UB2Q2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UB2Q2_HUMAN
• UniProt AC: Q8WVN8
• Protein Name: Ubiquitin-conjugating enzyme E2 Q2
• Gene Name: UBE2Q2
• Organism: Homo sapiens (Human).
• Sequence Length: 375
• Subcellular Localization: Cytoplasm .
• Protein Description: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination..
• Protein Sequence: MSVSGLKAELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPPLTLHCNITESYPSSSPIWFVDSEDPNLTSVLERLEDTKNNNLLRQQLKWLICELCSLYNLPKHLDVEMLDQPLPTGQNGTTEEVTSEEEEEEEEMAEDIEDLDHYEMKEEEPISGKKSEDEGIEKENLAILEKIRKTQRQDHLNGAVSGSVQASDRLMKELRDIYRSQSYKTGIYSVELINDSLYDWHVKLQKVDPDSPLHSDLQILKEKEGIEYILLNFSFKDNFPFDPPFVRVVLPVLSGGYVLGGGALCMELLTKQGWSSAYSIESVIMQINATLVKGKARVQFGANKNQYNLARAQQSYNSIVQIHEKNGWYTPPKEDG

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
2	Phosphorylation	------MSVSGLKAE ------CCCHHHHHH	25.62	22798277
7	Ubiquitination	-MSVSGLKAELKFLA -CCCHHHHHHHHHHH	43.25	33845483
11	Ubiquitination	SGLKAELKFLASIFD HHHHHHHHHHHHHHH	29.82	33845483
142	Ubiquitination	EVTSEEEEEEEEMAE CCCCHHHHHHHHHHH	74.18	29967540
161	Ubiquitination	LDHYEMKEEEPISGK HCCCCCCCCCCCCCC	67.30	29967540
166	Phosphorylation	MKEEEPISGKKSEDE CCCCCCCCCCCCCCC	56.10	29759185
170	Phosphorylation	EPISGKKSEDEGIEK CCCCCCCCCCCCCCH	54.49	25849741
177	Ubiquitination	SEDEGIEKENLAILE CCCCCCCHHHHHHHH	50.40	29967540
224	Phosphorylation	YRSQSYKTGIYSVEL HHCCCCCCCEEEEEE	22.15	29978859
227	Phosphorylation	QSYKTGIYSVELIND CCCCCCEEEEEEECC	14.17	29978859
228	Phosphorylation	SYKTGIYSVELINDS CCCCCEEEEEEECCC	13.75	29978859
235	Phosphorylation	SVELINDSLYDWHVK EEEEECCCCEEEEEE	25.08	29978859
237	Phosphorylation	ELINDSLYDWHVKLQ EEECCCCEEEEEEEE	22.42	29978859
273	Phosphorylation	EYILLNFSFKDNFPF EEEEEEEECCCCCCC	30.25	24719451
354	Phosphorylation	NLARAQQSYNSIVQI HHHHHHHHHHHHEEE	17.75	23312004
355	Phosphorylation	LARAQQSYNSIVQIH HHHHHHHHHHHEEEH	14.48	23312004
357	Phosphorylation	RAQQSYNSIVQIHEK HHHHHHHHHEEEHHH	18.86	23312004
368	Phosphorylation	IHEKNGWYTPPKEDG EHHHCCCCCCCCCCC	15.69	30257219
369	Phosphorylation	HEKNGWYTPPKEDG- HHHCCCCCCCCCCC-	26.97	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of UB2Q2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UB2Q2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of UB2Q2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCGF2_HUMAN	PCGF2	physical	19690564
RN111_HUMAN	RNF111	physical	19549727
MYO1C_HUMAN	MYO1C	physical	16300736
DREB_HUMAN	DBN1	physical	16300736
GELS_HUMAN	GSN	physical	16300736
ANM5_HUMAN	PRMT5	physical	16300736
MEP50_HUMAN	WDR77	physical	16300736
ARPC2_HUMAN	ARPC2	physical	16300736
CAPZB_HUMAN	CAPZB	physical	16300736
ARPC4_HUMAN	ARPC4	physical	16300736
ACTG_HUMAN	ACTG1	physical	16300736
UB2Q2_HUMAN	UBE2Q2	physical	20061386

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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 THR-369, AND MASSSPECTROMETRY.
PubMed: 18669648