O95045 (UPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uridine phosphorylase 2
Short name=UPase 2
Short name=UrdPase 2
EC=2.4.2.3

Gene names

Name:

UPP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. Shows substrate specificity and accept uridine, deoxyuridine, and thymidine as well as the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-2(')-deoxyuridine as substrates.
Catalytic activity	Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate.
Enzyme regulation	A conditional disulfide bridge can form within the protein that dislocates a critical phosphate-coordinating arginine Arg-100 away from the active site, disabling the enzyme. Ref.5
Pathway	Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1.
Tissue specificity	Predominantly expressed in kidney. Ref.1
Sequence similarities	Belongs to the PNP/UDP phosphorylase family.
Sequence caution	The sequence AAH33529.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Redox-active center
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway nucleotide catabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleobase metabolic process Traceable author statement. Source: Reactome pyrimidine nucleoside catabolic process Traceable author statement. Source: Reactome pyrimidine nucleoside salvage Traceable author statement. Source: Reactome uridine metabolic process Non-traceable author statement PubMed 11278417. Source: UniProtKB
Cellular_component	cytosol Non-traceable author statement PubMed 11278417. Source: UniProtKB type III intermediate filament Inferred from direct assay PubMed 11278417. Source: UniProtKB
Molecular_function	uridine phosphorylase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95045-1)

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: O95045-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLAPGCELDPDQEVVRTRPEDVPASPSTSTMIVSVLRPPSHASCTACGTVTFHIVERM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 317

317

Uridine phosphorylase 2

PRO_0000063193

Amino acid modifications

Disulfide bond

95 ↔ 102

Redox-active Ref.5

Natural variations

Alternative sequence

1

1

M → MLAPGCELDPDQEVVRTRPE DVPASPSTSTMIVSVLRPPS HASCTACGTVTFHIVERM in isoform 2.

VSP_043756

Natural variant

10

1

R → S.
Corresponds to variant rs6710480 [ dbSNP | Ensembl ].

VAR_024431

Natural variant

78

1

M → L.
Corresponds to variant rs7561584 [ dbSNP | Ensembl ].

VAR_034580

Experimental info

Sequence conflict

153

1

I → M in AAO61681. Ref.1

Sequence conflict

157

1

T → R in AAO61681. Ref.1

Sequence conflict

256 – 262

7

ESTVFAA → GIYSVCS in AAO61681. Ref.1

Secondary structure

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317

Helix Strand Turn

Details...

Helix

32 – 34

3

Helix

41 – 43

3

Turn

47 – 49

3

Helix

52 – 56

5

Beta strand

61 – 66

6

Helix

68 – 82

15

Turn

94 – 97

4

Beta strand

98 – 100

3

Beta strand

103 – 106

4

Beta strand

109 – 113

5

Helix

118 – 134

17

Beta strand

141 – 153

13

Beta strand

158 – 165

8

Beta strand

171 – 177

7

Beta strand

180 – 185

6

Helix

190 – 201

12

Beta strand

208 – 215

8

Helix

221 – 223

3

Beta strand

226 – 229

4

Helix

235 – 248

14

Beta strand

250 – 256

7

Helix

257 – 266

10

Beta strand

270 – 280

11

Turn

281 – 283

3

Helix

291 – 298

8

Helix

300 – 313

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 69F6BA1DC44977A3	FASTA	317	35,527
	10 20 30 40 50 60 MASVIPASNR SMRSDRNTYV GKRFVHVKNP YLDLMDEDIL YHLDLGTKTH NLPAMFGDVK 70 80 90 100 110 120 FVCVGGSPNR MKAFALFMHK ELGFEEAEED IKDICAGTDR YCMYKTGPVL AISHGMGIPS 130 140 150 160 170 180 ISIMLHELIK LLHHARCCDV TIIRIGTSGG IGIAPGTVVI TDIAVDSFFK PRFEQVILDN 190 200 210 220 230 240 IVTRSTELDK ELSEELFNCS KEIPNFPTLV GHTMCTYDFY EGQGRLDGAL CSFSREKKLD 250 260 270 280 290 300 YLKRAFKAGV RNIEMESTVF AAMCGLCGLK AAVVCVTLLD RLDCDQINLP HDVLVEYQQR 310 PQLLISNFIR RRLGLCD
	Isoform 2 [UniParc]. Checksum: F1FF70496CD41D8F	FASTA	374	41,602
	10 20 30 40 50 60 MLAPGCELDP DQEVVRTRPE DVPASPSTST MIVSVLRPPS HASCTACGTV TFHIVERMAS 70 80 90 100 110 120 VIPASNRSMR SDRNTYVGKR FVHVKNPYLD LMDEDILYHL DLGTKTHNLP AMFGDVKFVC 130 140 150 160 170 180 VGGSPNRMKA FALFMHKELG FEEAEEDIKD ICAGTDRYCM YKTGPVLAIS HGMGIPSISI 190 200 210 220 230 240 MLHELIKLLH HARCCDVTII RIGTSGGIGI APGTVVITDI AVDSFFKPRF EQVILDNIVT 250 260 270 280 290 300 RSTELDKELS EELFNCSKEI PNFPTLVGHT MCTYDFYEGQ GRLDGALCSF SREKKLDYLK 310 320 330 340 350 360 RAFKAGVRNI EMESTVFAAM CGLCGLKAAV VCVTLLDRLD CDQINLPHDV LVEYQQRPQL 370 LISNFIRRRL GLCD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel human uridine phosphorylase." Johansson M. Biochem. Biophys. Res. Commun. 307:41-46(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, TISSUE SPECIFICITY.
[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: Kidney.
[3]	"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].
[4]	"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 2). Tissue: Brain.
[5]	"A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity." Roosild T.P., Castronovo S., Villoso A., Ziemba A., Pizzorno G. J. Struct. Biol. 176:229-237(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-314, ENZYME REGULATION, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY225131 mRNA. Translation: AAO61681.1.
AK122743 mRNA. Translation: BAG53699.1.
AC005539 Genomic DNA. Translation: AAD12227.1.
BC033529 mRNA. Translation: AAH33529.1. Different initiation.

IPI

IPI00098522.

RefSeq

NP_001128570.1. NM_001135098.1.
NP_775491.1. NM_173355.3.

UniGene

Hs.128427.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XRF	X-ray	2.30	A/B/C	23-317	[»]
3P0E	X-ray	2.00	A/B/C/D/E/F	21-314	[»]
3P0F	X-ray	1.54	A	21-314	[»]

ProteinModelPortal

O95045.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000387230.

PTM databases

PhosphoSite

O95045.

Proteomic databases

PaxDb

O95045.

PRIDE

O95045.

Protocols and materials databases

DNASU

151531.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000005756; ENSP00000005756; ENSG00000007001.
ENST00000409859; ENSP00000387230; ENSG00000007001.

GeneID

151531.

KEGG

hsa:151531.

UCSC

uc002tzo.3. human.

Organism-specific databases

CTD

151531.

GeneCards

GC02P158815.

HGNC

HGNC:23061. UPP2.

HPA

HPA035225.
HPA035226.

neXtProt

NX_O95045.

PharmGKB

PA134866434.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2820.

HOGENOM

HOG000231747.

HOVERGEN

HBG047725.

InParanoid

O95045.

KO

K00757.

OMA

VGKRFVH.

OrthoDB

EOG412M66.

PhylomeDB

O95045.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

O95045.

SignaLink

O95045.

UniPathway

UPA00574; UER00633.

Gene expression databases

Bgee

O95045.

CleanEx

HS_UPP2.

Genevestigator

O95045.

GermOnline

ENSG00000007001. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1580. 1 hit.

InterPro

IPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
IPR010059. Uridine_phosphorylase_euk.
[Graphical view]

PANTHER

PTHR21234. PTHR21234. 1 hit.
PTHR21234:SF4. PTHR21234:SF4. 1 hit.

Pfam

PF01048. PNP_UDP_1. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01719. euk_UDPppase. 1 hit.

PROSITE

PS01232. PNP_UDP_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O95045.

ChEMBL

CHEMBL2471.

EvolutionaryTrace

O95045.

GenomeRNAi

151531.

NextBio

86721.

Entry information

Entry name

UPP2_HUMAN

Accession

Primary (citable) accession number: O95045
Secondary accession number(s): B3KV87

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	May 1, 1999
Last modified:	May 29, 2013
This is version 99 of the entry and version 1 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.