Full text data of USO1
USO1
(VDP)
[Confidence: low (only semi-automatic identification from reviews)]
General vesicular transport factor p115 (Protein USO1 homolog; Transcytosis-associated protein; TAP; Vesicle-docking protein)
General vesicular transport factor p115 (Protein USO1 homolog; Transcytosis-associated protein; TAP; Vesicle-docking protein)
UniProt
O60763
ID USO1_HUMAN Reviewed; 962 AA.
AC O60763; B2RAQ0; Q6PK63; Q86TB8; Q8N592;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=General vesicular transport factor p115;
DE AltName: Full=Protein USO1 homolog;
DE AltName: Full=Transcytosis-associated protein;
DE Short=TAP;
DE AltName: Full=Vesicle-docking protein;
GN Name=USO1; Synonyms=VDP;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP MUTAGENESIS OF SER-942, AND PHOSPHORYLATION AT SER-942.
RX PubMed=9478999; DOI=10.1074/jbc.273.9.5385;
RA Sohda M., Misumi Y., Yano A., Takami N., Ikehara Y.;
RT "Phosphorylation of the vesicle docking protein p115 regulates its
RT association with the Golgi membrane.";
RL J. Biol. Chem. 273:5385-5388(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 2).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MIF.
RX PubMed=19454686; DOI=10.4049/jimmunol.0803710;
RA Merk M., Baugh J., Zierow S., Leng L., Pal U., Lee S.J., Ebert A.D.,
RA Mizue Y., Trent J.O., Mitchell R., Nickel W., Kavathas P.B.,
RA Bernhagen J., Bucala R.;
RT "The Golgi-associated protein p115 mediates the secretion of
RT macrophage migration inhibitory factor.";
RL J. Immunol. 182:6896-6906(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-942, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 53-629, DOMAIN ARM REPEATS,
RP AND SUBUNIT.
RX PubMed=19247479; DOI=10.1371/journal.pone.0004656;
RA Striegl H., Roske Y., Kuemmel D., Heinemann U.;
RT "Unusual armadillo fold in the human general vesicular transport
RT factor p115.";
RL PLoS ONE 4:E4656-E4656(2009).
CC -!- FUNCTION: General vesicular transport factor required for
CC intercisternal transport in the Golgi stack; it is required for
CC transcytotic fusion and/or subsequent binding of the vesicles to
CC the target membrane. May well act as a vesicular anchor by
CC interacting with the target membrane and holding the vesicular and
CC target membranes in proximity (By similarity).
CC -!- SUBUNIT: Homodimer. Dimerizes by parallel association of the
CC tails, resulting in an elongated structure with two globular head
CC domains side by side, and a long rod-like tail structure
CC (Probable). Interacts with MIF.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus
CC membrane; Peripheral membrane protein. Note=Recycles between the
CC cytosol and the Golgi apparatus during interphase. During
CC interphase, the phosphorylated form is found exclusively in
CC cytosol; the unphosphorylated form is associated with Golgi
CC apparatus membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60763-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60763-2; Sequence=VSP_039120, VSP_039121;
CC -!- DOMAIN: Composed of a globular head, an elongated tail (coiled-
CC coil) and a highly acidic C-terminal domain.
CC -!- PTM: Phosphorylated in a cell cycle-specific manner;
CC phosphorylated in interphase but not in mitotic cells.
CC Dephosphorylated protein associates with the Golgi membrane;
CC phosphorylation promotes dissociation.
CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family.
CC -!- SIMILARITY: Contains 12 ARM repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; D86326; BAA25300.1; -; mRNA.
DR EMBL; AK314289; BAG36947.1; -; mRNA.
DR EMBL; AL832010; CAD89917.1; -; mRNA.
DR EMBL; AC110615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006398; AAH06398.1; ALT_SEQ; mRNA.
DR EMBL; BC032654; AAH32654.1; -; mRNA.
DR RefSeq; NP_003706.1; NM_003715.2.
DR UniGene; Hs.744877; -.
DR PDB; 2W3C; X-ray; 2.22 A; A=53-629.
DR PDBsum; 2W3C; -.
DR ProteinModelPortal; O60763; -.
DR SMR; O60763; 17-629.
DR IntAct; O60763; 11.
DR MINT; MINT-1136055; -.
DR STRING; 9606.ENSP00000411698; -.
DR PhosphoSite; O60763; -.
DR PaxDb; O60763; -.
DR PRIDE; O60763; -.
DR DNASU; 8615; -.
DR Ensembl; ENST00000264904; ENSP00000264904; ENSG00000138768.
DR GeneID; 8615; -.
DR KEGG; hsa:8615; -.
DR UCSC; uc003hiu.3; human.
DR CTD; 8615; -.
DR GeneCards; GC04P076649; -.
DR HGNC; HGNC:30904; USO1.
DR HPA; CAB010108; -.
DR MIM; 603344; gene.
DR neXtProt; NX_O60763; -.
DR PharmGKB; PA162408713; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000016409; -.
DR HOVERGEN; HBG018067; -.
DR InParanoid; O60763; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; USO1; human.
DR EvolutionaryTrace; O60763; -.
DR GeneWiki; USO1; -.
DR GenomeRNAi; 8615; -.
DR NextBio; 32287; -.
DR PRO; PR:O60763; -.
DR ArrayExpress; O60763; -.
DR Bgee; O60763; -.
DR CleanEx; HS_USO1; -.
DR Genevestigator; O60763; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR006955; Uso1_p115_C.
DR InterPro; IPR024095; Vesicle_P115-like.
DR InterPro; IPR006953; Vesicle_Uso1_P115_head.
DR PANTHER; PTHR10013; PTHR10013; 1.
DR Pfam; PF04871; Uso1_p115_C; 1.
DR Pfam; PF04869; Uso1_p115_head; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1 962 General vesicular transport factor p115.
FT /FTId=PRO_0000065774.
FT REPEAT 20 60 ARM 1.
FT REPEAT 61 121 ARM 2.
FT REPEAT 123 163 ARM 3.
FT REPEAT 166 207 ARM 4.
FT REPEAT 208 253 ARM 5.
FT REPEAT 255 310 ARM 6.
FT REPEAT 311 354 ARM 7.
FT REPEAT 363 408 ARM 8.
FT REPEAT 420 459 ARM 9.
FT REPEAT 473 513 ARM 10.
FT REPEAT 518 571 ARM 11.
FT REPEAT 573 630 ARM 12.
FT REGION 1 637 Globular head.
FT COILED 638 930 Potential.
FT COMPBIAS 935 962 Asp/Glu-rich (acidic).
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 202 202 N6-acetyllysine.
FT MOD_RES 942 942 Phosphoserine.
FT MOD_RES 952 952 Phosphoserine.
FT VAR_SEQ 98 98 V -> VDDVE (in isoform 2).
FT /FTId=VSP_039120.
FT VAR_SEQ 484 484 Q -> QGDKIDRR (in isoform 2).
FT /FTId=VSP_039121.
FT MUTAGEN 942 942 S->A: Loss of phosphorylation. Promotes
FT association with Golgi membranes.
FT MUTAGEN 942 942 S->D: Decreased association with Golgi
FT membranes.
FT CONFLICT 75 75 D -> G (in Ref. 3; CAD89917).
FT CONFLICT 85 85 T -> I (in Ref. 1; BAA25300).
FT CONFLICT 93 93 Missing (in Ref. 5; AAH32654).
FT CONFLICT 248 248 N -> Y (in Ref. 3; CAD89917).
FT CONFLICT 650 650 N -> D (in Ref. 3; CAD89917).
FT CONFLICT 877 877 Q -> R (in Ref. 2; BAG36947).
FT TURN 57 62
FT HELIX 63 71
FT HELIX 76 91
FT HELIX 112 119
FT HELIX 122 130
FT HELIX 136 152
FT HELIX 154 163
FT HELIX 167 172
FT HELIX 173 176
FT HELIX 180 194
FT HELIX 198 206
FT HELIX 209 219
FT HELIX 222 224
FT HELIX 227 240
FT HELIX 244 252
FT HELIX 256 259
FT HELIX 261 263
FT HELIX 274 290
FT HELIX 297 309
FT HELIX 312 321
FT HELIX 327 341
FT HELIX 345 352
FT HELIX 364 372
FT HELIX 379 393
FT HELIX 397 405
FT STRAND 414 416
FT HELIX 421 429
FT HELIX 434 448
FT HELIX 452 458
FT STRAND 466 469
FT HELIX 474 481
FT TURN 482 485
FT HELIX 488 502
FT HELIX 506 513
FT HELIX 518 527
FT TURN 531 534
FT HELIX 535 550
FT STRAND 557 559
FT HELIX 561 571
FT HELIX 574 582
FT TURN 583 586
FT HELIX 590 593
FT HELIX 604 606
FT HELIX 611 627
SQ 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
//
ID USO1_HUMAN Reviewed; 962 AA.
AC O60763; B2RAQ0; Q6PK63; Q86TB8; Q8N592;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=General vesicular transport factor p115;
DE AltName: Full=Protein USO1 homolog;
DE AltName: Full=Transcytosis-associated protein;
DE Short=TAP;
DE AltName: Full=Vesicle-docking protein;
GN Name=USO1; Synonyms=VDP;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP MUTAGENESIS OF SER-942, AND PHOSPHORYLATION AT SER-942.
RX PubMed=9478999; DOI=10.1074/jbc.273.9.5385;
RA Sohda M., Misumi Y., Yano A., Takami N., Ikehara Y.;
RT "Phosphorylation of the vesicle docking protein p115 regulates its
RT association with the Golgi membrane.";
RL J. Biol. Chem. 273:5385-5388(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 2).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MIF.
RX PubMed=19454686; DOI=10.4049/jimmunol.0803710;
RA Merk M., Baugh J., Zierow S., Leng L., Pal U., Lee S.J., Ebert A.D.,
RA Mizue Y., Trent J.O., Mitchell R., Nickel W., Kavathas P.B.,
RA Bernhagen J., Bucala R.;
RT "The Golgi-associated protein p115 mediates the secretion of
RT macrophage migration inhibitory factor.";
RL J. Immunol. 182:6896-6906(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-942, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 53-629, DOMAIN ARM REPEATS,
RP AND SUBUNIT.
RX PubMed=19247479; DOI=10.1371/journal.pone.0004656;
RA Striegl H., Roske Y., Kuemmel D., Heinemann U.;
RT "Unusual armadillo fold in the human general vesicular transport
RT factor p115.";
RL PLoS ONE 4:E4656-E4656(2009).
CC -!- FUNCTION: General vesicular transport factor required for
CC intercisternal transport in the Golgi stack; it is required for
CC transcytotic fusion and/or subsequent binding of the vesicles to
CC the target membrane. May well act as a vesicular anchor by
CC interacting with the target membrane and holding the vesicular and
CC target membranes in proximity (By similarity).
CC -!- SUBUNIT: Homodimer. Dimerizes by parallel association of the
CC tails, resulting in an elongated structure with two globular head
CC domains side by side, and a long rod-like tail structure
CC (Probable). Interacts with MIF.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus
CC membrane; Peripheral membrane protein. Note=Recycles between the
CC cytosol and the Golgi apparatus during interphase. During
CC interphase, the phosphorylated form is found exclusively in
CC cytosol; the unphosphorylated form is associated with Golgi
CC apparatus membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60763-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60763-2; Sequence=VSP_039120, VSP_039121;
CC -!- DOMAIN: Composed of a globular head, an elongated tail (coiled-
CC coil) and a highly acidic C-terminal domain.
CC -!- PTM: Phosphorylated in a cell cycle-specific manner;
CC phosphorylated in interphase but not in mitotic cells.
CC Dephosphorylated protein associates with the Golgi membrane;
CC phosphorylation promotes dissociation.
CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family.
CC -!- SIMILARITY: Contains 12 ARM repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR EMBL; D86326; BAA25300.1; -; mRNA.
DR EMBL; AK314289; BAG36947.1; -; mRNA.
DR EMBL; AL832010; CAD89917.1; -; mRNA.
DR EMBL; AC110615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006398; AAH06398.1; ALT_SEQ; mRNA.
DR EMBL; BC032654; AAH32654.1; -; mRNA.
DR RefSeq; NP_003706.1; NM_003715.2.
DR UniGene; Hs.744877; -.
DR PDB; 2W3C; X-ray; 2.22 A; A=53-629.
DR PDBsum; 2W3C; -.
DR ProteinModelPortal; O60763; -.
DR SMR; O60763; 17-629.
DR IntAct; O60763; 11.
DR MINT; MINT-1136055; -.
DR STRING; 9606.ENSP00000411698; -.
DR PhosphoSite; O60763; -.
DR PaxDb; O60763; -.
DR PRIDE; O60763; -.
DR DNASU; 8615; -.
DR Ensembl; ENST00000264904; ENSP00000264904; ENSG00000138768.
DR GeneID; 8615; -.
DR KEGG; hsa:8615; -.
DR UCSC; uc003hiu.3; human.
DR CTD; 8615; -.
DR GeneCards; GC04P076649; -.
DR HGNC; HGNC:30904; USO1.
DR HPA; CAB010108; -.
DR MIM; 603344; gene.
DR neXtProt; NX_O60763; -.
DR PharmGKB; PA162408713; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000016409; -.
DR HOVERGEN; HBG018067; -.
DR InParanoid; O60763; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR ChiTaRS; USO1; human.
DR EvolutionaryTrace; O60763; -.
DR GeneWiki; USO1; -.
DR GenomeRNAi; 8615; -.
DR NextBio; 32287; -.
DR PRO; PR:O60763; -.
DR ArrayExpress; O60763; -.
DR Bgee; O60763; -.
DR CleanEx; HS_USO1; -.
DR Genevestigator; O60763; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:ProtInc.
DR GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR006955; Uso1_p115_C.
DR InterPro; IPR024095; Vesicle_P115-like.
DR InterPro; IPR006953; Vesicle_Uso1_P115_head.
DR PANTHER; PTHR10013; PTHR10013; 1.
DR Pfam; PF04871; Uso1_p115_C; 1.
DR Pfam; PF04869; Uso1_p115_head; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1 962 General vesicular transport factor p115.
FT /FTId=PRO_0000065774.
FT REPEAT 20 60 ARM 1.
FT REPEAT 61 121 ARM 2.
FT REPEAT 123 163 ARM 3.
FT REPEAT 166 207 ARM 4.
FT REPEAT 208 253 ARM 5.
FT REPEAT 255 310 ARM 6.
FT REPEAT 311 354 ARM 7.
FT REPEAT 363 408 ARM 8.
FT REPEAT 420 459 ARM 9.
FT REPEAT 473 513 ARM 10.
FT REPEAT 518 571 ARM 11.
FT REPEAT 573 630 ARM 12.
FT REGION 1 637 Globular head.
FT COILED 638 930 Potential.
FT COMPBIAS 935 962 Asp/Glu-rich (acidic).
FT MOD_RES 50 50 Phosphoserine.
FT MOD_RES 202 202 N6-acetyllysine.
FT MOD_RES 942 942 Phosphoserine.
FT MOD_RES 952 952 Phosphoserine.
FT VAR_SEQ 98 98 V -> VDDVE (in isoform 2).
FT /FTId=VSP_039120.
FT VAR_SEQ 484 484 Q -> QGDKIDRR (in isoform 2).
FT /FTId=VSP_039121.
FT MUTAGEN 942 942 S->A: Loss of phosphorylation. Promotes
FT association with Golgi membranes.
FT MUTAGEN 942 942 S->D: Decreased association with Golgi
FT membranes.
FT CONFLICT 75 75 D -> G (in Ref. 3; CAD89917).
FT CONFLICT 85 85 T -> I (in Ref. 1; BAA25300).
FT CONFLICT 93 93 Missing (in Ref. 5; AAH32654).
FT CONFLICT 248 248 N -> Y (in Ref. 3; CAD89917).
FT CONFLICT 650 650 N -> D (in Ref. 3; CAD89917).
FT CONFLICT 877 877 Q -> R (in Ref. 2; BAG36947).
FT TURN 57 62
FT HELIX 63 71
FT HELIX 76 91
FT HELIX 112 119
FT HELIX 122 130
FT HELIX 136 152
FT HELIX 154 163
FT HELIX 167 172
FT HELIX 173 176
FT HELIX 180 194
FT HELIX 198 206
FT HELIX 209 219
FT HELIX 222 224
FT HELIX 227 240
FT HELIX 244 252
FT HELIX 256 259
FT HELIX 261 263
FT HELIX 274 290
FT HELIX 297 309
FT HELIX 312 321
FT HELIX 327 341
FT HELIX 345 352
FT HELIX 364 372
FT HELIX 379 393
FT HELIX 397 405
FT STRAND 414 416
FT HELIX 421 429
FT HELIX 434 448
FT HELIX 452 458
FT STRAND 466 469
FT HELIX 474 481
FT TURN 482 485
FT HELIX 488 502
FT HELIX 506 513
FT HELIX 518 527
FT TURN 531 534
FT HELIX 535 550
FT STRAND 557 559
FT HELIX 561 571
FT HELIX 574 582
FT TURN 583 586
FT HELIX 590 593
FT HELIX 604 606
FT HELIX 611 627
SQ 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
//
MIM
603344
*RECORD*
*FIELD* NO
603344
*FIELD* TI
*603344 USO1 VESICLE DOCKING PROTEIN, S. CEREVISIAE, HOMOLOG OF; USO1
;;VESICLE DOCKING PROTEIN, 115-KD; p115;;
read moreTRANSCYTOSIS-ASSOCIATED PROTEIN; TAP;;
TAP/p115
*FIELD* TX
CLONING
Vesicular transport of proteins is carried out by the formation of
coated vesicles from a donor compartment, followed by their uncoating
and subsequent docking and fusion of the vesicles with a target
compartment membrane. Waters et al. (1992) identified a 115-kD bovine
liver protein, designated p115, that is required for transport from the
cis to the medial compartments of the Golgi apparatus. Barroso et al.
(1995) found that p115 is identical to rat liver TAP
(transcytosis-associated protein), a protein found on transcytotic
vesicles and required for their fusion with the target membrane.
TAP/p115 is homologous to Usop1, an S. cerevisiae protein involved in
endoplasmic reticulum to Golgi transport. The authors suggested that
TAP/p115/Usop1 is a general factor acting within the secretory and
endocytic pathways to bind transport vesicles prior to membrane fusion.
By screening a liver library with a rat p115 cDNA, Sohda et al. (1998)
isolated a cDNA encoding human p115. The predicted 962-amino acid human
p115 is 95% and 92% identical to bovine and rat p115, respectively.
GENE FUNCTION
Sohda et al. (1998) stated that p115 is recycled between the cytosol and
the Golgi apparatus during interphase. They demonstrated that the
membrane interaction of p115 is regulated by phosphorylation:
dephosphorylated p115 associates with the Golgi membrane and dissociates
from the membrane upon phosphorylation.
Allan et al. (2000) demonstrated that the tethering factor p115 is a
RAB1 (179508) effector that binds directly to activated RAB1. RAB1
recruited p115 to coat protein complex II (COPII; see 601924) vesicles
during budding from the endoplasmic reticulum, where it interacted with
a select set of COPII vesicle-associated SNAREs (see 603215) to form a
cis-SNARE complex that promotes targeting to the Golgi apparatus. Allan
et al. (2000) proposed that RAB1-regulated assembly of functional
effector-SNARE complexes defines a conserved molecular mechanism to
coordinate recognition between subcellular compartments.
MAPPING
Gross (2012) mapped the USO1 gene to chromosome 4q21.1 based on an
alignment of a USO1 sequence (GenBank GENBANK BC006398) with the genomic
sequence (GRCh37).
*FIELD* RF
1. Allan, B. B.; Moyer, B. D.; Balch, W. E.: Rab1 recruitment of
p115 into a cis-SNARE complex: programming budding COPII vesicles
for fusion. Science 289: 444-448, 2000.
2. Barroso, M.; Nelson, D. S.; Sztul, E.: Transcytosis-associated
protein (TAP)/p115 is a general fusion factor required for binding
of vesicles to acceptor membranes. Proc. Nat. Acad. Sci. 92: 527-531,
1995.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 7/25/2012.
4. 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.
5. Waters, M. G.; Clary, D. O.; Rothman, J. E.: A novel 115-kD peripheral
membrane protein is required for intercisternal transport in the Golgi
stack. J. Cell Biol. 118: 1015-1026, 1992.
*FIELD* CN
Matthew B. Gross - updated: 07/25/2012
Ada Hamosh - updated: 8/2/2000
*FIELD* CD
Rebekah S. Rasooly: 12/7/1998
*FIELD* ED
mgross: 07/25/2012
carol: 6/22/2012
alopez: 8/2/2000
alopez: 12/7/1998
*RECORD*
*FIELD* NO
603344
*FIELD* TI
*603344 USO1 VESICLE DOCKING PROTEIN, S. CEREVISIAE, HOMOLOG OF; USO1
;;VESICLE DOCKING PROTEIN, 115-KD; p115;;
read moreTRANSCYTOSIS-ASSOCIATED PROTEIN; TAP;;
TAP/p115
*FIELD* TX
CLONING
Vesicular transport of proteins is carried out by the formation of
coated vesicles from a donor compartment, followed by their uncoating
and subsequent docking and fusion of the vesicles with a target
compartment membrane. Waters et al. (1992) identified a 115-kD bovine
liver protein, designated p115, that is required for transport from the
cis to the medial compartments of the Golgi apparatus. Barroso et al.
(1995) found that p115 is identical to rat liver TAP
(transcytosis-associated protein), a protein found on transcytotic
vesicles and required for their fusion with the target membrane.
TAP/p115 is homologous to Usop1, an S. cerevisiae protein involved in
endoplasmic reticulum to Golgi transport. The authors suggested that
TAP/p115/Usop1 is a general factor acting within the secretory and
endocytic pathways to bind transport vesicles prior to membrane fusion.
By screening a liver library with a rat p115 cDNA, Sohda et al. (1998)
isolated a cDNA encoding human p115. The predicted 962-amino acid human
p115 is 95% and 92% identical to bovine and rat p115, respectively.
GENE FUNCTION
Sohda et al. (1998) stated that p115 is recycled between the cytosol and
the Golgi apparatus during interphase. They demonstrated that the
membrane interaction of p115 is regulated by phosphorylation:
dephosphorylated p115 associates with the Golgi membrane and dissociates
from the membrane upon phosphorylation.
Allan et al. (2000) demonstrated that the tethering factor p115 is a
RAB1 (179508) effector that binds directly to activated RAB1. RAB1
recruited p115 to coat protein complex II (COPII; see 601924) vesicles
during budding from the endoplasmic reticulum, where it interacted with
a select set of COPII vesicle-associated SNAREs (see 603215) to form a
cis-SNARE complex that promotes targeting to the Golgi apparatus. Allan
et al. (2000) proposed that RAB1-regulated assembly of functional
effector-SNARE complexes defines a conserved molecular mechanism to
coordinate recognition between subcellular compartments.
MAPPING
Gross (2012) mapped the USO1 gene to chromosome 4q21.1 based on an
alignment of a USO1 sequence (GenBank GENBANK BC006398) with the genomic
sequence (GRCh37).
*FIELD* RF
1. Allan, B. B.; Moyer, B. D.; Balch, W. E.: Rab1 recruitment of
p115 into a cis-SNARE complex: programming budding COPII vesicles
for fusion. Science 289: 444-448, 2000.
2. Barroso, M.; Nelson, D. S.; Sztul, E.: Transcytosis-associated
protein (TAP)/p115 is a general fusion factor required for binding
of vesicles to acceptor membranes. Proc. Nat. Acad. Sci. 92: 527-531,
1995.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 7/25/2012.
4. 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.
5. Waters, M. G.; Clary, D. O.; Rothman, J. E.: A novel 115-kD peripheral
membrane protein is required for intercisternal transport in the Golgi
stack. J. Cell Biol. 118: 1015-1026, 1992.
*FIELD* CN
Matthew B. Gross - updated: 07/25/2012
Ada Hamosh - updated: 8/2/2000
*FIELD* CD
Rebekah S. Rasooly: 12/7/1998
*FIELD* ED
mgross: 07/25/2012
carol: 6/22/2012
alopez: 8/2/2000
alopez: 12/7/1998