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O60763

- USO1_HUMAN

UniProt

O60763 - USO1_HUMAN

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Protein
General vesicular transport factor p115
Gene
USO1, VDP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

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

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 p115
PRO_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.1 Publication

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 Inferred. Interacts with MIF.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO60763.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili638 – 930293 Reviewed prediction
Add
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.
Contains 12 ARM repeats.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei98 – 981V → VDDVE in isoform 2.
VSP_039120
Alternative sequencei484 – 4841Q → QGDKIDRR in isoform 2.
VSP_039121

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751D → G in CAD89917. 1 Publication
Sequence conflicti85 – 851T → I in BAA25300. 1 Publication
Sequence conflicti93 – 931Missing in AAH32654. 1 Publication
Sequence conflicti248 – 2481N → Y in CAD89917. 1 Publication
Sequence conflicti650 – 6501N → D in CAD89917. 1 Publication
Sequence conflicti877 – 8771Q → R in BAG36947. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 123 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

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