9QIN

Human Mortalin (mitochondrial Hsp70) in complex with GrpE1 phosphorylated at Ser-47

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001401	cellular_component	SAM complex
A	0001405	cellular_component	PAM complex, Tim23 associated import motor
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0005744	cellular_component	TIM23 mitochondrial import inner membrane translocase complex
A	0005759	cellular_component	mitochondrial matrix
A	0005925	cellular_component	focal adhesion
A	0006886	biological_process	intracellular protein transport
A	0007007	biological_process	inner mitochondrial membrane organization
A	0009636	biological_process	response to toxic substance
A	0016226	biological_process	iron-sulfur cluster assembly
A	0016887	molecular_function	ATP hydrolysis activity
A	0017134	molecular_function	fibroblast growth factor binding
A	0019899	molecular_function	enzyme binding
A	0030150	biological_process	protein import into mitochondrial matrix
A	0030218	biological_process	erythrocyte differentiation
A	0031072	molecular_function	heat shock protein binding
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0036444	biological_process	calcium import into the mitochondrion
A	0042026	biological_process	protein refolding
A	0042645	cellular_component	mitochondrial nucleoid
A	0043066	biological_process	negative regulation of apoptotic process
A	0044183	molecular_function	protein folding chaperone
A	0045646	biological_process	regulation of erythrocyte differentiation
A	0045647	biological_process	negative regulation of erythrocyte differentiation
A	0051082	molecular_function	obsolete unfolded protein binding
A	0051087	molecular_function	protein-folding chaperone binding
A	0051593	biological_process	response to folic acid
A	0070062	cellular_component	extracellular exosome
A	0071347	biological_process	cellular response to interleukin-1
A	0097068	biological_process	response to thyroxine
A	0140275	cellular_component	MIB complex
A	1902037	biological_process	negative regulation of hematopoietic stem cell differentiation
A	1903707	biological_process	negative regulation of hemopoiesis

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKSEDKVIAvyDL

Chain	Residue	Details
A	ASP234-LEU246

---

site_id	PS00297
Number of Residues	8
Details	HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS

Chain	Residue	Details
A	ILE59-SER66

---

site_id	PS00329
Number of Residues	14
Details	HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSIL

Chain	Residue	Details
A	VAL243-LEU256

---

site_id	PS01036
Number of Residues	15
Details	HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGmTRMPkVqQ

Chain	Residue	Details
A	VAL384-GLN398

---

site_id	PS01071
Number of Residues	44
Details	GRPE grpE protein signature. FDPyeHeALfhtpvegkepgtvalvskv..GYklh.Grt.LRpAlVgV

Chain	Residue	Details
B	PHE170-VAL213

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	368
Details	Region: {"description":"Nucleotide-binding domain (NBD)","evidences":[{"source":"PubMed","id":"24687350","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Region: {"description":"Interdomain linker","evidences":[{"source":"PubMed","id":"24687350","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30933555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NHK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	7
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P38647","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99LP6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99LP6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99LP6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---