5SZJ

Structure of human Rab10 in complex with the bMERB domain of Mical-cL

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0000145	cellular_component	exocyst
A	0000166	molecular_function	nucleotide binding
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005764	cellular_component	lysosome
A	0005768	cellular_component	endosome
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0005802	cellular_component	trans-Golgi network
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005912	cellular_component	adherens junction
A	0005925	cellular_component	focal adhesion
A	0005929	cellular_component	cilium
A	0006887	biological_process	exocytosis
A	0006893	biological_process	Golgi to plasma membrane transport
A	0007409	biological_process	axonogenesis
A	0010008	cellular_component	endosome membrane
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0016192	biological_process	vesicle-mediated transport
A	0016197	biological_process	endosomal transport
A	0016787	molecular_function	hydrolase activity
A	0019003	molecular_function	GDP binding
A	0019882	biological_process	antigen processing and presentation
A	0030659	cellular_component	cytoplasmic vesicle membrane
A	0030667	cellular_component	secretory granule membrane
A	0030670	cellular_component	phagocytic vesicle membrane
A	0030859	biological_process	polarized epithelial cell differentiation
A	0031410	cellular_component	cytoplasmic vesicle
A	0031489	molecular_function	myosin V binding
A	0032593	cellular_component	insulin-responsive compartment
A	0032869	biological_process	cellular response to insulin stimulus
A	0043001	biological_process	Golgi to plasma membrane protein transport
A	0045055	biological_process	regulated exocytosis
A	0045200	biological_process	establishment of neuroblast polarity
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0055037	cellular_component	recycling endosome
A	0055038	cellular_component	recycling endosome membrane
A	0070062	cellular_component	extracellular exosome
A	0070382	cellular_component	exocytic vesicle
A	0071782	cellular_component	endoplasmic reticulum tubular network
A	0071786	biological_process	endoplasmic reticulum tubular network organization
A	0072659	biological_process	protein localization to plasma membrane
A	0090150	biological_process	establishment of protein localization to membrane
A	0097051	biological_process	establishment of protein localization to endoplasmic reticulum membrane
A	0098609	biological_process	cell-cell adhesion
A	0098641	molecular_function	cadherin binding involved in cell-cell adhesion
A	0099503	cellular_component	secretory vesicle
A	1903361	biological_process	protein localization to basolateral plasma membrane
A	1905504	biological_process	negative regulation of motile cilium assembly

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	binding site for residue GNP A 301

Chain	Residue
A	SER18
A	THR36
A	PHE38
A	SER40
A	THR41
A	THR65
A	ALA66
A	GLY67
A	ASN122
A	LYS123
A	ASP125
A	GLY19
A	MET126
A	SER152
A	ALA153
A	LYS154
A	MG302
A	HOH405
A	HOH409
A	HOH412
A	HOH414
A	VAL20
A	GLY21
A	LYS22
A	THR23
A	CYS24
A	PHE34
A	ASN35

---

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 302

Chain	Residue
A	THR23
A	THR41
A	ASP64
A	GNP301
A	HOH405
A	HOH414

---

site_id	AC3
Number of Residues	6
Details	binding site for residue PEG B 701

Chain	Residue
A	LYS47
B	GLU617
B	GLN620
B	SER621
B	GLU624
B	ARG660

---

Functional Information from PROSITE/UniProt

site_id	PS00675
Number of Residues	14
Details	SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKtcV

Chain	Residue	Details
A	LEU12-VAL25

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Motif: {"description":"Switch 1","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	17
Details	Motif: {"description":"Switch 2","evidences":[{"source":"UniProtKB","id":"P62820","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SZJ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27552051","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LPN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by LRRK2","evidences":[{"source":"PubMed","id":"26824392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29125462","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29127255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29212815","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29562525","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30209220","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30398148","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30635421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38127736","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"31540829","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---