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Protein

UDP-N-acetylhexosamine pyrophosphorylase

Gene

UAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

UTP + N-acetyl-alpha-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-galactosamine.1 Publication
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei223 – 2231Substrate1 Publication
Binding sitei407 – 4071Substrate1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: Ensembl
  2. UDP-N-acetylglucosamine diphosphorylase activity Source: Reactome

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein N-linked glycosylation via asparagine Source: Reactome
  5. UDP-N-acetylglucosamine biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_22394. Synthesis of UDP-N-acetyl-glucosamine.
SABIO-RKQ16222.
UniPathwayiUPA00113; UER00533.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylhexosamine pyrophosphorylase
Alternative name(s):
Antigen X
Short name:
AGX
Sperm-associated antigen 2
Including the following 2 domains:
UDP-N-acetylgalactosamine pyrophosphorylase (EC:2.7.7.83)
Alternative name(s):
AGX-1
UDP-N-acetylglucosamine pyrophosphorylase (EC:2.7.7.23)
Alternative name(s):
AGX-2
Gene namesi
Name:UAP1
Synonyms:SPAG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12457. UAP1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: HPA
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37107.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522UDP-N-acetylhexosamine pyrophosphorylasePRO_0000185767Add
BLAST

Proteomic databases

MaxQBiQ16222.
PaxDbiQ16222.
PRIDEiQ16222.

2D gel databases

REPRODUCTION-2DPAGEIPI00217816.

PTM databases

PhosphoSiteiQ16222.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ16222.
CleanExiHS_UAP1.
GenevestigatoriQ16222.

Organism-specific databases

HPAiHPA014659.

Interactioni

Subunit structurei

Monomer and homodimer. Isoform AGX1 is a homodimer. Isoform AGX2 is a monomer.1 Publication

Protein-protein interaction databases

BioGridi112557. 10 interactions.
STRINGi9606.ENSP00000356903.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Helixi16 – 194Combined sources
Helixi22 – 243Combined sources
Helixi27 – 3812Combined sources
Helixi42 – 5413Combined sources
Helixi74 – 763Combined sources
Beta strandi77 – 793Combined sources
Turni80 – 834Combined sources
Helixi84 – 863Combined sources
Helixi87 – 9913Combined sources
Beta strandi103 – 1086Combined sources
Helixi114 – 1163Combined sources
Helixi122 – 1243Combined sources
Helixi135 – 15420Combined sources
Beta strandi162 – 1665Combined sources
Turni168 – 1703Combined sources
Helixi171 – 18010Combined sources
Helixi181 – 1855Combined sources
Helixi188 – 1903Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi218 – 2203Combined sources
Helixi223 – 2253Combined sources
Helixi226 – 2327Combined sources
Helixi235 – 2417Combined sources
Beta strandi246 – 2516Combined sources
Helixi262 – 2709Combined sources
Beta strandi274 – 2818Combined sources
Beta strandi291 – 2955Combined sources
Beta strandi298 – 3025Combined sources
Helixi304 – 3063Combined sources
Helixi309 – 3135Combined sources
Beta strandi319 – 3235Combined sources
Beta strandi325 – 33410Combined sources
Helixi335 – 3439Combined sources
Helixi346 – 3483Combined sources
Beta strandi352 – 3565Combined sources
Beta strandi375 – 3795Combined sources
Helixi382 – 3887Combined sources
Beta strandi390 – 3978Combined sources
Helixi399 – 4024Combined sources
Beta strandi412 – 4176Combined sources
Helixi418 – 43518Combined sources
Beta strandi439 – 4413Combined sources
Beta strandi481 – 4833Combined sources
Turni485 – 4873Combined sources
Beta strandi489 – 4913Combined sources
Helixi495 – 4984Combined sources
Beta strandi505 – 5106Combined sources
Beta strandi513 – 5164Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JV1X-ray1.90A/B1-522[»]
1JV3X-ray2.20A/B1-522[»]
1JVDX-ray2.40A/B1-522[»]
1JVGX-ray2.30A/B1-522[»]
DisProtiDP00363.
ProteinModelPortaliQ16222.
SMRiQ16222. Positions 1-518.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16222.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi108 – 1114Substrate binding
Motifi303 – 3042Substrate binding

Sequence similaritiesi

Belongs to the UDPGP type 1 family.Curated

Phylogenomic databases

eggNOGiCOG4284.
GeneTreeiENSGT00390000010072.
HOGENOMiHOG000186273.
HOVERGENiHBG018024.
InParanoidiQ16222.
KOiK00972.
OMAiGQRWIEK.
PhylomeDBiQ16222.
TreeFamiTF300611.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR002618. UDPGP_trans_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 1 hit.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform AGX2 (identifier: Q16222-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ
60 70 80 90 100
KAIEGFNQSS HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ
110 120 130 140 150
NKVAVLLLAG GQGTRLGVAY PKGMYDVGLP SRKTLFQIQA ERILKLQQVA
160 170 180 190 200
EKYYGNKCII PWYIMTSGRT MESTKEFFTK HKYFGLKKEN VIFFQQGMLP
210 220 230 240 250
AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME QRGIWSIHVY
260 270 280 290 300
CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ
310 320 330 340 350
VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ
360 370 380 390 400
HHVAQKKIPY VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE
410 420 430 440 450
DEFSPLKNAD SQNGKDNPTT ARHALMSLHH CWVLNAGGHF IDENGSRLPA
460 470 480 490 500
IPRSATNGKS ETITADVNHN LKDANDVPIQ CEISPLISYA GEGLESYVAD
510 520
KEFHAPLIID ENGVHELVKN GI
Length:522
Mass (Da):58,769
Last modified:July 5, 2005 - v3
Checksum:i8A69B36D852B9472
GO
Isoform AGX1 (identifier: Q16222-2) [UniParc]FASTAAdd to basket

Also known as: AGX-1

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

Show »
Length:505
Mass (Da):57,028
Checksum:i6BDB4DA54D637317
GO
Isoform 3 (identifier: Q16222-3) [UniParc]FASTAAdd to basket

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

Show »
Length:521
Mass (Da):58,682
Checksum:i64D0360EFB15A528
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611H → Y in AAH09377 (PubMed:15489334).Curated
Sequence conflicti445 – 4451G → S (PubMed:8025165).Curated
Sequence conflicti445 – 4451G → S (PubMed:9603950).Curated
Sequence conflicti454 – 4541S → Q (PubMed:8025165).Curated
Sequence conflicti454 – 4541S → Q (PubMed:9603950).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti418 – 4181P → H.
Corresponds to variant rs1128539 [ dbSNP | Ensembl ].
VAR_014935

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 47017Missing in isoform AGX1. 4 PublicationsVSP_004483Add
BLAST
Alternative sequencei454 – 4541Missing in isoform 3. 1 PublicationVSP_014523

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73498 mRNA. Translation: AAB31210.2.
AB011004 mRNA. Translation: BAA31202.1.
AK312685 mRNA. Translation: BAG35565.1.
AL596325 Genomic DNA. Translation: CAH72978.1.
AL596325 Genomic DNA. Translation: CAH72979.1.
AL596325 Genomic DNA. Translation: CAH72980.1.
CH471067 Genomic DNA. Translation: EAW90710.1.
BC009377 mRNA. Translation: AAH09377.1.
CCDSiCCDS1240.1. [Q16222-2]
RefSeqiNP_003106.3. NM_003115.4. [Q16222-2]
XP_005245519.1. XM_005245462.1. [Q16222-1]
XP_005245522.1. XM_005245465.2. [Q16222-3]
UniGeneiHs.492859.

Genome annotation databases

EnsembliENST00000271469; ENSP00000271469; ENSG00000117143. [Q16222-1]
ENST00000367924; ENSP00000356901; ENSG00000117143. [Q16222-3]
ENST00000367925; ENSP00000356902; ENSG00000117143. [Q16222-1]
ENST00000367926; ENSP00000356903; ENSG00000117143. [Q16222-2]
GeneIDi6675.
KEGGihsa:6675.
UCSCiuc001gce.4. human. [Q16222-2]

Polymorphism databases

DMDMi68846235.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S73498 mRNA. Translation: AAB31210.2.
AB011004 mRNA. Translation: BAA31202.1.
AK312685 mRNA. Translation: BAG35565.1.
AL596325 Genomic DNA. Translation: CAH72978.1.
AL596325 Genomic DNA. Translation: CAH72979.1.
AL596325 Genomic DNA. Translation: CAH72980.1.
CH471067 Genomic DNA. Translation: EAW90710.1.
BC009377 mRNA. Translation: AAH09377.1.
CCDSiCCDS1240.1. [Q16222-2]
RefSeqiNP_003106.3. NM_003115.4. [Q16222-2]
XP_005245519.1. XM_005245462.1. [Q16222-1]
XP_005245522.1. XM_005245465.2. [Q16222-3]
UniGeneiHs.492859.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JV1X-ray1.90A/B1-522[»]
1JV3X-ray2.20A/B1-522[»]
1JVDX-ray2.40A/B1-522[»]
1JVGX-ray2.30A/B1-522[»]
DisProtiDP00363.
ProteinModelPortaliQ16222.
SMRiQ16222. Positions 1-518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112557. 10 interactions.
STRINGi9606.ENSP00000356903.

PTM databases

PhosphoSiteiQ16222.

Polymorphism databases

DMDMi68846235.

2D gel databases

REPRODUCTION-2DPAGEIPI00217816.

Proteomic databases

MaxQBiQ16222.
PaxDbiQ16222.
PRIDEiQ16222.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000271469; ENSP00000271469; ENSG00000117143. [Q16222-1]
ENST00000367924; ENSP00000356901; ENSG00000117143. [Q16222-3]
ENST00000367925; ENSP00000356902; ENSG00000117143. [Q16222-1]
ENST00000367926; ENSP00000356903; ENSG00000117143. [Q16222-2]
GeneIDi6675.
KEGGihsa:6675.
UCSCiuc001gce.4. human. [Q16222-2]

Organism-specific databases

CTDi6675.
GeneCardsiGC01P162531.
H-InvDBHIX0001264.
HGNCiHGNC:12457. UAP1.
HPAiHPA014659.
MIMi602862. gene.
neXtProtiNX_Q16222.
PharmGKBiPA37107.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4284.
GeneTreeiENSGT00390000010072.
HOGENOMiHOG000186273.
HOVERGENiHBG018024.
InParanoidiQ16222.
KOiK00972.
OMAiGQRWIEK.
PhylomeDBiQ16222.
TreeFamiTF300611.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00533.
ReactomeiREACT_22394. Synthesis of UDP-N-acetyl-glucosamine.
SABIO-RKQ16222.

Miscellaneous databases

ChiTaRSiUAP1. human.
EvolutionaryTraceiQ16222.
GeneWikiiUAP1.
GenomeRNAii6675.
NextBioi26027.
PROiQ16222.
SOURCEiSearch...

Gene expression databases

BgeeiQ16222.
CleanExiHS_UAP1.
GenevestigatoriQ16222.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR002618. UDPGP_trans_fam.
[Graphical view]
PANTHERiPTHR11952. PTHR11952. 1 hit.
PfamiPF01704. UDPGP. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a human antigen with sera from infertile patients."
    Diekman A.B., Goldberg E.
    Biol. Reprod. 50:1087-1093(1994) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AGX1).
    Tissue: Testis.
  3. "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 AGX1).
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS AGX1; AGX2 AND 3).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 AGX1).
    Tissue: Muscle.
  7. "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] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, ALTERNATIVE SPLICING, CATALYTIC ACTIVITY, CHARACTERIZATION.
    Tissue: Mammary cancer.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.

Entry informationi

Entry nameiUAP1_HUMAN
AccessioniPrimary (citable) accession number: Q16222
Secondary accession number(s): B2R6R8
, Q5VTA9, Q5VTB0, Q5VTB1, Q96GM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 5, 2005
Last modified: March 4, 2015
This is version 150 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.