1AOA

N-TERMINAL ACTIN-CROSSLINKING DOMAIN FROM HUMAN FIMBRIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0051015	molecular_function	actin filament binding
A	0051017	biological_process	actin filament bundle assembly

Functional Information from PROSITE/UniProt

site_id	PS00019
Number of Residues	10
Details	ACTININ_1 Actinin-type actin-binding domain signature 1. EKyAFVNWIN

Chain	Residue	Details
A	GLU125-ASN134

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site_id	PS00020
Number of Residues	25
Details	ACTININ_2 Actinin-type actin-binding domain signature 2. VvNIGAeDLrAgkphLvLGLLWqII

Chain	Residue	Details
A	VAL211-ILE235

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	116
Details	Domain: {"description":"Calponin-homology (CH) 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99K51","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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