Reviewed, UniProtKB/Swiss-Prot Q16222 (UAP1_HUMAN)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylhexosamine pyrophosphorylase
Alternative name(s):
    Antigen X
      Short name=AGX
    Sperm-associated antigen 2
Including the following 2 domains:
    1- Recommended name:
            UDP-N-acetylgalactosamine pyrophosphorylase
              EC=2.7.7.-
        Alternative name(s):
            AGX-1
    2- Recommended name:
            UDP-N-acetylglucosamine pyrophosphorylase
              EC=2.7.7.23
        Alternative name(s):
            AGX-2

Gene names

Name:	UAP1
Synonyms:	SPAG2

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	522 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.
Catalytic activity	UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine.
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-D-glucosamine biosynthesis; UDP-N-acetyl-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
Subunit structure	Monomer and homodimer. Isoform AGX1 is a homodimer. Isoform AGX2 is a monomer.
Subcellular location	Cytoplasm. Note: In spermatozoa, localized to the principal piece of the tail, the neck region of the head and to a lesser extent, the midpiece of the tail.
Tissue specificity	Widely expressed. Isoform AGX1 is more abundant in testis than isoform AGX2, while isoform AGX2 is more abundant than isoform AGX1 in somatic tissue. Expressed at low level in placenta, muscle and liver.
Involvement in disease	Antigen implicated in antibody-mediated male infertility.
Sequence similarities	Belongs to the UDPGP type 1 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	UDP-N-acetylglucosamine biosynthetic process Ref.2 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetylglucosamine diphosphorylase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform AGX2 (identifier: Q16222-1)

Also known as: AGX-2;

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 AGX1 (identifier: Q16222-2)

Also known as: AGX-1;

The sequence of this isoform differs from the canonical sequence as follows:
     454-470: Missing.

Isoform 3 (identifier: Q16222-3)

The sequence of this isoform differs from the canonical sequence as follows:
     454-454: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

UDP-N-acetylhexosamine pyrophosphorylase

PRO_0000185767

Regions

Motif

108 – 111

4

Substrate binding

Motif

303 – 304

2

Substrate binding

Sites

Binding site

223

1

Substrate

Binding site

407

1

Substrate

Natural variations

Alternative sequence

454 – 470

17

Missing in isoform AGX1.

VSP_004483

Alternative sequence

454

1

Missing in isoform 3.

VSP_014523

Natural variant

418

1

P → H: dbSNP rs1128539.

VAR_014935

Experimental info

Sequence conflict

61

1

H → Y in AAH09377. Ref.5

Sequence conflict

445

1

G → S Ref.1

Sequence conflict

445

1

G → S Ref.2

Sequence conflict

454

1

S → Q Ref.1

Sequence conflict

454

1

S → Q Ref.2

Secondary structure

1

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522

Helix Strand Turn

Details...

Helix

3 – 12

10

Helix

16 – 19

4

Helix

22 – 24

3

Helix

27 – 38

12

Helix

42 – 54

13

Helix

74 – 76

3

Beta strand

77 – 79

3

Turn

80 – 83

4

Helix

84 – 86

3

Helix

87 – 99

13

Beta strand

103 – 108

6

Helix

122 – 124

3

Helix

135 – 154

20

Beta strand

162 – 166

5

Turn

168 – 170

3

Helix

171 – 180

10

Helix

181 – 185

5

Helix

188 – 190

3

Beta strand

191 – 195

5

Beta strand

198 – 200

3

Beta strand

210 – 212

3

Beta strand

218 – 220

3

Helix

223 – 225

3

Helix

226 – 232

7

Helix

235 – 241

7

Beta strand

246 – 251

6

Helix

262 – 270

9

Beta strand

274 – 281

8

Beta strand

291 – 295

5

Beta strand

298 – 302

5

Helix

304 – 306

3

Helix

309 – 313

5

Beta strand

319 – 323

5

Beta strand

325 – 334

10

Helix

335 – 343

9

Helix

346 – 348

3

Beta strand

352 – 356

5

Beta strand

375 – 379

5

Helix

382 – 388

7

Beta strand

390 – 397

8

Helix

399 – 402

4

Beta strand

412 – 417

6

Helix

418 – 435

18

Beta strand

439 – 441

3

Beta strand

481 – 483

3

Turn

485 – 487

3

Beta strand

489 – 491

3

Helix

495 – 498

4

Beta strand

505 – 510

6

Beta strand

513 – 516

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform AGX2 (AGX-2) [UniParc]. Last modified July 5, 2005. Version 3. Checksum: 8A69B36D852B9472	FASTA	522	58,769
	10 20 30 40 50 60 MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ KAIEGFNQSS 70 80 90 100 110 120 HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ NKVAVLLLAG GQGTRLGVAY 130 140 150 160 170 180 PKGMYDVGLP SRKTLFQIQA ERILKLQQVA EKYYGNKCII PWYIMTSGRT MESTKEFFTK 190 200 210 220 230 240 HKYFGLKKEN VIFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME 250 260 270 280 290 300 QRGIWSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ 310 320 330 340 350 360 VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ HHVAQKKIPY 370 380 390 400 410 420 VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT 430 440 450 460 470 480 ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRSATNGKS ETITADVNHN LKDANDVPIQ 490 500 510 520 CEISPLISYA GEGLESYVAD KEFHAPLIID ENGVHELVKN GI
	Isoform AGX1 (AGX-1). Checksum: 6BDB4DA54D637317	FASTA	505	57,028
	10 20 30 40 50 60 MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ KAIEGFNQSS 70 80 90 100 110 120 HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ NKVAVLLLAG GQGTRLGVAY 130 140 150 160 170 180 PKGMYDVGLP SRKTLFQIQA ERILKLQQVA EKYYGNKCII PWYIMTSGRT MESTKEFFTK 190 200 210 220 230 240 HKYFGLKKEN VIFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME 250 260 270 280 290 300 QRGIWSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ 310 320 330 340 350 360 VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ HHVAQKKIPY 370 380 390 400 410 420 VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT 430 440 450 460 470 480 ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRLKDANDV PIQCEISPLI SYAGEGLESY 490 500 VADKEFHAPL IIDENGVHEL VKNGI
	Isoform 3. Checksum: 64D0360EFB15A528	FASTA	521	58,682
	10 20 30 40 50 60 MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ KAIEGFNQSS 70 80 90 100 110 120 HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ NKVAVLLLAG GQGTRLGVAY 130 140 150 160 170 180 PKGMYDVGLP SRKTLFQIQA ERILKLQQVA EKYYGNKCII PWYIMTSGRT MESTKEFFTK 190 200 210 220 230 240 HKYFGLKKEN VIFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME 250 260 270 280 290 300 QRGIWSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ 310 320 330 340 350 360 VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ HHVAQKKIPY 370 380 390 400 410 420 VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT 430 440 450 460 470 480 ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRATNGKSE TITADVNHNL KDANDVPIQC 490 500 510 520 EISPLISYAG EGLESYVADK EFHAPLIIDE NGVHELVKNG I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a human antigen with sera from infertile patients." Diekman A.B., Goldberg E. Biol. Reprod. 50:1087-1093(1994) [PubMed: 8025165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS AGX1; AGX2 AND 3). Tissue: Testis.
[2]	"The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases: gene cloning, protein expression, and catalytic mechanism." Mio T., Yabe T., Arisawa M., Yamada-Okabe H. J. Biol. Chem. 273:14392-14397(1998) [PubMed: 9603950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AGX1). Tissue: Testis.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS AGX1; AGX2 AND 3).
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AGX1). Tissue: Muscle.
[5]	"A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc." Wang-Gillam A., Pastuszak I., Elbein A.D. J. Biol. Chem. 273:27055-27057(1998) [PubMed: 9765219] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, CHARACTERIZATION. Tissue: Mammary cancer.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture." Peneff C., Ferrari P., Charrier V., Taburet Y., Monnier C., Zamboni V., Winter J., Harnois M., Fassy F., Bourne Y. EMBO J. 20:6191-6202(2001) [PubMed: 11707391] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.

Cross-references

Sequence databases

EMBLGenBankDDBJ

S73498 mRNA. Translation: AAB31210.2.
AB011004 mRNA. Translation: BAA31202.1.
AL596325 Genomic DNA. Translation: CAH72978.1.
AL596325 Genomic DNA. Translation: CAH72979.1.
AL596325 Genomic DNA. Translation: CAH72980.1.
BC009377 mRNA. Translation: AAH09377.1.

IPI

IPI00000684.
IPI00217816.
IPI00607787.

RefSeq

NP_003106.3.

UniGene

Hs.492859

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JV1	X-ray	1.90	A/B	1-522	[»]
1JV3	X-ray	2.20	A/B	1-522	[»]
1JVD	X-ray	2.40	A/B	1-522	[»]
1JVG	X-ray	2.30	A/B	1-522	[»]

DisProt

DP00363.

ModBase

Search...

2-D gel databases

REPRODUCTION-2DPAGE

IPI00217816.

Proteomic databases

PRIDE

Q16222.

Genome annotation databases

Ensembl

ENSG00000117143. Homo sapiens. [Contig view]

GeneID

6675.

KEGG

hsa:6675.

Organism-specific databases

GeneCards

GC01P160797.

H-InvDB

HIX0020615.

HGNC

HGNC:12457. UAP1.

HPA

HPA014659.

MIM

602862. gene.

PharmGKB

PA128394600.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q16222.

HOVERGEN

Q16222.

OMA

Q16222. VIPWYIM.

Enzyme and pathway databases

BRENDA

2.7.7.23. 247.

Gene expression databases

ArrayExpress

Q16222.

Bgee

Q16222.

CleanEx

HS_UAP1.

GermOnline

ENSG00000117143. Homo sapiens.

Family and domain databases

InterPro

IPR002618. UDPGP_trans.
[Graphical view]

PANTHER

PTHR11952. UDPGP_trans. 1 hit.

Pfam

PF01704. UDPGP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

26027.

SOURCE

Search...

Entry information

Entry name

UAP1_HUMAN

Accession

Primary (citable) accession number: Q16222
Secondary accession number(s): Q5VTA9 , Q5VTB0, Q5VTB1, Q96GM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)