3AQQ

Crystal structure of human CRHSP-24

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000177	cellular_component	cytoplasmic exosome (RNase complex)
A	0000932	cellular_component	P-body
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0003730	molecular_function	mRNA 3'-UTR binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0019902	molecular_function	phosphatase binding
A	0035556	biological_process	intracellular signal transduction
A	0043186	cellular_component	P granule
A	0043488	biological_process	regulation of mRNA stability
B	0000177	cellular_component	cytoplasmic exosome (RNase complex)
B	0000932	cellular_component	P-body
B	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
B	0003730	molecular_function	mRNA 3'-UTR binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0019902	molecular_function	phosphatase binding
B	0035556	biological_process	intracellular signal transduction
B	0043186	cellular_component	P granule
B	0043488	biological_process	regulation of mRNA stability
C	0000177	cellular_component	cytoplasmic exosome (RNase complex)
C	0000932	cellular_component	P-body
C	0003676	molecular_function	nucleic acid binding
C	0003723	molecular_function	RNA binding
C	0003730	molecular_function	mRNA 3'-UTR binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0019902	molecular_function	phosphatase binding
C	0035556	biological_process	intracellular signal transduction
C	0043186	cellular_component	P granule
C	0043488	biological_process	regulation of mRNA stability
D	0000177	cellular_component	cytoplasmic exosome (RNase complex)
D	0000932	cellular_component	P-body
D	0003676	molecular_function	nucleic acid binding
D	0003723	molecular_function	RNA binding
D	0003730	molecular_function	mRNA 3'-UTR binding
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0019902	molecular_function	phosphatase binding
D	0035556	biological_process	intracellular signal transduction
D	0043186	cellular_component	P granule
D	0043488	biological_process	regulation of mRNA stability

Functional Information from PROSITE/UniProt

site_id	PS00352
Number of Residues	20
Details	CSD_1 Cold-shock (CSD) domain signature. HGFItpadggpDIFlHiSdV

Chain	Residue	Details
A	HIS76-VAL95

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692

Chain	Residue	Details
A	SER2
C	SER2
B	SER2
D	SER2

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site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15910284, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER30
A	SER32
C	SER30
C	SER32
B	SER30
B	SER32
D	SER30
D	SER32

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15910284, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER41
C	SER41
B	SER41
D	SER41

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21406692

Chain	Residue	Details
A	THR45
C	THR45
B	THR45
D	THR45

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site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15910284, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER52
C	SER52
B	SER52
D	SER52

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site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER58
C	SER58
B	SER58
D	SER58

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site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER146
A	SER147
C	SER146
C	SER147
B	SER146
B	SER147
D	SER146
D	SER147

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