about
Proteinase A YPL154CTransformation related protein 53Fibronectin 1Glyceraldehyde-3-phosphate dehydrogenaseCatenin (cadherin associated protein), beta 1SMAD family member 2Potassium voltage-gated channel, shaker-related subfamily, member 1Cyclin dependent kinase inhibitor 2AMyosin VATEA domain family member 2Gap junction protein, alpha 1Catenin beta 1DNA fragmentation factor subunit betaPeptidylprolyl isomerase like 1Heat shock protein 90 alpha family class A member 1BCL2 like 2Clathrin heavy chainFKBP prolyl isomerase 8RB transcriptional corepressor 1Gap junction protein alpha 5Heat shock protein family A (Hsp70) member 2Adaptor related protein complex 2 subunit alpha 2Heat shock protein HSP 90-alpha A2Putative heat shock protein HSP 90-alpha A4Heat shock protein family A (Hsp70) member 1BRibonucleotide reductase catalytic subunit M1Heat shock protein 90 alpha family class B member 1Kelch like ECH associated protein 1Siah E3 ubiquitin protein ligase 1ANuclear receptor coactivator 3Transformed mouse 3T3 cell double minute 2CREB-binding proteinCalmodulin 3Clathrin, heavy polypeptide (Hc)EzrinBCL2-like 2FK506 binding protein 8Heat shock protein 90, alpha (cytosolic), class A member 1Tumor suppressor ARFKelch-like ECH-associated protein 1
P680
The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signalingStructural and functional analysis of the YAP-binding domain of human TEAD2Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivatorsHSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptorsThe flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38)BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand bindingUnusual structural organization of the endocytic proteins AP180 and epsin 1Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered moleculeBim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targetsDisorder in a target for the smad2 mad homology 2 domain and its implications for binding and specificityNMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylationIntrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2Hsp72 recognizes a P binding motif in the measles virus N protein C-terminusA large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR
P921
Q12907949-034D408F-58A6-4FC7-9CF0-BFBCBF29CC01Q14818136-8C00FDD0-F963-4495-B295-075ED6AC896DQ14818136-CCBE77CE-1CD2-4D6D-9D53-D3343D8D89DFQ14819493-15473C8F-A09B-436F-9C0B-D0AEA1510C8DQ14890093-6DC70BA2-A4E4-40A3-ADEB-3523FFC07FD8Q14902827-98256744-231B-4012-8D2C-583D0ACB7EE4Q14903951-E2106FBC-8D5C-48E2-9C0D-FB3996968E40Q14905969-273F6DAA-A015-4D9C-90EB-799794A559D0Q14907028-A2ED4442-8536-426F-BD68-9E6E577CF066Q15320975-20907A2E-1B79-41FD-B40C-A43EF273E53CQ15330266-26D18105-2723-4A51-9DAE-EC1B88C9333EQ15330604-778D42E2-7E3E-4BF9-A534-CBC9CAF6A7F7Q1634046-37399A9F-108A-4F48-AF78-D72091C09250Q21101094-6B554DA0-CC34-4BED-B3F4-6CB3E1EF552DQ21106962-9917AD21-39E5-4CAE-9FCD-6A555824A463Q21108142-28BA9791-9192-45A1-B5E2-58A80B0229EBQ21108142-DCE95CE7-8C5B-4266-99EB-995593AE5AD2Q21109504-CB892D6A-F0C6-4257-8389-B586CAB2BA83Q21109804-8F5AE223-EEAC-48C4-9137-5E062287B02DQ21110123-E89ABCE2-A5F5-4342-A87C-A4ADD9FE3A59Q21111463-E242980D-6EF2-4329-97AA-0D343BF30D03Q21113152-E28926F7-C83C-43BD-95D3-569B2849FFA2Q21115440-9275A2ED-C22D-4D33-8DC0-87D2BDF5AF83Q21116548-029437DC-1881-46F0-88FB-CF9CBDC423AFQ21118358-CCFD2061-6BB6-4C2D-9FA6-F6EDB0053E79Q21118362-CF5369C6-424B-4599-8694-F342080DDF0CQ21119777-041730AC-489C-49EF-BCE1-EF0C4C11E04FQ21121233-2DABC61E-DBF2-4D6E-AF56-E7A29A335004Q21132860-C7BE75D6-AC3C-4EB8-9F68-587B7DF77CB3Q21173646-159CBF73-7920-4CC5-8E32-A1A481834BF6Q21425045-E05ED982-2EB9-4771-9C32-A8E8FBE17E29Q21436559-365B134A-DF56-4FCE-A78F-BB869E08F9D9Q21493890-415A3873-BC35-49C0-BF2E-7CB31314424FQ21494907-E810D708-1132-448C-ADC2-84216E7F4912Q21494929-D6D3F2A8-638C-4B7F-B535-757F03E37DE7Q21495098-DD67F520-3BC7-4648-88BE-D581BBC53257Q21496347-61A17D88-BAF7-4A45-B801-7C2A86F3DAD9Q21497052-A37472B9-B8B8-4925-B650-DCA41827BF39Q21498439-94390EF8-E441-449D-AFA0-312E3D43A930Q21498917-392AD12E-89E8-4C07-9419-DBBB1F996503
P680
Q24322710-DF5CD8CE-840B-4786-9528-1BD1FB96D16DQ24623055-C911944E-3D91-4840-8D9D-9267DCBE4BC6Q24629962-D2D66A0F-7775-4892-9A12-D1BBFCA8D3F1Q27637572-BAF5E469-0A98-4249-83E3-435FB98D748DQ28215191-C2D3B4D3-AF3C-41FD-B8F2-90237B686239Q28236916-62881BBF-005D-4E13-AAC0-361B5ED7BE4EQ28902813-2E807009-A82C-4EE2-AA5E-8F137AA99A20Q28909703-20C5783C-46DF-4E69-BC3E-84B55142EAD5Q28909814-7E5F8450-C4D0-4006-AA9B-53EE1C8A0497Q28910218-A2509E76-E089-4280-B6F5-27F12FCCD226Q28910316-87D3396B-0051-4C8B-9D3A-D40AD0856D10Q28910317-CCC2887B-1CD0-473C-8171-08EE4C67AE5DQ28910370-3F4480ED-5F41-4658-9853-25F96C8A2093Q28910411-CF770E4D-1624-4471-AB76-B29FF5B5B41EQ28910448-A145324D-2E88-4F39-9035-8A99FDB32173
P921
description
Interacting selectively and non-covalently with a disordered domain of a protein.
@en
moleculaire functie
@nl
name
disordered domain specific binding
@en
type
label
disordered domain specific binding
@en
altLabel
GO:0097718
@en
prefLabel
disordered domain specific binding
@en
P2888
P686
GO:0097718