Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8BUV3

- GEPH_MOUSE

UniProt

Q8BUV3 - GEPH_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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.By similarity

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

GO - Biological processi

  1. establishment of synaptic specificity at neuromuscular junction Source: MGI
  2. glycine receptor clustering Source: MGI
  3. Mo-molybdopterin cofactor biosynthetic process 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 By similarity; Peripheral membrane protein By similarity; 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-KW
  4. extrinsic component of plasma membrane Source: MGI
  5. inhibitory synapse Source: MGI
  6. intracellular Source: MGI
  7. postsynaptic membrane Source: UniProtKB-KW
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 – 769769GephyrinPRO_0000269039Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BUV3.
PaxDbiQ8BUV3.
PRIDEiQ8BUV3.

PTM databases

PhosphoSiteiQ8BUV3.

Expressioni

Gene expression databases

BgeeiQ8BUV3.
CleanExiMM_GPHN.
ExpressionAtlasiQ8BUV3. baseline and differential.
GenevestigatoriQ8BUV3.

Interactioni

Subunit structurei

Homotrimer, homodimer and homooligomer. Interacts with GLRB and GABARAP (By similarity). Interacts with SRGAP2 (via SH3 domain).By similarity1 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 153140MPT Mo-transferaseAdd
BLAST
Regioni140 – 349210Interaction with GABARAPBy similarityAdd
BLAST
Regioni327 – 769443MPT adenylyltransferaseAdd
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.Curated
In the C-terminal section; belongs to the MoeA family.Curated

Phylogenomic databases

eggNOGiCOG0303.
GeneTreeiENSGT00390000016577.
HOGENOMiHOG000280651.
HOVERGENiHBG005828.
InParanoidiQ8BUV3.
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

        10         20         30         40         50
MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG
60 70 80 90 100
GTISAYKIVP DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT
110 120 130 140 150
KEVIEREAPG MALAMLMGSL NVTPLGMLSR PVCGIRGKTL IINLPGSKKG
160 170 180 190 200
SQECFQFILP ALPHAIDLLR DAIVKVKEVH DELEDLPSPP PPLSPPPTTS
210 220 230 240 250
PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAL AAKIPDSIIS
260 270 280 290 300
RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKQI RRPDESKGVA
310 320 330 340 350
SRVGSLKARL PSCSSTYSVS EVQSRCSSKE NILRASHSAV DITKVARRHR
360 370 380 390 400
MSPFPLTSMD KAFITVLEMT PVLGTEIINY RDGMGRVLAQ DVYAKDNLPP
410 420 430 440 450
FPASVKDGYA VRAADGPGDR FIIGESQAGE QPTQTVMPGQ VMRVTTGAPI
460 470 480 490 500
PCGADAVVQV EDTELIRESD DGTEELEVRI LVQARPGQDI RPIGHDIKRG
510 520 530 540 550
ECVLAKGTHM GPSEIGLLAT VGVTEVEVNK FPVVAVMSTG NELLNPEDDL
560 570 580 590 600
LPGKIRDSNR STLLATIQEH GYPTINLGIV GDNPDDLLNA LNEGISRADV
610 620 630 640 650
IITSGGVSMG EKDYLKQVLD IDLHAQIHFG RVFMKPGLPT TFATLDIDGV
660 670 680 690 700
RKIIFALPGN PVSAVVTCNL FVVPALRKMQ GILDPRPTII KARLSCDVKL
710 720 730 740 750
DPRPEYHRCI LTWHHQEPLP WAQSTGNQMS SRLMSMRSAN GLLMLPPKTE
760
QYVELHKGEV VDVMVIGRL
Length:769
Mass (Da):83,282
Last modified:July 27, 2011 - v2
Checksum:iD0EF325CC3CF87E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621S → T in BAC38476. (PubMed:16141072)Curated
Sequence conflicti463 – 4631T → S in BAC38476. (PubMed:16141072)Curated

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.
InParanoidi Q8BUV3.
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

Bgeei Q8BUV3.
CleanExi MM_GPHN.
ExpressionAtlasi Q8BUV3. baseline and differential.
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: October 29, 2014
This is version 99 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