1KKU

Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000309	molecular_function	nicotinamide-nucleotide adenylyltransferase activity
A	0000785	cellular_component	chromatin
A	0003824	molecular_function	catalytic activity
A	0004515	molecular_function	nicotinate-nucleotide adenylyltransferase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0009058	biological_process	biosynthetic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0009435	biological_process	NAD biosynthetic process
A	0009611	biological_process	response to wounding
A	0016604	cellular_component	nuclear body
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0042802	molecular_function	identical protein binding
A	0043410	biological_process	positive regulation of MAPK cascade
A	0043524	biological_process	negative regulation of neuron apoptotic process
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0070566	molecular_function	adenylyltransferase activity
A	0140768	molecular_function	protein ADP-ribosyltransferase-substrate adaptor activity
A	1902511	biological_process	negative regulation of apoptotic DNA fragmentation
A	1990966	biological_process	ATP generation from poly-ADP-D-ribose

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	13
Details	BINDING: BINDING => ECO:0000269|PubMed:11788603, ECO:0007744|PDB:1KQN

Chain	Residue	Details
A	SER16
A	PHE17
A	MET23
A	LYS57
A	TRP92
A	THR95
A	GLY156
A	ASP158
A	LEU168
A	TRP169
A	GLU215
A	ASN219
A	GLY15

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q96T66

Chain	Residue	Details
A	THR224
A	HIS24
A	LYS58

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:11959140, ECO:0007744|PDB:1GZU

Chain	Residue	Details
A	TYR55

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER117

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR119

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