about
Insulin degrading enzymeUbiquitin carboxy-terminal hydrolase L1Parkin RBR E3 ubiquitin protein ligaseChemokine (C-X-C motif) receptor 4SMAD family member 3Heat shock protein 1Nucleoporin 62Nucleoporin 62FA core complex associated protein 20F-box protein 7Golgi associated, gamma adaptin ear containing, ARF binding protein 3Ubiquitin conjugating enzyme E2 L6Tripartite motif containing 32RAD23 homolog A, nucleotide excision repair proteinOTU deubiquitinase, ubiquitin aldehyde binding 2Sequestosome 1NBR1 autophagy cargo receptorNEDD4 E3 ubiquitin protein ligaseMembrane associated ring-CH-type finger 7BUB3 mitotic checkpoint proteinSirtuin 2Ubiquitin protein ligase E3 component n-recognin 5DNA topoisomerase II alphaTNF alpha induced protein 3Target of myb1 like 1 membrane trafficking proteinRing finger protein 185UBX domain protein 7Phospholipase A2 activating proteinAdhesion regulating molecule 1Baculoviral IAP repeat containing 2OTU deubiquitinase, ubiquitin aldehyde binding 1UBA domain containing 2UBX domain protein 2BUbiquitin specific peptidase 5Zinc finger AN1-type containing 2BDNA damage inducible 1 homolog 2DNA damage inducible 1 homolog 1F-box and WD repeat domain containing 7Tumor susceptibility 101UBX domain protein 11
P680
Ubiquitin-specific protease-like 1 (USPL1) is a SUMO isopeptidase with essential, non-catalytic functionsSpartan/C1orf124 is important to prevent UV-induced mutagenesisProliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a regulator of translesion synthesisRole for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycleDVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA damageCXC chemokine receptor 4 is a cell surface receptor for extracellular ubiquitinSolution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitinInteractions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnoverUBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnoverLigand-dependent ubiquitination of Smad3 is regulated by casein kinase 1 gamma 2, an inhibitor of TGF-beta signalingISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitinUbiquitin dimers control the hydrolase activity of UCH-L3Regulation of MITF stability by the USP13 deubiquitinaseIdentification of polyubiquitin binding proteins involved in NF-kappaB signaling using protein arraysThe solution structure of the ZnF UBP domain of USP33/VDU1Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylationHuman DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog.Ubiquitin regulates GGA3-mediated degradation of BACE1
P921
Q1225690-88C25399-9F71-4F1D-85A1-D06888D22133Q14864242-D8FAC99C-CD4F-4530-A433-853D805BAEB7Q14864264-6F8CF0B2-88A8-4871-9099-DD244F88E439Q14874287-1B32A14B-CC2A-4359-8D12-002594630677Q14903978-38CC699F-224B-4520-93C4-169CA8B99814Q14905265-38DE6678-2E23-4528-A762-F0099A4AF233Q15316702-89D88D41-8253-45B3-88F6-18C090DA42D1Q15316702-B6CE685A-91E0-4C07-A79F-312B4607FB2EQ15316762-F2E885C0-081D-43AB-9A2C-4599491CC9EAQ21101278-477647C5-D4A3-4A09-A8C8-69D0816635BAQ21101386-5B4CD6B1-1FB3-4E20-A012-E47502C781FBQ21101608-9651F098-2B43-4FF9-B518-1AAC7100A351Q21101900-D5B38702-0BEE-46F8-9801-723FECB2202FQ21104807-681EF9ED-CCF7-477E-A522-9EBE05A3ACDBQ21105151-9BB94430-5B62-4D1F-8AD1-76E2D3EA5188Q21105278-937B6937-567B-4CDD-81CD-A695084694A4Q21106590-AF25C9EF-5487-4673-931C-6CAD095E906BQ21106591-0930C4CE-174F-4277-BBE3-FB2219F30C58Q21106591-3F473304-9EF2-45ED-8031-6396B1221650Q21107331-03CE4A67-9128-4AF7-8E50-4D1D7ACFD622Q21108016-310E9D47-3ACF-44F4-8CE8-4A000BABC97AQ21108016-3C9A58C8-A0AE-4C0E-BF90-692EF92F3AE1Q21108016-87CEFEF1-F0E6-4CAD-892B-56B2AA0CB7B4Q21108280-A5E486C3-C7AC-4BA7-A2EB-1DEC8E241392Q21108304-1ACE88DC-5E55-4F65-B93B-843116D400DBQ21108475-41411E06-589C-411E-BCF4-C744A3D5ACB1Q21108482-AC0D9137-0C22-4030-B95D-13FB1C931001Q21109230-6777FBEE-C053-4E69-BE51-668AA2B5DB74Q21109784-98EC68BE-6D9C-4967-8854-0C4995C73A00Q21110686-2DA9CE09-028C-4DD4-87F6-F2DA29581FE1Q21111016-ABE2BE08-663A-4237-A6B7-9974FB895D3AQ21111101-23E4D86F-F947-4FE7-A412-114238BD03DEQ21111101-E0BFC781-9452-4D45-B069-14DF82FCC5F5Q21111230-7BDB2D71-F001-4928-B0C5-85DB2F8AE78EQ21111704-FE8FA7D6-14FD-4898-BFD4-E15B06AE6882Q21111725-584DDEF6-3A22-4968-8002-6BED97BEE5E2Q21111725-901E2944-7C59-43C0-945B-D11436E8543BQ21111819-2D99DEB0-04C1-487C-A7CA-E12420780A50Q21112056-2B851317-1E00-4A21-BE50-069A3FC49105Q21112093-AFF87653-A833-4871-85DA-D79119962A66
P680
Q24295247-9848D3C7-2CBB-44D7-95AC-3A8DA7243795Q24296499-13773489-F78B-43E7-8336-C5ACD3C063E6Q24296912-40AD6615-9B62-4060-83E6-3ED35715F889Q24299947-8A6BF874-1D78-4608-BAC4-C167E43647BCQ24300408-675EB789-23CC-42A4-97F6-C1ACB0325573Q24302660-93D78822-ACB0-4267-99ED-2C58B9A8EA60Q24306397-13ABC2A1-C9EE-4AB6-8C7B-1A31E86F3385Q24309203-788424EB-3E7B-4AFB-A061-0EDC32426731Q24310742-9EE4A5AF-53DF-4334-9A8B-4E105235C8DCQ24313188-6378E621-8FC7-4A45-A61E-0BB8610FA30FQ24317640-3151564E-47FB-41C3-B050-273045BFE0CFQ24318689-DB715B45-B8E0-4C4C-BF2B-D723BEFBE83FQ24318832-C20CFD8C-DAB0-4F83-BAF8-BAC63E609804Q24321446-A3186D20-1ABC-42DF-89BD-8EFB79843C94Q24338879-9B454A1B-910C-4CE8-92AB-6B5351D20977Q24563471-0A48980F-9D11-4983-A1DD-E69F66416CB1Q30668626-CDD07055-2D3B-43A8-ABEA-748B0C73CA99Q34025306-EDB4274D-462F-4B3C-9394-6B6DFC3265EB
P921
description
Interacting selectively and no ...... m for proteolytic degradation.
@en
moleculaire functie
@nl
name
ubikvitinbinding
@nn
ubiquitin binding
@en
type
label
ubikvitinbinding
@nn
ubiquitin binding
@en
altLabel
GO:0043130
@en
prefLabel
ubikvitinbinding
@nn
ubiquitin binding
@en
P2888
P686
GO:0043130