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Q8BUV3 (GEPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Protein existenceEvidence 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.6

Subcellular location

Cell junctionsynapse. Cell junctionsynapsepostsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytoskeleton 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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 769769Gephyrin
PRO_0000269039

Regions

Region14 – 153140MPT Mo-transferase
Region140 – 349210Interaction with GABARAP By similarity
Region327 – 769443MPT adenylyltransferase
Compositional bias187 – 1926Poly-Pro
Compositional bias213 – 2186Glu-rich (acidic)

Amino acid modifications

Modified residue1881Phosphoserine Ref.4
Modified residue1941Phosphoserine Ref.4
Modified residue2661Phosphothreonine By similarity
Modified residue3381Phosphoserine Ref.5

Experimental info

Sequence conflict2621S → T in BAC38476. Ref.1
Sequence conflict4631T → S in BAC38476. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BUV3 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: D0EF325CC3CF87E9

FASTA76983,282
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"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.
RefSeqNP_766540.2. NM_172952.3.
UniGeneMm.341742.
Mm.363753.
Mm.453131.

3D structure databases

ProteinModelPortalQ8BUV3.
SMRQ8BUV3. Positions 13-181, 351-769.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid234521. 1 interaction.
IntActQ8BUV3. 6 interactions.
MINTMINT-1869852.

PTM databases

PhosphoSiteQ8BUV3.

Proteomic databases

PaxDbQ8BUV3.
PRIDEQ8BUV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052472; ENSMUSP00000054064; ENSMUSG00000047454.
GeneID268566.
KEGGmmu:268566.
UCSCuc007nzc.2. mouse.

Organism-specific databases

CTD10243.
MGIMGI:109602. Gphn.

Phylogenomic databases

eggNOGCOG0303.
GeneTreeENSGT00390000016577.
HOGENOMHOG000280651.
HOVERGENHBG005828.
KOK15376.

Enzyme and pathway databases

UniPathwayUPA00344.

Gene expression databases

ArrayExpressQ8BUV3.
BgeeQ8BUV3.
CleanExMM_GPHN.
GenevestigatorQ8BUV3.

Family and domain databases

Gene3D2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProIPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd_dom.
[Graphical view]
PfamPF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTSM00852. MoCF_biosynth. 2 hits.
[Graphical view]
SUPFAMSSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsTIGR00177. molyb_syn. 2 hits.
PROSITEPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGPHN. mouse.
NextBio392389.
PROQ8BUV3.
SOURCESearch...

Entry information

Entry nameGEPH_MOUSE
AccessionPrimary (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: March 19, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot