about
Synuclein, alphaPlasminogen activator, tissueMechanistic target of rapamycin kinaseGrowth factor receptor bound protein 2FK506 binding protein 4Erythrocyte membrane protein band 4.1Transient receptor potential cation channel, subfamily V, member 1Insulin-like growth factor 2 receptorPlatelet-activating factor acetylhydrolase, isoform 1b, subunit 1LYN proto-oncogene, Src family tyrosine kinaseAprataxinPlatelet activating factor acetylhydrolase 1b regulatory subunit 1Insulin like growth factor 2 receptorArrestin 3Polycystin 2, transient receptor potential cation channelS-antigen visual arrestinPIH1 domain containing 1URI1 prefoldin like chaperonePaired like homeodomain 2Chromobox 4Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein betaArrestin beta 1Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein epsilonSRC proto-oncogene, non-receptor tyrosine kinaseTANK binding kinase 1RB transcriptional corepressor 1Casein kinase 1 gamma 2LDL receptor related protein 11Protein kinase C substrate 80K-HUbiquitin associated and SH3 domain containing BThyroid hormone receptor associated protein 3Peptidylprolyl cis/trans isomerase, NIMA-interacting 1Ras related GTP binding AMidline 2Transducin beta like 2StratifinG protein regulated inducer of neurite outgrowth 1Midline 1PHD finger protein 6TOX high mobility group box family member 3
P680
MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disordersPhosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicingInteraction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducersThe plasminogen activation system in bovine milk: differential localization of tissue-type plasminogen activator and urokinase in milk fractions is caused by binding to casein and urokinase receptorFunctional specialization of beta-arrestin interactions revealed by proteomic analysisPRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradationIsomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites.
P921
Q14862284-625DED72-C0B8-4D03-B9CC-A3D14571C422Q14863050-08221F17-0FBB-4819-9EF2-108A4D391A9BQ14876092-20BE62A9-FDE0-40D8-91A2-CA27FCDBF3FBQ14905190-DDA11148-D445-4C04-914F-2C1E5C9CBD01Q14907981-E87E6E6F-7E0A-4E7F-87AE-25F8B37AF8A6Q14908150-7A7105A5-224D-448D-A687-4DF44449698AQ14908176-3F783141-97D8-46FC-93DD-A0F959A8E8BFQ14911789-74DC014D-05DB-4498-968E-472B6BEF74CCQ14911789-F9780CCE-6CE5-4C2D-A8F8-6FFFEFE0D269Q15319474-57E5354F-90B9-47BC-A6C5-7127FCBB67ABQ15331919-67446A30-5E5D-43F1-A1FC-7E90096D09CEQ15996558-C3AAF14B-52DD-4BA0-A32D-0F1B3F0BCD50Q1982330-51E10D94-CCA6-490C-B1DC-15178A946DE6Q2005191-A743B615-4124-4EAB-9E66-7B38CA91CD62Q2005191-CDA49503-3276-42FE-8BFE-13FA6F9FE494Q2005191-DDE4B07C-E1B7-46F2-B4ED-06D91D5C1A38Q21102030-884F7BAC-B243-4874-9A91-EA9BB02853FDQ21103321-5A3D9772-5269-4A35-B425-3D6C2D571EDAQ21105252-12DB1E64-EA4E-447E-B10D-91EC54ABF72EQ21107252-47B57494-60EF-4340-BEBB-6CAE2DD84D2BQ21108139-EEBD100C-C407-45E1-B227-785370180152Q21108503-57E83FF0-8C85-4704-8990-2E7CE69B41D2Q21109155-8778DC6A-3E76-4A6D-B59B-0A93D630EF0BQ21109244-82632ED8-C56F-4DB7-8A97-A8BED1794DD4Q21109259-257C329C-E4DF-46E2-BA52-311F60BDFEF4Q21109282-9B52EC68-42CC-46A2-8242-6ED6AFE1AFD3Q21109354-85C3BDF5-236E-48A7-BECB-B6724EA39973Q21111280-29A2CB8B-C549-45E6-8512-129F9AD92BCEQ21111463-2B28AE13-D533-4DC5-8D5C-EFB2A8601717Q21111521-17B25C18-4D79-4A43-9667-EFAAC9F8CD1BQ21113607-E080650A-EAE2-4A07-90DD-178AB70EC133Q21114617-6ED5B9E4-233D-4CEF-9C8A-6D1ABF329783Q21115617-A74D9FD7-068D-43E6-B94B-BA83C75B3E70Q21116038-C889E4E4-89C3-4CB2-822D-9057A82EBC0DQ21116190-6BAAD134-AF0F-4504-9558-4B911D8BEE8BQ21119361-5B684D5E-D627-47BE-9F39-04F7C52DEA44Q21122244-38ECD91C-E5DC-418D-AA25-DA699942537FQ21124609-6B3AE704-BDC3-43F7-AA63-8A8763B793B3Q21131010-11D9177E-2BE5-433C-AB76-DA38C404C184Q21132249-C668031C-0D9A-40C7-BA6F-DCFBE1F4020B
P680
Q21284182-D36117DF-328D-4B36-B2DB-1B4C8AF838AEQ24302148-2C4E47A5-3237-40A4-9AF7-482143BD6A0FQ24313249-C3A673CC-2B29-4821-BC52-5DC6624C9D5DQ24314562-BB4E4461-48CC-4644-AE83-46B9CD6B2965Q24318455-F403DAC9-8A2A-4AB3-8D27-06EEE8A4E731Q24321394-54384797-6448-4912-823A-845D62714E21Q41115192-BFF803B0-4D5E-416C-80F2-B2D79BE8557F
P921
description
Interacting selectively and non-covalently with a phosphorylated protein.
@en
moleculaire functie
@nl
name
phosphoprotein binding
@en
type
label
phosphoprotein binding
@en
altLabel
GO:0051219
@en
phosphorylated protein binding
@en
prefLabel
phosphoprotein binding
@en
P279
P2888
P686
GO:0051219