Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Gephyrin (Putative glycine receptor-tubulin linker protein) [Includes: Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (Domain G); Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) (Domain E)]

 GEPH_RAT                Reviewed;         768 AA.
Q03555;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 3.
10-OCT-2018, entry version 182.
RecName: Full=Gephyrin;
AltName: Full=Putative glycine receptor-tubulin linker protein;
Includes:
RecName: Full=Molybdopterin adenylyltransferase;
Short=MPT adenylyltransferase;
EC=2.7.7.75 {ECO:0000305|PubMed:9990024};
AltName: Full=Domain G;
Includes:
RecName: Full=Molybdopterin molybdenumtransferase;
Short=MPT Mo-transferase;
EC=2.10.1.1 {ECO:0000305|PubMed:9990024};
AltName: Full=Domain E;
Name=Gphn; Synonyms=Gph;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Wistar; TISSUE=Brain;
PubMed=1319186; DOI=10.1016/0896-6273(92)90136-2;
Prior P., Schmitt B., Grenningloh G., Pribilla I., Multhaup G.,
Beyreuther K., Maulet Y., Werner P., Langosch D., Kirsch J., Betz H.;
"Primary structure and alternative splice variants of gephyrin, a
putative glycine receptor-tubulin linker protein.";
Neuron 8:1161-1170(1992).
[2]
SEQUENCE REVISION TO 255.
Schmitt B.;
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
INTERACTION WITH GLRB.
PubMed=11083919; DOI=10.1006/mcne.2000.0899;
Meier J., De Chaldee M., Triller A., Vannier C.;
"Functional heterogeneity of gephyrins.";
Mol. Cell. Neurosci. 16:566-577(2000).
[4]
PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, X-RAY
CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 348-768 IN COMPLEX WITH GLRB, AND
SUBUNIT.
PubMed=15201864; DOI=10.1038/sj.emboj.7600256;
Sola M., Bavro V.N., Timmins J., Franz T., Ricard-Blum S., Schoehn G.,
Ruigrok R.W.H., Paarmann I., Saiyed T., O'Sullivan G.A., Schmitt B.,
Betz H., Weissenhorn W.;
"Structural basis of dynamic glycine receptor clustering by
gephyrin.";
EMBO J. 23:2510-2519(2004).
[5]
FUNCTION.
PubMed=8264797; DOI=10.1038/366745a0;
Kirsch J., Wolters I., Triller A., Betz H.;
"Gephyrin antisense oligonucleotides prevent glycine receptor
clustering in spinal neurons.";
Nature 366:745-748(1993).
[6]
INTERACTION WITH GABARAP.
PubMed=10900017; DOI=10.1073/pnas.97.15.8594;
Kneussel M., Haverkamp S., Fuhrmann J.C., Wang H., Waessle H.,
Olsen R.W., Betz H.;
"The gamma-aminobutyric acid type A receptor (GABAAR)-associated
protein GABARAP interacts with gephyrin but is not involved in
receptor anchoring at the synapse.";
Proc. Natl. Acad. Sci. U.S.A. 97:8594-8599(2000).
[7]
FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
PubMed=9990024; DOI=10.1073/pnas.96.4.1333;
Stallmeyer B., Schwarz G., Schulze J., Nerlich A., Reiss J.,
Kirsch J., Mendel R.R.;
"The neurotransmitter receptor-anchoring protein gephyrin
reconstitutes molybdenum cofactor biosynthesis in bacteria, plants,
and mammalian cells.";
Proc. Natl. Acad. Sci. U.S.A. 96:1333-1338(1999).
[8]
SUBCELLULAR LOCATION.
PubMed=12684523; DOI=10.1074/jbc.M301070200;
Rees M.I., Harvey K., Ward H., White J.H., Evans L., Duguid I.C.,
Hsu C.-C., Coleman S.L., Miller J., Baer K., Waldvogel H.J.,
Gibbon F., Smart T.G., Owen M.J., Harvey R.J., Snell R.G.;
"Isoform heterogeneity of the human gephyrin gene (GPHN), binding
domains to the glycine receptor, and mutation analysis in
hyperekplexia.";
J. Biol. Chem. 278:24688-24696(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201; SER-207 AND
SER-283, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201, AND SUBUNIT.
PubMed=11325967; DOI=10.1074/jbc.M101923200;
Sola M., Kneussel M., Heck I.S., Betz H., Weissenhorn W.;
"X-ray crystal structure of the trimeric N-terminal domain of
gephyrin.";
J. Biol. Chem. 276:25294-25301(2001).
[11]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 350-768 IN COMPLEX WITH GLRB,
SUBCELLULAR LOCATION, INTERACTION WITH GLRB, AND MUTAGENESIS OF
PHE-362; PRO-745 AND 745-PRO-PRO-746.
PubMed=16511563; DOI=10.1038/sj.emboj.7601029;
Kim E.Y., Schrader N., Smolinsky B., Bedet C., Vannier C., Schwarz G.,
Schindelin H.;
"Deciphering the structural framework of glycine receptor anchoring by
gephyrin.";
EMBO J. 25:1385-1395(2006).
[12]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 350-768, INTERACTION WITH
GLRB, AND SUBUNIT.
PubMed=25137389; DOI=10.1021/cb500303a;
Maric H.M., Kasaragod V.B., Schindelin H.;
"Modulation of gephyrin-glycine receptor affinity by multivalency.";
ACS Chem. Biol. 9:2554-2562(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 350-768 IN COMPLEX WITH
GABRA3, INTERACTION WITH GABRA3 AND GLRB, AND SUBUNIT.
PubMed=25531214; DOI=10.1038/ncomms6767;
Maric H.M., Kasaragod V.B., Hausrat T.J., Kneussel M., Tretter V.,
Stromgaard K., Schindelin H.;
"Molecular basis of the alternative recruitment of GABA(A) versus
glycine receptors through gephyrin.";
Nat. Commun. 5:5767-5767(2014).
-!- FUNCTION: Microtubule-associated protein involved in membrane
protein-cytoskeleton interactions. It is thought to anchor the
inhibitory glycine receptor (GLYR) to subsynaptic microtubules
(PubMed:8264797). 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 (PubMed:9990024).
{ECO:0000269|PubMed:8264797, ECO:0000269|PubMed:9990024}.
-!- CATALYTIC ACTIVITY: ATP + molybdopterin = diphosphate + adenylyl-
molybdopterin. {ECO:0000305|PubMed:9990024}.
-!- CATALYTIC ACTIVITY: Adenylyl-molybdopterin + molybdate =
molybdenum cofactor + AMP. {ECO:0000305|PubMed:9990024}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Inhibited by copper and tungsten.
{ECO:0000250}.
-!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
{ECO:0000305|PubMed:9990024}.
-!- SUBUNIT: Homotrimer, homodimer and homooligomer (PubMed:11325967,
PubMed:25137389, PubMed:25531214). Interacts with SRGAP2 (via SH3
domain) (By similarity). Interacts with GLRB (PubMed:15201864,
PubMed:16511563, PubMed:25137389, PubMed:25531214). Interacts with
GABARAP (PubMed:10900017). Interacts with GABRA3
(PubMed:25531214). GABRA3 and GLRB occupy overlapping binding
sites (PubMed:25531214). Interacts with ARHGAP32; IQSEC3, INSYN1
and INSYN2 (By similarity). {ECO:0000250|UniProtKB:Q8BUV3,
ECO:0000269|PubMed:10900017, ECO:0000269|PubMed:11325967,
ECO:0000269|PubMed:15201864, ECO:0000269|PubMed:16511563}.
-!- INTERACTION:
P20236:Gabra3; NbExp=5; IntAct=EBI-5273276, EBI-5273284;
P48168:Glrb (xeno); NbExp=4; IntAct=EBI-349317, EBI-7069198;
-!- SUBCELLULAR LOCATION: Cell junction, synapse
{ECO:0000269|PubMed:16511563}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000269|PubMed:16511563};
Peripheral membrane protein {ECO:0000269|PubMed:16511563};
Cytoplasmic side {ECO:0000269|PubMed:16511563}. Cytoplasm,
cytoskeleton {ECO:0000269|PubMed:16511563}. Cell membrane
{ECO:0000269|PubMed:12684523}; Peripheral membrane protein
{ECO:0000269|PubMed:12684523}; Cytoplasmic side
{ECO:0000269|PubMed:12684523}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q9NQX3}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000250|UniProtKB:Q8BUV3}. Note=Cytoplasmic face of
glycinergic postsynaptic membranes. {ECO:0000269|PubMed:16511563}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=6;
IsoId=Q03555-1; Sequence=Displayed;
Name=1; Synonyms=GE124'56;
IsoId=Q03555-2; Sequence=VSP_003238;
Name=2; Synonyms=GE236;
IsoId=Q03555-3; Sequence=VSP_003239, VSP_003240, VSP_003243;
Name=3; Synonyms=GE24'6;
IsoId=Q03555-4; Sequence=VSP_003239;
Name=4; Synonyms=GE245;
IsoId=Q03555-5; Sequence=VSP_003241, VSP_003242;
Name=5; Synonyms=GE26;
IsoId=Q03555-6; Sequence=VSP_003239, VSP_003243;
-!- TISSUE SPECIFICITY: Expressed in tissues including spinal cord,
brain, liver, kidney and lung.
-!- PTM: Phosphorylated.
-!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X66366; CAA47009.2; -; mRNA.
PIR; JH0681; JH0681.
RefSeq; NP_074056.2; NM_022865.3. [Q03555-6]
UniGene; Rn.11032; -.
PDB; 1IHC; X-ray; 1.90 A; A=1-201.
PDB; 1T3E; X-ray; 3.25 A; A/B=348-768.
PDB; 2FTS; X-ray; 2.41 A; A=350-768.
PDB; 2FU3; X-ray; 2.70 A; A/B=350-768.
PDB; 4PD0; X-ray; 1.70 A; A=350-768.
PDB; 4PD1; X-ray; 1.98 A; A=350-768.
PDB; 4TK1; X-ray; 2.70 A; A/B=350-768.
PDB; 4TK2; X-ray; 4.10 A; A/B=350-768.
PDB; 4TK3; X-ray; 2.70 A; A/B=350-768.
PDB; 4TK4; X-ray; 3.60 A; A/B=350-768.
PDB; 4U90; X-ray; 2.00 A; A=350-768.
PDB; 4U91; X-ray; 2.00 A; A=350-768.
PDB; 5ERQ; X-ray; 1.55 A; A=350-768.
PDB; 5ERR; X-ray; 1.65 A; A=350-768.
PDB; 5ERS; X-ray; 1.70 A; A=350-768.
PDB; 5ERT; X-ray; 2.00 A; A=350-768.
PDB; 5ERU; X-ray; 1.60 A; A=350-768.
PDB; 5ERV; X-ray; 1.80 A; A=350-768.
PDBsum; 1IHC; -.
PDBsum; 1T3E; -.
PDBsum; 2FTS; -.
PDBsum; 2FU3; -.
PDBsum; 4PD0; -.
PDBsum; 4PD1; -.
PDBsum; 4TK1; -.
PDBsum; 4TK2; -.
PDBsum; 4TK3; -.
PDBsum; 4TK4; -.
PDBsum; 4U90; -.
PDBsum; 4U91; -.
PDBsum; 5ERQ; -.
PDBsum; 5ERR; -.
PDBsum; 5ERS; -.
PDBsum; 5ERT; -.
PDBsum; 5ERU; -.
PDBsum; 5ERV; -.
ProteinModelPortal; Q03555; -.
SMR; Q03555; -.
BioGrid; 249211; 8.
DIP; DIP-33263N; -.
IntAct; Q03555; 9.
MINT; Q03555; -.
iPTMnet; Q03555; -.
PhosphoSitePlus; Q03555; -.
SwissPalm; Q03555; -.
PRIDE; Q03555; -.
GeneID; 64845; -.
KEGG; rno:64845; -.
UCSC; RGD:69194; rat. [Q03555-1]
CTD; 10243; -.
RGD; 69194; Gphn.
HOGENOM; HOG000280651; -.
HOVERGEN; HBG005828; -.
InParanoid; Q03555; -.
KO; K15376; -.
PhylomeDB; Q03555; -.
UniPathway; UPA00344; -.
EvolutionaryTrace; Q03555; -.
PRO; PR:Q03555; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0060077; C:inhibitory synapse; IDA:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0099572; C:postsynaptic specialization; IDA:SynGO.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IDA:MGI.
GO; GO:0061599; F:molybdopterin molybdotransferase activity; IDA:MGI.
GO; GO:0030674; F:protein binding, bridging; TAS:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0032947; F:protein-containing complex scaffold activity; IDA:RGD.
GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
GO; GO:0015631; F:tubulin binding; TAS:RGD.
GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL.
GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISS:UniProtKB.
GO; GO:0072579; P:glycine receptor clustering; IBA:GO_Central.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IDA:MGI.
GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0006605; P:protein targeting; TAS:RGD.
GO; GO:0007416; P:synapse assembly; IEP:RGD.
CDD; cd00887; MoeA; 1.
CDD; cd00886; MogA_MoaB; 1.
Gene3D; 2.40.340.10; -; 1.
Gene3D; 3.40.980.10; -; 2.
InterPro; IPR036425; MoaB/Mog-like_dom_sf.
InterPro; IPR001453; MoaB/Mog_dom.
InterPro; IPR008284; MoCF_biosynth_CS.
InterPro; IPR038987; MoeA-like.
InterPro; IPR005111; MoeA_C_domain_IV.
InterPro; IPR036688; MoeA_C_domain_IV_sf.
InterPro; IPR005110; MoeA_linker/N.
InterPro; IPR036135; MoeA_linker/N_sf.
PANTHER; PTHR10192; PTHR10192; 1.
Pfam; PF00994; MoCF_biosynth; 2.
Pfam; PF03454; MoeA_C; 1.
Pfam; PF03453; MoeA_N; 1.
SMART; SM00852; MoCF_biosynth; 2.
SUPFAM; SSF53218; SSF53218; 2.
SUPFAM; SSF63867; SSF63867; 1.
SUPFAM; SSF63882; SSF63882; 1.
TIGRFAMs; TIGR00177; molyb_syn; 2.
PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Magnesium; Membrane;
Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Synapse; Transferase.
CHAIN 1 768 Gephyrin.
/FTId=PRO_0000170965.
REGION 14 166 MPT Mo-transferase.
REGION 153 348 Interaction with GABARAP.
{ECO:0000269|PubMed:10900017}.
REGION 326 768 MPT adenylyltransferase.
COMPBIAS 213 218 Glu-rich (acidic).
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9NQX3}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BUV3}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BUV3}.
MOD_RES 278 278 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8BUV3}.
MOD_RES 279 279 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9NQX3}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BUV3}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQX3}.
VAR_SEQ 1 22 MATEGMILTNHDHQIRVGVLTV -> MSFPLSPAFTLLHIL
V (in isoform 1).
{ECO:0000303|PubMed:11083919}.
/FTId=VSP_003238.
VAR_SEQ 99 111 Missing (in isoform 5, isoform 2 and
isoform 3). {ECO:0000303|PubMed:11083919,
ECO:0000303|PubMed:1319186}.
/FTId=VSP_003239.
VAR_SEQ 256 256 K -> KNHPFYTSPAVFMANHGQPIPGLISYSHHATGSADK
R (in isoform 2).
{ECO:0000303|PubMed:11083919}.
/FTId=VSP_003240.
VAR_SEQ 302 320 Missing (in isoform 5 and isoform 2).
{ECO:0000303|PubMed:11083919,
ECO:0000303|PubMed:1319186}.
/FTId=VSP_003243.
VAR_SEQ 302 315 QIRRPDESKGVASR -> ARLPSCSSTYSVSE (in
isoform 4).
{ECO:0000303|PubMed:11083919}.
/FTId=VSP_003241.
VAR_SEQ 316 320 Missing (in isoform 4).
{ECO:0000303|PubMed:11083919}.
/FTId=VSP_003242.
MUTAGEN 362 362 F->A: Reduced GLRB binding.
{ECO:0000269|PubMed:16511563}.
MUTAGEN 745 746 PP->AA: Reduced GLRB binding.
{ECO:0000269|PubMed:16511563}.
MUTAGEN 745 745 P->A: Loss of GLRB binding.
{ECO:0000269|PubMed:16511563}.
CONFLICT 255 255 A -> R (in Ref. 3). {ECO:0000305}.
STRAND 16 22 {ECO:0000244|PDB:1IHC}.
HELIX 24 27 {ECO:0000244|PDB:1IHC}.
HELIX 34 44 {ECO:0000244|PDB:1IHC}.
TURN 46 49 {ECO:0000244|PDB:1IHC}.
STRAND 52 59 {ECO:0000244|PDB:1IHC}.
HELIX 63 75 {ECO:0000244|PDB:1IHC}.
STRAND 80 86 {ECO:0000244|PDB:1IHC}.
STRAND 89 91 {ECO:0000244|PDB:1IHC}.
HELIX 112 116 {ECO:0000244|PDB:1IHC}.
STRAND 118 120 {ECO:0000244|PDB:1IHC}.
HELIX 122 135 {ECO:0000244|PDB:1IHC}.
HELIX 137 141 {ECO:0000244|PDB:1IHC}.
STRAND 146 149 {ECO:0000244|PDB:1IHC}.
STRAND 152 157 {ECO:0000244|PDB:1IHC}.
HELIX 161 171 {ECO:0000244|PDB:1IHC}.
HELIX 172 174 {ECO:0000244|PDB:1IHC}.
HELIX 175 182 {ECO:0000244|PDB:1IHC}.
HELIX 188 193 {ECO:0000244|PDB:1IHC}.
STRAND 355 357 {ECO:0000244|PDB:4U90}.
HELIX 358 368 {ECO:0000244|PDB:5ERQ}.
STRAND 374 378 {ECO:0000244|PDB:5ERQ}.
HELIX 379 381 {ECO:0000244|PDB:5ERQ}.
STRAND 386 389 {ECO:0000244|PDB:5ERQ}.
STRAND 397 400 {ECO:0000244|PDB:5ERQ}.
STRAND 402 410 {ECO:0000244|PDB:5ERQ}.
HELIX 412 414 {ECO:0000244|PDB:5ERQ}.
STRAND 416 425 {ECO:0000244|PDB:5ERQ}.
STRAND 439 443 {ECO:0000244|PDB:5ERQ}.
STRAND 455 458 {ECO:0000244|PDB:5ERQ}.
HELIX 459 461 {ECO:0000244|PDB:5ERQ}.
STRAND 462 467 {ECO:0000244|PDB:5ERQ}.
STRAND 471 479 {ECO:0000244|PDB:5ERQ}.
TURN 485 488 {ECO:0000244|PDB:5ERQ}.
STRAND 494 496 {ECO:0000244|PDB:5ERQ}.
STRAND 501 503 {ECO:0000244|PDB:5ERQ}.
HELIX 511 520 {ECO:0000244|PDB:5ERQ}.
STRAND 524 528 {ECO:0000244|PDB:5ERQ}.
STRAND 533 538 {ECO:0000244|PDB:5ERQ}.
HELIX 558 568 {ECO:0000244|PDB:5ERQ}.
STRAND 573 579 {ECO:0000244|PDB:5ERQ}.
HELIX 583 596 {ECO:0000244|PDB:5ERQ}.
STRAND 598 605 {ECO:0000244|PDB:5ERQ}.
STRAND 607 609 {ECO:0000244|PDB:5ERQ}.
TURN 610 613 {ECO:0000244|PDB:5ERQ}.
HELIX 614 620 {ECO:0000244|PDB:5ERQ}.
STRAND 625 632 {ECO:0000244|PDB:5ERQ}.
STRAND 640 646 {ECO:0000244|PDB:5ERQ}.
STRAND 649 656 {ECO:0000244|PDB:5ERQ}.
HELIX 660 669 {ECO:0000244|PDB:5ERQ}.
HELIX 671 678 {ECO:0000244|PDB:5ERQ}.
STRAND 688 695 {ECO:0000244|PDB:5ERQ}.
STRAND 704 711 {ECO:0000244|PDB:5ERQ}.
STRAND 716 718 {ECO:0000244|PDB:1T3E}.
STRAND 720 723 {ECO:0000244|PDB:5ERQ}.
STRAND 728 730 {ECO:0000244|PDB:2FTS}.
HELIX 731 734 {ECO:0000244|PDB:5ERQ}.
STRAND 740 744 {ECO:0000244|PDB:5ERQ}.
STRAND 752 754 {ECO:0000244|PDB:5ERU}.
STRAND 759 764 {ECO:0000244|PDB:5ERQ}.
SEQUENCE 768 AA; 83266 MW; FAD1B6DD76ED79EA CRC64;
MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEKF PTFPFCGLQK GATKEVIERE
APGMALAMLM GSLNVTPLGM LSRPVCGIRG KTLIINLPGS KKGSQECFQF ILPALPHAID
LLRDAIVKVK EVHDELEDLP SPPPPLSPPP TTSPHKQTED KGVQCEEEEE EKKDSGVAST
EDSSSSHITA AALAAKIPDS IISRGVQVLP RDTASLSTTP SESPRAQATS RLSTASCPTP
KQIRRPDESK GVASRVGSLK VQSRCSSKEN ILRASHSAVD ITKVARRHRM SPFPLTSMDK
AFITVLEMTP VLGTEIINYR DGMGRVLAQD VYAKDNLPPF PASVKDGYAV RAADGPGDRF
IIGESQAGEQ PTQTVMPGQV MRVTTGAPIP CGADAVVQVE DTELIRESDD GTEELEVRIL
VQARPGQDIR PIGHDIKRGE CVLAKGTHMG PSEIGLLATV GVTEVEVNKF PVVAVMSTGN
ELLNPEDDLL PGKIRDSNRS TLLATIQEHG YPTINLGIVG DNPDDLLNAL NEGISRADVI
ITSGGVSMGE KDYLKQVLDI DLHAQIHFGR VFMKPGLPTT FATLDIDGVR KIIFALPGNP
VSAVVTCNLF VVPALRKMQG ILDPRPTIIK ARLSCDVKLD PRPEYHRCIL TWHHQEPLPW
AQSTGNQMSS RLMSMRSANG LLMLPPKTEQ YVELHKGEVV DVMVIGRL


Related products :

Catalog number Product name Quantity
CSB-EL009716RA Rat Gephyrin [Includes: Molybdopterin adenylyltransferase(GPHN) ELISA kit 96T
CSB-EL009716MO Mouse Gephyrin [Includes: Molybdopterin adenylyltransferase(GPHN) ELISA kit 96T
CSB-EL009716CH Chicken Gephyrin [Includes: Molybdopterin adenylyltransferase(GPHN) ELISA kit 96T
CSB-EL009716RA Rat Gephyrin [Includes Molybdopterin adenylyltransferase(GPHN) ELISA kit SpeciesRat 96T
CSB-EL009716HU Human Gephyrin [Includes: Molybdopterin adenylyltransferase(GPHN) ELISA kit 96T
CSB-EL009716HU Human Gephyrin [Includes Molybdopterin adenylyltransferase(GPHN) ELISA kit SpeciesHuman 96T
CSB-EL009716CH Chicken Gephyrin [Includes Molybdopterin adenylyltransferase(GPHN) ELISA kit SpeciesChicken 96T
CSB-EL009716MO Mouse Gephyrin [Includes Molybdopterin adenylyltransferase(GPHN) ELISA kit SpeciesMouse 96T
EIAAB27400 Kiaa0479,Mouse,Mus musculus,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 2,Nmnat2
EIAAB27398 D4Cole1e,Mouse,Mus musculus,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 1,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 1,Nmnat,Nmnat1
EIAAB27397 Homo sapiens,Human,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 1,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 1,NMNAT,NMNAT1
EIAAB27402 NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 2,Nmnat2,Rat,Rattus norvegicus
EIAAB27405 Mouse,Mus musculus,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 3,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 3,Nmnat3
EIAAB27399 Bos taurus,Bovine,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 1,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 1,NMNAT1
EIAAB27401 Bos taurus,Bovine,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 2,NMNAT2
EIAAB27403 C1orf15,Homo sapiens,Human,KIAA0479,NaMN adenylyltransferase 2,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 2,NMN adenylyltransferase 2,NMNAT2
EIAAB27404 FKSG76,Homo sapiens,Human,NaMN adenylyltransferase 3,Nicotinamide mononucleotide adenylyltransferase 3,Nicotinate-nucleotide adenylyltransferase 3,NMN adenylyltransferase 3,NMNAT3,PNAT-3,Pyridine nucl
EIAAB25090 Adenylyltransferase and sulfurtransferase MOCS3,Homo sapiens,Human,MOCS3,Molybdenum cofactor synthesis protein 3,Molybdopterin synthase sulfurylase,MPT synthase sulfurylase,UBA4
EIAAB25078 Homo sapiens,Human,MOCO1,MOCO1-A,MOCS2,MOCS2A,Molybdenum cofactor synthesis protein 2 small subunit,Molybdenum cofactor synthesis protein 2A,Molybdopterin synthase sulfur carrier subunit,Molybdopterin
EIAAB29835 Mouse,Mtpap,Mus musculus,PAP,PAP-associated domain-containing protein 1,Papd1,Poly(A) RNA polymerase, mitochondrial,Polynucleotide adenylyltransferase
EIAAB29834 Homo sapiens,Human,mtPAP,MTPAP,PAP,PAP-associated domain-containing protein 1,PAPD1,Poly(A) RNA polymerase, mitochondrial,Polynucleotide adenylyltransferase,Terminal uridylyltransferase 1,TUTase 1
EIAAB09918 ATPBD3,ATP-binding domain-containing protein 3,Cancer-associated gene protein,CTU1,Cytoplasmic tRNA 2-thiolation protein 1,Cytoplasmic tRNA adenylyltransferase 1,Homo sapiens,Human,NCS6
EIAAB09919 ATPBD3,ATP-binding domain-containing protein 3,Bos taurus,Bovine,CTU1,Cytoplasmic tRNA 2-thiolation protein 1,Cytoplasmic tRNA adenylyltransferase 1,NCS6
EIAAB09917 Atpbd3,ATP-binding domain-containing protein 3,Ctu1,Cytoplasmic tRNA 2-thiolation protein 1,Cytoplasmic tRNA adenylyltransferase 1,Ncs6,Rat,Rattus norvegicus
EIAAB09916 Atpbd3,ATP-binding domain-containing protein 3,Ctu1,Cytoplasmic tRNA 2-thiolation protein 1,Cytoplasmic tRNA adenylyltransferase 1,Mouse,Mus musculus,Ncs6


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur