4H75

Crystal structure of human Spindlin1 in complex with a histone H3K4(me3) peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000785	cellular_component	chromatin
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0006325	biological_process	chromatin organization
A	0006355	biological_process	regulation of DNA-templated transcription
A	0007276	biological_process	gamete generation
A	0009303	biological_process	rRNA transcription
A	0016055	biological_process	Wnt signaling pathway
A	0030177	biological_process	positive regulation of Wnt signaling pathway
A	0035064	molecular_function	obsolete methylated histone binding
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0051321	biological_process	meiotic cell cycle
A	0071168	biological_process	protein localization to chromatin
A	0140002	molecular_function	histone H3K4me3 reader activity
A	0140566	molecular_function	histone reader activity
A	0141196	biological_process	transposable element silencing by piRNA-mediated DNA methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	PRO68
A	VAL69
A	SER121
A	MET162
A	ASN163
A	THR164
A	TRP165
A	GLN180

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 302

Chain	Residue
A	ALA110
A	HOH486
A	SER109

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 303

Chain	Residue
A	ASP183
A	ASP184
A	GLU187
A	HOH481
B	ARG2

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NHE A 304

Chain	Residue
A	TRP62
A	GLU64
A	TRP72
A	LYS73
A	TYR91
A	LEU100
A	PHE251
A	HOH436
A	HOH464
A	HOH492
B	ARG8

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 101

Chain	Residue
A	GLN59
B	THR6
B	ALA7
B	ARG8
B	HOH211

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	63
Details	Region: {"description":"Tudor-like domain 1","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Region: {"description":"Histone H3K4me3 and H3R8me2a binding","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	61
Details	Region: {"description":"Tudor-like domain 2","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Site: {"description":"Histone H3K4me3 and H3R8me2a binding","evidences":[{"source":"PubMed","id":"23077255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24589551","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by AURKA","evidences":[{"source":"PubMed","id":"22258766","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by AURKA","evidences":[{"source":"PubMed","id":"22258766","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---