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Q8BUV3

- GEPH_MOUSE

UniProt

Q8BUV3 - GEPH_MOUSE

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Protein
Gephyrin
Gene
Gphn
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.
Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Cofactori

Magnesium By similarity.

Enzyme regulationi

Inhibited by copper and tungsten By similarity.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cytoskeletal protein binding Source: MGI
  3. metal ion binding Source: UniProtKB-KW
  4. molybdopterin adenylyltransferase activity Source: UniProtKB-EC
  5. molybdopterin molybdotransferase activity Source: UniProtKB-EC
  6. protein binding Source: IntAct

GO - Biological processi

  1. Mo-molybdopterin cofactor biosynthetic process Source: MGI
  2. establishment of synaptic specificity at neuromuscular junction Source: MGI
  3. glycine receptor clustering Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Molybdenum, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198541. Molybdenum cofactor biosynthesis.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Gephyrin
Including the following 2 domains:
Molybdopterin adenylyltransferase (EC:2.7.7.75)
Short name:
MPT adenylyltransferase
Alternative name(s):
Domain G
Molybdopterin molybdenumtransferase (EC:2.10.1.1)
Short name:
MPT Mo-transferase
Alternative name(s):
Domain E
Gene namesi
Name:Gphn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:109602. Gphn.

Subcellular locationi

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.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-SubCell
  4. extrinsic component of plasma membrane Source: MGI
  5. inhibitory synapse Source: MGI
  6. intracellular Source: MGI
  7. postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 769769Gephyrin
PRO_0000269039Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine1 Publication
Modified residuei266 – 2661Phosphothreonine By similarity
Modified residuei338 – 3381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BUV3.
PaxDbiQ8BUV3.
PRIDEiQ8BUV3.

PTM databases

PhosphoSiteiQ8BUV3.

Expressioni

Gene expression databases

ArrayExpressiQ8BUV3.
BgeeiQ8BUV3.
CleanExiMM_GPHN.
GenevestigatoriQ8BUV3.

Interactioni

Subunit structurei

Homotrimer, homodimer and homooligomer. Interacts with GLRB and GABARAP By similarity. Interacts with SRGAP2 (via SH3 domain).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GlrbP481684EBI-771218,EBI-7069198
Pin1Q9QUR76EBI-771218,EBI-2432975

Protein-protein interaction databases

BioGridi234521. 1 interaction.
IntActiQ8BUV3. 6 interactions.
MINTiMINT-1869852.

Structurei

3D structure databases

ProteinModelPortaliQ8BUV3.
SMRiQ8BUV3. Positions 13-181, 351-769.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 153140MPT Mo-transferase
Add
BLAST
Regioni140 – 349210Interaction with GABARAP By similarity
Add
BLAST
Regioni327 – 769443MPT adenylyltransferase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi187 – 1926Poly-Pro
Compositional biasi213 – 2186Glu-rich (acidic)

Sequence similaritiesi

In the N-terminal section; belongs to the MoaB/Mog family.
In the C-terminal section; belongs to the MoeA family.

Phylogenomic databases

eggNOGiCOG0303.
GeneTreeiENSGT00390000016577.
HOGENOMiHOG000280651.
HOVERGENiHBG005828.
KOiK15376.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProiIPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd_dom.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 2 hits.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BUV3-1 [UniParc]FASTAAdd to Basket

« Hide

MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG    50
GTISAYKIVP DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT 100
KEVIEREAPG MALAMLMGSL NVTPLGMLSR PVCGIRGKTL IINLPGSKKG 150
SQECFQFILP ALPHAIDLLR DAIVKVKEVH DELEDLPSPP PPLSPPPTTS 200
PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAL AAKIPDSIIS 250
RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKQI RRPDESKGVA 300
SRVGSLKARL PSCSSTYSVS EVQSRCSSKE NILRASHSAV DITKVARRHR 350
MSPFPLTSMD KAFITVLEMT PVLGTEIINY RDGMGRVLAQ DVYAKDNLPP 400
FPASVKDGYA VRAADGPGDR FIIGESQAGE QPTQTVMPGQ VMRVTTGAPI 450
PCGADAVVQV EDTELIRESD DGTEELEVRI LVQARPGQDI RPIGHDIKRG 500
ECVLAKGTHM GPSEIGLLAT VGVTEVEVNK FPVVAVMSTG NELLNPEDDL 550
LPGKIRDSNR STLLATIQEH GYPTINLGIV GDNPDDLLNA LNEGISRADV 600
IITSGGVSMG EKDYLKQVLD IDLHAQIHFG RVFMKPGLPT TFATLDIDGV 650
RKIIFALPGN PVSAVVTCNL FVVPALRKMQ GILDPRPTII KARLSCDVKL 700
DPRPEYHRCI LTWHHQEPLP WAQSTGNQMS SRLMSMRSAN GLLMLPPKTE 750
QYVELHKGEV VDVMVIGRL 769
Length:769
Mass (Da):83,282
Last modified:July 27, 2011 - v2
Checksum:iD0EF325CC3CF87E9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621S → T in BAC38476. 1 Publication
Sequence conflicti463 – 4631T → S in BAC38476. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26000.1.
RefSeqiNP_766540.2. NM_172952.3.
UniGeneiMm.341742.
Mm.363753.
Mm.453131.

Genome annotation databases

EnsembliENSMUST00000052472; ENSMUSP00000054064; ENSMUSG00000047454.
GeneIDi268566.
KEGGimmu:268566.
UCSCiuc007nzc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS26000.1.
RefSeqi NP_766540.2. NM_172952.3.
UniGenei Mm.341742.
Mm.363753.
Mm.453131.

3D structure databases

ProteinModelPortali Q8BUV3.
SMRi Q8BUV3. Positions 13-181, 351-769.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 234521. 1 interaction.
IntActi Q8BUV3. 6 interactions.
MINTi MINT-1869852.

PTM databases

PhosphoSitei Q8BUV3.

Proteomic databases

MaxQBi Q8BUV3.
PaxDbi Q8BUV3.
PRIDEi Q8BUV3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000052472 ; ENSMUSP00000054064 ; ENSMUSG00000047454 .
GeneIDi 268566.
KEGGi mmu:268566.
UCSCi uc007nzc.2. mouse.

Organism-specific databases

CTDi 10243.
MGIi MGI:109602. Gphn.

Phylogenomic databases

eggNOGi COG0303.
GeneTreei ENSGT00390000016577.
HOGENOMi HOG000280651.
HOVERGENi HBG005828.
KOi K15376.

Enzyme and pathway databases

UniPathwayi UPA00344 .
Reactomei REACT_198541. Molybdenum cofactor biosynthesis.

Miscellaneous databases

ChiTaRSi GPHN. mouse.
NextBioi 392389.
PROi Q8BUV3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BUV3.
Bgeei Q8BUV3.
CleanExi MM_GPHN.
Genevestigatori Q8BUV3.

Family and domain databases

Gene3Di 2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProi IPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd_dom.
[Graphical view ]
Pfami PF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view ]
SMARTi SM00852. MoCF_biosynth. 2 hits.
[Graphical view ]
SUPFAMi SSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsi TIGR00177. molyb_syn. 2 hits.
PROSITEi PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiGEPH_MOUSE
AccessioniPrimary (citable) accession number: Q8BUV3
Secondary accession number(s): E9QKJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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