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Protein

Protein unc-13 homolog A

Gene

Unc13a

Organism
Rattus norvegicus (Rat)
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 similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi580 – 5801Zinc 1
Metal bindingi583 – 5831Zinc 1
Metal bindingi597 – 5971Zinc 2
Metal bindingi600 – 6001Zinc 2
Metal bindingi608 – 6081Zinc 1
Metal bindingi616 – 6161Zinc 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri566 – 61651Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • diacylglycerol binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD
  • protein N-terminus binding Source: RGD
  • SNARE binding Source: RGD
  • spectrin binding Source: RGD
  • syntaxin-1 binding Source: RGD

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • intracellular signal transduction Source: InterPro
  • long-term synaptic potentiation Source: RGD
  • neurotransmitter secretion Source: RGD
  • synaptic vesicle priming Source: RGD
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:Unc13a
Synonyms:Unc13h1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619722. Unc13a.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB-SubCell
  • excitatory synapse Source: BHF-UCL
  • neuron projection Source: RGD
  • presynaptic membrane Source: RGD
  • protein complex Source: RGD
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221T → I: No effect on binding to RIMS1. 1 Publication
Mutagenesisi23 – 231Y → N: No effect on binding to RIMS1. 1 Publication
Mutagenesisi64 – 641V → M: No effect on binding to RIMS1. 1 Publication
Mutagenesisi119 – 1191H → R: No effect on binding to RIMS1. 1 Publication
Mutagenesisi121 – 1211I → N: Abolishes binding to RIMS1. 1 Publication
Mutagenesisi567 – 5671H → K: Loss of phorbol-ester binding. 1 Publication
Mutagenesisi1190 – 11901Q → R: Loss of binding to STX1B and priming activity; when associated with P-1279 and E-1655. 1 Publication
Mutagenesisi1279 – 12791L → P: Loss of binding to STX1B and priming activity; when associated with R-1190 and E-1655. 1 Publication
Mutagenesisi1364 – 13641I → F: Loss of binding to STX1B and priming activity. 1 Publication
Mutagenesisi1603 – 16031V → D: Loss of binding to STX1B and priming activity. 1 Publication
Mutagenesisi1655 – 16551D → E: Loss of binding to STX1B and priming activity; when associated with R-1190 and P-1279. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17351735Protein unc-13 homolog APRO_0000188574Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ62768.
PRIDEiQ62768.

PTM databases

iPTMnetiQ62768.
PhosphoSiteiQ62768.
SwissPalmiQ62768.

Expressioni

Tissue specificityi

Expressed in brain, with highest levels in the olfactory bulb, striatum, cerebral cortex, hippocampus and cerebellum. Also expressed in pancreatic islet cells.3 Publications

Developmental stagei

First detected at birth, after which expression level is steadily increasing until it reaches a plateau at P15.1 Publication

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. Interacts with FBXO45 (via SRY domain); leading to the degradation of UNC13A by the proteasome (By similarity).By similarity

GO - Molecular functioni

  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: RGD
  • protein N-terminus binding Source: RGD
  • SNARE binding Source: RGD
  • spectrin binding Source: RGD
  • syntaxin-1 binding Source: RGD

Protein-protein interaction databases

DIPiDIP-29191N.
STRINGi10116.ENSRNOP00000025162.

Structurei

Secondary structure

1
1735
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1211Combined sources
Helixi17 – 193Combined sources
Beta strandi21 – 288Combined sources
Beta strandi31 – 344Combined sources
Beta strandi38 – 425Combined sources
Beta strandi44 – 5310Combined sources
Beta strandi57 – 6610Combined sources
Beta strandi72 – 8110Combined sources
Helixi82 – 843Combined sources
Beta strandi95 – 984Combined sources
Beta strandi102 – 1065Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi120 – 1289Combined sources
Helixi135 – 15016Combined sources
Helixi459 – 47820Combined sources
Helixi487 – 4904Combined sources
Beta strandi569 – 5735Combined sources
Turni581 – 5833Combined sources
Beta strandi593 – 5975Combined sources
Turni598 – 6003Combined sources
Helixi608 – 6114Combined sources
Beta strandi689 – 70012Combined sources
Beta strandi712 – 7187Combined sources
Beta strandi721 – 7244Combined sources
Beta strandi735 – 74410Combined sources
Beta strandi750 – 7578Combined sources
Helixi762 – 7676Combined sources
Turni768 – 7703Combined sources
Beta strandi774 – 78411Combined sources
Helixi785 – 7873Combined sources
Beta strandi790 – 7978Combined sources
Beta strandi810 – 8189Combined sources
Helixi943 – 96119Combined sources
Helixi964 – 9674Combined sources
Helixi973 – 99523Combined sources
Helixi1005 – 102622Combined sources
Helixi1028 – 10358Combined sources
Beta strandi1039 – 10413Combined sources
Beta strandi1051 – 10533Combined sources
Helixi1059 – 107719Combined sources
Helixi1079 – 10824Combined sources
Turni1087 – 10893Combined sources
Helixi1092 – 111827Combined sources
Helixi1123 – 114018Combined sources
Turni1141 – 11433Combined sources
Helixi1145 – 11484Combined sources
Helixi1159 – 118729Combined sources
Beta strandi1192 – 11954Combined sources
Helixi1201 – 121818Combined sources
Helixi1224 – 125633Combined sources
Helixi1259 – 12613Combined sources
Helixi1263 – 128523Combined sources
Turni1286 – 12905Combined sources
Helixi1293 – 132028Combined sources
Helixi1322 – 133716Combined sources
Helixi1353 – 137826Combined sources
Helixi1381 – 140222Combined sources
Beta strandi1454 – 14563Combined sources
Beta strandi1458 – 14614Combined sources
Helixi1472 – 148716Combined sources
Helixi1488 – 14903Combined sources
Helixi1495 – 14995Combined sources
Helixi1502 – 151312Combined sources
Turni1516 – 15183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8FNMR-A567-616[»]
2CJSX-ray1.78A/B2-150[»]
2CJTX-ray1.44A/B/C/D1-128[»]
2KDUNMR-B458-492[»]
3KWTX-ray1.89A675-820[»]
3KWUX-ray1.37A675-820[»]
3SWHX-ray2.65A/B1148-1407[»]
A/B1453-1531[»]
4Y21X-ray2.90A942-1407[»]
A1453-1523[»]
ProteinModelPortaliQ62768.
SMRiQ62768. Positions 2-128, 567-616.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62768.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7979C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini676 – 782107C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini1106 – 1249144MHD1PROSITE-ProRule annotationAdd
BLAST
Domaini1358 – 1525168MHD2PROSITE-ProRule annotationAdd
BLAST
Domaini1564 – 1691128C2 3PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili319 – 37052Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi320 – 452133Glu-richAdd
BLAST

Domaini

The C2 domains are not involved in calcium-dependent phospholipid binding.1 Publication
The C-terminal region containing both MHD domains and the third C2 domain is required for synaptic vesicle priming activity.1 Publication

Sequence similaritiesi

Belongs to the unc-13 family.Curated
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 fingeri566 – 61651Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1011. Eukaryota.
ENOG410XS5D. LUCA.
HOVERGENiHBG057340.
InParanoidiQ62768.
KOiK15293.
PhylomeDBiQ62768.

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. 3 hits.
PfamiPF00130. C1_1. 1 hit.
PF00168. C2. 3 hits.
PF06292. DUF1041. 1 hit.
PF10540. Membr_traf_MHD. 1 hit.
[Graphical view]
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q62768-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 KDSPRWDQDE EDLEDLEDLE DEELPEEEEL EEEELEEEEE
360 370 380 390 400
LEEEELELEE EEEVPDDLAS YTQQEDTTVA EPKEFKRISF PTAAPQKEDK
410 420 430 440 450
VSAVPIEAPD VSKGIPKAAT PEEKAAAECA QEAEPPKSEE SFRSREAEEG
460 470 480 490 500
QEGQDAMSRA KANWLRAFNK VRMQLQEARG EGEMSKSLWF KGGPGGGLII
510 520 530 540 550
IDSMPDIRKR KPIPLVSDLA MSLVQSRKAG ITSALASSTL NNEELKNHVY
560 570 580 590 600
KKTLQALIYP ISCTTPHNFE VWTATTPTYC YECEGLLWGI ARQGMRCTEC
610 620 630 640 650
GVKCHEKCQD LLNADCLQRA AEKSSKHGAE DRTQNIIMVL KDRMKIRERN
660 670 680 690 700
KPEIFELIQE VFAVTKSAHT QQMKAVKQSV LDGTSKWSAK ISITVVCAQG
710 720 730 740 750
LQAKDKTGSS DPYVTVQVGK TKKRTKTIYG NLNPVWEENF HFECHNSSDR
760 770 780 790 800
IKVRVLDEDD DIKSRVKQRF KRESDDFLGQ TIIEVRTLSG EMDVWYNLDK
810 820 830 840 850
RTDKSAVSGA IRLHISVEIK GEEKVAPYHV QYTCLHENLF HFVTDVQNNG
860 870 880 890 900
VVKIPDAKGD DAWKVYYDET AQEIVDEFAM RYGVESIYQA MTHFACLSSK
910 920 930 940 950
YMCPGVPAVM STLLANINAY YAHTTASTNV SASDRFAASN FGKERFVKLL
960 970 980 990 1000
DQLHNSLRID LSMYRNNFPA SSPERLQDLK STVDLLTSIT FFRMKVQELQ
1010 1020 1030 1040 1050
SPPRASQVVK DCVKACLNST YEYIFNNCHE LYGREYQTDP AKKGEVPPEE
1060 1070 1080 1090 1100
QGPSIKNLDF WSKLITLIVS IIEEDKNSYT PCLNQFPQEL NVGKISAEVM
1110 1120 1130 1140 1150
WSLFAQDMKY AMEEHDKHRL CKSADYMNLH FKVKWLYNEY VAELPTFKDR
1160 1170 1180 1190 1200
VPEYPAWFEP FVIQWLDENE EVSRDFLHGA LERDKKDGFQ QTSEHALFSC
1210 1220 1230 1240 1250
SVVDVFSQLN QSFEIIKKLE CPDPQIVGHY MRRFAKTISN VLLQYADIVS
1260 1270 1280 1290 1300
KDFASYCSKE KEKVPCILMN NTQQLRVQLE KMFEAMGGKE LDAEASGTLK
1310 1320 1330 1340 1350
ELQVKLNNVL DELSHVFATS FQPHIEECVR QMGDILSQVK GTGNVPASAC
1360 1370 1380 1390 1400
SSVAQDADNV LQPIMDLLDS NLTLFAKICE KTVLKRVLKE LWKLVMNTME
1410 1420 1430 1440 1450
RTIVLPPLTD QTMIGTLLRK HGKGLEKGRV KLPSHSDGTQ MIFNAAKELG
1460 1470 1480 1490 1500
QLSKLKDHMV REEAKSLTPK QCAVVELALD TIKQYFHAGG VGLKKTFLEK
1510 1520 1530 1540 1550
SPDLQSLRYA LSLYTQATDL LIKTFVQTQS AQVHGGKGTR FTLSEDVCPE
1560 1570 1580 1590 1600
MGSGVEDPVG EVSVHVELFT HPGTGEQKVT VKVVAANDLK WQTSGIFRPF
1610 1620 1630 1640 1650
IEVNIVGPQL SDKKRKFATK SKNNSWAPKY NESFQFSLSA DAGPECYELQ
1660 1670 1680 1690 1700
VCVKDYCFAR EDRTVELAVL QLRELAQRGS AACWLPLGRR IHMDDTGLTV
1710 1720 1730
LRILSQRSND EVAKEFVKLK SDTRSAEEGG AAPAP
Length:1,735
Mass (Da):196,356
Last modified:November 1, 1996 - v1
Checksum:iBFE7D0467D258900
GO
Isoform 2 (identifier: Q62768-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1434-1456: Missing.

Show »
Length:1,712
Mass (Da):193,870
Checksum:i567EDEFA1D78F775
GO
Isoform 3 (identifier: Q62768-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1541-1559: Missing.

Show »
Length:1,716
Mass (Da):194,363
Checksum:i2F917D1CE8A33D1E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1434 – 145623Missing in isoform 2. CuratedVSP_011382Add
BLAST
Alternative sequencei1541 – 155919Missing in isoform 3. CuratedVSP_011383Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24070 mRNA. Translation: AAC52266.1.
PIRiA57607.
RefSeqiNP_074052.1. NM_022861.1. [Q62768-1]
UniGeneiRn.10126.

Genome annotation databases

GeneIDi64829.
KEGGirno:64829.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24070 mRNA. Translation: AAC52266.1.
PIRiA57607.
RefSeqiNP_074052.1. NM_022861.1. [Q62768-1]
UniGeneiRn.10126.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8FNMR-A567-616[»]
2CJSX-ray1.78A/B2-150[»]
2CJTX-ray1.44A/B/C/D1-128[»]
2KDUNMR-B458-492[»]
3KWTX-ray1.89A675-820[»]
3KWUX-ray1.37A675-820[»]
3SWHX-ray2.65A/B1148-1407[»]
A/B1453-1531[»]
4Y21X-ray2.90A942-1407[»]
A1453-1523[»]
ProteinModelPortaliQ62768.
SMRiQ62768. Positions 2-128, 567-616.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29191N.
STRINGi10116.ENSRNOP00000025162.

PTM databases

iPTMnetiQ62768.
PhosphoSiteiQ62768.
SwissPalmiQ62768.

Proteomic databases

PaxDbiQ62768.
PRIDEiQ62768.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64829.
KEGGirno:64829.

Organism-specific databases

CTDi23025.
RGDi619722. Unc13a.

Phylogenomic databases

eggNOGiKOG1011. Eukaryota.
ENOG410XS5D. LUCA.
HOVERGENiHBG057340.
InParanoidiQ62768.
KOiK15293.
PhylomeDBiQ62768.

Miscellaneous databases

EvolutionaryTraceiQ62768.
PROiQ62768.

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. 3 hits.
PfamiPF00130. C1_1. 1 hit.
PF00168. C2. 3 hits.
PF06292. DUF1041. 1 hit.
PF10540. Membr_traf_MHD. 1 hit.
[Graphical view]
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. "Mammalian homologues of Caenorhabditis elegans unc-13 gene define novel family of C2-domain proteins."
    Brose N., Hofmann K., Hata Y., Suedhof T.C.
    J. Biol. Chem. 270:25273-25280(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin."
    Betz A., Okamoto M., Benseler F., Brose N.
    J. Biol. Chem. 272:2520-2526(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNTAXIN 1.
  3. "Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery."
    Orita S., Naito A., Sakaguchi G., Maeda M., Igarashi H., Sasaki T., Takai Y.
    J. Biol. Chem. 272:16081-16084(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOC2A.
  4. "Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release."
    Betz A., Ashery U., Rickmann M., Augustin I., Neher E., Suedhof T.C., Rettig J., Brose N.
    Neuron 21:123-136(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-567.
  5. "Role of the Doc2 alpha-Munc13-1 interaction in the neurotransmitter release process."
    Mochida S., Orita S., Sakaguchi G., Sasaki T., Takai Y.
    Proc. Natl. Acad. Sci. U.S.A. 95:11418-11422(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOC2A.
  6. "Differential expression of two novel Munc13 proteins in rat brain."
    Augustin I., Betz A., Herrmann C., Jo T., Brose N.
    Biochem. J. 337:363-371(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming."
    Betz A., Thakur P., Junge H.J., Ashery U., Rhee J.S., Scheuss V., Rosenmund C., Rettig J., Brose N.
    Neuron 30:183-196(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RIMS1.
  8. "Beta phorbol ester- and diacylglycerol-induced augmentation of transmitter release is mediated by Munc13s and not by PKCs."
    Rhee J.S., Betz A., Pyott S., Reim K., Varoqueaux F., Augustin I., Hesse D., Suedhof T.C., Takahashi M., Rosenmund C., Brose N.
    Cell 108:121-133(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and Munc13-1."
    Ohtsuka T., Takao-Rikitsu E., Inoue E., Inoue M., Takeuchi M., Matsubara K., Deguchi-Tawarada M., Satoh K., Morimoto K., Nakanishi H., Takai Y.
    J. Cell Biol. 158:577-590(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BSN, IDENTIFICATION IN A COMPLEX WITH ERC2 AND RIMS1.
  10. Cited for: TISSUE SPECIFICITY.
  11. "Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release."
    Takao-Rikitsu E., Mochida S., Inoue E., Deguchi-Tawarada M., Inoue M., Ohtsuka T., Takai Y.
    J. Cell Biol. 164:301-311(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BSN.
  12. "Identification of the minimal protein domain required for priming activity of Munc13-1."
    Stevens D.R., Wu Z.-X., Matti U., Junge H.J., Schirra C., Becherer U., Wojcik S.M., Brose N., Rettig J.
    Curr. Biol. 15:2243-2248(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF GLN-1190; LEU-1279; ILE-1364; VAL-1603 AND ASP-1655.
  13. "A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?"
    Dulubova I., Lou X., Lu J., Huryeva I., Alam A., Schneggenburger R., Suedhof T.C., Rizo J.
    EMBO J. 24:2839-2850(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIMS2.
  14. "Binding to Rab3A-interacting molecule RIM regulates the presynaptic recruitment of Munc13-1 and ubMunc13-2."
    Andrews-Zwilling Y.S., Kawabe H., Reim K., Varoqueaux F., Brose N.
    J. Biol. Chem. 281:19720-19731(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIMS1, MUTAGENESIS OF THR-22; TYR-23; VAL-64; HIS-119 AND ILE-121.
  15. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239; SER-241; SER-244 AND SER-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Intramolecular occlusion of the diacylglycerol-binding site in the C1 domain of munc13-1."
    Shen N., Guryev O., Rizo J.
    Biochemistry 44:1089-1096(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 567-616.
  17. "Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer switch."
    Lu J., Machius M., Dulubova I., Dai H., Suedhof T.C., Tomchick D.R., Rizo J.
    PLoS Biol. 4:1159-1172(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 1-128, X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 2-150 IN COMPLEX WITH RIMS2.

Entry informationi

Entry nameiUN13A_RAT
AccessioniPrimary (citable) accession number: Q62768
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.