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O60763

- USO1_HUMAN

UniProt

O60763 - USO1_HUMAN

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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

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
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.

GO - Cellular componenti

  1. endoplasmic reticulum Source: RefGenome
  2. ER to Golgi transport vesicle membrane Source: RefGenome
  3. Golgi apparatus Source: HPA
  4. Golgi membrane Source: ProtInc
  5. Golgi stack Source: RefGenome
  6. membrane Source: UniProtKB
  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 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

BgeeiO60763.
CleanExiHS_USO1.
ExpressionAtlasiO60763. baseline and differential.
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. 43 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 – 626Combined sources
Helixi63 – 719Combined sources
Helixi76 – 9116Combined sources
Helixi112 – 1198Combined sources
Helixi122 – 1309Combined sources
Helixi136 – 15217Combined sources
Helixi154 – 16310Combined sources
Helixi167 – 1726Combined sources
Helixi173 – 1764Combined sources
Helixi180 – 19415Combined sources
Helixi198 – 2069Combined sources
Helixi209 – 21911Combined sources
Helixi222 – 2243Combined sources
Helixi227 – 24014Combined sources
Helixi244 – 2529Combined sources
Helixi256 – 2594Combined sources
Helixi261 – 2633Combined sources
Helixi274 – 29017Combined sources
Helixi297 – 30913Combined sources
Helixi312 – 32110Combined sources
Helixi327 – 34115Combined sources
Helixi345 – 3528Combined sources
Helixi364 – 3729Combined sources
Helixi379 – 39315Combined sources
Helixi397 – 4059Combined sources
Beta strandi414 – 4163Combined sources
Helixi421 – 4299Combined sources
Helixi434 – 44815Combined sources
Helixi452 – 4587Combined sources
Beta strandi466 – 4694Combined sources
Helixi474 – 4818Combined sources
Turni482 – 4854Combined sources
Helixi488 – 50215Combined sources
Helixi506 – 5138Combined sources
Helixi518 – 52710Combined sources
Turni531 – 5344Combined sources
Helixi535 – 55016Combined sources
Beta strandi557 – 5593Combined sources
Helixi561 – 57111Combined sources
Helixi574 – 5829Combined sources
Turni583 – 5864Combined sources
Helixi590 – 5934Combined sources
Helixi604 – 6063Combined sources
Helixi611 – 62717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000017018.
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

        10         20         30         40         50
MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS
60 70 80 90 100
KKYRLEVGIQ AMEHLIHVLQ TDRSDSEIIG YALDTLYNII SNEEEEEVEE
110 120 130 140 150
NSTRQSEDLG SQFTEIFIKQ QENVTLLLSL LEEFDFHVRW PGVKLLTSLL
160 170 180 190 200
KQLGPQVQQI ILVSPMGVSR LMDLLADSRE VIRNDGVLLL QALTRSNGAI
210 220 230 240 250
QKIVAFENAF ERLLDIISEE GNSDGGIVVE DCLILLQNLL KNNNSNQNFF
260 270 280 290 300
KEGSYIQRMK PWFEVGDENS GWSAQKVTNL HLMLQLVRVL VSPTNPPGAT
310 320 330 340 350
SSCQKAMFQC GLLQQLCTIL MATGVPADIL TETINTVSEV IRGCQVNQDY
360 370 380 390 400
FASVNAPSNP PRPAIVVLLM SMVNERQPFV LRCAVLYCFQ CFLYKNQKGQ
410 420 430 440 450
GEIVSTLLPS TIDATGNSVS AGQLLCGGLF STDSLSNWCA AVALAHALQE
460 470 480 490 500
NATQKEQLLR VQLATSIGNP PVSLLQQCTN ILSQGSKIQT RVGLLMLLCT
510 520 530 540 550
WLSNCPIAVT HFLHNSANVP FLTGQIAENL GEEEQLVQGL CALLLGISIY
560 570 580 590 600
FNDNSLESYM KEKLKQLIEK RIGKENFIEK LGFISKHELY SRASQKPQPN
610 620 630 640 650
FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDN
660 670 680 690 700
IVTHYKNMIR EQDLQLEELR QQVSTLKCQN EQLQTAVTQQ VSQIQQHKDQ
710 720 730 740 750
YNLLKIQLGK DNQHQGSYSE GAQMNGIQPE EIGRLREEIE ELKRNQELLQ
760 770 780 790 800
SQLTEKDSMI ENMKSSQTSG TNEQSSAIVS ARDSEQVAEL KQELATLKSQ
810 820 830 840 850
LNSQSVEITK LQTEKQELLQ KTEAFAKSVE VQGETETIIA TKTTDVEGRL
860 870 880 890 900
SALLQETKEL KNEIKALSEE RTAIKEQLDS SNSTIAILQT EKDKLELEIT
910 920 930 940 950
DSKKEQDDLL VLLADQDQKI LSLKNKLKDL GHPVEEEDEL ESGDQEDEDD
960
ESEDPGKDLD HI
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.Curated

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:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS75144.1. [O60763-1]
RefSeqiNP_001276978.1. NM_001290049.1. [O60763-2]
NP_003706.2. NM_003715.3. [O60763-1]
UniGeneiHs.744877.

Genome annotation databases

EnsembliENST00000264904; ENSP00000264904; ENSG00000138768. [O60763-2]
ENST00000514213; ENSP00000444850; ENSG00000138768. [O60763-1]
GeneIDi8615.
KEGGihsa:8615.
UCSCiuc003hiu.3. human. [O60763-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 .
CCDSi CCDS75144.1. [O60763-1 ]
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:
PDBei
RCSB PDBi
PDBji
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. 43 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 . [O60763-2 ]
ENST00000514213 ; ENSP00000444850 ; ENSG00000138768 . [O60763-1 ]
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.
GeneTreei ENSGT00390000017018.
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

Bgeei O60763.
CleanExi HS_USO1.
ExpressionAtlasi O60763. baseline and differential.
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: November 26, 2014
This is version 126 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