7S05

Cryo-EM structure of human GlcNAc-1-phosphotransferase A2B2 subcomplex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0003976	molecular_function	UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005794	cellular_component	Golgi apparatus
A	0007040	biological_process	lysosome organization
A	0009306	biological_process	protein secretion
A	0016020	cellular_component	membrane
A	0016256	biological_process	N-glycan processing to lysosome
A	0016740	molecular_function	transferase activity
A	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
A	0033299	biological_process	secretion of lysosomal enzymes
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
A	0051649	biological_process	establishment of localization in cell
B	0000139	cellular_component	Golgi membrane
B	0003976	molecular_function	UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005794	cellular_component	Golgi apparatus
B	0007040	biological_process	lysosome organization
B	0009306	biological_process	protein secretion
B	0016020	cellular_component	membrane
B	0016256	biological_process	N-glycan processing to lysosome
B	0016740	molecular_function	transferase activity
B	0016772	molecular_function	transferase activity, transferring phosphorus-containing groups
B	0033299	biological_process	secretion of lysosomal enzymes
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
B	0051649	biological_process	establishment of localization in cell

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	ASP1018-ILE1030

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00525

Chain	Residue	Details
B	ASP449
A	ASP516
A	ASP531
A	ASP534
B	ASP464
B	ASP467
B	ASP516
B	ASP531
B	ASP534
A	ASP449
A	ASP464
A	ASP467

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
B	ASP1018
B	ASP1020
B	SER1022
B	GLU1029
A	ASP1018
A	ASP1020
A	SER1022
A	GLU1029

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Cleavage; by MBTPS1

Chain	Residue	Details
B	ARG928
A	ARG928

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site_id	SWS_FT_FI4
Number of Residues	20
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
B	ASN83
B	ASN1129
A	ASN83
A	ASN114
A	ASN148
A	ASN179
A	ASN250
A	ASN614
A	ASN729
A	ASN829
A	ASN1009
B	ASN114
A	ASN1129
B	ASN148
B	ASN179
B	ASN250
B	ASN614
B	ASN729
B	ASN829
B	ASN1009

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site_id	SWS_FT_FI5
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
B	ASN699
A	ASN699

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