SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q16222

- UAP1_HUMAN

UniProt

Q16222 - UAP1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
UDP-N-acetylhexosamine pyrophosphorylase
Gene
UAP1, SPAG2
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 2231Substrate
Binding sitei407 – 4071Substrate

GO - Molecular functioni

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

GO - Biological processi

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

Protein-protein interaction databases

BioGridi112557. 10 interactions.
STRINGi9606.ENSP00000356903.

Structurei

Secondary structure

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.

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.

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

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.
VSP_004483Add
BLAST
Alternative sequencei454 – 4541Missing in isoform 3.
VSP_014523

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611H → Y in AAH09377. 1 Publication
Sequence conflicti445 – 4451G → S1 Publication
Sequence conflicti445 – 4451G → S1 Publication
Sequence conflicti454 – 4541S → Q1 Publication
Sequence conflicti454 – 4541S → Q1 Publication

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

« 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. "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: September 3, 2014
This is version 144 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