About: heme binding

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.

Attributes	Values
rdf:type	Item
description	Heme bindend (nl) Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring. (en)
exact match	wds:Q14358516-1F9D178B-F39B-4C29-A36F-AD9EA4D80057
exact match	http://purl.obolibrary.org/obo/GO_0020037
rdfs:label	Heme binding (nl) Häm-bindend (de) heme bindin (sco) heme binding (en) hæm binding (da) vezava hema (sl) ヘム結合 (ja)
skos:prefLabel	Heme binding (nl) Häm-bindend (de) heme bindin (sco) heme binding (en) hæm binding (da) vezava hema (sl) ヘム結合 (ja)
name	Heme binding (nl) Häm-bindend (de) heme bindin (sco) heme binding (en) hæm binding (da) vezava hema (sl) ヘム結合 (ja)
Gene Ontology ID	wds:Q14358516-45C3BD91-C1CF-44E9-AEDC-851FD0097061
Gene Ontology ID	GO:0020037
instance of	wds:Q14358516-EDFB81A4-C5B8-4366-8DAB-B2327918F4CC
instance of	molecular function
subclass of	wds:Q14358516-60E526EF-A8AD-4033-9FCA-928D1AC83BB3
subclass of	tetrapyrrole binding
has part(s)	wds:Q14358516-3DDB35D6-0D57-4EDE-BE37-7BCDEB04DD1D
has part(s)	heme
skos:altLabel	GO:0020037 (en) Häm-bindende (de) Häm-bindender (de) Häm-bindendes (de) haem binding (en) hæm-bindende (da)
UMLS CUI	wds:Q14358516-50EAE923-7BB8-4A09-91BE-5808BE28CB1A
UMLS CUI	C1148616
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q14358516
is part of of	heme
is part of of	wds:Q189621-C3A966DB-365E-4E54-9E8B-058655A89B0A
is main subject of	Heme controls the regulation of protein tyrosine kinases Jak2 and Src Cytochrome c in the apoptotic and antioxidant cascades Structural characterization of the complex between alpha-naphthoflavone and human cytochrome P450 1B1 Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates The BTB and CNC homology 1 (BACH1) target genes are involved in the oxidative stress response and in control of the cell cycle Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins Structural basis of drug binding to CYP46A1, an enzyme that controls cholesterol turnover in the brain Binding of a Cyano- and Fluoro-containing Drug Bicalutamide to Cytochrome P450 46A1: UNUSUAL FEATURES AND SPECTRAL RESPONSE cDNA cloning of human retinoic acid-metabolizing enzyme (hP450RAI) identifies a novel family of cytochromes P450 Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen Crystal structure of a cytochrome P450 2B6 genetic variant in complex with the inhibitor 4-(4-chlorophenyl)imidazole at 2.0-A resolution Structure of the human lung cytochrome P450 2A13 Analysis of Oligomerization Properties of Heme a Synthase Provides Insights into Its Function in Eukaryotes. Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2 Crystal structure of human cytochrome P450 2D6 Identification of a mammalian mitochondrial porphyrin transporter Structural basis of human CYP51 inhibition by antifungal azoles Identification of thromboxane synthase amino acid residues involved in heme-propionate binding Human Cytochrome P450 21A2, the Major Steroid 21-Hydroxylase: STRUCTURE OF THE ENZYME·PROGESTERONE SUBSTRATE COMPLEX AND RATE-LIMITING C-H BOND CLEAVAGE Structural characterization of human cytochrome P450 2C19: active site differences between P450s 2C8, 2C9, and 2C19 Crystal structure of the human prostacyclin synthase Structures of Prostacyclin Synthase and Its Complexes with Substrate Analog and Inhibitor Reveal a Ligand-specific Heme Conformation Change The Fowler syndrome-associated protein FLVCR2 is an importer of heme Structure of tetragonal crystals of human erythrocyte catalase The molecular basis of transient heme-protein interactions: analysis, concept and implementation Functional expression and characterization of human 101F6 protein, a homologue of cytochrome b561 and a candidate tumor suppressor gene product
is main subject of	wds:Q24301823-5A96B002-33BA-4F7E-A87C-DDAC396676E3 wds:Q24313478-FD130F4A-146F-43E1-9C6E-24026E4E35C7 wds:Q24305008-D3DE0C7B-E8BD-49AE-81E9-27FD9D1F05F7 wds:Q24297785-FF7194E9-E559-4AEC-9F9D-7D59DE8142D8 wds:Q24299075-C5EC0FB1-2D4A-4F29-B503-8ADF3DCBAFA7 wds:Q27675738-62334FF6-F66C-4232-ADAB-8D8F81919DBF wds:Q28138838-3598CD12-7CF7-41CD-BE2C-E1E87F331997 wds:Q28117252-6D9BA506-3C7C-4ECE-828E-9A50B46453D2 wds:Q24318445-BF40995E-D08E-438E-B7FD-A5DFCCE6D7CA wds:Q24298998-921214E4-B801-417A-BA42-AE32ADC54AC4 wds:Q24294558-26DC5980-FE68-4572-8515-504ACF240310 wds:Q61805821-5090D1B2-B3A1-4C92-89D1-A52FAAAE938B wds:Q24318915-23F2AD51-E938-4EA5-9BAB-B3D9DF7ABF76 wds:Q27931313-49842DC5-228F-4507-8AD4-A3F5177ADBC1 wds:Q24305553-6A057B68-9A96-48C0-8A77-6AE59C585B3C wds:Q24302407-92A5E863-192C-4CCB-8C33-1891BE5122D9 wds:Q28115078-16EEC41D-3CCE-4CC2-B932-855A707B1A85 wds:Q24290679-8EF4D4D0-F432-482E-8A34-21C81F569CC9 wds:Q24316102-A1155D47-70B1-49A6-ACEC-FA6C67191F65 wds:Q24305018-F245162F-2071-4AC3-AC89-EE2E8B1D8CA2 wds:Q24298673-018993AB-B5D6-44BD-8C9F-D3ECA9AD09D6 wds:Q27649121-0CD097ED-E9B4-4B5F-B7CF-4670C08F061E wds:Q33500523-34BFB3ED-D577-4B62-88F2-64C92EECA996 wds:Q24314798-9C8077FE-2D06-4595-8384-7DE00A9D9F86 wds:Q24302187-3763C2A4-B1F7-4313-9E7A-CF4C3A1EAEDA wds:Q24293342-BD0176A7-420F-42C8-9F70-108B3CD1F152
is molecular function of	tryptophan 2,3-dioxygenase Hemoglobin subunit mu wd:Q1417916

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