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Protein

Protein unc-13 homolog A

Gene

Unc13a

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

Functioni

Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Also involved in secretory granule priming in insulin secretion. Plays a role in dendrite formation by melanocytes (By similarity).By similarity7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi576 – 5761Zinc 1By similarity
Metal bindingi579 – 5791Zinc 1By similarity
Metal bindingi593 – 5931Zinc 2By similarity
Metal bindingi596 – 5961Zinc 2By similarity
Metal bindingi604 – 6041Zinc 1By similarity
Metal bindingi612 – 6121Zinc 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri562 – 61251Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • diacylglycerol binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • protein N-terminus binding Source: ParkinsonsUK-UCL
  • syntaxin-1 binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • beta-amyloid metabolic process Source: MGI
  • innervation Source: MGI
  • intracellular signal transduction Source: InterPro
  • neuromuscular junction development Source: MGI
  • neurotransmitter secretion Source: ParkinsonsUK-UCL
  • positive regulation of dendrite extension Source: MGI
  • positive regulation of neurotransmitter secretion Source: MGI
  • regulation of short-term neuronal synaptic plasticity Source: MGI
  • regulation of synaptic vesicle priming Source: ParkinsonsUK-UCL
  • synaptic transmission, glutamatergic Source: MGI
  • synaptic vesicle docking Source: MGI
  • synaptic vesicle maturation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Differentiation, Exocytosis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein unc-13 homolog A
Alternative name(s):
Munc13-1
Gene namesi
Name:Unc13aImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:3051532. Unc13a.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Cell junctionsynapsepresynaptic cell membrane By similarity; Peripheral membrane protein By similarity

  • Note: Localized to the active zone of presynaptic density. Translocated to the plasma membrane in response to phorbol ester binding (By similarity).By similarity

GO - Cellular componenti

  • axon Source: MGI
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB-SubCell
  • neuromuscular junction Source: MGI
  • neuron projection Source: ParkinsonsUK-UCL
  • presynapse Source: MGI
  • presynaptic membrane Source: ParkinsonsUK-UCL
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mice display normal synapse formation but abnormal synaptic vesicle maturation and die shortly after birth. Heterozygotes exhibit impaired insulin secretion and abnormal glucose tolerance.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi563 – 5631H → V: Reduces number of fusion-competent vesicles in neurons. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17121712Protein unc-13 homolog APRO_0000306285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391PhosphoserineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei244 – 2441PhosphoserineBy similarity
Modified residuei255 – 2551PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ4KUS2.
PaxDbiQ4KUS2.
PeptideAtlasiQ4KUS2.
PRIDEiQ4KUS2.

PTM databases

iPTMnetiQ4KUS2.
PhosphoSiteiQ4KUS2.

Expressioni

Gene expression databases

BgeeiQ4KUS2.
CleanExiMM_UNC13A.
ExpressionAtlasiQ4KUS2. baseline and differential.
GenevisibleiQ4KUS2. MM.

Interactioni

Subunit structurei

Interacts with the N-termini of STX1A and/or STX1B1 and DOC2A. Interacts with BSN. Interacts with RIMS1 which recruits UNC13A to the active zone. Forms homodimers via its first C2 domain. Also interacts via this domain with the zinc finger domain of RIMS2. Part of a complex consisting of ERC2, RIMS1 and UNC13A. Also part of a complex consisting of UNC13A, RIMS2 and RAB3A (By similarity). Interacts with FBXO45 (via SRY domain); leading to the degradation of UNC13A by the proteasome.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ4KUS2. 1 interaction.
STRINGi10090.ENSMUSP00000030170.

Structurei

3D structure databases

ProteinModelPortaliQ4KUS2.
SMRiQ4KUS2. Positions 2-128, 454-488, 563-612, 683-815, 938-1519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7979C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini672 – 778107C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini1102 – 1245144MHD1PROSITE-ProRule annotationAdd
BLAST
Domaini1354 – 1521168MHD2PROSITE-ProRule annotationAdd
BLAST
Domaini1541 – 1646106C2 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili321 – 36040Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi321 – 448128Glu-richSequence analysisAdd
BLAST

Domaini

The C2 domains are not involved in calcium-dependent phospholipid binding.By similarity
The C-terminal region containing both MHD domains and the third C2 domain is required for synaptic vesicle priming activity.By similarity

Sequence similaritiesi

Contains 3 C2 domains.PROSITE-ProRule annotation
Contains 1 MHD1 (MUNC13 homology domain 1) domain.PROSITE-ProRule annotation
Contains 1 MHD2 (MUNC13 homology domain 2) domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri562 – 61251Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1011. Eukaryota.
ENOG410XS5D. LUCA.
GeneTreeiENSGT00730000110590.
HOGENOMiHOG000231404.
HOVERGENiHBG057340.
InParanoidiQ4KUS2.
KOiK15293.
OrthoDBiEOG76738V.
TreeFamiTF312844.

Family and domain databases

Gene3Di2.60.40.150. 3 hits.
InterProiIPR000008. C2_dom.
IPR010439. CAPS_dom.
IPR014770. Munc13_1.
IPR014772. Munc13_dom-2.
IPR019558. Munc13_subgr_dom-2.
IPR002219. PE/DAG-bd.
IPR027080. Unc-13.
[Graphical view]
PANTHERiPTHR10480. PTHR10480. 2 hits.
PfamiPF00130. C1_1. 1 hit.
PF00168. C2. 3 hits.
PF06292. DUF1041. 1 hit.
PF10540. Membr_traf_MHD. 1 hit.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00239. C2. 3 hits.
SM01145. DUF1041. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 3 hits.
PROSITEiPS50004. C2. 2 hits.
PS51258. MHD1. 1 hit.
PS51259. MHD2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4KUS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM
60 70 80 90 100
FEINRLDLGL TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD
110 120 130 140 150
SQAIMADSEI CGTKDPTFHR ILLDAHFELP LDIPEEEARY WAKKLEQLNA
160 170 180 190 200
MRDQDEYSFQ DQQDKPLPVP SSQCCNWNYF GWGEQNDDPD SAVDDRDSDY
210 220 230 240 250
RSETSNSIPP PYYTTSQPNA SVHQYSVRPP PLGSRESYSD SMHSYEEFSE
260 270 280 290 300
PRALSPTGSS RYASSGELSQ GSSQLSEDFD PDEHSLQGSE LDDERDRDSY
310 320 330 340 350
HSCHSSVSYH KDSPRWDQDD EDLEDLEDLE DEELPEEEEE LEEEGEEELE
360 370 380 390 400
EEDLEEEEEV PDDLASYTQQ EDTTVAEPKE FKRISFPTAA PQKDDKVSAV
410 420 430 440 450
PTEAPEVAKG IPKAATPEEK AAAERAQEAE PPKSEESFRS REEEEGQEGQ
460 470 480 490 500
DAMSRAKANW LRAFNKVRMQ LQEARGEGDM SKSLWFKGGP GGGLIIIDSM
510 520 530 540 550
PDIRKRKPIP LVSDLAMSLV QSRKAGITSA LASSTLNNEE LKNHVYKKTL
560 570 580 590 600
QALIYPISCT TPHNFEVWTA TTPTYCYECE GLLWGIARQG MRCTECGVKC
610 620 630 640 650
HEKCQDLLNA DCLQRAAEKS SKHGAEDRTQ NIIMVLKDRM KIRERNKPEI
660 670 680 690 700
FELIQEIFAV TKSAHTQQMK AVKQSVLDGT SKWSAKISIT VVCAQGLQAK
710 720 730 740 750
DKTGSSDPYV TVQVGKTKKR TKTIYGNLNP VWEENFHFEC HNSSDRIKVR
760 770 780 790 800
VWDEDDDIKS RVKQRFKRES DDFLGQTIIE VRTLSGEMDV WYNLDKRTDK
810 820 830 840 850
SAVSGAIRLH ISVEIKGEEK VAPYHVQYTC LHENLFHFVT DVQNNGVVKI
860 870 880 890 900
PDAKGDDAWK VYYDETAQEI VDEFAMRYGV ESIYQAMTHF ACLSSKYMCP
910 920 930 940 950
GVPAVMSTLL ANINAYYAHT TASTNVSASD RFAASNFGKE RFVKLLDQLH
960 970 980 990 1000
NSLRIDLSMY RNNFPASSPE RLQDLKSTVD LLTSITFFRM KVQELQSPPR
1010 1020 1030 1040 1050
ASQVVKDCVK ACLNSTYEYI FNNCHELYGR EYQTDPAKKG EVPPEEQGPS
1060 1070 1080 1090 1100
IKNLDFWSKL ITLIVSIIEE DKNSYTPCLN QFPQELNVGK ISAEVMWSLF
1110 1120 1130 1140 1150
AQDMKYAMEE HDKHRLCKSA DYMNLHFKVK WLYNEYVAEL PTFKDRVPEY
1160 1170 1180 1190 1200
PAWFEPFVIQ WLDENEEVSR DFLHGALERD KKDGFQQTSE HALFSCSVVD
1210 1220 1230 1240 1250
VFSQLNQSFE IIKKLECPDP QIVGHYMRRF AKTISNVLLQ YADIVSKDFA
1260 1270 1280 1290 1300
SYCSKEKEKV PCILMNNTQQ LRVQLEKMFE AMGGKELDAE ASGTLKELQV
1310 1320 1330 1340 1350
KLNNVLDELS HVFATSFQPH IEECVRQMGD ILSQVKGTGN VPASACSSVA
1360 1370 1380 1390 1400
QDADNVLQPI MDLLDSNLTL FAKICEKTVL KRVLKELWKL VMNTMEKTIV
1410 1420 1430 1440 1450
LPPLTDQTMI GTLLRKHGKG LEKGRVKLPS HSDGTQMIFN AAKELGQLSK
1460 1470 1480 1490 1500
LKDHMVREEA KSLTPKQCAV VELALDTIKQ YFHAGGVGLK KTFLEKSPDL
1510 1520 1530 1540 1550
QSLRYALSLY TQATDLLIKT FVQTQSAQGS GVEDPVGEVS VHVELFTHPG
1560 1570 1580 1590 1600
TGEQKVTVKV VAANDLKWQT SGIFRPFIEV NIVGPQLSDK KRKFATKSKN
1610 1620 1630 1640 1650
NSWAPKYNES FQFSLSADAG PECYELQVCV KDYCFAREDR TVGLAVLQLR
1660 1670 1680 1690 1700
ELAQRGSAAC WLPLGRRIHM DDTGLTVLRI LSQRSNDEVA KEFVKLKSDT
1710
RSAEEGGAAP AP
Length:1,712
Mass (Da):193,782
Last modified:July 27, 2011 - v3
Checksum:iAA498D15557454EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271F → I in BAE27895 (PubMed:16141072).Curated
Sequence conflicti479 – 4791D → E in AAX09281 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY753536 mRNA. Translation: AAX09281.1.
AC162033 Genomic DNA. No translation available.
AK147408 mRNA. Translation: BAE27895.1.
CCDSiCCDS22402.2.
RefSeqiNP_001025044.2. NM_001029873.2.
UniGeneiMm.334606.

Genome annotation databases

EnsembliENSMUST00000030170; ENSMUSP00000030170; ENSMUSG00000034799.
GeneIDi382018.
KEGGimmu:382018.
UCSCiuc033jgb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY753536 mRNA. Translation: AAX09281.1.
AC162033 Genomic DNA. No translation available.
AK147408 mRNA. Translation: BAE27895.1.
CCDSiCCDS22402.2.
RefSeqiNP_001025044.2. NM_001029873.2.
UniGeneiMm.334606.

3D structure databases

ProteinModelPortaliQ4KUS2.
SMRiQ4KUS2. Positions 2-128, 454-488, 563-612, 683-815, 938-1519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ4KUS2. 1 interaction.
STRINGi10090.ENSMUSP00000030170.

PTM databases

iPTMnetiQ4KUS2.
PhosphoSiteiQ4KUS2.

Proteomic databases

MaxQBiQ4KUS2.
PaxDbiQ4KUS2.
PeptideAtlasiQ4KUS2.
PRIDEiQ4KUS2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030170; ENSMUSP00000030170; ENSMUSG00000034799.
GeneIDi382018.
KEGGimmu:382018.
UCSCiuc033jgb.1. mouse.

Organism-specific databases

CTDi23025.
MGIiMGI:3051532. Unc13a.

Phylogenomic databases

eggNOGiKOG1011. Eukaryota.
ENOG410XS5D. LUCA.
GeneTreeiENSGT00730000110590.
HOGENOMiHOG000231404.
HOVERGENiHBG057340.
InParanoidiQ4KUS2.
KOiK15293.
OrthoDBiEOG76738V.
TreeFamiTF312844.

Miscellaneous databases

PROiQ4KUS2.
SOURCEiSearch...

Gene expression databases

BgeeiQ4KUS2.
CleanExiMM_UNC13A.
ExpressionAtlasiQ4KUS2. baseline and differential.
GenevisibleiQ4KUS2. MM.

Family and domain databases

Gene3Di2.60.40.150. 3 hits.
InterProiIPR000008. C2_dom.
IPR010439. CAPS_dom.
IPR014770. Munc13_1.
IPR014772. Munc13_dom-2.
IPR019558. Munc13_subgr_dom-2.
IPR002219. PE/DAG-bd.
IPR027080. Unc-13.
[Graphical view]
PANTHERiPTHR10480. PTHR10480. 2 hits.
PfamiPF00130. C1_1. 1 hit.
PF00168. C2. 3 hits.
PF06292. DUF1041. 1 hit.
PF10540. Membr_traf_MHD. 1 hit.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00239. C2. 3 hits.
SM01145. DUF1041. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 3 hits.
PROSITEiPS50004. C2. 2 hits.
PS51258. MHD1. 1 hit.
PS51259. MHD2. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse Munc13-1 sequence."
    Wang X., Honsbein A., Kilimann M.W.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: BrainImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] OF 127-1712.
    Strain: C57BL/6JImported.
  4. "Munc13-1 is essential for fusion competence of glutamatergic synaptic vesicles."
    Augustin I., Rosenmund C., Suedhof T.C., Brose N.
    Nature 400:457-461(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Total arrest of spontaneous and evoked synaptic transmission but normal synaptogenesis in the absence of Munc13-mediated vesicle priming."
    Varoqueaux F., Sigler A., Rhee J.-S., Brose N., Enk C., Reim K., Rosenmund C.
    Proc. Natl. Acad. Sci. U.S.A. 99:9037-9042(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Aberrant morphology and residual transmitter release at the Munc13-deficient mouse neuromuscular synapse."
    Varoqueaux F., Sons M.S., Plomp J.J., Brose N.
    Mol. Cell. Biol. 25:5973-5984(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Munc13-1 is required for the sustained release of insulin from pancreatic beta cells."
    Kang L., He Z., Xu P., Fan J., Betz A., Brose N., Xu T.
    Cell Metab. 3:463-468(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Munc13-1 deficiency reduces insulin secretion and causes abnormal glucose tolerance."
    Kwan E.P., Xie L., Sheu L., Nolan C.J., Prentki M., Betz A., Brose N., Gaisano H.Y.
    Diabetes 55:1421-1429(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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.
  10. "Munc13-1 C1 domain activation lowers the energy barrier for synaptic vesicle fusion."
    Basu J., Betz A., Brose N., Rosenmund C.
    J. Neurosci. 27:1200-1210(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-563.
  11. "Interaction between Munc13-1 and RIM is critical for glucagon-like peptide-1 mediated rescue of exocytotic defects in Munc13-1 deficient pancreatic beta-cells."
    Kwan E.P., Xie L., Sheu L., Ohtsuka T., Gaisano H.Y.
    Diabetes 56:2579-2588(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  13. Cited for: INTERACTION WITH FBXO45.

Entry informationi

Entry nameiUN13A_MOUSE
AccessioniPrimary (citable) accession number: Q4KUS2
Secondary accession number(s): E9QKH9, Q3UHG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.