8F18

Apo KIF20A[1-565] class-2 in complex with a microtubule

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000226	biological_process	microtubule cytoskeleton organization
A	0000278	biological_process	mitotic cell cycle
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	0005856	cellular_component	cytoskeleton
A	0005874	cellular_component	microtubule
A	0007017	biological_process	microtubule-based process
A	0015630	cellular_component	microtubule cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
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	0007010	biological_process	cytoskeleton organization
B	0007017	biological_process	microtubule-based process
K	0003777	molecular_function	microtubule motor activity
K	0005524	molecular_function	ATP binding
K	0007018	biological_process	microtubule-based movement
K	0008017	molecular_function	microtubule binding

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

---

site_id	PS00411
Number of Residues	12
Details	KINESIN_MOTOR_1 Kinesin motor domain signature. SELsLCDLAGSE

Chain	Residue	Details
K	SER401-GLU412

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00283

Chain	Residue	Details
K	GLY159

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:O95235

Chain	Residue	Details
K	SER2
A	GLU71
A	SER140
A	GLY144
A	THR145
A	THR179
A	ASN206
A	ASN228

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O95235

Chain	Residue	Details
K	SER7
K	SER14
K	SER21

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PLK1 => ECO:0000250|UniProtKB:O95235

Chain	Residue	Details
K	SER527

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	SER48
A	SER232

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P68373

Chain	Residue	Details
A	TYR282

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	ARG339

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68373

Chain	Residue	Details
A	SER439

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	GLU443

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:P68369

Chain	Residue	Details
A	GLU445

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:Q71U36

Chain	Residue	Details
A	TYR451

---

site_id	SWS_FT_FI12
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363

Chain	Residue	Details
A	LYS326
A	LYS370

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