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P78381

- S35A2_HUMAN

UniProt

P78381 - S35A2_HUMAN

Protein

UDP-galactose translocator

Gene

SLC35A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Transports nucleotide sugars from the cytosol into Golgi vesicles where glycosyltransferases function.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. sugar:proton symporter activity Source: InterPro
    3. UDP-galactose transmembrane transporter activity Source: ProtInc

    GO - Biological processi

    1. galactose metabolic process Source: ProtInc
    2. transmembrane transport Source: Reactome
    3. UDP-galactose transport Source: ProtInc

    Keywords - Biological processi

    Sugar transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_22151. Transport of nucleotide sugars.

    Protein family/group databases

    TCDBi2.A.7.12.6. the drug/metabolite transporter (dmt) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-galactose translocator
    Alternative name(s):
    Solute carrier family 35 member A2
    UDP-galactose transporter
    Short name:
    UDP-Gal-Tr
    Short name:
    UGT
    Gene namesi
    Name:SLC35A2
    Synonyms:UGALT, UGT, UGTL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11022. SLC35A2.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: HPA
    2. Golgi membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 2M (CDG2M) [MIM:300896]: A disorder characterized by developmental delay, hypotonia, ocular anomalies, and brain malformations. Othere more variable clinical features included seizures, hypsarrhythmia, poor feeding, microcephaly, recurrent infections, dysmorphic features, shortened limbs, and coagulation defects. Congenital disorders of glycosylation are caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins and a wide variety of clinical features. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti331 – 3311V → I in CDG2M. 1 Publication
    VAR_069773

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation

    Organism-specific databases

    MIMi300896. phenotype.
    Orphaneti356961. SLC35A2-CDG.
    PharmGKBiPA35890.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 396396UDP-galactose translocatorPRO_0000213353Add
    BLAST

    Proteomic databases

    MaxQBiP78381.
    PaxDbiP78381.
    PRIDEiP78381.

    PTM databases

    PhosphoSiteiP78381.

    Expressioni

    Gene expression databases

    ArrayExpressiP78381.
    BgeeiP78381.
    CleanExiHS_SLC35A2.
    GenevestigatoriP78381.

    Organism-specific databases

    HPAiHPA036087.

    Interactioni

    Subunit structurei

    Interacts with SLC35A3.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SLC35A3Q9Y2D23EBI-8101118,EBI-3917581

    Protein-protein interaction databases

    BioGridi113202. 2 interactions.
    IntActiP78381. 3 interactions.
    STRINGi9606.ENSP00000247138.

    Structurei

    3D structure databases

    ProteinModelPortaliP78381.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3 – 2321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei37 – 5721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei65 – 8521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei97 – 11721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei140 – 16021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei169 – 18921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei200 – 22021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei238 – 25821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei269 – 28921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei315 – 33521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0697.
    HOGENOMiHOG000231358.
    HOVERGENiHBG071267.
    InParanoidiP78381.
    KOiK15272.
    OMAiCMRESGG.
    PhylomeDBiP78381.
    TreeFamiTF315345.

    Family and domain databases

    InterProiIPR007271. Nuc_sug_transpt.
    IPR021189. UDP/CMP-sugar_transptr.
    IPR004689. UDPgal_transpt.
    [Graphical view]
    PANTHERiPTHR10231. PTHR10231. 1 hit.
    PfamiPF04142. Nuc_sug_transp. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005799. UDP-gal_transpt. 1 hit.
    TIGRFAMsiTIGR00803. nst. 1 hit.

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78381-1) [UniParc]FASTAAdd to Basket

    Also known as: UGT2

    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

    MAAVGAGGST AAPGPGAVSA GALEPGTASA AHRRLKYISL AVLVVQNASL    50
    ILSIRYARTL PGDRFFATTA VVMAEVLKGL TCLLLLFAQK RGNVKHLVLF 100
    LHEAVLVQYV DTLKLAVPSL IYTLQNNLQY VAISNLPAAT FQVTYQLKIL 150
    TTALFSVLML NRSLSRLQWA SLLLLFTGVA IVQAQQAGGG GPRPLDQNPG 200
    AGLAAVVASC LSSGFAGVYF EKILKGSSGS VWLRNLQLGL FGTALGLVGL 250
    WWAEGTAVAT RGFFFGYTPA VWGVVLNQAF GGLLVAVVVK YADNILKGFA 300
    TSLSIVLSTV ASIRLFGFHV DPLFALGAGL VIGAVYLYSL PRGAAKAIAS 350
    ASASASGPCV HQQPPGQPPP PQLSSHRGDL ITEPFLPKLL TKVKGS 396
    Length:396
    Mass (Da):41,307
    Last modified:May 1, 1997 - v1
    Checksum:i6EC1DC9532FE9221
    GO
    Isoform 2 (identifier: P78381-2) [UniParc]FASTAAdd to Basket

    Also known as: UGT1

    The sequence of this isoform differs from the canonical sequence as follows:
         389-396: LLTKVKGS → SVLVK

    Show »
    Length:393
    Mass (Da):41,007
    Checksum:i34D31807D3805A7A
    GO
    Isoform 3 (identifier: P78381-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         143-396: VTYQLKILTT...PKLLTKVKGS → PSPRCSQSHS...FGRWSFLPGH

    Show »
    Length:242
    Mass (Da):25,184
    Checksum:i7AB122B6343CC9EC
    GO
    Isoform 4 (identifier: P78381-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         30-30: A → AELLLTWEEAEARGQGLPQPLPDTSVRIP
         389-396: LLTKVKGS → SVLVK

    Note: No experimental confirmation available.

    Show »
    Length:421
    Mass (Da):44,106
    Checksum:i11D42242F410B56C
    GO
    Isoform 5 (identifier: P78381-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-91: Missing.
         389-396: LLTKVKGS → SVLVK

    Note: No experimental confirmation available.

    Show »
    Length:332
    Mass (Da):34,194
    Checksum:i7FC8A3C442E4C31B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti85 – 851L → P in BAF82973. (PubMed:14702039)Curated
    Sequence conflicti110 – 1101V → A in BAG60694. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti252 – 2521W → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036579
    Natural varianti331 – 3311V → I in CDG2M. 1 Publication
    VAR_069773

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei30 – 301A → AELLLTWEEAEARGQGLPQP LPDTSVRIP in isoform 4. 1 PublicationVSP_054335
    Alternative sequencei31 – 9161Missing in isoform 5. 1 PublicationVSP_055197Add
    BLAST
    Alternative sequencei143 – 396254VTYQL…KVKGS → PSPRCSQSHSLCLCLRLRAL RSPAASRAATTTAAVFPPWR PHHGALSAKVSAGEVRAGSN GGTQGRGTGVEGVGHLQDPS RHPPGPGSSGFGRWSFLPGH in isoform 3. 2 PublicationsVSP_042029Add
    BLAST
    Alternative sequencei389 – 3968LLTKVKGS → SVLVK in isoform 2, isoform 4 and isoform 5. 2 PublicationsVSP_003728

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88146 mRNA. Translation: BAA13545.1.
    D84454 mRNA. Translation: BAA12673.1.
    AB042425 Genomic DNA. Translation: BAA95614.1.
    AB042425 Genomic DNA. Translation: BAA95615.1.
    AK290284 mRNA. Translation: BAF82973.1.
    AK292816 mRNA. Translation: BAF85505.1.
    AK293415 mRNA. Translation: BAG56922.1.
    AK298484 mRNA. Translation: BAG60694.1.
    AF207550 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50733.1.
    CH471224 Genomic DNA. Translation: EAW50734.1.
    BC035747 mRNA. Translation: AAH35747.1.
    CCDSiCCDS14311.1. [P78381-1]
    CCDS35247.1. [P78381-3]
    CCDS43937.1. [P78381-2]
    CCDS65253.1. [P78381-5]
    CCDS65254.1. [P78381-4]
    PIRiJC5022.
    RefSeqiNP_001027460.1. NM_001032289.2. [P78381-3]
    NP_001035963.1. NM_001042498.2. [P78381-2]
    NP_001269576.1. NM_001282647.1.
    NP_001269577.1. NM_001282648.1.
    NP_001269578.1. NM_001282649.1.
    NP_001269579.1. NM_001282650.1.
    NP_001269580.1. NM_001282651.1. [P78381-4]
    NP_005651.1. NM_005660.2. [P78381-1]
    UniGeneiHs.21899.

    Genome annotation databases

    EnsembliENST00000247138; ENSP00000247138; ENSG00000102100. [P78381-1]
    ENST00000376521; ENSP00000365704; ENSG00000102100. [P78381-2]
    ENST00000413561; ENSP00000393233; ENSG00000102100. [P78381-5]
    ENST00000445167; ENSP00000402726; ENSG00000102100. [P78381-3]
    ENST00000452555; ENSP00000416002; ENSG00000102100. [P78381-4]
    GeneIDi7355.
    KEGGihsa:7355.
    UCSCiuc004dlo.1. human. [P78381-1]
    uc004dlp.1. human. [P78381-2]
    uc004dlq.3. human. [P78381-3]

    Polymorphism databases

    DMDMi2499228.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88146 mRNA. Translation: BAA13545.1 .
    D84454 mRNA. Translation: BAA12673.1 .
    AB042425 Genomic DNA. Translation: BAA95614.1 .
    AB042425 Genomic DNA. Translation: BAA95615.1 .
    AK290284 mRNA. Translation: BAF82973.1 .
    AK292816 mRNA. Translation: BAF85505.1 .
    AK293415 mRNA. Translation: BAG56922.1 .
    AK298484 mRNA. Translation: BAG60694.1 .
    AF207550 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50733.1 .
    CH471224 Genomic DNA. Translation: EAW50734.1 .
    BC035747 mRNA. Translation: AAH35747.1 .
    CCDSi CCDS14311.1. [P78381-1 ]
    CCDS35247.1. [P78381-3 ]
    CCDS43937.1. [P78381-2 ]
    CCDS65253.1. [P78381-5 ]
    CCDS65254.1. [P78381-4 ]
    PIRi JC5022.
    RefSeqi NP_001027460.1. NM_001032289.2. [P78381-3 ]
    NP_001035963.1. NM_001042498.2. [P78381-2 ]
    NP_001269576.1. NM_001282647.1.
    NP_001269577.1. NM_001282648.1.
    NP_001269578.1. NM_001282649.1.
    NP_001269579.1. NM_001282650.1.
    NP_001269580.1. NM_001282651.1. [P78381-4 ]
    NP_005651.1. NM_005660.2. [P78381-1 ]
    UniGenei Hs.21899.

    3D structure databases

    ProteinModelPortali P78381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113202. 2 interactions.
    IntActi P78381. 3 interactions.
    STRINGi 9606.ENSP00000247138.

    Protein family/group databases

    TCDBi 2.A.7.12.6. the drug/metabolite transporter (dmt) superfamily.

    PTM databases

    PhosphoSitei P78381.

    Polymorphism databases

    DMDMi 2499228.

    Proteomic databases

    MaxQBi P78381.
    PaxDbi P78381.
    PRIDEi P78381.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000247138 ; ENSP00000247138 ; ENSG00000102100 . [P78381-1 ]
    ENST00000376521 ; ENSP00000365704 ; ENSG00000102100 . [P78381-2 ]
    ENST00000413561 ; ENSP00000393233 ; ENSG00000102100 . [P78381-5 ]
    ENST00000445167 ; ENSP00000402726 ; ENSG00000102100 . [P78381-3 ]
    ENST00000452555 ; ENSP00000416002 ; ENSG00000102100 . [P78381-4 ]
    GeneIDi 7355.
    KEGGi hsa:7355.
    UCSCi uc004dlo.1. human. [P78381-1 ]
    uc004dlp.1. human. [P78381-2 ]
    uc004dlq.3. human. [P78381-3 ]

    Organism-specific databases

    CTDi 7355.
    GeneCardsi GC0XM048760.
    HGNCi HGNC:11022. SLC35A2.
    HPAi HPA036087.
    MIMi 300896. phenotype.
    314375. gene.
    neXtProti NX_P78381.
    Orphaneti 356961. SLC35A2-CDG.
    PharmGKBi PA35890.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0697.
    HOGENOMi HOG000231358.
    HOVERGENi HBG071267.
    InParanoidi P78381.
    KOi K15272.
    OMAi CMRESGG.
    PhylomeDBi P78381.
    TreeFami TF315345.

    Enzyme and pathway databases

    Reactomei REACT_22151. Transport of nucleotide sugars.

    Miscellaneous databases

    ChiTaRSi SLC35A2. human.
    GeneWikii SLC35A2.
    GenomeRNAii 7355.
    NextBioi 28796.
    PROi P78381.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78381.
    Bgeei P78381.
    CleanExi HS_SLC35A2.
    Genevestigatori P78381.

    Family and domain databases

    InterProi IPR007271. Nuc_sug_transpt.
    IPR021189. UDP/CMP-sugar_transptr.
    IPR004689. UDPgal_transpt.
    [Graphical view ]
    PANTHERi PTHR10231. PTHR10231. 1 hit.
    Pfami PF04142. Nuc_sug_transp. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005799. UDP-gal_transpt. 1 hit.
    TIGRFAMsi TIGR00803. nst. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human UDP-galactose translocator: molecular cloning of a complementary DNA that complements the genetic defect of a mutant cell line deficient in UDP-galactose translocator."
      Miura N., Ishida N., Hoshino M., Yamauchi M., Hara T., Ayusawa D., Kawakita M.
      J. Biochem. 120:236-241(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning and characterization of a novel isoform of the human UDP-galactose transporter, and of related complementary DNAs belonging to the nucleotide-sugar transporter gene family."
      Ishida N., Miura N., Yoshioka S., Kawakita M.
      J. Biochem. 120:1074-1078(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fibroblast.
    3. "The UDP-galactose translocator gene is mapped to band Xp11.23-p11.22 containing the Wiskott-Aldrich syndrome locus."
      Hara T., Yamauchi M., Takahashi E., Hoshino M., Aoki K., Ayusawa D., Kawakita M.
      Somat. Cell Mol. Genet. 19:571-575(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Genomic organization of the human UDP-galactose transporter gene."
      Ishida N., Miura N., Yamauchi M., Kawakita M.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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] (ISOFORMS 2; 3; 4 AND 5).
      Tissue: Colon, Lymphoblast and Trachea.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 3).
      Tissue: Pancreas.
    9. "UDP-N-acetylglucosamine transporter and UDP-galactose transporter form heterologous complexes in the Golgi membrane."
      Maszczak-Seneczko D., Sosicka P., Majkowski M., Olczak T., Olczak M.
      FEBS Lett. 586:4082-4087(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC35A3.
    10. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-252.
    11. Cited for: VARIANT CDG2M ILE-331.

    Entry informationi

    Entry nameiS35A2_HUMAN
    AccessioniPrimary (citable) accession number: P78381
    Secondary accession number(s): A8K2L9
    , A8K9V1, B4DE11, B4DPT2, E7EW45, Q8IV21, Q92553
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3