about
Selectin, plateletVery low density lipoprotein receptorCeroid lipofuscinosis, neuronal 3, juvenile (Batten, Spielmeyer-Vogt disease)Mannan binding lectin serine peptidase 1Mannan-binding lectin serine peptidase 2Mannose-binding lectin (protein C) 2ANXA1Annexin A1Annexin A2Myosin VAVery low density lipoprotein receptorCalsequestrin 2C-type lectin domain family 4 member MSperm acrosome associated 9Deleted in malignant brain tumors 1S100 calcium binding protein BS100 calcium binding protein PTroponin I3, cardiac typeS100 calcium binding protein A4Programmed cell death 6ALG2 alpha-1,3/1,6-mannosyltransferaseProgrammed cell death 6 interacting proteinTumor susceptibility 101Copine 3Complexin 2S100 calcium binding protein A6VPS37B subunit of ESCRT-IVPS37C subunit of ESCRT-ISEC31 homolog A, COPII coat complex componentMyosin IDSolute carrier family 9 member A1Syntaxin 2Neurexin 1Synaptotagmin 6Synaptotagmin 8Troponin C2, fast skeletal typeTroponin C1, slow skeletal and cardiac typeRNA binding motif protein 22Synapsin IS100P binding protein
P680
Cloning of gp-340, a putative opsonin receptor for lung surfactant protein DS100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivoALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent mannerALG-2 oscillates in subcellular localization, unitemporally with calcium oscillationsDC-SIGN and L-SIGN are high affinity binding receptors for hepatitis C virus glycoprotein E2Identification and characterization of the acidic pH binding sites for growth regulatory ligands of low density lipoprotein receptor-related protein-1Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1Calsequestrin mutant D307H exhibits depressed binding to its protein targets and a depressed response to calciumNuclear translocation of the calcium-binding protein ALG-2 induced by the RNA-binding protein RBM22Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolinsIdentification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutantsThe penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1VPS37 isoforms differentially modulate the ternary complex formation of ALIX, ALG-2, and ESCRT-ICharacterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2Overexpression of human cardiac troponin-I and troponin-C in Escherichia coli and their purification and characterisation. Two point mutations allow high-level expression of troponin-IExpression of S100P and its novel binding partner S100PBPR in early pancreatic cancerPenta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101
P921
Q14881076-E3FC76C6-D918-4738-8628-3D000890163DQ14901298-98927504-4BFD-442C-B0E2-7BC6D0CE5F3CQ14905130-7483900F-38D5-4985-995C-5FA92086B5F3Q14905310-0052CCEA-4F39-4952-B045-62753DCA5FF1Q14905316-FB101679-D856-4E28-B7A8-005E4DA23B8DQ14907668-61C94D6F-E4E7-4C18-9855-E035600A1622Q14908222-8E627304-C5E0-4953-9650-D1C6FAB056EFQ14908226-9495D99A-D4B1-469D-8D0E-32DD91D6BBD2Q14908226-C88381D3-CA4A-4868-97AE-ED9DA2FAD949Q14908237-85FE5DB7-E464-40BC-A54F-0CF07200A5CDQ15320975-8638E0B7-BD0D-4049-9D89-3BCD3B8C9D1FQ1979313-E4854588-E795-4346-AC2B-EAA55110BC50Q21100532-11284F50-A2A7-4D66-B4CA-46E6FD218898Q21100841-F24E34E5-9ED0-4BBE-968B-FC69CA622669Q21102397-D35EE8B7-E05F-4509-935D-5B4ED18FDD60Q21102654-2355EB81-8CC5-4009-A049-DA86218394B5Q21108021-7D4FA0B6-369E-4038-B898-1CB758C45F6EQ21108519-75C5EEDA-DB74-4A24-BB4A-129812D8BFF1Q21108986-EA136A41-D7DA-42ED-9FD5-51D2DC109FF0Q21109469-A6B92E56-B4DE-4DC0-B548-FC6B608E67C2Q21112089-C690F284-2861-41F8-A7FB-BAEA41016DCFQ21113862-314020AC-6F7E-400B-BAA4-CB3368C063B7Q21114029-E6624F6B-8F56-489E-8F82-BCC92B60C37DQ21114033-8A57A5BF-B8F5-4226-A365-CB66E6AAC656Q21115687-CC0F71EE-DCB2-4A88-9795-0D83EF59D501Q21115695-85C41D93-9BDD-424F-A30D-C064EFA7384AQ21115897-B0369360-C35C-4A98-BF0A-F6CF7BB2EF22Q21116285-DBB4E954-E249-43C7-9EA6-4E03E864DD9CQ21116313-37CC1303-4328-471C-A44D-536AF0108DF5Q21119692-C1016E65-3683-4228-9F7D-E21E409B4FC5Q21120909-C52BFFE1-D9EC-42B1-B264-3D4300CAE689Q21120909-CED251F8-AF7B-4124-B670-2871255807C4Q21123415-ADAB5277-8149-47CC-9227-81A34ECBEF0AQ21123906-DC60B869-1784-4410-80CC-CEAF98960B6BQ21124095-BD76D9F0-B493-4757-AB92-74D6145DB498Q21124597-27D5519A-1B4C-45A7-A209-D88FB4488937Q21124601-E0F28110-0186-4986-99F0-3861818A7397Q21124635-6841A5BF-C27A-4F2D-89B2-FAAF3E3AC7FDQ21124649-6F2F9D21-2D05-44C6-AEA3-03700968B4BAQ21124649-8CD2A6CD-D476-4813-B938-D9C24EBBE3FC
P680
Q22010373-60690349-2C28-458E-8523-6ACB4F47C9B5Q22010373-DE071D0E-66F2-46D8-A021-358F31A3303CQ22254674-B83D2BD4-9E4B-4046-8C18-18E4EB725724Q24292416-765EB17B-0586-4A18-BE00-147CFEEF1A47Q24292758-14BF6B48-74B9-4048-A017-11B5B5A54ED4Q24296260-EA3BA76E-C8C6-4575-B088-C96F44BB01C5Q24298175-609136C4-B6C6-4FDF-9A4E-95E8B5B6C73FQ24306198-2C2A046E-B248-40BB-B397-8AE1F7F70FE9Q24306830-F6BF894D-2955-4451-AAAB-DA18E5078F44Q24307334-46FFA929-A3FA-48AC-8975-FFE08C6AA9BCQ24309206-1F96EC8D-7776-4CC0-A7EA-95BEBF6DA6F4Q24311319-B750C733-E13A-41C6-A71C-B0BA0C7CC5E2Q24313774-37170002-F6B2-482B-A1B7-CD114A9597BBQ24315984-8D2E5DEC-C79A-48B7-A426-343CC314A806Q24317280-6A6A4DA4-5941-4A09-A65F-094F7F2CC951Q24336634-630EC75B-D03E-465D-9EC2-BBC38F298046Q24337345-BB81F467-550E-42DB-BF01-7CEE0C68F544Q24337744-5D87EB1F-5E54-422C-82DF-EEBD9FB482E0
P921
description
Interacting selectively and no ...... ), in the presence of calcium.
@en
moleculaire functie
@nl
name
calcium-dependent protein binding
@en
type
label
calcium-dependent protein binding
@en
altLabel
GO:0048306
@en
prefLabel
calcium-dependent protein binding
@en
P279
P2888
P686
GO:0048306