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O60763

- USO1_HUMAN

UniProt

O60763 - USO1_HUMAN

Protein

General vesicular transport factor p115

Gene

USO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein transporter activity Source: RefGenome

    GO - Biological processi

    1. ER to Golgi vesicle-mediated transport Source: RefGenome
    2. Golgi vesicle docking Source: RefGenome
    3. intracellular protein transport Source: RefGenome
    4. membrane fusion Source: RefGenome
    5. mitotic cell cycle Source: Reactome
    6. transcytosis Source: RefGenome
    7. vesicle fusion with Golgi apparatus Source: InterPro

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    General vesicular transport factor p115
    Alternative name(s):
    Protein USO1 homolog
    Transcytosis-associated protein
    Short name:
    TAP
    Vesicle-docking protein
    Gene namesi
    Name:USO1
    Synonyms:VDP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:30904. USO1.

    Subcellular locationi

    Cytoplasmcytosol. Golgi apparatus membrane; Peripheral membrane protein
    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.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: RefGenome
    3. ER to Golgi transport vesicle membrane Source: RefGenome
    4. Golgi apparatus Source: HPA
    5. Golgi membrane Source: ProtInc
    6. Golgi stack Source: RefGenome
    7. membrane Source: UniProtKB
    8. nucleolus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi942 – 9421S → A: Loss of phosphorylation. Promotes association with Golgi membranes. 1 Publication
    Mutagenesisi942 – 9421S → D: Decreased association with Golgi membranes. 1 Publication

    Organism-specific databases

    PharmGKBiPA162408713.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 962962General vesicular transport factor p115PRO_0000065774Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei50 – 501Phosphoserine1 Publication
    Modified residuei202 – 2021N6-acetyllysine1 Publication
    Modified residuei942 – 9421Phosphoserine6 Publications
    Modified residuei952 – 9521Phosphoserine2 Publications

    Post-translational modificationi

    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.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60763.
    PaxDbiO60763.
    PRIDEiO60763.

    PTM databases

    PhosphoSiteiO60763.

    Expressioni

    Gene expression databases

    ArrayExpressiO60763.
    BgeeiO60763.
    CleanExiHS_USO1.
    GenevestigatoriO60763.

    Organism-specific databases

    HPAiCAB010108.
    HPA038282.
    HPA038283.

    Interactioni

    Subunit structurei

    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.2 PublicationsCurated

    Protein-protein interaction databases

    BioGridi114173. 35 interactions.
    IntActiO60763. 11 interactions.
    MINTiMINT-1136055.
    STRINGi9606.ENSP00000411698.

    Structurei

    Secondary structure

    1
    962
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni57 – 626
    Helixi63 – 719
    Helixi76 – 9116
    Helixi112 – 1198
    Helixi122 – 1309
    Helixi136 – 15217
    Helixi154 – 16310
    Helixi167 – 1726
    Helixi173 – 1764
    Helixi180 – 19415
    Helixi198 – 2069
    Helixi209 – 21911
    Helixi222 – 2243
    Helixi227 – 24014
    Helixi244 – 2529
    Helixi256 – 2594
    Helixi261 – 2633
    Helixi274 – 29017
    Helixi297 – 30913
    Helixi312 – 32110
    Helixi327 – 34115
    Helixi345 – 3528
    Helixi364 – 3729
    Helixi379 – 39315
    Helixi397 – 4059
    Beta strandi414 – 4163
    Helixi421 – 4299
    Helixi434 – 44815
    Helixi452 – 4587
    Beta strandi466 – 4694
    Helixi474 – 4818
    Turni482 – 4854
    Helixi488 – 50215
    Helixi506 – 5138
    Helixi518 – 52710
    Turni531 – 5344
    Helixi535 – 55016
    Beta strandi557 – 5593
    Helixi561 – 57111
    Helixi574 – 5829
    Turni583 – 5864
    Helixi590 – 5934
    Helixi604 – 6063
    Helixi611 – 62717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W3CX-ray2.22A53-629[»]
    ProteinModelPortaliO60763.
    SMRiO60763. Positions 17-629.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60763.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati20 – 6041ARM 1Add
    BLAST
    Repeati61 – 12161ARM 2Add
    BLAST
    Repeati123 – 16341ARM 3Add
    BLAST
    Repeati166 – 20742ARM 4Add
    BLAST
    Repeati208 – 25346ARM 5Add
    BLAST
    Repeati255 – 31056ARM 6Add
    BLAST
    Repeati311 – 35444ARM 7Add
    BLAST
    Repeati363 – 40846ARM 8Add
    BLAST
    Repeati420 – 45940ARM 9Add
    BLAST
    Repeati473 – 51341ARM 10Add
    BLAST
    Repeati518 – 57154ARM 11Add
    BLAST
    Repeati573 – 63058ARM 12Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 637637Globular headAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili638 – 930293Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi935 – 96228Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    Composed of a globular head, an elongated tail (coiled-coil) and a highly acidic C-terminal domain.1 Publication

    Sequence similaritiesi

    Belongs to the VDP/USO1/EDE1 family.Curated
    Contains 12 ARM repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000016409.
    HOVERGENiHBG018067.
    InParanoidiO60763.
    PhylomeDBiO60763.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR006955. Uso1_p115_C.
    IPR024095. Vesicle_P115-like.
    IPR006953. Vesicle_Uso1_P115_head.
    [Graphical view]
    PANTHERiPTHR10013. PTHR10013. 1 hit.
    PfamiPF04871. Uso1_p115_C. 1 hit.
    PF04869. Uso1_p115_head. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50176. ARM_REPEAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60763-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS    50
    KKYRLEVGIQ AMEHLIHVLQ TDRSDSEIIG YALDTLYNII SNEEEEEVEE 100
    NSTRQSEDLG SQFTEIFIKQ QENVTLLLSL LEEFDFHVRW PGVKLLTSLL 150
    KQLGPQVQQI ILVSPMGVSR LMDLLADSRE VIRNDGVLLL QALTRSNGAI 200
    QKIVAFENAF ERLLDIISEE GNSDGGIVVE DCLILLQNLL KNNNSNQNFF 250
    KEGSYIQRMK PWFEVGDENS GWSAQKVTNL HLMLQLVRVL VSPTNPPGAT 300
    SSCQKAMFQC GLLQQLCTIL MATGVPADIL TETINTVSEV IRGCQVNQDY 350
    FASVNAPSNP PRPAIVVLLM SMVNERQPFV LRCAVLYCFQ CFLYKNQKGQ 400
    GEIVSTLLPS TIDATGNSVS AGQLLCGGLF STDSLSNWCA AVALAHALQE 450
    NATQKEQLLR VQLATSIGNP PVSLLQQCTN ILSQGSKIQT RVGLLMLLCT 500
    WLSNCPIAVT HFLHNSANVP FLTGQIAENL GEEEQLVQGL CALLLGISIY 550
    FNDNSLESYM KEKLKQLIEK RIGKENFIEK LGFISKHELY SRASQKPQPN 600
    FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDN 650
    IVTHYKNMIR EQDLQLEELR QQVSTLKCQN EQLQTAVTQQ VSQIQQHKDQ 700
    YNLLKIQLGK DNQHQGSYSE GAQMNGIQPE EIGRLREEIE ELKRNQELLQ 750
    SQLTEKDSMI ENMKSSQTSG TNEQSSAIVS ARDSEQVAEL KQELATLKSQ 800
    LNSQSVEITK LQTEKQELLQ KTEAFAKSVE VQGETETIIA TKTTDVEGRL 850
    SALLQETKEL KNEIKALSEE RTAIKEQLDS SNSTIAILQT EKDKLELEIT 900
    DSKKEQDDLL VLLADQDQKI LSLKNKLKDL GHPVEEEDEL ESGDQEDEDD 950
    ESEDPGKDLD HI 962
    Length:962
    Mass (Da):107,895
    Last modified:March 6, 2007 - v2
    Checksum:iC963652209031008
    GO
    Isoform 2 (identifier: O60763-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         98-98: V → VDDVE
         484-484: Q → QGDKIDRR

    Show »
    Length:973
    Mass (Da):109,195
    Checksum:i4DE9E8C5ED44514E
    GO

    Sequence cautioni

    The sequence AAH06398.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751D → G in CAD89917. (PubMed:17974005)Curated
    Sequence conflicti85 – 851T → I in BAA25300. (PubMed:9478999)Curated
    Sequence conflicti93 – 931Missing in AAH32654. (PubMed:15489334)Curated
    Sequence conflicti248 – 2481N → Y in CAD89917. (PubMed:17974005)Curated
    Sequence conflicti650 – 6501N → D in CAD89917. (PubMed:17974005)Curated
    Sequence conflicti877 – 8771Q → R in BAG36947. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei98 – 981V → VDDVE in isoform 2. 1 PublicationVSP_039120
    Alternative sequencei484 – 4841Q → QGDKIDRR in isoform 2. 1 PublicationVSP_039121

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86326 mRNA. Translation: BAA25300.1.
    AK314289 mRNA. Translation: BAG36947.1.
    AL832010 mRNA. Translation: CAD89917.1.
    AC110615 Genomic DNA. No translation available.
    AC104828 Genomic DNA. No translation available.
    BC006398 mRNA. Translation: AAH06398.1. Sequence problems.
    BC032654 mRNA. Translation: AAH32654.1.
    RefSeqiNP_001276978.1. NM_001290049.1. [O60763-2]
    NP_003706.2. NM_003715.3. [O60763-1]
    UniGeneiHs.744877.

    Genome annotation databases

    EnsembliENST00000264904; ENSP00000264904; ENSG00000138768.
    GeneIDi8615.
    KEGGihsa:8615.
    UCSCiuc003hiu.3. human. [O60763-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86326 mRNA. Translation: BAA25300.1 .
    AK314289 mRNA. Translation: BAG36947.1 .
    AL832010 mRNA. Translation: CAD89917.1 .
    AC110615 Genomic DNA. No translation available.
    AC104828 Genomic DNA. No translation available.
    BC006398 mRNA. Translation: AAH06398.1 . Sequence problems.
    BC032654 mRNA. Translation: AAH32654.1 .
    RefSeqi NP_001276978.1. NM_001290049.1. [O60763-2 ]
    NP_003706.2. NM_003715.3. [O60763-1 ]
    UniGenei Hs.744877.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W3C X-ray 2.22 A 53-629 [» ]
    ProteinModelPortali O60763.
    SMRi O60763. Positions 17-629.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114173. 35 interactions.
    IntActi O60763. 11 interactions.
    MINTi MINT-1136055.
    STRINGi 9606.ENSP00000411698.

    PTM databases

    PhosphoSitei O60763.

    Proteomic databases

    MaxQBi O60763.
    PaxDbi O60763.
    PRIDEi O60763.

    Protocols and materials databases

    DNASUi 8615.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264904 ; ENSP00000264904 ; ENSG00000138768 .
    GeneIDi 8615.
    KEGGi hsa:8615.
    UCSCi uc003hiu.3. human. [O60763-1 ]

    Organism-specific databases

    CTDi 8615.
    GeneCardsi GC04P076649.
    HGNCi HGNC:30904. USO1.
    HPAi CAB010108.
    HPA038282.
    HPA038283.
    MIMi 603344. gene.
    neXtProti NX_O60763.
    PharmGKBi PA162408713.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000016409.
    HOVERGENi HBG018067.
    InParanoidi O60763.
    PhylomeDBi O60763.

    Enzyme and pathway databases

    Reactomei REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

    Miscellaneous databases

    ChiTaRSi USO1. human.
    EvolutionaryTracei O60763.
    GeneWikii USO1.
    GenomeRNAii 8615.
    NextBioi 32287.
    PROi O60763.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60763.
    Bgeei O60763.
    CleanExi HS_USO1.
    Genevestigatori O60763.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR000225. Armadillo.
    IPR006955. Uso1_p115_C.
    IPR024095. Vesicle_P115-like.
    IPR006953. Vesicle_Uso1_P115_head.
    [Graphical view ]
    PANTHERi PTHR10013. PTHR10013. 1 hit.
    Pfami PF04871. Uso1_p115_C. 1 hit.
    PF04869. Uso1_p115_head. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50176. ARM_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phosphorylation of the vesicle docking protein p115 regulates its association with the Golgi membrane."
      Sohda M., Misumi Y., Yano A., Takami N., Ikehara Y.
      J. Biol. Chem. 273:5385-5388(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, MUTAGENESIS OF SER-942, PHOSPHORYLATION AT SER-942.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Skeletal muscle.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      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.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The Golgi-associated protein p115 mediates the secretion of macrophage migration inhibitory factor."
      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.
      J. Immunol. 182:6896-6906(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MIF.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-942, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Unusual armadillo fold in the human general vesicular transport factor p115."
      Striegl H., Roske Y., Kuemmel D., Heinemann U.
      PLoS ONE 4:E4656-E4656(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 53-629, DOMAIN ARM REPEATS, SUBUNIT.

    Entry informationi

    Entry nameiUSO1_HUMAN
    AccessioniPrimary (citable) accession number: O60763
    Secondary accession number(s): B2RAQ0
    , Q6PK63, Q86TB8, Q8N592
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3