5YVG

Crystal structure of Karyopherin beta2 in complex with FUS(full length)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006606	biological_process	protein import into nucleus
A	0006886	biological_process	intracellular protein transport
A	0031267	molecular_function	small GTPase binding
B	0006606	biological_process	protein import into nucleus
B	0006886	biological_process	intracellular protein transport
B	0031267	molecular_function	small GTPase binding
X	0003676	molecular_function	nucleic acid binding
X	0003677	molecular_function	DNA binding
X	0003682	molecular_function	chromatin binding
X	0003712	molecular_function	transcription coregulator activity
X	0003713	molecular_function	transcription coactivator activity
X	0003723	molecular_function	RNA binding
X	0003730	molecular_function	mRNA 3'-UTR binding
X	0005515	molecular_function	protein binding
X	0005634	cellular_component	nucleus
X	0005654	cellular_component	nucleoplasm
X	0005737	cellular_component	cytoplasm
X	0006355	biological_process	regulation of DNA-templated transcription
X	0006357	biological_process	regulation of transcription by RNA polymerase II
X	0008380	biological_process	RNA splicing
X	0010467	biological_process	gene expression
X	0042802	molecular_function	identical protein binding
X	0043232	cellular_component	intracellular non-membrane-bounded organelle
X	0043484	biological_process	regulation of RNA splicing
X	0045893	biological_process	positive regulation of DNA-templated transcription
X	0046872	molecular_function	metal ion binding
X	0048255	biological_process	mRNA stabilization
X	0051260	biological_process	protein homooligomerization
X	0140693	molecular_function	molecular condensate scaffold activity
X	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
X	1990000	biological_process	amyloid fibril formation
Y	0003676	molecular_function	nucleic acid binding
Y	0003677	molecular_function	DNA binding
Y	0003682	molecular_function	chromatin binding
Y	0003712	molecular_function	transcription coregulator activity
Y	0003713	molecular_function	transcription coactivator activity
Y	0003723	molecular_function	RNA binding
Y	0003730	molecular_function	mRNA 3'-UTR binding
Y	0005515	molecular_function	protein binding
Y	0005634	cellular_component	nucleus
Y	0005654	cellular_component	nucleoplasm
Y	0005737	cellular_component	cytoplasm
Y	0006355	biological_process	regulation of DNA-templated transcription
Y	0006357	biological_process	regulation of transcription by RNA polymerase II
Y	0008380	biological_process	RNA splicing
Y	0010467	biological_process	gene expression
Y	0042802	molecular_function	identical protein binding
Y	0043232	cellular_component	intracellular non-membrane-bounded organelle
Y	0043484	biological_process	regulation of RNA splicing
Y	0045893	biological_process	positive regulation of DNA-templated transcription
Y	0046872	molecular_function	metal ion binding
Y	0048255	biological_process	mRNA stabilization
Y	0051260	biological_process	protein homooligomerization
Y	0140693	molecular_function	molecular condensate scaffold activity
Y	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
Y	1990000	biological_process	amyloid fibril formation

Functional Information from PROSITE/UniProt

site_id	PS01358
Number of Residues	22
Details	ZF_RANBP2_1 Zinc finger RanBP2-type signature. WkCpnptCenmNfswrneCnqC

Chain	Residue	Details
X	TRP426-CYS447

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	62
Details	ZN_FING: RanBP2-type => ECO:0000255|PROSITE-ProRule:PRU00322

Chain	Residue	Details
X	ARG422-ASP453
Y	ARG422-ASP453
B	TRP460
B	TRP730

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Breakpoint for translocation to form chimeric FUS/ATF1 protein

Chain	Residue	Details
X	GLY175
Y	GLY175

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Breakpoint for translocation to form FUS/TLS-CHOP oncogene

Chain	Residue	Details
X	GLY266
Y	GLY266

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:29897835

Chain	Residue	Details
Y	SER26
Y	SER30
X	SER26
X	SER30

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by ATM => ECO:0000269|PubMed:18620545

Chain	Residue	Details
X	SER42
Y	SER42

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Omega-N-methylarginine; alternate => ECO:0007744|PubMed:24129315

Chain	Residue	Details
X	ARG503
Y	ARG216
Y	ARG218
Y	ARG503
X	ARG216
X	ARG218

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692

Chain	Residue	Details
Y	SER221
X	SER221

---

site_id	SWS_FT_FI8
Number of Residues	36
Details	MOD_RES: Asymmetric dimethylarginine => ECO:0000269|PubMed:12964758

Chain	Residue	Details
X	ARG248
X	ARG251
X	ARG259
X	ARG377
X	ARG383
X	ARG386
X	ARG388
X	ARG394
X	ARG473
X	ARG476
X	ARG481
X	ARG485
X	ARG487
X	ARG491
X	ARG495
X	ARG498
Y	ARG242
Y	ARG244
Y	ARG248
Y	ARG251
Y	ARG259
Y	ARG377
Y	ARG383
Y	ARG386
Y	ARG388
Y	ARG394
Y	ARG473
Y	ARG476
Y	ARG481
Y	ARG485
Y	ARG487
Y	ARG491
Y	ARG495
Y	ARG498
X	ARG242
X	ARG244

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
Y	SER277
X	SER277

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
X	THR286
Y	THR286

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
X	SER340
Y	SER340

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine; alternate => ECO:0000250|UniProtKB:P56959

Chain	Residue	Details
X	ARG407
Y	ARG407

---

site_id	SWS_FT_FI13
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
X	LYS334
Y	LYS334

---