Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5LPX

Crystal structure of PKC phosphorylation-mimicking mutant (S26E) Annexin A2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001525	biological_process	angiogenesis
A	0001533	cellular_component	cornified envelope
A	0001765	biological_process	membrane raft assembly
A	0001786	molecular_function	phosphatidylserine binding
A	0001921	biological_process	positive regulation of receptor recycling
A	0002020	molecular_function	protease binding
A	0002091	biological_process	negative regulation of receptor internalization
A	0003723	molecular_function	RNA binding
A	0004859	molecular_function	phospholipase inhibitor activity
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005544	molecular_function	calcium-dependent phospholipid binding
A	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
A	0005576	cellular_component	extracellular region
A	0005604	cellular_component	basement membrane
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005768	cellular_component	endosome
A	0005769	cellular_component	early endosome
A	0005811	cellular_component	lipid droplet
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005912	cellular_component	adherens junction
A	0006900	biological_process	vesicle budding from membrane
A	0007155	biological_process	cell adhesion
A	0008092	molecular_function	cytoskeletal protein binding
A	0009986	cellular_component	cell surface
A	0010756	biological_process	positive regulation of plasminogen activation
A	0012506	cellular_component	vesicle membrane
A	0016020	cellular_component	membrane
A	0016323	cellular_component	basolateral plasma membrane
A	0016363	cellular_component	nuclear matrix
A	0019834	molecular_function	phospholipase A2 inhibitor activity
A	0030496	cellular_component	midbody
A	0031012	cellular_component	extracellular matrix
A	0031340	biological_process	positive regulation of vesicle fusion
A	0031902	cellular_component	late endosome membrane
A	0031982	cellular_component	vesicle
A	0032804	biological_process	negative regulation of low-density lipoprotein particle receptor catabolic process
A	0035578	cellular_component	azurophil granule lumen
A	0035749	cellular_component	myelin sheath adaxonal region
A	0036035	biological_process	osteoclast development
A	0042383	cellular_component	sarcolemma
A	0042470	cellular_component	melanosome
A	0042789	biological_process	mRNA transcription by RNA polymerase II
A	0042802	molecular_function	identical protein binding
A	0043220	cellular_component	Schmidt-Lanterman incisure
A	0044090	biological_process	positive regulation of vacuole organization
A	0044548	molecular_function	S100 protein binding
A	0045121	cellular_component	membrane raft
A	0045921	biological_process	positive regulation of exocytosis
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0048306	molecular_function	calcium-dependent protein binding
A	0050767	biological_process	regulation of neurogenesis
A	0051051	biological_process	negative regulation of transport
A	0051240	biological_process	positive regulation of multicellular organismal process
A	0070062	cellular_component	extracellular exosome
A	0098609	biological_process	cell-cell adhesion
A	0098641	molecular_function	cadherin binding involved in cell-cell adhesion
A	1905581	biological_process	positive regulation of low-density lipoprotein particle clearance
A	1905602	biological_process	positive regulation of receptor-mediated endocytosis involved in cholesterol transport
A	1905686	biological_process	positive regulation of plasma membrane repair
A	1990665	cellular_component	AnxA2-p11 complex
A	1990667	cellular_component	PCSK9-AnxA2 complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue CA A 401

Chain	Residue
A	GLY50
A	VAL51
A	GLU53
A	HOH722
A	HOH799
A	HOH842
A	HOH850

site_id	AC2
Number of Residues	7
Details	binding site for residue CA A 402

Chain	Residue
A	GLU96
A	HOH801
A	HOH813
A	HOH863
A	HOH885
A	LYS88
A	LEU91

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 403

Chain	Residue
A	MET118
A	GLY120
A	GLY122
A	ASP162
A	HOH536
A	HOH699

site_id	AC4
Number of Residues	6
Details	binding site for residue CA A 404

Chain	Residue
A	GLY202
A	ARG205
A	GLY207
A	GLU247
A	HOH715
A	HOH840

site_id	AC5
Number of Residues	4
Details	binding site for residue CA A 405

Chain	Residue
A	MET278
A	GLY280
A	GLY282
A	ASP322

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL A 406

Chain	Residue
A	CYS133
A	SER134
A	ARG135
A	ARG179
A	LYS266
A	HOH532
A	HOH629

site_id	AC7
Number of Residues	9
Details	binding site for residue GOL A 407

Chain	Residue
A	ALA180
A	GLU181
A	GLY183
A	ARG220
A	SER221
A	HIS224
A	HOH512
A	HOH528
A	HOH585

Functional Information from PROSITE/UniProt

site_id	PS00223
Number of Residues	53
Details	ANNEXIN_1 Annexin repeat signature. GVdevtivniLtnRsneQrqDiafaYqrrtkkeLasaLksalsGhletvIlgL

Chain	Residue	Details
A	GLY50-LEU102
A	GLY122-LEU174
A	GLY207-LEU259
A	GLY282-LEU334

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	71
Details	Repeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	71
Details	Repeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	72
Details	Repeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"28669632","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2946940","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)