Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00069
Entry Name
UniProt Accession
Theoretical PI
5.25
Molecular Weight
79748.4
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Molybdopterin molybdenumtransferase
Protein Synonyms/Alias
MPT adenylyltransferase; 2.7.7.75; Domain G; MPT Mo-transferase; 2.10.1.1; Domain E;
Gene Name
GPHN
Gene Synonyms/Alias
GPH; KIAA1385;
Created Date
27-APR-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
212
Canonical
TEDKGVQCEEEEEEK
[1]
S-Palmitoylation
284
Canonical
SRLSTASCPTPKVQS
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Dejanovic B, Semtner M, Ebert S, Lamkemeyer T, Neuser F, Lüscher B, Meier JC, Schwarz G. Palmitoylation of gephyrin controls receptor clustering and plasticityof GABAergic synapses. PLoS Biol. 2014 Jul 15;12(7):e1001908. doi:10.1371/journal.pbio.1001908. eCollection 2014 Jul.[PMID:25025157]
Functional Description
Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Sequence Annotation
Region: 14 166 MPT Mo-transferase.
Region: 140 316 Interaction with GABARAP.
Region: 326 736 MPT adenylyltransferase.
Modified residue: 188 188 Phosphoserine.
Modified residue: 194 194 Phosphoserine.
Modified residue: 266 266 Phosphothreonine.
Modified residue: 305 305 Phosphoserine.
Protein Length
736 AA.
Protein Sequence
(Canonical)
MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP  60
DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MALAMLMGSL  120
NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH  180
DELEDLPSPP PPLSPPPTTS PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAI  240
AAKIPDSIIS RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKVQ SRCSSKENIL  300
RASHSAVDIT KVARRHRMSP FPLTSMDKAF ITVLEMTPVL GTEIINYRDG MGRVLAQDVY  360
AKDNLPPFPA SVKDGYAVRA ADGPGDRFII GESQAGEQPT QTVMPGQVMR VTTGAPIPCG  420
ADAVVQVEDT ELIRESDDGT EELEVRILVQ ARPGQDIRPI GHDIKRGECV LAKGTHMGPS  480
EIGLLATVGV TEVEVNKFPV VAVMSTGNEL LNPEDDLLPG KIRDSNRSTL LATIQEHGYP  540
TINLGIVGDN PDDLLNALNE GISRADVIIT SGGVSMGEKD YLKQVLDIDL HAQIHFGRVF  600
MKPGLPTTFA TLDIDGVRKI IFALPGNPVS AVVTCNLFVV PALRKMQGIL DPRPTIIKAR  660
LSCDVKLDPR PEYHRCILTW HHQEPLPWAQ STGNQMSSRL MSMRSANGLL MLPPKTEQYV  720
ELHKGEVVDV MVIGRL                                                  736
FASTA
(Canonical)
>LipidDB-9606-00069|Q9NQX3
MATEGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPSLLGGTISAYKIVP
DEIEEIKETLIDWCDEKELNLILTTGGTGFAPRDVTPEATKEVIEREAPGMALAMLMGSL
NVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVH
DELEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAAAI
AAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKVQSRCSSKENIL
RASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVY
AKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTGAPIPCG
ADAVVQVEDTELIRESDDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPS
EIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYP
TINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVF
MKPGLPTTFATLDIDGVRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPTIIKAR
LSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYV
ELHKGEVVDVMVIGRL
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0060077; C:inhibitory synapse; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC
GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC
GO:0016740; F:transferase activity; TAS:Reactome
GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IEA:Ensembl
GO:0072579; P:glycine receptor clustering; IEA:Ensembl
GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW
GO:0032324; P:molybdopterin cofactor biosynthetic process; TAS:Reactome
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0006766; P:vitamin metabolic process; TAS:Reactome
GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome
Interpro
InterPro; IPR020817; Mo_cofactor_synthesis
InterPro; IPR008284; MoCF_biosynth_CS
InterPro; IPR005111; MoeA_C_domain_IV
InterPro; IPR005110; MoeA_linker/N
InterPro; IPR001453; Mopterin-bd_dom
Pfam
Pfam; PF00994; MoCF_biosynth;
Pfam; PF03454; MoeA_C;
Pfam; PF03453; MoeA_N;
SMART
SMART; SM00852; MoCF_biosynth;
PROSITE
PROSITE; PS01078; MOCF_BIOSYNTHESIS_1;
PROSITE; PS01079; MOCF_BIOSYNTHESIS_2;
PRINTS