5LPU

Crystal structure of Annexin A2 complexed with S100A4

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
B	0001525	biological_process	angiogenesis
B	0001533	cellular_component	cornified envelope
B	0001765	biological_process	membrane raft assembly
B	0001786	molecular_function	phosphatidylserine binding
B	0001921	biological_process	positive regulation of receptor recycling
B	0002020	molecular_function	protease binding
B	0002091	biological_process	negative regulation of receptor internalization
B	0003723	molecular_function	RNA binding
B	0004859	molecular_function	phospholipase inhibitor activity
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005544	molecular_function	calcium-dependent phospholipid binding
B	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
B	0005576	cellular_component	extracellular region
B	0005604	cellular_component	basement membrane
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005765	cellular_component	lysosomal membrane
B	0005768	cellular_component	endosome
B	0005769	cellular_component	early endosome
B	0005811	cellular_component	lipid droplet
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005912	cellular_component	adherens junction
B	0006900	biological_process	vesicle budding from membrane
B	0007155	biological_process	cell adhesion
B	0008092	molecular_function	cytoskeletal protein binding
B	0009986	cellular_component	cell surface
B	0010756	biological_process	positive regulation of plasminogen activation
B	0012506	cellular_component	vesicle membrane
B	0016020	cellular_component	membrane
B	0016323	cellular_component	basolateral plasma membrane
B	0016363	cellular_component	nuclear matrix
B	0019834	molecular_function	phospholipase A2 inhibitor activity
B	0030496	cellular_component	midbody
B	0031012	cellular_component	extracellular matrix
B	0031340	biological_process	positive regulation of vesicle fusion
B	0031902	cellular_component	late endosome membrane
B	0031982	cellular_component	vesicle
B	0032804	biological_process	negative regulation of low-density lipoprotein particle receptor catabolic process
B	0035578	cellular_component	azurophil granule lumen
B	0035749	cellular_component	myelin sheath adaxonal region
B	0036035	biological_process	osteoclast development
B	0042383	cellular_component	sarcolemma
B	0042470	cellular_component	melanosome
B	0042789	biological_process	mRNA transcription by RNA polymerase II
B	0042802	molecular_function	identical protein binding
B	0043220	cellular_component	Schmidt-Lanterman incisure
B	0044090	biological_process	positive regulation of vacuole organization
B	0044548	molecular_function	S100 protein binding
B	0045121	cellular_component	membrane raft
B	0045921	biological_process	positive regulation of exocytosis
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0048306	molecular_function	calcium-dependent protein binding
B	0050767	biological_process	regulation of neurogenesis
B	0051051	biological_process	negative regulation of transport
B	0051240	biological_process	positive regulation of multicellular organismal process
B	0070062	cellular_component	extracellular exosome
B	0098609	biological_process	cell-cell adhesion
B	0098641	molecular_function	cadherin binding involved in cell-cell adhesion
B	1905581	biological_process	positive regulation of low-density lipoprotein particle clearance
B	1905602	biological_process	positive regulation of receptor-mediated endocytosis involved in cholesterol transport
B	1905686	biological_process	positive regulation of plasma membrane repair
B	1990665	cellular_component	AnxA2-p11 complex
B	1990667	cellular_component	PCSK9-AnxA2 complex
C	0001837	biological_process	epithelial to mesenchymal transition
C	0003723	molecular_function	RNA binding
C	0003779	molecular_function	actin binding
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0031012	cellular_component	extracellular matrix
C	0042056	molecular_function	chemoattractant activity
C	0042802	molecular_function	identical protein binding
C	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
C	0046872	molecular_function	metal ion binding
C	0046914	molecular_function	transition metal ion binding
C	0048306	molecular_function	calcium-dependent protein binding
C	0048471	cellular_component	perinuclear region of cytoplasm
C	0050786	molecular_function	RAGE receptor binding
C	0050918	biological_process	positive chemotaxis
C	0070062	cellular_component	extracellular exosome
D	0001837	biological_process	epithelial to mesenchymal transition
D	0003723	molecular_function	RNA binding
D	0003779	molecular_function	actin binding
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0031012	cellular_component	extracellular matrix
D	0042056	molecular_function	chemoattractant activity
D	0042802	molecular_function	identical protein binding
D	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
D	0046872	molecular_function	metal ion binding
D	0046914	molecular_function	transition metal ion binding
D	0048306	molecular_function	calcium-dependent protein binding
D	0048471	cellular_component	perinuclear region of cytoplasm
D	0050786	molecular_function	RAGE receptor binding
D	0050918	biological_process	positive chemotaxis
D	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA A 401

Chain	Residue
A	GLY50
A	VAL51
A	GLU53
A	HOH633
A	HOH694

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CA A 402

Chain	Residue
A	LYS88
A	LEU91
A	GLU96
A	HOH664

---

site_id	AC3
Number of Residues	4
Details	binding site for residue CA A 403

Chain	Residue
A	MET118
A	GLY120
A	THR123
A	ASP162

---

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	HOH617
A	HOH676

---

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	HOH527
A	HOH531

---

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL A 407

Chain	Residue
A	PRO106
A	ASP110
A	GLU139
A	SER294
A	ARG295
A	HOH538
A	HOH606

---

site_id	AC8
Number of Residues	7
Details	binding site for residue GOL A 408

Chain	Residue
A	GLY183
A	ARG220
A	SER221
A	HIS224
A	HOH506
A	HOH507
A	HOH613

---

site_id	AC9
Number of Residues	5
Details	binding site for residue CA B 401

Chain	Residue
B	LYS88
B	LEU91
B	GLU96
B	HOH524
B	HOH528

---

site_id	AD1
Number of Residues	5
Details	binding site for residue CA B 402

Chain	Residue
B	MET118
B	GLY120
B	GLY122
B	THR123
B	ASP162

---

site_id	AD2
Number of Residues	4
Details	binding site for residue CA B 403

Chain	Residue
B	GLY50
B	VAL51
B	HOH526
B	HOH527

---

site_id	AD3
Number of Residues	6
Details	binding site for residue CA B 404

Chain	Residue
B	GLY202
B	VAL203
B	ARG205
B	GLY207
B	GLU247
B	HOH525

---

site_id	AD4
Number of Residues	5
Details	binding site for residue CA B 405

Chain	Residue
B	MET278
B	GLY280
B	GLY282
B	ASP322
B	HOH505

---

site_id	AD5
Number of Residues	6
Details	binding site for residue GOL B 406

Chain	Residue
B	CYS133
B	ARG135
B	ARG179
B	LEU259
B	LYS266
B	HOH517

---

site_id	AD6
Number of Residues	1
Details	binding site for residue GOL B 407

Chain	Residue
B	SER221

---

site_id	AD7
Number of Residues	6
Details	binding site for residue CA C 201

Chain	Residue
C	SER20
C	GLU23
C	ASP25
C	LYS28
C	GLU33
C	HOH312

---

site_id	AD8
Number of Residues	6
Details	binding site for residue CA C 202

Chain	Residue
C	ASP63
C	ASN65
C	ASP67
C	GLU69
C	GLU74
C	HOH305

---

site_id	AD9
Number of Residues	6
Details	binding site for residue CA D 201

Chain	Residue
D	SER20
D	GLU23
D	ASP25
D	LYS28
D	GLU33
D	HOH301

---

site_id	AE1
Number of Residues	6
Details	binding site for residue CA D 202

Chain	Residue
D	HOH303
D	ASP63
D	ASN65
D	ASP67
D	GLU69
D	GLU74

---

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DSNRDNEVDfqEY

Chain	Residue	Details
C	ASP63-TYR75

---

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

---

site_id	PS00303
Number of Residues	22
Details	S100_CABP S-100/ICaBP type calcium binding protein signature. LMsnLDsnrDnevDFqEYcvFL

Chain	Residue	Details
C	LEU58-LEU79

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	142
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	142
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	144
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	44
Details	Region: {"description":"S100A10-binding site","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Murray L.","Brunton V.G.","Frame M.C.","Bensaad K.","Vousden K.H."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"15302870","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28669632","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
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_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	4
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

---

site_id	SWS_FT_FI13
Number of Residues	70
Details	Domain: {"description":"EF-hand 1","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	70
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P35466","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---