8A2L

X-ray structure of TRIL-encapsulated human heavy chain ferritin

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0004322	molecular_function	ferroxidase activity
AAA	0005506	molecular_function	iron ion binding
AAA	0005515	molecular_function	protein binding
AAA	0005576	cellular_component	extracellular region
AAA	0005634	cellular_component	nucleus
AAA	0005737	cellular_component	cytoplasm
AAA	0005829	cellular_component	cytosol
AAA	0006826	biological_process	iron ion transport
AAA	0006879	biological_process	intracellular iron ion homeostasis
AAA	0006880	biological_process	intracellular sequestering of iron ion
AAA	0006955	biological_process	immune response
AAA	0008043	cellular_component	intracellular ferritin complex
AAA	0008198	molecular_function	ferrous iron binding
AAA	0008199	molecular_function	ferric iron binding
AAA	0008285	biological_process	negative regulation of cell population proliferation
AAA	0016020	cellular_component	membrane
AAA	0016491	molecular_function	oxidoreductase activity
AAA	0042802	molecular_function	identical protein binding
AAA	0044754	cellular_component	autolysosome
AAA	0046872	molecular_function	metal ion binding
AAA	0048147	biological_process	negative regulation of fibroblast proliferation
AAA	0070062	cellular_component	extracellular exosome
AAA	0110076	biological_process	negative regulation of ferroptosis
AAA	0140315	molecular_function	iron ion sequestering activity
AAA	1904724	cellular_component	tertiary granule lumen
AAA	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PROSITE/UniProt

site_id	PS00204
Number of Residues	21
Details	FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEthYLneqvkaIK

Chain	Residue	Details
AAA	ASP126-LYS146

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site_id	PS00540
Number of Residues	19
Details	FERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKLMklQNqRgGR

Chain	Residue	Details
AAA	GLU61-ARG79

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:1992356, ECO:0007744|PDB:1FHA

Chain	Residue	Details
AAA	GLU27
AAA	HIS65

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00085

Chain	Residue	Details
AAA	GLU62
AAA	GLU107
AAA	GLN141

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744|PubMed:22814378

Chain	Residue	Details
AAA	THR1

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
AAA	SER178

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18318008

Chain	Residue	Details
AAA	SER182

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