O60763 (USO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	962 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
Subcellular location	Cytoplasm › cytosol. 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.14
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 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Sequence similarities	Belongs to the VDP/USO1/EDE1 family. Contains 10 ARM repeats.
Sequence caution	The sequence AAH06398.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular protein transport Inferred from electronic annotation. Source: InterPro vesicle fusion with Golgi apparatus Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Traceable author statement. Source: ProtInc cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro protein transporter activity Inferred from electronic annotation. Source: InterPro
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 962

962

General vesicular transport factor p115

PRO_0000065774

Regions

Repeat

48 – 91

44

ARM 1

Repeat

112 – 151

40

ARM 2

Repeat

154 – 194

41

ARM 3

Repeat

196 – 241

46

ARM 4

Repeat

242 – 290

49

ARM 5

Repeat

292 – 341

50

ARM 6

Repeat

342 – 393

52

ARM 7

Repeat

394 – 448

55

ARM 8

Repeat

450 – 501

52

ARM 9

Repeat

503 – 548

46

ARM 10

Region

1 – 637

637

Globular head

Coiled coil

638 – 930

293

Potential

Compositional bias

935 – 962

28

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

202

1

N6-acetyllysine Ref.12

Modified residue

942

1

Phosphoserine Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11

Modified residue

952

1

Phosphoserine Ref.7 Ref.11

Natural variations

Alternative sequence

98

1

V → VDDVE in isoform 2.

VSP_039120

Alternative sequence

484

1

Q → QGDKIDRR in isoform 2.

VSP_039121

Experimental info

Mutagenesis

942

1

S → A: Loss of phosphorylation. Promotes association with Golgi membranes. Ref.1

Mutagenesis

942

1

S → D: Decreased association with Golgi membranes. Ref.1

Sequence conflict

75

1

D → G in CAD89917. Ref.3

Sequence conflict

85

1

T → I in BAA25300. Ref.1

Sequence conflict

93

1

Missing in AAH32654. Ref.5

Sequence conflict

248

1

N → Y in CAD89917. Ref.3

Sequence conflict

650

1

N → D in CAD89917. Ref.3

Sequence conflict

877

1

Q → R in BAG36947. Ref.2

Secondary structure

1

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962

Helix Strand Turn

Details...

Turn

60 – 62

3

Helix

63 – 71

9

Turn

76 – 78

3

Helix

82 – 91

10

Helix

112 – 119

8

Helix

122 – 130

9

Helix

136 – 139

4

Helix

144 – 152

9

Helix

156 – 163

8

Helix

169 – 172

4

Helix

173 – 176

4

Helix

180 – 184

5

Helix

188 – 194

7

Helix

200 – 206

7

Helix

209 – 219

11

Helix

228 – 240

13

Helix

244 – 251

8

Helix

256 – 259

4

Helix

261 – 263

3

Helix

274 – 290

17

Helix

300 – 309

10

Helix

313 – 321

9

Helix

327 – 341

15

Helix

345 – 352

8

Helix

364 – 372

9

Helix

379 – 393

15

Helix

405 – 407

3

Helix

434 – 448

15

Helix

452 – 458

7

Helix

474 – 481

8

Helix

495 – 502

8

Helix

506 – 513

8

Helix

518 – 522

5

Turn

534 – 537

4

Helix

541 – 544

4

Turn

548 – 551

4

Beta strand

557 – 559

3

Helix

561 – 571

11

Helix

575 – 580

6

Helix

590 – 593

4

Helix

604 – 606

3

Helix

611 – 620

10

Helix

624 – 627

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: C963652209031008	FASTA	962	107,895
	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
	Isoform 2 [UniParc]. Checksum: 4DE9E8C5ED44514E	FASTA	973	109,195
	10 20 30 40 50 60 MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS KKYRLEVGIQ 70 80 90 100 110 120 AMEHLIHVLQ TDRSDSEIIG YALDTLYNII SNEEEEEVDD VEEENSTRQS EDLGSQFTEI 130 140 150 160 170 180 FIKQQENVTL LLSLLEEFDF HVRWPGVKLL TSLLKQLGPQ VQQIILVSPM GVSRLMDLLA 190 200 210 220 230 240 DSREVIRNDG VLLLQALTRS NGAIQKIVAF ENAFERLLDI ISEEGNSDGG IVVEDCLILL 250 260 270 280 290 300 QNLLKNNNSN QNFFKEGSYI QRMKPWFEVG DENSGWSAQK VTNLHLMLQL VRVLVSPTNP 310 320 330 340 350 360 PGATSSCQKA MFQCGLLQQL CTILMATGVP ADILTETINT VSEVIRGCQV NQDYFASVNA 370 380 390 400 410 420 PSNPPRPAIV VLLMSMVNER QPFVLRCAVL YCFQCFLYKN QKGQGEIVST LLPSTIDATG 430 440 450 460 470 480 NSVSAGQLLC GGLFSTDSLS NWCAAVALAH ALQENATQKE QLLRVQLATS IGNPPVSLLQ 490 500 510 520 530 540 QCTNILSQGD KIDRRGSKIQ TRVGLLMLLC TWLSNCPIAV THFLHNSANV PFLTGQIAEN 550 560 570 580 590 600 LGEEEQLVQG LCALLLGISI YFNDNSLESY MKEKLKQLIE KRIGKENFIE KLGFISKHEL 610 620 630 640 650 660 YSRASQKPQP NFPSPEYMIF DHEFTKLVKE LEGVITKAIY KSSEEDKKEE EVKKTLEQHD 670 680 690 700 710 720 NIVTHYKNMI REQDLQLEEL RQQVSTLKCQ NEQLQTAVTQ QVSQIQQHKD QYNLLKIQLG 730 740 750 760 770 780 KDNQHQGSYS EGAQMNGIQP EEIGRLREEI EELKRNQELL QSQLTEKDSM IENMKSSQTS 790 800 810 820 830 840 GTNEQSSAIV SARDSEQVAE LKQELATLKS QLNSQSVEIT KLQTEKQELL QKTEAFAKSV 850 860 870 880 890 900 EVQGETETII ATKTTDVEGR LSALLQETKE LKNEIKALSE ERTAIKEQLD SSNSTIAILQ 910 920 930 940 950 960 TEKDKLELEI TDSKKEQDDL LVLLADQDQK ILSLKNKLKD LGHPVEEEDE LESGDQEDED 970 DESEDPGKDL DHI

References

	« Hide 'large scale' referencesShow '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: 9478999] [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: 14702039] [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: 17974005] [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. , 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: 15815621] [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: 15489334] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, MASS SPECTROMETRY. 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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, MASS SPECTROMETRY. 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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19454686] [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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, MASS SPECTROMETRY.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"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: 19247479] [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.

IPI

IPI00031583.
IPI00941161.

RefSeq

NP_003706.1. NM_003715.2.

UniGene

Hs.292689.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W3C	X-ray	2.22	A	53-629	[»]

ProteinModelPortal

O60763.

SMR

O60763. Positions 17-629.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60763. 7 interactions.

MINT

MINT-1136055.

STRING

O60763.

PTM databases

PhosphoSite

O60763.

Proteomic databases

PRIDE

O60763.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264904; ENSP00000264904; ENSG00000138768.

GeneID

8615.

KEGG

hsa:8615.

Organism-specific databases

CTD

8615.

GeneCards

GC04P076649.

HGNC

HGNC:30904. USO1.

HPA

CAB010108.

MIM

603344. gene.

neXtProt

NX_O60763.

PharmGKB

PA162408713.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000017018.

HOVERGEN

HBG018067.

InParanoid

O60763.

PhylomeDB

O60763.

Enzyme and pathway databases

Pathway_Interaction_DB

arf_3pathway. Arf1 pathway.

Gene expression databases

ArrayExpress

O60763.

Bgee

O60763.

CleanEx

HS_USO1.

Genevestigator

O60763.

GermOnline

ENSG00000138768. Homo sapiens.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR006955. Uso1_p115_C.
IPR024095. Vesicle_P115-like.
IPR006953. Vesicle_Uso1_P115_head.
[Graphical view]

PANTHER

PTHR10013. PTHR10013. 1 hit.

Pfam

PF04871. Uso1_p115_C. 1 hit.
PF04869. Uso1_p115_head. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 2 hits.

PROSITE

PS50176. ARM_REPEAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

32287.

SOURCE

Search...

Entry information

Entry name

USO1_HUMAN

Accession

Primary (citable) accession number: O60763
Secondary accession number(s): B2RAQ0 , Q6PK63, Q86TB8, Q8N592

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	March 6, 2007
Last modified:	January 25, 2012
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.