5M5C

Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000278	biological_process	mitotic cell cycle
A	0003725	molecular_function	double-stranded RNA binding
A	0003924	molecular_function	GTPase activity
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0005881	cellular_component	cytoplasmic microtubule
A	0005929	cellular_component	cilium
A	0007017	biological_process	microtubule-based process
A	0015630	cellular_component	microtubule cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0046872	molecular_function	metal ion binding
A	0071353	biological_process	cellular response to interleukin-4
B	0000166	molecular_function	nucleotide binding
B	0000226	biological_process	microtubule cytoskeleton organization
B	0000278	biological_process	mitotic cell cycle
B	0001764	biological_process	neuron migration
B	0003924	molecular_function	GTPase activity
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005874	cellular_component	microtubule
B	0007017	biological_process	microtubule-based process
B	0007399	biological_process	nervous system development
B	0015630	cellular_component	microtubule cytoskeleton
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	1902669	biological_process	positive regulation of axon guidance
C	0005516	molecular_function	calmodulin binding
C	0008017	molecular_function	microtubule binding
D	0000166	molecular_function	nucleotide binding
D	0000226	biological_process	microtubule cytoskeleton organization
D	0000278	biological_process	mitotic cell cycle
D	0003725	molecular_function	double-stranded RNA binding
D	0003924	molecular_function	GTPase activity
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005856	cellular_component	cytoskeleton
D	0005874	cellular_component	microtubule
D	0005881	cellular_component	cytoplasmic microtubule
D	0005929	cellular_component	cilium
D	0007017	biological_process	microtubule-based process
D	0015630	cellular_component	microtubule cytoskeleton
D	0016787	molecular_function	hydrolase activity
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0046872	molecular_function	metal ion binding
D	0071353	biological_process	cellular response to interleukin-4
E	0000166	molecular_function	nucleotide binding
E	0000226	biological_process	microtubule cytoskeleton organization
E	0000278	biological_process	mitotic cell cycle
E	0001764	biological_process	neuron migration
E	0003924	molecular_function	GTPase activity
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005874	cellular_component	microtubule
E	0007017	biological_process	microtubule-based process
E	0007399	biological_process	nervous system development
E	0015630	cellular_component	microtubule cytoskeleton
E	0046872	molecular_function	metal ion binding
E	0046982	molecular_function	protein heterodimerization activity
E	1902669	biological_process	positive regulation of axon guidance

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue GTP D 501

Chain	Residue
D	GLY10
D	THR145
D	GLY146
D	ILE171
D	THR179
D	GLU183
D	ASN206
D	TYR224
D	ASN228
D	MG502
D	HOH601
D	GLN11
D	HOH602
D	HOH603
D	HOH604
E	LYS254
D	ALA12
D	GLN15
D	ASP98
D	ALA99
D	ASN101
D	GLY143
D	GLY144

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG D 502

Chain	Residue
D	GLN11
D	GTP501
D	HOH602
D	HOH603
D	HOH604

---

site_id	AC3
Number of Residues	12
Details	binding site for residue GDP E 501

Chain	Residue
E	GLN11
E	CYS12
E	GLN15
E	ASN101
E	GLY143
E	GLY144
E	THR145
E	GLY146
E	GLU183
E	ASN206
E	TYR224
E	ASN228

---

site_id	AC4
Number of Residues	10
Details	binding site for residue TA1 E 502

Chain	Residue
E	ASP26
E	GLU27
E	ASP226
E	HIS229
E	LEU230
E	ALA233
E	SER236
E	PRO274
E	THR276
E	ARG369

---

site_id	AC5
Number of Residues	22
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLN11
A	ALA12
A	GLN15
A	ASP98
A	ASN101
A	GLY143
A	GLY144
A	THR145
A	GLY146
A	ILE171
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	MG502
A	HOH601
A	HOH602
A	HOH603
A	HOH604
B	LYS254

---

site_id	AC6
Number of Residues	4
Details	binding site for residue MG A 502

Chain	Residue
A	THR145
A	GTP501
A	HOH601
A	HOH604

---

site_id	AC7
Number of Residues	14
Details	binding site for residue GDP B 501

Chain	Residue
B	GLY10
B	GLN11
B	CYS12
B	GLN15
B	ILE16
B	ASN101
B	GLY143
B	GLY144
B	THR145
B	GLY146
B	GLU183
B	ASN206
B	TYR224
B	ASN228

---

site_id	AC8
Number of Residues	11
Details	binding site for residue TA1 B 502

Chain	Residue
B	ARG369
B	LEU371
B	VAL23
B	ASP26
B	GLU27
B	ASP226
B	HIS229
B	LEU230
B	SER236
B	PRO274
B	THR276

---

Functional Information from PROSITE/UniProt

site_id	PS00227
Number of Residues	7
Details	TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG

Chain	Residue	Details
D	GLY142-GLY148
E	GLY142-GLY148

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q3KRE8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P99024","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"UniProtKB","id":"Q9BVA1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---