Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

General vesicular transport factor p115 (Protein USO1 homolog) (Transcytosis-associated protein) (TAP) (Vesicle-docking protein)

 USO1_HUMAN              Reviewed;         962 AA.
O60763; B2RAQ0; Q6PK63; Q86TB8; Q8N592;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
25-OCT-2017, entry version 155.
RecName: Full=General vesicular transport factor p115;
AltName: Full=Protein USO1 homolog;
AltName: Full=Transcytosis-associated protein;
Short=TAP;
AltName: Full=Vesicle-docking protein;
Name=USO1; Synonyms=VDP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
MUTAGENESIS OF SER-942, AND PHOSPHORYLATION AT SER-942.
PubMed=9478999; DOI=10.1074/jbc.273.9.5385;
Sohda M., Misumi Y., Yano A., Takami N., Ikehara Y.;
"Phosphorylation of the vesicle docking protein p115 regulates its
association with the Golgi membrane.";
J. Biol. Chem. 273:5385-5388(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH MIF.
PubMed=19454686; DOI=10.4049/jimmunol.0803710;
Merk M., Baugh J., Zierow S., Leng L., Pal U., Lee S.J., Ebert A.D.,
Mizue Y., Trent J.O., Mitchell R., Nickel W., Kavathas P.B.,
Bernhagen J., Bucala R.;
"The Golgi-associated protein p115 mediates the secretion of
macrophage migration inhibitory factor.";
J. Immunol. 182:6896-6906(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-942, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 53-629, DOMAIN ARM REPEATS,
AND SUBUNIT.
PubMed=19247479; DOI=10.1371/journal.pone.0004656;
Striegl H., Roske Y., Kuemmel D., Heinemann U.;
"Unusual armadillo fold in the human general vesicular transport
factor p115.";
PLoS ONE 4:E4656-E4656(2009).
-!- FUNCTION: General vesicular transport factor required for
intercisternal transport in the Golgi stack; it is required for
transcytotic fusion and/or subsequent binding of the vesicles to
the target membrane. May well act as a vesicular anchor by
interacting with the target membrane and holding the vesicular and
target membranes in proximity. {ECO:0000250|UniProtKB:P41542}.
-!- SUBUNIT: Homodimer. Dimerizes by parallel association of the
tails, resulting in an elongated structure with two globular head
domains side by side, and a long rod-like tail structure
(Probable). Interacts with MIF. {ECO:0000269|PubMed:19247479,
ECO:0000269|PubMed:19454686, ECO:0000305}.
-!- INTERACTION:
Q99996-2:AKAP9; NbExp=3; IntAct=EBI-356164, EBI-9641546;
Q9UNI6:DUSP12; NbExp=3; IntAct=EBI-356164, EBI-715161;
Q8IUZ5:PHYKPL; NbExp=3; IntAct=EBI-356164, EBI-751947;
Q9UIA9:XPO7; NbExp=3; IntAct=EBI-356164, EBI-286668;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}. Golgi
apparatus membrane {ECO:0000269|PubMed:19454686,
ECO:0000269|PubMed:9478999}; Peripheral membrane protein
{ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}.
Note=Recycles between the cytosol and the Golgi apparatus during
interphase. During interphase, the phosphorylated form is found
exclusively in cytosol; the unphosphorylated form is associated
with Golgi apparatus membranes. {ECO:0000269|PubMed:19454686,
ECO:0000269|PubMed:9478999}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60763-1; Sequence=Displayed;
Name=2;
IsoId=O60763-2; Sequence=VSP_039120, VSP_039121;
-!- DOMAIN: Composed of a globular head, an elongated tail (coiled-
coil) and a highly acidic C-terminal domain.
{ECO:0000269|PubMed:19247479}.
-!- PTM: Phosphorylated in a cell cycle-specific manner;
phosphorylated in interphase but not in mitotic cells.
Dephosphorylated protein associates with the Golgi membrane;
phosphorylation promotes dissociation.
{ECO:0000269|PubMed:9478999}.
-!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH06398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D86326; BAA25300.1; -; mRNA.
EMBL; AK314289; BAG36947.1; -; mRNA.
EMBL; AL832010; CAD89917.1; -; mRNA.
EMBL; AC110615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006398; AAH06398.1; ALT_SEQ; mRNA.
EMBL; BC032654; AAH32654.1; -; mRNA.
CCDS; CCDS75144.1; -. [O60763-1]
CCDS; CCDS77929.1; -. [O60763-2]
RefSeq; NP_001276978.1; NM_001290049.1. [O60763-2]
RefSeq; NP_003706.2; NM_003715.3. [O60763-1]
UniGene; Hs.744877; -.
PDB; 2W3C; X-ray; 2.22 A; A=53-629.
PDBsum; 2W3C; -.
ProteinModelPortal; O60763; -.
SMR; O60763; -.
BioGrid; 114173; 73.
IntAct; O60763; 25.
MINT; MINT-1136055; -.
iPTMnet; O60763; -.
PhosphoSitePlus; O60763; -.
SwissPalm; O60763; -.
BioMuta; USO1; -.
EPD; O60763; -.
MaxQB; O60763; -.
PeptideAtlas; O60763; -.
PRIDE; O60763; -.
DNASU; 8615; -.
Ensembl; ENST00000264904; ENSP00000264904; ENSG00000138768. [O60763-2]
Ensembl; ENST00000514213; ENSP00000444850; ENSG00000138768. [O60763-1]
GeneID; 8615; -.
KEGG; hsa:8615; -.
UCSC; uc003hiv.5; human. [O60763-1]
CTD; 8615; -.
DisGeNET; 8615; -.
EuPathDB; HostDB:ENSG00000138768.14; -.
GeneCards; USO1; -.
HGNC; HGNC:30904; USO1.
HPA; CAB010108; -.
HPA; HPA038282; -.
HPA; HPA038283; -.
MIM; 603344; gene.
neXtProt; NX_O60763; -.
OpenTargets; ENSG00000138768; -.
PharmGKB; PA162408713; -.
GeneTree; ENSGT00390000017018; -.
HOGENOM; HOG000016409; -.
HOVERGEN; HBG018067; -.
InParanoid; O60763; -.
OMA; QQFFKEG; -.
OrthoDB; EOG091G046H; -.
PhylomeDB; O60763; -.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
SIGNOR; O60763; -.
ChiTaRS; USO1; human.
EvolutionaryTrace; O60763; -.
GeneWiki; USO1; -.
GenomeRNAi; 8615; -.
PRO; PR:O60763; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138768; -.
CleanEx; HS_USO1; -.
ExpressionAtlas; O60763; baseline and differential.
Genevisible; O60763; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0008565; F:protein transporter activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
GO; GO:0048211; P:Golgi vesicle docking; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0045056; P:transcytosis; IBA:GO_Central.
GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR006955; Uso1_p115_C.
InterPro; IPR006953; Vesicle_Uso1_P115_head.
Pfam; PF04871; Uso1_p115_C; 1.
Pfam; PF04869; Uso1_p115_head; 1.
SMART; SM00185; ARM; 3.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50176; ARM_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus;
Membrane; Phosphoprotein; Protein transport; Reference proteome;
Repeat; Transport.
CHAIN 1 962 General vesicular transport factor p115.
/FTId=PRO_0000065774.
REPEAT 20 60 ARM 1.
REPEAT 61 121 ARM 2.
REPEAT 123 163 ARM 3.
REPEAT 166 207 ARM 4.
REPEAT 208 253 ARM 5.
REPEAT 255 310 ARM 6.
REPEAT 311 354 ARM 7.
REPEAT 363 408 ARM 8.
REPEAT 420 459 ARM 9.
REPEAT 473 513 ARM 10.
REPEAT 518 571 ARM 11.
REPEAT 573 630 ARM 12.
REGION 1 637 Globular head.
COILED 638 930 {ECO:0000255}.
COMPBIAS 935 962 Asp/Glu-rich (acidic).
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 202 202 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 942 942 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:9478999}.
MOD_RES 952 952 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 98 98 V -> VDDVE (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039120.
VAR_SEQ 484 484 Q -> QGDKIDRR (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039121.
MUTAGEN 942 942 S->A: Loss of phosphorylation. Promotes
association with Golgi membranes.
{ECO:0000269|PubMed:9478999}.
MUTAGEN 942 942 S->D: Decreased association with Golgi
membranes. {ECO:0000269|PubMed:9478999}.
CONFLICT 75 75 D -> G (in Ref. 3; CAD89917).
{ECO:0000305}.
CONFLICT 85 85 T -> I (in Ref. 1; BAA25300).
{ECO:0000305}.
CONFLICT 93 93 Missing (in Ref. 5; AAH32654).
{ECO:0000305}.
CONFLICT 248 248 N -> Y (in Ref. 3; CAD89917).
{ECO:0000305}.
CONFLICT 650 650 N -> D (in Ref. 3; CAD89917).
{ECO:0000305}.
CONFLICT 877 877 Q -> R (in Ref. 2; BAG36947).
{ECO:0000305}.
TURN 57 62 {ECO:0000244|PDB:2W3C}.
HELIX 63 71 {ECO:0000244|PDB:2W3C}.
HELIX 76 91 {ECO:0000244|PDB:2W3C}.
HELIX 112 119 {ECO:0000244|PDB:2W3C}.
HELIX 122 130 {ECO:0000244|PDB:2W3C}.
HELIX 136 152 {ECO:0000244|PDB:2W3C}.
HELIX 154 163 {ECO:0000244|PDB:2W3C}.
HELIX 167 172 {ECO:0000244|PDB:2W3C}.
HELIX 173 176 {ECO:0000244|PDB:2W3C}.
HELIX 180 194 {ECO:0000244|PDB:2W3C}.
HELIX 198 206 {ECO:0000244|PDB:2W3C}.
HELIX 209 219 {ECO:0000244|PDB:2W3C}.
HELIX 222 224 {ECO:0000244|PDB:2W3C}.
HELIX 227 240 {ECO:0000244|PDB:2W3C}.
HELIX 244 252 {ECO:0000244|PDB:2W3C}.
HELIX 256 259 {ECO:0000244|PDB:2W3C}.
HELIX 261 263 {ECO:0000244|PDB:2W3C}.
HELIX 274 290 {ECO:0000244|PDB:2W3C}.
HELIX 297 309 {ECO:0000244|PDB:2W3C}.
HELIX 312 321 {ECO:0000244|PDB:2W3C}.
HELIX 327 341 {ECO:0000244|PDB:2W3C}.
HELIX 345 352 {ECO:0000244|PDB:2W3C}.
HELIX 364 372 {ECO:0000244|PDB:2W3C}.
HELIX 379 393 {ECO:0000244|PDB:2W3C}.
HELIX 397 405 {ECO:0000244|PDB:2W3C}.
STRAND 414 416 {ECO:0000244|PDB:2W3C}.
HELIX 421 429 {ECO:0000244|PDB:2W3C}.
HELIX 434 448 {ECO:0000244|PDB:2W3C}.
HELIX 452 458 {ECO:0000244|PDB:2W3C}.
STRAND 466 469 {ECO:0000244|PDB:2W3C}.
HELIX 474 481 {ECO:0000244|PDB:2W3C}.
TURN 482 485 {ECO:0000244|PDB:2W3C}.
HELIX 488 502 {ECO:0000244|PDB:2W3C}.
HELIX 506 513 {ECO:0000244|PDB:2W3C}.
HELIX 518 527 {ECO:0000244|PDB:2W3C}.
TURN 531 534 {ECO:0000244|PDB:2W3C}.
HELIX 535 550 {ECO:0000244|PDB:2W3C}.
STRAND 557 559 {ECO:0000244|PDB:2W3C}.
HELIX 561 571 {ECO:0000244|PDB:2W3C}.
HELIX 574 582 {ECO:0000244|PDB:2W3C}.
TURN 583 586 {ECO:0000244|PDB:2W3C}.
HELIX 590 593 {ECO:0000244|PDB:2W3C}.
HELIX 604 606 {ECO:0000244|PDB:2W3C}.
HELIX 611 627 {ECO:0000244|PDB:2W3C}.
SEQUENCE 962 AA; 107895 MW; C963652209031008 CRC64;
MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS KKYRLEVGIQ
AMEHLIHVLQ TDRSDSEIIG YALDTLYNII SNEEEEEVEE NSTRQSEDLG SQFTEIFIKQ
QENVTLLLSL LEEFDFHVRW PGVKLLTSLL KQLGPQVQQI ILVSPMGVSR LMDLLADSRE
VIRNDGVLLL QALTRSNGAI QKIVAFENAF ERLLDIISEE GNSDGGIVVE DCLILLQNLL
KNNNSNQNFF KEGSYIQRMK PWFEVGDENS GWSAQKVTNL HLMLQLVRVL VSPTNPPGAT
SSCQKAMFQC GLLQQLCTIL MATGVPADIL TETINTVSEV IRGCQVNQDY FASVNAPSNP
PRPAIVVLLM SMVNERQPFV LRCAVLYCFQ CFLYKNQKGQ GEIVSTLLPS TIDATGNSVS
AGQLLCGGLF STDSLSNWCA AVALAHALQE NATQKEQLLR VQLATSIGNP PVSLLQQCTN
ILSQGSKIQT RVGLLMLLCT WLSNCPIAVT HFLHNSANVP FLTGQIAENL GEEEQLVQGL
CALLLGISIY FNDNSLESYM KEKLKQLIEK RIGKENFIEK LGFISKHELY SRASQKPQPN
FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDN IVTHYKNMIR
EQDLQLEELR QQVSTLKCQN EQLQTAVTQQ VSQIQQHKDQ YNLLKIQLGK DNQHQGSYSE
GAQMNGIQPE EIGRLREEIE ELKRNQELLQ SQLTEKDSMI ENMKSSQTSG TNEQSSAIVS
ARDSEQVAEL KQELATLKSQ LNSQSVEITK LQTEKQELLQ KTEAFAKSVE VQGETETIIA
TKTTDVEGRL SALLQETKEL KNEIKALSEE RTAIKEQLDS SNSTIAILQT EKDKLELEIT
DSKKEQDDLL VLLADQDQKI LSLKNKLKDL GHPVEEEDEL ESGDQEDEDD ESEDPGKDLD
HI


Related products :

Catalog number Product name Quantity
EIAAB45468 General vesicular transport factor p115,Mouse,Mus musculus,Protein USO1 homolog,TAP,Transcytosis-associated protein,Uso1,Vdp,Vesicle-docking protein
EIAAB45467 Bos taurus,Bovine,General vesicular transport factor p115,Protein USO1 homolog,TAP,Transcytosis-associated protein,USO1,VDP,Vesicle-docking protein
EIAAB45465 General vesicular transport factor p115,Protein USO1 homolog,Rat,Rattus norvegicus,TAP,Transcytosis-associated protein,Uso1,Vdp,Vesicle-docking protein
EIAAB45466 General vesicular transport factor p115,Homo sapiens,Human,Protein USO1 homolog,TAP,Transcytosis-associated protein,USO1,VDP,Vesicle-docking protein
CSB-EL025694RA Rat General vesicular transport factor p115(USO1) ELISA kit 96T
CSB-EL025694RA Rat General vesicular transport factor p115(USO1) ELISA kit SpeciesRat 96T
CSB-EL025694MO Mouse General vesicular transport factor p115(USO1) ELISA kit 96T
CSB-EL025694BO Bovine General vesicular transport factor p115(USO1) ELISA kit 96T
CSB-EL025694MO Mouse General vesicular transport factor p115(USO1) ELISA kit SpeciesMouse 96T
CSB-EL025694BO Bovine General vesicular transport factor p115(USO1) ELISA kit SpeciesBovine 96T
USO1_MOUSE ELISA Kit FOR General vesicular transport factor p115; organism: Mouse; gene name: Uso1 96T
USO1 USO1 Gene USO1 vesicle docking protein homolog (yeast)
201-20-6285 USO1{USO1 homolog, vesicle docking protein (yeast)}rabbit.pAb 0.2ml
CSB-EL025694RA Rat USO1 homolog, vesicle docking protein (yeast) (USO1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
orb103700 Vesicle docking protein p115 antibody Polyclonal Rabbit Polyclonal to Vesicle docking protein p115. 100
orb101624 Vesicle docking protein p115 antibody Polyclonal Rabbit Polyclonal to Vesicle docking protein p115. 100
CSB-EL025694BO Bovine USO1 homolog, vesicle docking protein (yeast) (USO1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL025694MO Mouse USO1 homolog, vesicle docking protein (yeast) (USO1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
abx116551 Polyclonal Rabbit Uso1 Homolog, Vesicle Docking Protein (Yeast) Antibody 50 μl
EB06982 General vesicular transport factor p115 0.1 mg
EB06982 General vesicular transport factor p115 0.1 mg
USO1_RAT Rat ELISA Kit FOR General vesicular transport factor p115 96T
NB100-2430PEP General vesicular transport factor p115 Control Peptide 0.1 mg
orb101624 Vesicle docking protein p115 antibody 200 ug
orb101624 Vesicle docking protein p115 antibody 100 ug


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur