ID USO1_HUMAN Reviewed; 962 AA. AC O60763; B2RAQ0; Q6PK63; Q86TB8; Q8N592; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 2. DT 27-MAR-2024, entry version 195. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, MUTAGENESIS RP 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT 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 IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 enrichment RT and fractionation of phosphopeptides with strong anion exchange RT 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., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [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., Bernhagen J., RA Bucala R.; RT "The Golgi-associated protein p115 mediates the secretion of macrophage RT migration inhibitory factor."; RL J. Immunol. 182:6896-6906(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA 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 RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 53-629, DOMAIN ARM REPEATS, AND RP 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 factor RT 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 the CC target membrane. May well act as a vesicular anchor by interacting with CC the target membrane and holding the vesicular and target membranes in CC proximity. {ECO:0000250|UniProtKB:P41542}. CC -!- SUBUNIT: Homodimer. Dimerizes by parallel association of the tails, CC resulting in an elongated structure with two globular head domains side CC by side, and a long rod-like tail structure (Probable). Interacts with CC MIF. {ECO:0000269|PubMed:19247479, ECO:0000269|PubMed:19454686, CC ECO:0000305}. CC -!- INTERACTION: CC O60763; Q99996-2: AKAP9; NbExp=3; IntAct=EBI-356164, EBI-9641546; CC O60763; Q9UNI6: DUSP12; NbExp=3; IntAct=EBI-356164, EBI-715161; CC O60763; Q8IUZ5: PHYKPL; NbExp=3; IntAct=EBI-356164, EBI-751947; CC O60763; Q9UIA9: XPO7; NbExp=3; IntAct=EBI-356164, EBI-286668; CC O60763; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-356164, EBI-25475856; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19454686, CC ECO:0000269|PubMed:9478999}. Golgi apparatus membrane CC {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}; Peripheral CC membrane protein {ECO:0000269|PubMed:19454686, CC ECO:0000269|PubMed:9478999}. Note=Recycles between the cytosol and the CC Golgi apparatus during interphase. During interphase, the CC phosphorylated form is found exclusively in cytosol; the CC unphosphorylated form is associated with Golgi apparatus membranes. CC {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}. 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-coil) CC and a highly acidic C-terminal domain. {ECO:0000269|PubMed:19247479}. CC -!- PTM: Phosphorylated in a cell cycle-specific manner; phosphorylated in CC interphase but not in mitotic cells. Dephosphorylated protein CC associates with the Golgi membrane; phosphorylation promotes CC dissociation. {ECO:0000269|PubMed:9478999}. CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH06398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS75144.1; -. [O60763-1] DR CCDS; CCDS77929.1; -. [O60763-2] DR RefSeq; NP_001276978.1; NM_001290049.1. [O60763-2] DR RefSeq; NP_003706.2; NM_003715.3. [O60763-1] DR PDB; 2W3C; X-ray; 2.22 A; A=53-629. DR PDBsum; 2W3C; -. DR AlphaFoldDB; O60763; -. DR SMR; O60763; -. DR BioGRID; 114173; 222. DR IntAct; O60763; 63. DR MINT; O60763; -. DR STRING; 9606.ENSP00000264904; -. DR ChEMBL; CHEMBL4295669; -. DR GlyGen; O60763; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O60763; -. DR MetOSite; O60763; -. DR PhosphoSitePlus; O60763; -. DR SwissPalm; O60763; -. DR BioMuta; USO1; -. DR CPTAC; CPTAC-293; -. DR CPTAC; CPTAC-294; -. DR EPD; O60763; -. DR jPOST; O60763; -. DR MassIVE; O60763; -. DR MaxQB; O60763; -. DR PaxDb; 9606-ENSP00000444850; -. DR PeptideAtlas; O60763; -. DR ProteomicsDB; 49590; -. [O60763-1] DR ProteomicsDB; 49591; -. [O60763-2] DR Pumba; O60763; -. DR Antibodypedia; 4113; 423 antibodies from 39 providers. DR DNASU; 8615; -. DR Ensembl; ENST00000264904.8; ENSP00000264904.7; ENSG00000138768.15. [O60763-2] DR Ensembl; ENST00000514213.7; ENSP00000444850.2; ENSG00000138768.15. [O60763-1] DR GeneID; 8615; -. DR KEGG; hsa:8615; -. DR MANE-Select; ENST00000514213.7; ENSP00000444850.2; NM_003715.4; NP_003706.2. DR UCSC; uc003hiv.5; human. [O60763-1] DR AGR; HGNC:30904; -. DR CTD; 8615; -. DR DisGeNET; 8615; -. DR GeneCards; USO1; -. DR HGNC; HGNC:30904; USO1. DR HPA; ENSG00000138768; Tissue enhanced (skeletal). DR MIM; 603344; gene. DR neXtProt; NX_O60763; -. DR OpenTargets; ENSG00000138768; -. DR PharmGKB; PA162408713; -. DR VEuPathDB; HostDB:ENSG00000138768; -. DR eggNOG; KOG0946; Eukaryota. DR GeneTree; ENSGT00390000017018; -. DR HOGENOM; CLU_006318_2_0_1; -. DR InParanoid; O60763; -. DR OMA; LLDYEYC; -. DR OrthoDB; 1774at2759; -. DR PhylomeDB; O60763; -. DR PathwayCommons; O60763; -. DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR SignaLink; O60763; -. DR SIGNOR; O60763; -. DR BioGRID-ORCS; 8615; 79 hits in 337 CRISPR screens. DR ChiTaRS; USO1; human. DR EvolutionaryTrace; O60763; -. DR GeneWiki; USO1; -. DR GenomeRNAi; 8615; -. DR Pharos; O60763; Tbio. DR PRO; PR:O60763; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O60763; Protein. DR Bgee; ENSG00000138768; Expressed in gluteal muscle and 215 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005815; C:microtubule organizing center; TAS:Reactome. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0030133; C:transport vesicle; TAS:Reactome. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB. DR GO; GO:0048211; P:Golgi vesicle docking; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central. DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IEA:Ensembl. DR GO; GO:0032252; P:secretory granule localization; IEA:Ensembl. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl. DR GO; GO:0045056; P:transcytosis; IBA:GO_Central. DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR041209; P115_Arm_rpt. DR InterPro; IPR006955; Uso1_p115_C. DR InterPro; IPR006953; Vesicle_Uso1_P115_head. DR PANTHER; PTHR10013; GENERAL VESICULAR TRANSPORT FACTOR P115; 1. DR PANTHER; PTHR10013:SF0; GENERAL VESICULAR TRANSPORT FACTOR P115; 1. DR Pfam; PF18770; Arm_vescicular; 1. DR Pfam; PF04871; Uso1_p115_C; 1. DR Pfam; PF04869; Uso1_p115_head; 1. DR SMART; SM00185; ARM; 3. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 1. DR Genevisible; O60763; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm; KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein; KW Protein transport; Reference proteome; Repeat; Transport. FT CHAIN 1..962 FT /note="General vesicular transport factor p115" FT /id="PRO_0000065774" FT REPEAT 20..60 FT /note="ARM 1" FT REPEAT 61..121 FT /note="ARM 2" FT REPEAT 123..163 FT /note="ARM 3" FT REPEAT 166..207 FT /note="ARM 4" FT REPEAT 208..253 FT /note="ARM 5" FT REPEAT 255..310 FT /note="ARM 6" FT REPEAT 311..354 FT /note="ARM 7" FT REPEAT 363..408 FT /note="ARM 8" FT REPEAT 420..459 FT /note="ARM 9" FT REPEAT 473..513 FT /note="ARM 10" FT REPEAT 518..571 FT /note="ARM 11" FT REPEAT 573..630 FT /note="ARM 12" FT REGION 1..637 FT /note="Globular head" FT REGION 763..783 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 926..962 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 638..930 FT /evidence="ECO:0000255" FT COMPBIAS 763..782 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 936..955 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 202 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 942 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:9478999, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 952 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 98 FT /note="V -> VDDVE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_039120" FT VAR_SEQ 484 FT /note="Q -> QGDKIDRR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_039121" FT MUTAGEN 942 FT /note="S->A: Loss of phosphorylation. Promotes association FT with Golgi membranes." FT /evidence="ECO:0000269|PubMed:9478999" FT MUTAGEN 942 FT /note="S->D: Decreased association with Golgi membranes." FT /evidence="ECO:0000269|PubMed:9478999" FT CONFLICT 75 FT /note="D -> G (in Ref. 3; CAD89917)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="T -> I (in Ref. 1; BAA25300)" FT /evidence="ECO:0000305" FT CONFLICT 93 FT /note="Missing (in Ref. 5; AAH32654)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="N -> Y (in Ref. 3; CAD89917)" FT /evidence="ECO:0000305" FT CONFLICT 650 FT /note="N -> D (in Ref. 3; CAD89917)" FT /evidence="ECO:0000305" FT CONFLICT 877 FT /note="Q -> R (in Ref. 2; BAG36947)" FT /evidence="ECO:0000305" FT TURN 57..62 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 76..91 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 112..119 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 122..130 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 136..152 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 154..163 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 167..172 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 173..176 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 180..194 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 198..206 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 209..219 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 227..240 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 244..252 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 256..259 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 274..290 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 297..309 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 312..321 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 327..341 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 345..352 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 364..372 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 379..393 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 397..405 FT /evidence="ECO:0007829|PDB:2W3C" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 421..429 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 434..448 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 452..458 FT /evidence="ECO:0007829|PDB:2W3C" FT STRAND 466..469 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 474..481 FT /evidence="ECO:0007829|PDB:2W3C" FT TURN 482..485 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 488..502 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 506..513 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 518..527 FT /evidence="ECO:0007829|PDB:2W3C" FT TURN 531..534 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 535..550 FT /evidence="ECO:0007829|PDB:2W3C" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 561..571 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 574..582 FT /evidence="ECO:0007829|PDB:2W3C" FT TURN 583..586 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 590..593 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 604..606 FT /evidence="ECO:0007829|PDB:2W3C" FT HELIX 611..627 FT /evidence="ECO:0007829|PDB:2W3C" 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 //