about
Cyclin dependent kinase 1Minichromosome maintenance complex component 6Integrin linked kinaseInsulin degrading enzymeGephyrinATM serine/threonine kinaseTransformation related protein 53N-ethylmaleimide sensitive fusion proteinGlycyl-tRNA synthetaseGlucokinaseInsulin receptorCystic fibrosis transmembrane conductance regulatorHeat shock protein 1 (chaperonin)Heat shock protein 1 (chaperonin 10)ATP-binding cassette, sub-family B (MDR/TAP), member 1APyruvate dehydrogenase kinase, isoenzyme 1Ataxia telangiectasia mutatedPotassium inwardly-rectifying channel, subfamily J, member 1C-abl oncogene 1, non-receptor tyrosine kinaseUbiquitin-like modifier activating enzyme 1Minichromosome maintenance complex component 6Mechanistic target of rapamycin kinaseMyosin, heavy polypeptide 7, cardiac muscle, betaRibonuclease L (2', 5'-oligoisoadenylate synthetase-dependent)Erb-b2 receptor tyrosine kinase 2Glutamate dehydrogenase 1Werner syndrome RecQ like helicaseATPase, Cu++ transporting, alpha polypeptideLymphocyte protein tyrosine kinasePhosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alphaPhosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit deltaGuanylate cyclase 2cHeat shock protein 8Neurotrophic tyrosine kinase, receptor, type 1Neurotrophic tyrosine kinase, receptor, type 2Neurotrophic tyrosine kinase, receptor, type 3Insulin-like growth factor I receptorV-raf-leukemia viral oncogene 1Bone morphogenetic protein receptor, type 1AActivin A receptor, type IC
P680
The nature of the catalytic domain of 2'-5'-oligoadenylate synthetasesCharacterization of the ATPase cycle of human ABCA1: implications for its function as a regulator rather than an active transporterHelicase structure and mechanismIntegrity of ATP binding site is essential for effective inhibition of the intrinsic apoptosis pathway by NAIPThe distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104FFunctional analysis of disease-causing mutations in human galactokinaseRegulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligandsCrystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complexSelective and ATP-dependent translocation of peptides by the homodimeric ATP binding cassette transporter TAP-like (ABCB9)Kinetic mechanism of AKT/PKB enzyme familyMolecular mechanism for ATP-dependent closure of the K+ channel Kir6.2Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutationsAML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localizationHuman p53 directs DNA strand reassociation and is photolabelled by 8-azido ATPStructural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4aAF10 is split by MLL and HEAB, a human homolog to a putative Caenorhabditis elegans ATP/GTP-binding protein in an invins(10;11)(p12;q23q12)Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activityTwo classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteinsNeuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-BHuman erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteinsCloning of a new kinesin-related gene located at the centromeric end of the human MHC regionApoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-activated protein kinase kinase kinase in a heteromeric complex with ASK1Insights into the evolution of divergent nucleotide-binding mechanisms among pseudokinases revealed by crystal structures of human and mouse MLKLStructural basis for an inositol pyrophosphate kinase surmounting phosphate crowdingVaricelloviruses avoid T cell recognition by UL49.5-mediated inactivation of the transporter associated with antigen processingA robust methodology to subclassify pseudokinases based on their nucleotide-binding properties.Structural basis for MTR4-ZCCHC8 interactions that stimulate the MTR4 helicase in the nuclear exosome-targeting complex.The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs
P921
Q1147372-EDB39129-3E3E-4D07-9D61-57EB3807E9D6Q1154611-9C419075-F8A2-4F2A-BFEB-33A83B3626C8Q11913806-CD62B195-D280-483E-ACDA-A6A3A93784CBQ1225690-29398F36-6664-4E3E-AD93-0BDB8466046DQ1270676-259A3990-D9BF-4403-AE24-CEAD0C871325Q141591-16725782-F233-4D53-8225-E59F02B138D7Q14818136-CE2ACEFD-8687-4961-A2C8-E41D9A7BDD79Q14818136-FD298884-51C1-4F7F-B667-A0E81A5F30ACQ14860414-6526D1A5-CB76-48DF-BB42-76D1DE3C013FQ14861872-967F308F-C140-4806-BF03-1033C6417918Q14863086-7E62BD07-BF53-4ED2-B81F-9081083FD81FQ14863366-129509D9-B351-49C1-A4F5-C1537B31B746Q14864718-F910F668-9B0B-491B-9C3B-973255D8B01AQ14865001-4FF246B5-8D5C-4EFF-A42F-C704C97BCA6CQ14865009-11F63F49-F2E7-45D9-8DCB-311407D982ADQ14865107-16E19DB8-58C4-496C-A86C-8CFEF536415CQ14865386-A8535987-05A8-425A-AF53-AA639B0F762AQ14865386-ED52573D-7F6A-4141-BE22-5994F738C2F0Q14872812-5592A54C-CF1A-472D-B073-2AA4006E849FQ14873958-00F12829-FEDF-4104-99E8-4418C32F3B88Q14874000-045F81AF-4F1D-430B-BA47-B07BAB52B66EQ14874539-DDD95298-E8BC-4A3E-BAAA-7C315E843134Q14875032-6EB261DE-AA2F-4B5F-8E3E-F943B859AA55Q14876092-EFFC2554-2CA2-432D-8A6A-A25EF63394EEQ14876111-8C19AEFA-D865-448A-A33E-2C033BDFA9A8Q14877436-D20EBDFB-F032-4A63-8ACD-F116F58E7D4CQ14877504-5B05216C-034E-4178-BE92-43BA3F812099Q14878318-D665207B-85C5-4780-9D5B-7D472C0F29B8Q14883757-87FBAA28-7464-4723-9CCA-9B8C0C951A68Q14884615-A11A1D20-4B64-491F-BC70-BC5DF4DF8E50Q14885208-F88DC950-8B53-4099-89F6-8EE9A65BBD1BQ14887711-66F8AEFC-EE4A-48A0-B5D2-AC5D0B7FDD88Q14887753-D3DDBFBC-45D9-45D8-BC50-0EAFC0AF98D9Q14888940-1B7F236B-2431-4078-8758-E1890FA84CAFQ14888957-3CE118C9-2BEC-4B77-AAE4-5113C1EC8AB1Q14888957-3FC31B81-4F16-4562-B0C0-A9D4FDEB05DDQ14901156-162DF234-4BC8-4EDF-A31E-C8AAC9232EB9Q14901163-0C03423C-32E0-4AB3-9221-1A520C579B9AQ14901301-E0D365CF-7344-4C02-999F-DBBDA2F9ACB6Q14901460-FEBEAAF4-442A-4BBB-ADA9-1C10512C69B7
P680
Q22010488-7C1AA611-B1EC-45F3-9EA4-FFFB5EA7560DQ24291886-56EB0DDD-4625-4BF7-9093-3E2857E40042Q24292281-2BAFD0B9-80A2-4448-B77B-D25C9B9A3F7CQ24294723-63CDEF40-00EF-40F5-8926-07990533D873Q24297174-0AAC01F2-3F6C-4C89-9997-89D46078181AQ24299794-8B0B24BE-280A-4812-94FA-6053CCA7F237Q24300555-C6DBFA98-42E5-49E9-92C8-A56136284677Q24301004-5691E77E-43C5-4E1E-8FA8-A4E5205E253AQ24301098-599EA1F2-DF4A-4625-88F9-711C44241F87Q24307898-FBA1CC27-F783-4B34-9268-458C778BC102Q24308180-3E56E912-4633-4A6B-8804-CE8D2A4EBA97Q24310820-C4F998AF-6772-4A77-B54D-48A5027F1DABQ24311698-10E864AA-0D54-411D-AA85-E9679D39BBFCQ24314287-800CCC80-DF57-4936-AB6D-90C408E5840FQ24316348-1AD94BDA-FCC6-418A-8EE2-0A77EAC7ABF8Q24317047-5053E344-6D2E-44DD-8E91-4DCA9A55D6C1Q24317423-D147F685-2879-4E40-99D2-4D350CDB6F4CQ24317609-0249E8AF-5A2E-4974-B2E8-F8A8DC04C620Q24322418-AA753AD8-9863-438F-AA0C-D7014A548905Q24324103-32381FE9-DBAB-4C80-B6B0-7474ECFA0354Q24324402-4A38B307-FAE3-4417-9558-F061C1D9AC32Q24338868-F5626AF2-B556-402B-A274-1C426E43489EQ24339564-BF144ED8-25F0-4890-94B3-217B1007BD7DQ27675827-20BE2014-CFB7-4F0B-8146-72AC77B0AA37Q28115772-B160F0B1-AC7E-420E-A394-7580F26BE5D5Q34376382-79C18811-FDB8-4E3F-898F-6F249DE2C35EQ55339687-515BFBB8-4A1B-4609-8B59-92B95C453880Q92265654-AA9C2092-ACF2-4CB5-907D-B6BA331FA466
P921
description
Interacting selectively and no ...... coenzyme and enzyme regulator.
@en
moleculaire functie
@nl
name
ATP binding
@en
ATP-Bindung
@de
ATP-binding
@nl
liaison ATP
@fr
АТФ-связанные
@ru
קשירת ATP
@he
type
label
ATP binding
@en
ATP-Bindung
@de
ATP-binding
@nl
liaison ATP
@fr
АТФ-связанные
@ru
קשירת ATP
@he
altLabel
GO:0005524
@en
prefLabel
ATP binding
@en
ATP-Bindung
@de
ATP-binding
@nl
liaison ATP
@fr
АТФ-связанные
@ru
קשירת ATP
@he
P279
P2888
P686
GO:0005524