Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5IJ9

Cryo EM density of microtubule assembled from human TUBB3-D417H mutant

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	0005198	molecular_function	structural molecule activity
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
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	0030705	biological_process	cytoskeleton-dependent intracellular transport
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0051301	biological_process	cell division
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	0003924	molecular_function	GTPase activity
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005874	cellular_component	microtubule
B	0007017	biological_process	microtubule-based process
B	0007411	biological_process	axon guidance
B	0015630	cellular_component	microtubule cytoskeleton
B	0030027	cellular_component	lamellipodium
B	0030175	cellular_component	filopodium
B	0030182	biological_process	neuron differentiation
B	0030424	cellular_component	axon
B	0030425	cellular_component	dendrite
B	0030426	cellular_component	growth cone
B	0038007	biological_process	netrin-activated signaling pathway
B	0042277	molecular_function	peptide binding
B	0042995	cellular_component	cell projection
B	0043025	cellular_component	neuronal cell body
B	0045171	cellular_component	intercellular bridge
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome
B	0071944	cellular_component	cell periphery
B	0072686	cellular_component	mitotic spindle
B	1990791	biological_process	dorsal root ganglion development
B	1990890	molecular_function	netrin receptor binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue GTP A 501

Chain	Residue
A	GLY10
A	GLY144
A	THR145
A	ILE171
A	THR179
A	GLU183
A	ASN206
A	TYR224
A	ASN228
A	MG502
B	LEU246
A	GLN11
B	LYS252
A	ALA12
A	GLN15
A	ASP98
A	ALA99
A	ALA100
A	ASN101
A	SER140

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 502

Chain	Residue
A	ASP69
A	GLU71
A	GTP501

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

Chain	Residue
B	GLN11
B	CYS12
B	GLN15
B	ASN99
B	SER138
B	GLY141
B	GLY142
B	THR143
B	ASP177
B	ASN204
B	TYR222
B	ASN226

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
B	GLY140-GLY146
A	GLY142-GLY148

site_id	PS00228
Number of Residues	4
Details	TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI

Chain	Residue	Details
B	MET1-ILE4

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Motif: {"description":"MREC motif","evidences":[{"source":"PubMed","id":"31727855","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35482892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38609661","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8VT7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P68373","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	3
Details	Motif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35482892","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SJ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Z6S","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"34996871","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SJ7","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"16371510","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)