STXB4_HUMAN
ID STXB4_HUMAN Reviewed; 553 AA.
AC Q6ZWJ1; Q8IVZ5;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Syntaxin-binding protein 4;
DE AltName: Full=Syntaxin 4-interacting protein;
DE Short=STX4-interacting protein;
DE Short=Synip;
GN Name=STXBP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-92.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12; SER-212 AND
RP SER-463, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP STRUCTURE BY NMR OF 498-530.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the WW domain from the human syntaxin-binding
RT protein 4.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the translocation of transport vesicles from
CC the cytoplasm to the plasma membrane. Inhibits the translocation of
CC SLC2A4 from intracellular vesicles to the plasma membrane by STX4A
CC binding and preventing the interaction between STX4A and VAMP2.
CC Stimulation with insulin disrupts the interaction with STX4A, leading
CC to increased levels of SLC2A4 at the plasma membrane. May also play a
CC role in the regulation of insulin release by pancreatic beta cells
CC after stimulation by glucose (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STX4A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZWJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZWJ1-2; Sequence=VSP_017175, VSP_017176, VSP_017177,
CC VSP_017178;
CC -!- PTM: Phosphorylated on Ser-99 by PKB/AKT2 after insulin treatment.
CC Phosphorylation on Ser-99 abolishes the interaction with STX4A (By
CC similarity). {ECO:0000250}.
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DR EMBL; AK122865; BAC85511.1; -; mRNA.
DR EMBL; AC005177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041485; AAH41485.1; -; mRNA.
DR CCDS; CCDS11584.2; -. [Q6ZWJ1-1]
DR RefSeq; NP_848604.3; NM_178509.5. [Q6ZWJ1-1]
DR PDB; 2YSG; NMR; -; A=498-530.
DR PDBsum; 2YSG; -.
DR AlphaFoldDB; Q6ZWJ1; -.
DR SMR; Q6ZWJ1; -.
DR BioGRID; 128947; 84.
DR IntAct; Q6ZWJ1; 30.
DR MINT; Q6ZWJ1; -.
DR STRING; 9606.ENSP00000365530; -.
DR GlyGen; Q6ZWJ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZWJ1; -.
DR PhosphoSitePlus; Q6ZWJ1; -.
DR BioMuta; STXBP4; -.
DR DMDM; 296452915; -.
DR EPD; Q6ZWJ1; -.
DR jPOST; Q6ZWJ1; -.
DR MassIVE; Q6ZWJ1; -.
DR MaxQB; Q6ZWJ1; -.
DR PaxDb; Q6ZWJ1; -.
DR PeptideAtlas; Q6ZWJ1; -.
DR PRIDE; Q6ZWJ1; -.
DR ProteomicsDB; 68487; -. [Q6ZWJ1-1]
DR ProteomicsDB; 68488; -. [Q6ZWJ1-2]
DR Antibodypedia; 3574; 120 antibodies from 26 providers.
DR DNASU; 252983; -.
DR Ensembl; ENST00000376352.6; ENSP00000365530.2; ENSG00000166263.13. [Q6ZWJ1-1]
DR Ensembl; ENST00000398391.6; ENSP00000381427.2; ENSG00000166263.13. [Q6ZWJ1-2]
DR GeneID; 252983; -.
DR KEGG; hsa:252983; -.
DR MANE-Select; ENST00000376352.6; ENSP00000365530.2; NM_178509.6; NP_848604.3.
DR UCSC; uc002iuf.2; human. [Q6ZWJ1-1]
DR CTD; 252983; -.
DR DisGeNET; 252983; -.
DR GeneCards; STXBP4; -.
DR HGNC; HGNC:19694; STXBP4.
DR HPA; ENSG00000166263; Low tissue specificity.
DR MIM; 610415; gene.
DR neXtProt; NX_Q6ZWJ1; -.
DR OpenTargets; ENSG00000166263; -.
DR PharmGKB; PA134962267; -.
DR VEuPathDB; HostDB:ENSG00000166263; -.
DR eggNOG; KOG1892; Eukaryota.
DR GeneTree; ENSGT00390000002226; -.
DR InParanoid; Q6ZWJ1; -.
DR OMA; DQHQALR; -.
DR OrthoDB; 307920at2759; -.
DR PhylomeDB; Q6ZWJ1; -.
DR TreeFam; TF331084; -.
DR PathwayCommons; Q6ZWJ1; -.
DR SignaLink; Q6ZWJ1; -.
DR SIGNOR; Q6ZWJ1; -.
DR BioGRID-ORCS; 252983; 21 hits in 1089 CRISPR screens.
DR ChiTaRS; STXBP4; human.
DR EvolutionaryTrace; Q6ZWJ1; -.
DR GenomeRNAi; 252983; -.
DR Pharos; Q6ZWJ1; Tbio.
DR PRO; PR:Q6ZWJ1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6ZWJ1; protein.
DR Bgee; ENSG00000166263; Expressed in buccal mucosa cell and 121 other tissues.
DR ExpressionAtlas; Q6ZWJ1; baseline and differential.
DR Genevisible; Q6ZWJ1; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; IEA:Ensembl.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..553
FT /note="Syntaxin-binding protein 4"
FT /id="PRO_0000076330"
FT DOMAIN 19..105
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 496..529
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT COILED 291..417
FT /evidence="ECO:0000255"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV89"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017175"
FT VAR_SEQ 95
FT /note="L -> LST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017176"
FT VAR_SEQ 316..320
FT /note="EKLLE -> WPGQN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017177"
FT VAR_SEQ 321..553
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017178"
FT VARIANT 92
FT /note="G -> R (in dbSNP:rs1156287)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_063103"
FT VARIANT 120
FT /note="C -> R (in dbSNP:rs34870302)"
FT /id="VAR_056999"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:2YSG"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:2YSG"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:2YSG"
SQ SEQUENCE 553 AA; 61662 MW; 86CCAFD0D3967DD7 CRC64;
MNKNTSTVVS PSLLEKDPAF QMITIAKETG LGLKVLGGIN RNEGPLVYIQ EIIPGGDCYK
DGRLKPGDQL VSVNKESMIG VSFEEAKSII TGAKLRLESA WEIAFIRQKS DNIQPENLSC
TSLIEASGEY GPQASTLSLF SSPPEILIPK TSSTPKTNND ILSSCEIKTG YNKTVQIPIT
SENSTVGLSN TDVASAWTEN YGLQEKISLN PSVRFKAEKL EMALNYLGIQ PTKEQHQALR
QQVQADSKGT VSFGDFVQVA RNLFCLQLDE VNVGAHEISN ILDSQLLPCD SSEADEMERL
KCERDDALKE VNTLKEKLLE SDKQRKQLTE ELQNVKQEAK AVVEETRALR SRIHLAEAAQ
RQAHGMEMDY EEVIRLLEAK ITELKAQLAD YSDQNKESVQ DLKKRIMVLD CQLRKSEMAR
KTFEASTEKL LHFVEAIQEV FSDNSTPLSN LSERRAVLAS QTSLTPLGRN GRSIPATLAL
ESKELVKSVR ALLDMDCLPY GWEEAYTADG IKYFINHVTQ TTSWIHPVMS VLNLSRSEEN
EEDCSRELPN QKS
