SYBU_MOUSE
ID SYBU_MOUSE Reviewed; 665 AA.
AC Q8BHS8; Q3TQN7; Q401F3; Q401F4; Q571C1; Q6P1J2; Q80XH0; Q8BHS7; Q8BI27;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Syntabulin;
DE AltName: Full=Golgi-localized syntaphilin-related protein;
DE Short=m-Golsyn;
DE AltName: Full=Syntaxin-1-binding protein;
GN Name=Sybu; Synonyms=Golsyn, Kiaa1472;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain;
RX PubMed=15656992; DOI=10.1016/j.gene.2004.10.024;
RA Funakoshi E., Nakagawa K.-Y., Hamano A., Hori T., Shimizu A., Asakawa S.,
RA Shimizu N., Ito F.;
RT "Molecular cloning and characterization of gene for Golgi-localized
RT syntaphilin-related protein on human chromosome 8q23.";
RL Gene 344:259-271(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Embryo, Pituitary anterior lobe, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Fetal brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-557, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Part of a kinesin motor-adapter complex that is critical for
CC the anterograde axonal transport of active zone components and
CC contributes to activity-dependent presynaptic assembly during neuronal
CC development. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STX1A and KIF5B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}. Note=Colocalizes with syntaxin
CC vesicles along microtubules in neuronal processes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8BHS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHS8-2; Sequence=VSP_019727;
CC Name=3; Synonyms=Golsyn B;
CC IsoId=Q8BHS8-3; Sequence=VSP_019725, VSP_019728;
CC Name=4; Synonyms=Golsyn A;
CC IsoId=Q8BHS8-4; Sequence=VSP_019726;
CC Name=5;
CC IsoId=Q8BHS8-5; Sequence=VSP_019724;
CC Name=6;
CC IsoId=Q8BHS8-6; Sequence=VSP_019723;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90193.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB232447; BAE19961.1; -; mRNA.
DR EMBL; AB232448; BAE19962.1; -; mRNA.
DR EMBL; AB232449; BAE19963.1; -; mRNA.
DR EMBL; AK029072; BAC26277.1; -; mRNA.
DR EMBL; AK030482; BAC26984.1; -; mRNA.
DR EMBL; AK030720; BAC27098.1; -; mRNA.
DR EMBL; AK163432; BAE37345.1; -; mRNA.
DR EMBL; AK220268; BAD90193.1; ALT_INIT; mRNA.
DR EMBL; BC048945; AAH48945.1; -; mRNA.
DR EMBL; BC065045; AAH65045.1; -; mRNA.
DR CCDS; CCDS37069.1; -. [Q8BHS8-4]
DR CCDS; CCDS37070.1; -. [Q8BHS8-3]
DR CCDS; CCDS37071.1; -. [Q8BHS8-1]
DR CCDS; CCDS88763.1; -. [Q8BHS8-2]
DR RefSeq; NP_001027899.1; NM_001032727.1. [Q8BHS8-3]
DR RefSeq; NP_001272769.1; NM_001285840.1. [Q8BHS8-1]
DR RefSeq; NP_001272770.1; NM_001285841.1.
DR RefSeq; NP_001272771.1; NM_001285842.1.
DR RefSeq; NP_001272772.1; NM_001285843.1.
DR RefSeq; NP_001272773.1; NM_001285844.1.
DR RefSeq; NP_795972.2; NM_176998.4. [Q8BHS8-4]
DR RefSeq; NP_848880.2; NM_178765.3. [Q8BHS8-1]
DR RefSeq; XP_006521135.1; XM_006521072.3.
DR RefSeq; XP_006521138.1; XM_006521075.3.
DR RefSeq; XP_017172155.1; XM_017316666.1.
DR AlphaFoldDB; Q8BHS8; -.
DR SMR; Q8BHS8; -.
DR BioGRID; 235398; 1.
DR STRING; 10090.ENSMUSP00000087511; -.
DR iPTMnet; Q8BHS8; -.
DR PhosphoSitePlus; Q8BHS8; -.
DR MaxQB; Q8BHS8; -.
DR PaxDb; Q8BHS8; -.
DR PeptideAtlas; Q8BHS8; -.
DR PRIDE; Q8BHS8; -.
DR ProteomicsDB; 257509; -. [Q8BHS8-1]
DR ProteomicsDB; 257510; -. [Q8BHS8-2]
DR ProteomicsDB; 257511; -. [Q8BHS8-3]
DR ProteomicsDB; 257512; -. [Q8BHS8-4]
DR ProteomicsDB; 257513; -. [Q8BHS8-5]
DR ProteomicsDB; 257514; -. [Q8BHS8-6]
DR Antibodypedia; 42935; 23 antibodies from 13 providers.
DR DNASU; 319613; -.
DR Ensembl; ENSMUST00000090057; ENSMUSP00000087511; ENSMUSG00000022340. [Q8BHS8-4]
DR Ensembl; ENSMUST00000110267; ENSMUSP00000105896; ENSMUSG00000022340. [Q8BHS8-1]
DR Ensembl; ENSMUST00000110269; ENSMUSP00000105898; ENSMUSG00000022340. [Q8BHS8-3]
DR Ensembl; ENSMUST00000227305; ENSMUSP00000154372; ENSMUSG00000022340. [Q8BHS8-2]
DR Ensembl; ENSMUST00000228057; ENSMUSP00000153759; ENSMUSG00000022340. [Q8BHS8-1]
DR GeneID; 319613; -.
DR KEGG; mmu:319613; -.
DR UCSC; uc007vqc.2; mouse. [Q8BHS8-1]
DR UCSC; uc007vqf.2; mouse. [Q8BHS8-2]
DR UCSC; uc007vqg.2; mouse. [Q8BHS8-4]
DR UCSC; uc007vqh.2; mouse. [Q8BHS8-3]
DR CTD; 55638; -.
DR MGI; MGI:2442392; Sybu.
DR VEuPathDB; HostDB:ENSMUSG00000022340; -.
DR eggNOG; ENOG502QQZ1; Eukaryota.
DR GeneTree; ENSGT00520000055634; -.
DR HOGENOM; CLU_019458_0_0_1; -.
DR InParanoid; Q8BHS8; -.
DR OMA; IVPTVMW; -.
DR OrthoDB; 391092at2759; -.
DR PhylomeDB; Q8BHS8; -.
DR TreeFam; TF332407; -.
DR BioGRID-ORCS; 319613; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Sybu; mouse.
DR PRO; PR:Q8BHS8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BHS8; protein.
DR Bgee; ENSMUSG00000022340; Expressed in cortical plate and 171 other tissues.
DR ExpressionAtlas; Q8BHS8; baseline and differential.
DR Genevisible; Q8BHS8; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0097433; C:dense body; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:InterPro.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0019896; P:axonal transport of mitochondrion; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0060025; P:regulation of synaptic activity; ISO:MGI.
DR GO; GO:0060074; P:synapse maturation; ISO:MGI.
DR InterPro; IPR026198; Syntabulin.
DR InterPro; IPR028197; Syntaphilin/Syntabulin.
DR PANTHER; PTHR16208:SF4; PTHR16208:SF4; 1.
DR Pfam; PF15290; Syntaphilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..665
FT /note="Syntabulin"
FT /id="PRO_0000245510"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..421
FT /note="Sufficient for interaction with KIF5B"
FT /evidence="ECO:0000250"
FT REGION 314..421
FT /note="Sufficient for interaction with STX1A"
FT /evidence="ECO:0000250"
FT COILED 275..357
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX95"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX95"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..167
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019723"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019724"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15656992"
FT /id="VSP_019725"
FT VAR_SEQ 1
FT /note="M -> MRPHLPVQSLRPPATVPTCSEAPGAAVLAPEVKRPRGPERAGSCRTT
FT CANRAGGAGGAGRGWFLQPQRKPLATRCVAGRRPSPAQASRAFGDTVWTAQWTRSAKET
FT VPPPGRRRRRQRRRGEPAGSSEM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15656992"
FT /id="VSP_019726"
FT VAR_SEQ 8
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019727"
FT VAR_SEQ 73..80
FT /note="ISSNSFCS -> MDTVCKGN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15656992"
FT /id="VSP_019728"
FT CONFLICT 210
FT /note="S -> C (in Ref. 2; BAC27098)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="S -> T (in Ref. 2; BAC27098)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="R -> G (in Ref. 2; BAE37345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 73024 MW; 2DADB83A2BE20BBD CRC64;
MGPLRESKKE QRVQHQEKEI SRSRIPRLIL RPHRPQQQQQ QQNKVSPASE SPFSEEESRE
FNPSSSGRSA RTISSNSFCS DDTGCPSSQS VSPVKTPSDT GHSPIGFCPG SDEDFTRKKC
RIGMVGEGSI QSARHKKEPK GGIIKPGSEA DFSSSSSTGS ISAPEVHMST TGNKRASFSR
NRGPHGRSNG ASSHKSGSSP PSPREKDLVS MLCRNPLSPS NIHPSYAPSS PSSSNSGSYK
GSDCSPVMRR SGRYMSCGEN HGVKPPNPEQ YLTPLQQKEV TVRHLRTKLK ESERRLHERE
SEIMELKSQL ARMREDWIEE ECHRVEAQLA LKEARKEIKQ LKQVIETMRS SLADKDKGIQ
KYFVDINIQN KKLESLLQSM EMAHNSSLRD ELCLDFSFDS PEKSLPLSST FDKLPDGLSL
EEQITEEGAD SELLVGDSMA EGTDLLDEMV TATTTESSGL EFVHSTPGPQ ALKALPLVSH
EEGIAVMEQA VQTDVVPFSP AISELIQSVL KLQDYCPTSS ASPDESGADS MESFSESISA
LMLDLTPRSP NSAILLSPVE IPFSKGAMEA HANRLMRELD FAAYTEERLD SVLSLSQGSV
VRQYWSSNFL VDLLAVAAPV VPTVLWAFST QRGGTDPVYN IGALLRGCCV VALHSLRRTA
FHMKT
