Full text data of USE1
USE1
(USE1L)
[Confidence: high (present in two of the MS resources)]
Vesicle transport protein USE1 (Putative MAPK-activating protein PM26; USE1-like protein; p31)
Vesicle transport protein USE1 (Putative MAPK-activating protein PM26; USE1-like protein; p31)
hRBCD
IPI00020515
IPI00020515 Uncharacterized hematopoietic stem/progenitor cells protein MDS032 Uncharacterized hematopoietic stem/progenitor cells protein MDS032 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a Type II membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00020515 Uncharacterized hematopoietic stem/progenitor cells protein MDS032 Uncharacterized hematopoietic stem/progenitor cells protein MDS032 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a Type II membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q9NZ43
ID USE1_HUMAN Reviewed; 259 AA.
AC Q9NZ43; Q8NCK1; Q9BRT4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Vesicle transport protein USE1;
DE AltName: Full=Putative MAPK-activating protein PM26;
DE AltName: Full=USE1-like protein;
DE AltName: Full=p31;
GN Name=USE1; Synonyms=USE1L; ORFNames=MDS032;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-154.
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary gland;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-154.
RC TISSUE=Hematopoietic stem cell;
RA Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-154.
RC TISSUE=Brain, and Skeletal muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH STX18 AND
RP SEC22B, AND INTERACTION WITH STX18.
RX PubMed=15029241; DOI=10.1038/sj.emboj.7600135;
RA Hirose H., Arasaki K., Dohmae N., Takio K., Hatsuzawa K., Nagahama M.,
RA Tani K., Yamamoto A., Tohyama M., Tagaya M.;
RT "Implication of ZW10 in membrane trafficking between the endoplasmic
RT reticulum and Golgi.";
RL EMBO J. 23:1267-1278(2004).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH STX18; BNIP1 AND
RP SEC22B.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: SNARE that may be involved in targeting and fusion of
CC Golgi-derived retrograde transport vesicles with the ER.
CC -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC BNIP1/SEC20L and SEC22B. Interacts directly with STX18.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type IV membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NZ43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZ43-2; Sequence=VSP_012664, VSP_012665;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NZ43-3; Sequence=VSP_012662, VSP_012663;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the USE1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB097050; BAC77403.1; -; mRNA.
DR EMBL; AK074683; BAC11136.1; -; mRNA.
DR EMBL; AF220052; AAF67645.1; -; mRNA.
DR EMBL; AC020913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006005; AAH06005.1; -; mRNA.
DR EMBL; BC008455; AAH08455.1; -; mRNA.
DR RefSeq; NP_060937.1; NM_018467.3.
DR RefSeq; XP_005260043.1; XM_005259986.1.
DR UniGene; Hs.16187; -.
DR ProteinModelPortal; Q9NZ43; -.
DR IntAct; Q9NZ43; 2.
DR MINT; MINT-1463844; -.
DR STRING; 9606.ENSP00000263897; -.
DR PhosphoSite; Q9NZ43; -.
DR DMDM; 296452858; -.
DR PaxDb; Q9NZ43; -.
DR PRIDE; Q9NZ43; -.
DR DNASU; 55850; -.
DR Ensembl; ENST00000263897; ENSP00000263897; ENSG00000053501.
DR Ensembl; ENST00000595101; ENSP00000472362; ENSG00000053501.
DR Ensembl; ENST00000596136; ENSP00000473239; ENSG00000053501.
DR GeneID; 55850; -.
DR KEGG; hsa:55850; -.
DR UCSC; uc002nfo.2; human.
DR CTD; 55850; -.
DR GeneCards; GC19P017326; -.
DR HGNC; HGNC:30882; USE1.
DR HPA; HPA026851; -.
DR MIM; 610675; gene.
DR neXtProt; NX_Q9NZ43; -.
DR PharmGKB; PA162408692; -.
DR eggNOG; NOG299387; -.
DR HOGENOM; HOG000007677; -.
DR HOVERGEN; HBG079328; -.
DR InParanoid; Q9NZ43; -.
DR KO; K08507; -.
DR GeneWiki; USE1; -.
DR GenomeRNAi; 55850; -.
DR NextBio; 61111; -.
DR PMAP-CutDB; Q9NZ43; -.
DR PRO; PR:Q9NZ43; -.
DR ArrayExpress; Q9NZ43; -.
DR Bgee; Q9NZ43; -.
DR CleanEx; HS_USE1; -.
DR Genevestigator; Q9NZ43; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IEA:Ensembl.
DR GO; GO:0007041; P:lysosomal transport; ISS:HGNC.
DR GO; GO:0030163; P:protein catabolic process; ISS:HGNC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0032940; P:secretion by cell; ISS:HGNC.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR019150; Vesicle_transport_protein_Use1.
DR Pfam; PF09753; Use1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Polymorphism; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 259 Vesicle transport protein USE1.
FT /FTId=PRO_0000215579.
FT TOPO_DOM 1 231 Cytoplasmic (Potential).
FT TRANSMEM 232 252 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 253 259 Lumenal (Potential).
FT COILED 152 231 Potential.
FT VAR_SEQ 132 135 EPEM -> GESP (in isoform 3).
FT /FTId=VSP_012662.
FT VAR_SEQ 136 259 Missing (in isoform 3).
FT /FTId=VSP_012663.
FT VAR_SEQ 142 146 GVAGS -> PCHTH (in isoform 2).
FT /FTId=VSP_012664.
FT VAR_SEQ 147 259 Missing (in isoform 2).
FT /FTId=VSP_012665.
FT VARIANT 154 154 L -> S (in dbSNP:rs414528).
FT /FTId=VAR_021052.
FT CONFLICT 38 38 A -> V (in Ref. 4; AAH06005).
SQ SEQUENCE 259 AA; 29371 MW; 6538ED0B231AEC05 CRC64;
MAASRLELNL VRLLSRCEAM AAEKRDPDEW RLEKYVGALE DMLQALKVHA SKPASEVINE
YSWKVDFLKG MLQAEKLTSS SEKALANQFL APGRVPTTAR ERVPATKTVH LQSRARYTSE
MRSELLGTDS AEPEMDVRKR TGVAGSQPVS EKQLAAELDL VLQRHQNLQE KLAEEMLGLA
RSLKTNTLAA QSVIKKDNQT LSHSLKMADQ NLEKLKTESE RLEQHTQKSV NWLLWAMLII
VCFIFISMIL FIRIMPKLK
//
ID USE1_HUMAN Reviewed; 259 AA.
AC Q9NZ43; Q8NCK1; Q9BRT4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Vesicle transport protein USE1;
DE AltName: Full=Putative MAPK-activating protein PM26;
DE AltName: Full=USE1-like protein;
DE AltName: Full=p31;
GN Name=USE1; Synonyms=USE1L; ORFNames=MDS032;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-154.
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Mammary gland;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-154.
RC TISSUE=Hematopoietic stem cell;
RA Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-154.
RC TISSUE=Brain, and Skeletal muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH STX18 AND
RP SEC22B, AND INTERACTION WITH STX18.
RX PubMed=15029241; DOI=10.1038/sj.emboj.7600135;
RA Hirose H., Arasaki K., Dohmae N., Takio K., Hatsuzawa K., Nagahama M.,
RA Tani K., Yamamoto A., Tohyama M., Tagaya M.;
RT "Implication of ZW10 in membrane trafficking between the endoplasmic
RT reticulum and Golgi.";
RL EMBO J. 23:1267-1278(2004).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH STX18; BNIP1 AND
RP SEC22B.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: SNARE that may be involved in targeting and fusion of
CC Golgi-derived retrograde transport vesicles with the ER.
CC -!- SUBUNIT: Component of a SNARE complex consisting of STX18, USE1L,
CC BNIP1/SEC20L and SEC22B. Interacts directly with STX18.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type IV membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NZ43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZ43-2; Sequence=VSP_012664, VSP_012665;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NZ43-3; Sequence=VSP_012662, VSP_012663;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the USE1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB097050; BAC77403.1; -; mRNA.
DR EMBL; AK074683; BAC11136.1; -; mRNA.
DR EMBL; AF220052; AAF67645.1; -; mRNA.
DR EMBL; AC020913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006005; AAH06005.1; -; mRNA.
DR EMBL; BC008455; AAH08455.1; -; mRNA.
DR RefSeq; NP_060937.1; NM_018467.3.
DR RefSeq; XP_005260043.1; XM_005259986.1.
DR UniGene; Hs.16187; -.
DR ProteinModelPortal; Q9NZ43; -.
DR IntAct; Q9NZ43; 2.
DR MINT; MINT-1463844; -.
DR STRING; 9606.ENSP00000263897; -.
DR PhosphoSite; Q9NZ43; -.
DR DMDM; 296452858; -.
DR PaxDb; Q9NZ43; -.
DR PRIDE; Q9NZ43; -.
DR DNASU; 55850; -.
DR Ensembl; ENST00000263897; ENSP00000263897; ENSG00000053501.
DR Ensembl; ENST00000595101; ENSP00000472362; ENSG00000053501.
DR Ensembl; ENST00000596136; ENSP00000473239; ENSG00000053501.
DR GeneID; 55850; -.
DR KEGG; hsa:55850; -.
DR UCSC; uc002nfo.2; human.
DR CTD; 55850; -.
DR GeneCards; GC19P017326; -.
DR HGNC; HGNC:30882; USE1.
DR HPA; HPA026851; -.
DR MIM; 610675; gene.
DR neXtProt; NX_Q9NZ43; -.
DR PharmGKB; PA162408692; -.
DR eggNOG; NOG299387; -.
DR HOGENOM; HOG000007677; -.
DR HOVERGEN; HBG079328; -.
DR InParanoid; Q9NZ43; -.
DR KO; K08507; -.
DR GeneWiki; USE1; -.
DR GenomeRNAi; 55850; -.
DR NextBio; 61111; -.
DR PMAP-CutDB; Q9NZ43; -.
DR PRO; PR:Q9NZ43; -.
DR ArrayExpress; Q9NZ43; -.
DR Bgee; Q9NZ43; -.
DR CleanEx; HS_USE1; -.
DR Genevestigator; Q9NZ43; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IEA:Ensembl.
DR GO; GO:0007041; P:lysosomal transport; ISS:HGNC.
DR GO; GO:0030163; P:protein catabolic process; ISS:HGNC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0032940; P:secretion by cell; ISS:HGNC.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR019150; Vesicle_transport_protein_Use1.
DR Pfam; PF09753; Use1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Polymorphism; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 259 Vesicle transport protein USE1.
FT /FTId=PRO_0000215579.
FT TOPO_DOM 1 231 Cytoplasmic (Potential).
FT TRANSMEM 232 252 Helical; Anchor for type IV membrane
FT protein; (Potential).
FT TOPO_DOM 253 259 Lumenal (Potential).
FT COILED 152 231 Potential.
FT VAR_SEQ 132 135 EPEM -> GESP (in isoform 3).
FT /FTId=VSP_012662.
FT VAR_SEQ 136 259 Missing (in isoform 3).
FT /FTId=VSP_012663.
FT VAR_SEQ 142 146 GVAGS -> PCHTH (in isoform 2).
FT /FTId=VSP_012664.
FT VAR_SEQ 147 259 Missing (in isoform 2).
FT /FTId=VSP_012665.
FT VARIANT 154 154 L -> S (in dbSNP:rs414528).
FT /FTId=VAR_021052.
FT CONFLICT 38 38 A -> V (in Ref. 4; AAH06005).
SQ SEQUENCE 259 AA; 29371 MW; 6538ED0B231AEC05 CRC64;
MAASRLELNL VRLLSRCEAM AAEKRDPDEW RLEKYVGALE DMLQALKVHA SKPASEVINE
YSWKVDFLKG MLQAEKLTSS SEKALANQFL APGRVPTTAR ERVPATKTVH LQSRARYTSE
MRSELLGTDS AEPEMDVRKR TGVAGSQPVS EKQLAAELDL VLQRHQNLQE KLAEEMLGLA
RSLKTNTLAA QSVIKKDNQT LSHSLKMADQ NLEKLKTESE RLEQHTQKSV NWLLWAMLII
VCFIFISMIL FIRIMPKLK
//
MIM
610675
*RECORD*
*FIELD* NO
610675
*FIELD* TI
*610675 HEMATOPOIETIC STEM/PROGENITOR CELL PROTEIN MDS032
;;MDS032
*FIELD* TX
CLONING
read more
Using fluorescence localization-based, retrovirus-mediated expression
cloning with a signal sequence trap, Okumura et al. (2006) identified a
mouse clone, D12, with expression in endoplasmic reticulum (ER) and
cytoplasm. The authors subsequently isolated full-length D12 from a
mouse bone marrow mast cell cDNA library, and noted that EST sequence
variants of D12 exist, some containing a CAG insertion encoding an
additional ser residue. D12 contains 2 predicted coiled-coil domains, a
C-terminal transmembrane domain, a region weakly similar to the syntaxin
N-terminal domain, and a region weakly similar to the t-SNARE motif. D12
shows weak homology to yeast Use1p/Slt1p, and 84.9% identity to the
human protein MDS032. MDS032 does not contain the first 11 amino acids
of D12, and shows lower homology within an internal region (D12 residues
139-164). Fluorescence analysis and cell fractionation assays showed
that D12 localizes to the ER and to ER-Golgi intermediate compartments.
GENE FUNCTION
Using immunoprecipitation assays, Okumura et al. (2006) showed that D12
is a SNARE protein that binds to syntaxin-18 (606046), Sec22b (604029),
alpha-SNAP (603215), and VAMP7, thus showing that D12 interacts with
SNARES involved in the early and the post-Golgi secretory apparatus and
with endosome-lysosome transport. Immunofluorescence and siRNA assays
showed that neither overexpression nor knockdown of D12 affected ER,
Golgi, or ER-Golgi intermediate compartment structures, suggesting that
D12 does not regulate membrane trafficking in the early secretory
pathway. However, D12 knockdown did induce apoptosis, as measured by
condensed nuclear chromatin, caspase-3 (600636) activation, and BAX
(600040) conformational change. In addition, D12 downregulation caused
rapid appearance of lipofuscin granules, suggesting impaired degradation
of mitochondria by lysosomal degradative enzymes. Consistent with this,
confocal microscopy and fractionation of D12-deficient cells showed
impaired post-Golgi trafficking and maturation of the lysosomal
proteinase cathepsin-D (116840).
*FIELD* RF
1. Okumura, A. J.; Hatsuzawa, K.; Tamura, T.; Nagaya, H.; Saeki, K.;
Okumura, F.; Nagao, K.; Nishikawa, M.; Yoshimura, A.; Wada, I.: Involvement
of a novel Q-SNARE, D12, in quality control of the endomembrane system. J.
Biol. Chem. 281: 4495-4506, 2006.
*FIELD* CD
Laura L. Baxter: 1/2/2007
*FIELD* ED
alopez: 01/02/2007
alopez: 1/2/2007
*RECORD*
*FIELD* NO
610675
*FIELD* TI
*610675 HEMATOPOIETIC STEM/PROGENITOR CELL PROTEIN MDS032
;;MDS032
*FIELD* TX
CLONING
read more
Using fluorescence localization-based, retrovirus-mediated expression
cloning with a signal sequence trap, Okumura et al. (2006) identified a
mouse clone, D12, with expression in endoplasmic reticulum (ER) and
cytoplasm. The authors subsequently isolated full-length D12 from a
mouse bone marrow mast cell cDNA library, and noted that EST sequence
variants of D12 exist, some containing a CAG insertion encoding an
additional ser residue. D12 contains 2 predicted coiled-coil domains, a
C-terminal transmembrane domain, a region weakly similar to the syntaxin
N-terminal domain, and a region weakly similar to the t-SNARE motif. D12
shows weak homology to yeast Use1p/Slt1p, and 84.9% identity to the
human protein MDS032. MDS032 does not contain the first 11 amino acids
of D12, and shows lower homology within an internal region (D12 residues
139-164). Fluorescence analysis and cell fractionation assays showed
that D12 localizes to the ER and to ER-Golgi intermediate compartments.
GENE FUNCTION
Using immunoprecipitation assays, Okumura et al. (2006) showed that D12
is a SNARE protein that binds to syntaxin-18 (606046), Sec22b (604029),
alpha-SNAP (603215), and VAMP7, thus showing that D12 interacts with
SNARES involved in the early and the post-Golgi secretory apparatus and
with endosome-lysosome transport. Immunofluorescence and siRNA assays
showed that neither overexpression nor knockdown of D12 affected ER,
Golgi, or ER-Golgi intermediate compartment structures, suggesting that
D12 does not regulate membrane trafficking in the early secretory
pathway. However, D12 knockdown did induce apoptosis, as measured by
condensed nuclear chromatin, caspase-3 (600636) activation, and BAX
(600040) conformational change. In addition, D12 downregulation caused
rapid appearance of lipofuscin granules, suggesting impaired degradation
of mitochondria by lysosomal degradative enzymes. Consistent with this,
confocal microscopy and fractionation of D12-deficient cells showed
impaired post-Golgi trafficking and maturation of the lysosomal
proteinase cathepsin-D (116840).
*FIELD* RF
1. Okumura, A. J.; Hatsuzawa, K.; Tamura, T.; Nagaya, H.; Saeki, K.;
Okumura, F.; Nagao, K.; Nishikawa, M.; Yoshimura, A.; Wada, I.: Involvement
of a novel Q-SNARE, D12, in quality control of the endomembrane system. J.
Biol. Chem. 281: 4495-4506, 2006.
*FIELD* CD
Laura L. Baxter: 1/2/2007
*FIELD* ED
alopez: 01/02/2007
alopez: 1/2/2007