.27	29978859
193	Ubiquitination	TLAEYCVKTKAPAPD HHHHHHHHCCCCCCC	40.52	-
203	Phosphorylation	APAPDEGSDLFYDDY CCCCCCCCCCCCCCC	29.15	17461777
207	Phosphorylation	DEGSDLFYDDYYEDG CCCCCCCCCCCCCCC	18.40	26074081
222	Phosphorylation	EVEEEADSCFGDDED CCCCCHHHHCCCCCC	20.56	17461777
231	Phosphorylation	FGDDEDDSGTEES-- CCCCCCCCCCCCC--	60.99	12037680
233	Phosphorylation	DDEDDSGTEES---- CCCCCCCCCCC----	40.30	16123592
236	Phosphorylation	DDSGTEES------- CCCCCCCC-------	39.01	12037680

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
162	T	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
203	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
203	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
203	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
203	S	Phosphorylation	Kinase	CK2	-	Uniprot
222	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
222	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
222	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
222	S	Phosphorylation	Kinase	CK2	-	Uniprot
231	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
231	S	Phosphorylation	Kinase	CK2	-	Uniprot
231	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
231	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
233	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
233	T	Phosphorylation	Kinase	CK2	-	Uniprot
233	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
233	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
236	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
236	S	Phosphorylation	Kinase	CK2	-	Uniprot
236	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
236	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	SAG	P10523	PMID:10851089

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UB2R1_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 UB2R1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSK2B_HUMAN	CSNK2B	physical	11546811
FBW1A_HUMAN	BTRC	physical	12037680
FBW1A_HUMAN	BTRC	physical	10531035
FBXW2_HUMAN	FBXW2	physical	10531035
FBX7_HUMAN	FBXO7	physical	10531035
FBXL3_HUMAN	FBXL3	physical	10531035
FBX4_HUMAN	FBXO4	physical	10531035
CDN1B_HUMAN	CDKN1B	physical	19123975
ATF5_HUMAN	ATF5	physical	18458088
CUL1_HUMAN	CUL1	physical	16123592
RBX1_HUMAN	RBX1	physical	16123592
ICP0_HHV11	RL2	physical	12060736
RBX1_HUMAN	RBX1	physical	20663873
PIM1_HUMAN	PIM1	physical	20663873
IKBA_HUMAN	NFKBIA	physical	20347421
UBC_HUMAN	UBC	physical	20353940
CORO7_HUMAN	CORO7	physical	21130766
HIF1A_HUMAN	HIF1A	physical	15611064
TF65_HUMAN	RELA	physical	14690596
UB2R1_HUMAN	CDC34	physical	16210246
CUL1_HUMAN	CUL1	physical	18851830
CDN1B_HUMAN	CDKN1B	physical	22748924
UB2R1_HUMAN	CDC34	physical	8576261
HINT1_HUMAN	HINT1	physical	19112177
RBX1_HUMAN	RBX1	physical	19112177
TBL1X_HUMAN	TBL1X	physical	14980219
ZFAN6_HUMAN	ZFAND6	physical	11054541
UBC_HUMAN	UBC	physical	22496338
SKP2_HUMAN	SKP2	physical	17785450
CUL3_HUMAN	CUL3	physical	19256485
UBC_HUMAN	UBC	physical	22959436
RD23A_HUMAN	RAD23A	physical	22863883
UBC_HUMAN	UBC	physical	24316736
RBX1_HUMAN	RBX1	physical	24316736
UBI4P_YEAST	UBI4	physical	2842867
UB2R1_HUMAN	CDC34	physical	20061386
UBC_HUMAN	UBC	physical	24912152
SDCB1_HUMAN	SDCBP	physical	25416956
SIAH1_HUMAN	SIAH1	physical	25416956
ING4_HUMAN	ING4	physical	23624912
CUL1_HUMAN	CUL1	physical	25425648
CUL2_HUMAN	CUL2	physical	25425648
UBC_HUMAN	UBC	physical	23801757
CREM_HUMAN	CREM	physical	10373550
ATF5_HUMAN	ATF5	physical	10373550
CUL1_HUMAN	CUL1	physical	27001857
RBX1_HUMAN	RBX1	physical	27001857
RBX1_HUMAN	RBX1	physical	27910872
UB2D3_HUMAN	UBE2D3	physical	27910872

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 UB2R1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Cdc34 C-terminal tail phosphorylation regulates Skp1/cullin/F-box(SCF)-mediated ubiquitination and cell cycle progression."; Sadowski M., Mawson A., Baker R., Sarcevic B.; Biochem. J. 405:569-581(2007). Cited for: PHOSPHORYLATION AT SER-203; SER-222 AND SER-231, AND FUNCTION.	17461777 [Abstract]
"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: ENZYME ACTIVITY, FUNCTION, INTERACTION WITH BTRC, PHOSPHORYLATION ATSER-231, AND MUTAGENESIS OF CYS-93; LEU-97 AND SER-231.	12037680 [Abstract]
"Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, bycasein kinase 2."; Block K., Boyer T.G., Yew P.R.; J. Biol. Chem. 276:41049-41058(2001). Cited for: INTERACTION WITH CSNK2B, PHOSPHORYLATION AT SER-203; SER-222; SER-231;THR-233 AND SER-236, MUTAGENESIS OF SER-203; SER-222; SER-231; THR-233AND SER-236, AND SUBCELLULAR LOCATION.	11546811 [Abstract]