Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O60763 (USO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General vesicular transport factor p115
Alternative name(s):
Protein USO1 homolog
Transcytosis-associated protein
Short name=TAP
Vesicle-docking protein
Gene names
Name:USO1
Synonyms:VDP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length962 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.10 Ref.16

Subcellular location

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. Ref.1 Ref.10

Domain

Composed of a globular head, an elongated tail (coiled-coil) and a highly acidic C-terminal domain. Ref.16

Post-translational modification

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. Ref.1

Sequence similarities

Belongs to the VDP/USO1/EDE1 family.

Contains 12 ARM repeats.

Sequence caution

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

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

Golgi vesicle docking

Inferred from Biological aspect of Ancestor. Source: RefGenome

intracellular protein transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane fusion

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitotic cell cycle

Traceable author statement. Source: Reactome

transcytosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

vesicle fusion with Golgi apparatus

Inferred from electronic annotation. Source: InterPro

   Cellular_componentER to Golgi transport vesicle membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

Golgi apparatus

Inferred from direct assay. Source: HPA

Golgi membrane

Traceable author statement Ref.1. Source: ProtInc

Golgi stack

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleolus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein transporter activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60763-1)

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.
Isoform 2 (identifier: O60763-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 962962General vesicular transport factor p115
PRO_0000065774

Regions

Repeat20 – 6041ARM 1
Repeat61 – 12161ARM 2
Repeat123 – 16341ARM 3
Repeat166 – 20742ARM 4
Repeat208 – 25346ARM 5
Repeat255 – 31056ARM 6
Repeat311 – 35444ARM 7
Repeat363 – 40846ARM 8
Repeat420 – 45940ARM 9
Repeat473 – 51341ARM 10
Repeat518 – 57154ARM 11
Repeat573 – 63058ARM 12
Region1 – 637637Globular head
Coiled coil638 – 930293 Potential
Compositional bias935 – 96228Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue501Phosphoserine Ref.13
Modified residue2021N6-acetyllysine Ref.12
Modified residue9421Phosphoserine Ref.1 Ref.6 Ref.8 Ref.11 Ref.13 Ref.15
Modified residue9521Phosphoserine Ref.11 Ref.15

Natural variations

Alternative sequence981V → VDDVE in isoform 2.
VSP_039120
Alternative sequence4841Q → QGDKIDRR in isoform 2.
VSP_039121

Experimental info

Mutagenesis9421S → A: Loss of phosphorylation. Promotes association with Golgi membranes. Ref.1
Mutagenesis9421S → D: Decreased association with Golgi membranes. Ref.1
Sequence conflict751D → G in CAD89917. Ref.3
Sequence conflict851T → I in BAA25300. Ref.1
Sequence conflict931Missing in AAH32654. Ref.5
Sequence conflict2481N → Y in CAD89917. Ref.3
Sequence conflict6501N → D in CAD89917. Ref.3
Sequence conflict8771Q → R in BAG36947. Ref.2

Secondary structure

.................................................................................... 962
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: C963652209031008

FASTA962107,895
        10         20         30         40         50         60 
MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS KKYRLEVGIQ 

        70         80         90        100        110        120 
AMEHLIHVLQ TDRSDSEIIG YALDTLYNII SNEEEEEVEE NSTRQSEDLG SQFTEIFIKQ 

       130        140        150        160        170        180 
QENVTLLLSL LEEFDFHVRW PGVKLLTSLL KQLGPQVQQI ILVSPMGVSR LMDLLADSRE 

       190        200        210        220        230        240 
VIRNDGVLLL QALTRSNGAI QKIVAFENAF ERLLDIISEE GNSDGGIVVE DCLILLQNLL 

       250        260        270        280        290        300 
KNNNSNQNFF KEGSYIQRMK PWFEVGDENS GWSAQKVTNL HLMLQLVRVL VSPTNPPGAT 

       310        320        330        340        350        360 
SSCQKAMFQC GLLQQLCTIL MATGVPADIL TETINTVSEV IRGCQVNQDY FASVNAPSNP 

       370        380        390        400        410        420 
PRPAIVVLLM SMVNERQPFV LRCAVLYCFQ CFLYKNQKGQ GEIVSTLLPS TIDATGNSVS 

       430        440        450        460        470        480 
AGQLLCGGLF STDSLSNWCA AVALAHALQE NATQKEQLLR VQLATSIGNP PVSLLQQCTN 

       490        500        510        520        530        540 
ILSQGSKIQT RVGLLMLLCT WLSNCPIAVT HFLHNSANVP FLTGQIAENL GEEEQLVQGL 

       550        560        570        580        590        600 
CALLLGISIY FNDNSLESYM KEKLKQLIEK RIGKENFIEK LGFISKHELY SRASQKPQPN 

       610        620        630        640        650        660 
FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDN IVTHYKNMIR 

       670        680        690        700        710        720 
EQDLQLEELR QQVSTLKCQN EQLQTAVTQQ VSQIQQHKDQ YNLLKIQLGK DNQHQGSYSE 

       730        740        750        760        770        780 
GAQMNGIQPE EIGRLREEIE ELKRNQELLQ SQLTEKDSMI ENMKSSQTSG TNEQSSAIVS 

       790        800        810        820        830        840 
ARDSEQVAEL KQELATLKSQ LNSQSVEITK LQTEKQELLQ KTEAFAKSVE VQGETETIIA 

       850        860        870        880        890        900 
TKTTDVEGRL SALLQETKEL KNEIKALSEE RTAIKEQLDS SNSTIAILQT EKDKLELEIT 

       910        920        930        940        950        960 
DSKKEQDDLL VLLADQDQKI LSLKNKLKDL GHPVEEEDEL ESGDQEDEDD ESEDPGKDLD 


HI 

« Hide

Isoform 2 [UniParc].

Checksum: 4DE9E8C5ED44514E
Show »

FASTA973109,195

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001276978.1. NM_001290049.1. [O60763-2]
NP_003706.2. NM_003715.3. [O60763-1]
UniGeneHs.744877.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W3CX-ray2.22A53-629[»]
ProteinModelPortalO60763.
SMRO60763. Positions 17-629.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114173. 35 interactions.
IntActO60763. 11 interactions.
MINTMINT-1136055.
STRING9606.ENSP00000411698.

PTM databases

PhosphoSiteO60763.

Proteomic databases

MaxQBO60763.
PaxDbO60763.
PRIDEO60763.

Protocols and materials databases

DNASU8615.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264904; ENSP00000264904; ENSG00000138768.
GeneID8615.
KEGGhsa:8615.
UCSCuc003hiu.3. human. [O60763-1]

Organism-specific databases

CTD8615.
GeneCardsGC04P076649.
HGNCHGNC:30904. USO1.
HPACAB010108.
HPA038282.
HPA038283.
MIM603344. gene.
neXtProtNX_O60763.
PharmGKBPA162408713.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000016409.
HOVERGENHBG018067.
InParanoidO60763.
PhylomeDBO60763.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressO60763.
BgeeO60763.
CleanExHS_USO1.
GenevestigatorO60763.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR006955. Uso1_p115_C.
IPR024095. Vesicle_P115-like.
IPR006953. Vesicle_Uso1_P115_head.
[Graphical view]
PANTHERPTHR10013. PTHR10013. 1 hit.
PfamPF04871. Uso1_p115_C. 1 hit.
PF04869. Uso1_p115_head. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSO1. human.
EvolutionaryTraceO60763.
GeneWikiUSO1.
GenomeRNAi8615.
NextBio32287.
PROO60763.
SOURCESearch...

Entry information

Entry nameUSO1_HUMAN
AccessionPrimary (citable) accession number: O60763
Secondary accession number(s): B2RAQ0 expand/collapse secondary AC list , Q6PK63, Q86TB8, Q8N592
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM