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Q16222

- UAP1_HUMAN

UniProt

Q16222 - UAP1_HUMAN

Protein

UDP-N-acetylhexosamine pyrophosphorylase

Gene

UAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (05 Jul 2005)
      Previous versions | rss
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    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

    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. cytosol Source: Reactome

    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

    ArrayExpressiQ16222.
    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 – 1210
    Helixi16 – 194
    Helixi22 – 243
    Helixi27 – 3812
    Helixi42 – 5413
    Helixi74 – 763
    Beta strandi77 – 793
    Turni80 – 834
    Helixi84 – 863
    Helixi87 – 9913
    Beta strandi103 – 1086
    Helixi114 – 1163
    Helixi122 – 1243
    Helixi135 – 15420
    Beta strandi162 – 1665
    Turni168 – 1703
    Helixi171 – 18010
    Helixi181 – 1855
    Helixi188 – 1903
    Beta strandi191 – 1955
    Beta strandi198 – 2003
    Beta strandi210 – 2123
    Beta strandi218 – 2203
    Helixi223 – 2253
    Helixi226 – 2327
    Helixi235 – 2417
    Beta strandi246 – 2516
    Helixi262 – 2709
    Beta strandi274 – 2818
    Beta strandi291 – 2955
    Beta strandi298 – 3025
    Helixi304 – 3063
    Helixi309 – 3135
    Beta strandi319 – 3235
    Beta strandi325 – 33410
    Helixi335 – 3439
    Helixi346 – 3483
    Beta strandi352 – 3565
    Beta strandi375 – 3795
    Helixi382 – 3887
    Beta strandi390 – 3978
    Helixi399 – 4024
    Beta strandi412 – 4176
    Helixi418 – 43518
    Beta strandi439 – 4413
    Beta strandi481 – 4833
    Turni485 – 4873
    Beta strandi489 – 4913
    Helixi495 – 4984
    Beta strandi505 – 5106
    Beta strandi513 – 5164

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000186273.
    HOVERGENiHBG018024.
    InParanoidiQ16222.
    KOiK00972.
    OMAiVFFQQGM.
    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. Align

    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

    MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ    50
    KAIEGFNQSS HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ 100
    NKVAVLLLAG GQGTRLGVAY PKGMYDVGLP SRKTLFQIQA ERILKLQQVA 150
    EKYYGNKCII PWYIMTSGRT MESTKEFFTK HKYFGLKKEN VIFFQQGMLP 200
    AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME QRGIWSIHVY 250
    CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ 300
    VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ 350
    HHVAQKKIPY VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE 400
    DEFSPLKNAD SQNGKDNPTT ARHALMSLHH CWVLNAGGHF IDENGSRLPA 450
    IPRSATNGKS ETITADVNHN LKDANDVPIQ CEISPLISYA GEGLESYVAD 500
    KEFHAPLIID ENGVHELVKN GI 522
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1240.1. [Q16222-2 ]
    RefSeqi NP_003106.3. NM_003115.4. [Q16222-2 ]
    XP_005245519.1. XM_005245462.1. [Q16222-1 ]
    XP_005245522.1. XM_005245465.2. [Q16222-3 ]
    UniGenei Hs.492859.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    DisProti DP00363.
    ProteinModelPortali Q16222.
    SMRi Q16222. Positions 1-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112557. 10 interactions.
    STRINGi 9606.ENSP00000356903.

    PTM databases

    PhosphoSitei Q16222.

    Polymorphism databases

    DMDMi 68846235.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00217816.

    Proteomic databases

    MaxQBi Q16222.
    PaxDbi Q16222.
    PRIDEi Q16222.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000271469 ; ENSP00000271469 ; ENSG00000117143 . [Q16222-1 ]
    ENST00000367924 ; ENSP00000356901 ; ENSG00000117143 . [Q16222-3 ]
    ENST00000367925 ; ENSP00000356902 ; ENSG00000117143 . [Q16222-1 ]
    ENST00000367926 ; ENSP00000356903 ; ENSG00000117143 . [Q16222-2 ]
    GeneIDi 6675.
    KEGGi hsa:6675.
    UCSCi uc001gce.4. human. [Q16222-2 ]

    Organism-specific databases

    CTDi 6675.
    GeneCardsi GC01P162531.
    H-InvDB HIX0001264.
    HGNCi HGNC:12457. UAP1.
    HPAi HPA014659.
    MIMi 602862. gene.
    neXtProti NX_Q16222.
    PharmGKBi PA37107.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4284.
    HOGENOMi HOG000186273.
    HOVERGENi HBG018024.
    InParanoidi Q16222.
    KOi K00972.
    OMAi VFFQQGM.
    PhylomeDBi Q16222.
    TreeFami TF300611.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00533 .
    Reactomei REACT_22394. Synthesis of UDP-N-acetyl-glucosamine.
    SABIO-RK Q16222.

    Miscellaneous databases

    EvolutionaryTracei Q16222.
    GeneWikii UAP1.
    GenomeRNAii 6675.
    NextBioi 26027.
    PROi Q16222.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16222.
    Bgeei Q16222.
    CleanExi HS_UAP1.
    Genevestigatori Q16222.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR029044. Nucleotide-diphossugar_trans.
    IPR002618. UDPGP_trans_fam.
    [Graphical view ]
    PANTHERi PTHR11952. PTHR11952. 1 hit.
    Pfami PF01704. UDPGP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 145 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