Q8BUV3 (GEPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gephyrin

Including the following 2 domains:

1. Molybdopterin adenylyltransferase
   Short name=MPT adenylyltransferase
   EC=2.7.7.75
   Alternative name(s):
   Domain G
2. Molybdopterin molybdenumtransferase
   Short name=MPT Mo-transferase
   EC=2.10.1.1
   Alternative name(s):
   Domain E

Gene names

Name:

Gphn

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	769 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	ATP + molybdopterin = diphosphate + adenylyl-molybdopterin. Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.
Cofactor	Magnesium By similarity.
Enzyme regulation	Inhibited by copper and tungsten By similarity.
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Homotrimer, homodimer and homooligomer. Interacts with GLRB and GABARAP By similarity. Interacts with SRGAP2 (via SH3 domain). Ref.7
Subcellular location	Cell junction › synapse. Cell junction › synapse › postsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton By similarity. Note: Cytoplasmic face of glycinergic postsynaptic membranes By similarity.
Sequence similarities	In the N-terminal section; belongs to the MoaB/Mog family. In the C-terminal section; belongs to the MoeA family.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Postsynaptic cell membrane Synapse
Ligand	ATP-binding Magnesium Metal-binding Molybdenum Nucleotide-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW establishment of synaptic specificity at neuromuscular junction Inferred from mutant phenotype PubMed 10531433. Source: MGI
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to plasma membrane Traceable author statement PubMed 9089277. Source: MGI intracellular Inferred from direct assay PubMed 17145751. Source: MGI postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cytoskeletal protein binding Traceable author statement PubMed 10531433. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 769	769	Gephyrin		PRO_0000269039
Regions
	Region	14 – 153	140	MPT Mo-transferase
	Region	140 – 349	210	Interaction with GABARAP By similarity
	Region	327 – 769	443	MPT adenylyltransferase
	Compositional bias	187 – 192	6	Poly-Pro
	Compositional bias	213 – 218	6	Glu-rich (acidic)
Amino acid modifications
	Modified residue	188	1	Phosphoserine Ref.4 Ref.6
	Modified residue	194	1	Phosphoserine Ref.4 Ref.6
	Modified residue	266	1	Phosphothreonine By similarity
	Modified residue	338	1	Phosphoserine Ref.3 Ref.5
Experimental info
	Sequence conflict	262	1	S → T in BAC38476. Ref.1
	Sequence conflict	463	1	T → S in BAC38476. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BUV3 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: D0EF325CC3CF87E9	FASTA	769	83,282
	10 20 30 40 50 60 MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP 70 80 90 100 110 120 DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MALAMLMGSL 130 140 150 160 170 180 NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH 190 200 210 220 230 240 DELEDLPSPP PPLSPPPTTS PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAL 250 260 270 280 290 300 AAKIPDSIIS RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKQI RRPDESKGVA 310 320 330 340 350 360 SRVGSLKARL PSCSSTYSVS EVQSRCSSKE NILRASHSAV DITKVARRHR MSPFPLTSMD 370 380 390 400 410 420 KAFITVLEMT PVLGTEIINY RDGMGRVLAQ DVYAKDNLPP FPASVKDGYA VRAADGPGDR 430 440 450 460 470 480 FIIGESQAGE QPTQTVMPGQ VMRVTTGAPI PCGADAVVQV EDTELIRESD DGTEELEVRI 490 500 510 520 530 540 LVQARPGQDI RPIGHDIKRG ECVLAKGTHM GPSEIGLLAT VGVTEVEVNK FPVVAVMSTG 550 560 570 580 590 600 NELLNPEDDL LPGKIRDSNR STLLATIQEH GYPTINLGIV GDNPDDLLNA LNEGISRADV 610 620 630 640 650 660 IITSGGVSMG EKDYLKQVLD IDLHAQIHFG RVFMKPGLPT TFATLDIDGV RKIIFALPGN 670 680 690 700 710 720 PVSAVVTCNL FVVPALRKMQ GILDPRPTII KARLSCDVKL DPRPEYHRCI LTWHHQEPLP 730 740 750 760 WAQSTGNQMS SRLMSMRSAN GLLMLPPKTE QYVELHKGEV VDVMVIGRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, MASS SPECTROMETRY. Tissue: Brain.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, MASS SPECTROMETRY. Tissue: Melanoma.
[7]	"SH3 domain-based phototrapping in living cells reveals Rho family GAP signaling complexes." Okada H., Uezu A., Mason F.M., Soderblom E.J., Moseley M.A. III, Soderling S.H. Sci. Signal. 4:RS13-RS13(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRGAP2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK082353 mRNA. Translation: BAC38476.1. AC124346 Genomic DNA. No translation available. AC124572 Genomic DNA. No translation available. AC125057 Genomic DNA. No translation available. AC132097 Genomic DNA. No translation available. AC148324 Genomic DNA. No translation available.
IPI	IPI00225670.
RefSeq	NP_766540.2. NM_172952.3.
UniGene	Mm.341742. Mm.363753. Mm.453131.
3D structure databases
HSSP	HSSP built from PDB template 2FTS based on UniProtKB Q03555.
ProteinModelPortal	Q8BUV3.
SMR	Q8BUV3. Positions 13-181, 351-769.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BUV3. 2 interactions.
MINT	MINT-1869852.
PTM databases
PhosphoSite	Q8BUV3.
Proteomic databases
PaxDb	Q8BUV3.
PRIDE	Q8BUV3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000052472; ENSMUSP00000054064; ENSMUSG00000047454.
GeneID	268566.
KEGG	mmu:268566.
UCSC	uc007nzc.2. mouse.
Organism-specific databases
CTD	10243.
MGI	MGI:109602. Gphn.
Phylogenomic databases
eggNOG	COG0303.
GeneTree	ENSGT00390000016577.
HOGENOM	HOG000280651.
HOVERGEN	HBG005828.
KO	K15376.
OrthoDB	EOG4N30NB.
Enzyme and pathway databases
UniPathway	UPA00344.
Gene expression databases
ArrayExpress	Q8BUV3.
Bgee	Q8BUV3.
CleanEx	MM_GPHN.
Genevestigator	Q8BUV3.
Family and domain databases
Gene3D	2.40.340.10. 1 hit. 3.40.980.10. 2 hits.
InterPro	IPR020817. Mo_cofactor_synthesis. IPR008284. MoCF_biosynth_CS. IPR005111. MoeA_C_domain_IV. IPR005110. MoeA_linker/N. IPR001453. Mopterin-bd_dom. [Graphical view]
Pfam	PF00994. MoCF_biosynth. 2 hits. PF03454. MoeA_C. 1 hit. PF03453. MoeA_N. 1 hit. [Graphical view]
SMART	SM00852. MoCF_biosynth. 2 hits. [Graphical view]
SUPFAM	SSF53218. MoCF_biosynth. 2 hits. SSF63867. MoeA_C. 1 hit. SSF63882. MoeA_N. 1 hit.
TIGRFAMs	TIGR00177. molyb_syn. 2 hits.
PROSITE	PS01078. MOCF_BIOSYNTHESIS_1. 1 hit. PS01079. MOCF_BIOSYNTHESIS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GPHN. mouse.
NextBio	392389.
SOURCE	Search...

Entry information

Entry name

GEPH_MOUSE

Accession

Primary (citable) accession number: Q8BUV3
Secondary accession number(s): E9QKJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program