Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q9NP73

- ALG13_HUMAN

UniProt

Q9NP73 - ALG13_HUMAN

Protein

Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13

Gene

ALG13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Isoform 1: Possible multifunctional enzyme with both glycosyltransferase and deubiquitinase activities.
    Isoform 2: May be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway.

    Catalytic activityi

    UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol.
    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei239 – 2391For deubiquitinase activityBy similarity
    Active sitei242 – 2421Nucleophile; for deubiquitinase activityBy similarity
    Active sitei345 – 3451For deubiquitinase activityBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. cysteine-type peptidase activity Source: UniProtKB-KW
    3. N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
    4. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    3. lipid glycosylation Source: InterPro
    4. post-translational protein modification Source: Reactome
    5. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Hydrolase, Protease, Thiol protease, Transferase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.
    MEROPSiC85.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 (EC:2.4.1.141, EC:3.4.19.12)
    Alternative name(s):
    Asparagine-linked glycosylation 13 homolog
    Glycosyltransferase 28 domain-containing protein 1
    UDP-N-acetylglucosamine transferase subunit ALG13 homolog
    Gene namesi
    Name:ALG13
    Synonyms:CXorf45, GLT28D1
    ORF Names:MDS031
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:30881. ALG13.

    Subcellular locationi

    Isoform 2 : Endoplasmic reticulum Curated
    Note: Could be recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1S (CDG1S) [MIM:300884]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. 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 varianti94 – 941K → E in CDG1S; there is a decrease enzyme activity at about 17% of wild-type. 1 Publication
    VAR_069218

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation

    Organism-specific databases

    MIMi300884. phenotype.
    Orphaneti324422. ALG13-CDG.
    777. X-linked non-syndromic intellectual disability.
    PharmGKBiPA162376235.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11371137Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13PRO_0000254573Add
    BLAST

    Proteomic databases

    MaxQBiQ9NP73.
    PaxDbiQ9NP73.
    PeptideAtlasiQ9NP73.
    PRIDEiQ9NP73.

    PTM databases

    PhosphoSiteiQ9NP73.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NP73.
    BgeeiQ9NP73.
    CleanExiHS_ALG13.
    GenevestigatoriQ9NP73.

    Organism-specific databases

    HPAiHPA002853.

    Interactioni

    Subunit structurei

    Isoform 2 may interact with ALG14.By similarity

    Protein-protein interaction databases

    BioGridi122956. 6 interactions.
    IntActiQ9NP73. 5 interactions.
    MINTiMINT-2876406.
    STRINGi9606.ENSP00000361047.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NP73.
    SMRiQ9NP73. Positions 2-125, 230-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini231 – 352122OTUPROSITE-ProRule annotationAdd
    BLAST
    Domaini492 – 55261TudorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 125125Glycosyltransferase activityAdd
    BLAST
    Regioni126 – 400275Deubiquitinase activityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi887 – 97084Pro-richAdd
    BLAST

    Domaini

    Contains 1 OTU domain with intact active sites. No deubiquitinase activity has been detected when tested (PubMed:23827681).1 Publication

    Sequence similaritiesi

    Belongs to the glycosyltransferase 28 family.Curated
    Contains 1 OTU domain.PROSITE-ProRule annotation
    Contains 1 Tudor domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5017.
    HOVERGENiHBG081391.
    KOiK07432.
    OMAiVPFPQFD.
    OrthoDBiEOG7RFTGJ.
    PhylomeDBiQ9NP73.
    TreeFamiTF332789.

    Family and domain databases

    InterProiIPR007235. Glyco_trans_28_C.
    IPR003323. OTU.
    IPR002999. Tudor.
    [Graphical view]
    PfamiPF04101. Glyco_tran_28_C. 1 hit.
    PF02338. OTU. 1 hit.
    [Graphical view]
    PROSITEiPS50802. OTU. 1 hit.
    PS50304. TUDOR. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NP73-1) [UniParc]FASTAAdd to Basket

    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

    MKCVFVTVGT TSFDDLIACV SAPDSLQKIE SLGYNRLILQ IGRGTVVPEP     50
    FSTESFTLDV YRYKDSLKED IQKADLVISH AGAGSCLETL EKGKPLVVVI 100
    NEKLMNNHQL ELAKQLHKEG HLFYCTCRVL TCPGQAKSIA SAPGKCQDSA 150
    ALTSTAFSGL DFGLLSGYLH KQALVTATHP TCTLLFPSCH AFFPLPLTPT 200
    LYKMHKGWKN YCSQKSLNEA SMDEYLGSLG LFRKLTAKDA SCLFRAISEQ 250
    LFCSQVHHLE IRKACVSYMR ENQQTFESYV EGSFEKYLER LGDPKESAGQ 300
    LEIRALSLIY NRDFILYRFP GKPPTYVTDN GYEDKILLCY SSSGHYDSVY 350
    SKQFQSSAAV CQAVLYEILY KDVFVVDEEE LKTAIKLFRS GSKKNRNNAV 400
    TGSEDAHTDY KSSNQNRMEE WGACYNAENI PEGYNKGTEE TKSPENPSKM 450
    PFPYKVLKAL DPEIYRNVEF DVWLDSRKEL QKSDYMEYAG RQYYLGDKCQ 500
    VCLESEGRYY NAHIQEVGNE NNSVTVFIEE LAEKHVVPLA NLKPVTQVMS 550
    VPAWNAMPSR KGRGYQKMPG GYVPEIVISE MDIKQQKKMF KKIRGKEVYM 600
    TMAYGKGDPL LPPRLQHSMH YGHDPPMHYS QTAGNVMSNE HFHPQHPSPR 650
    QGRGYGMPRN SSRFINRHNM PGPKVDFYPG PGKRCCQSYD NFSYRSRSFR 700
    RSHRQMSCVN KESQYGFTPG NGQMPRGLEE TITFYEVEEG DETAYPTLPN 750
    HGGPSTMVPA TSGYCVGRRG HSSGKQTLNL EEGNGQSENG RYHEEYLYRA 800
    EPDYETSGVY STTASTANLS LQDRKSCSMS PQDTVTSYNY PQKMMGNIAA 850
    VAASCANNVP APVLSNGAAA NQAISTTSVS SQNAIQPLFV SPPTHGRPVI 900
    ASPSYPCHSA IPHAGASLPP PPPPPPPPPP PPPPPPPPPP PPPPPALDVG 950
    ETSNLQPPPP LPPPPYSCDP SGSDLPQDTK VLQYYFNLGL QCYYHSYWHS 1000
    MVYVPQMQQQ LHVENYPVYT EPPLVDQTVP QCYSEVRRED GIQAEASAND 1050
    TFPNADSSSV PHGAVYYPVM SDPYGQPPLP GFDSCLPVVP DYSCVPPWHP 1100
    VGTAYGGSSQ IHGAINPGPI GCIAPSPPAS HYVPQGM 1137
    Length:1,137
    Mass (Da):126,056
    Last modified:June 15, 2010 - v2
    Checksum:i4E56437BA2609589
    GO
    Isoform 2 (identifier: Q9NP73-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-165: RVLTCPGQAK...AFSGLDFGLL → STLPGLLQSM...FLDKVVGLQK
         166-1137: Missing.

    Show »
    Length:165
    Mass (Da):18,225
    Checksum:iCEE3C8E7EFFE4E31
    GO
    Isoform 3 (identifier: Q9NP73-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-78: Missing.
         79-81: SHA → MFT

    Note: No experimental confirmation available.

    Show »
    Length:1,059
    Mass (Da):117,468
    Checksum:i2309259465BED07E
    GO
    Isoform 4 (identifier: Q9NP73-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-104: Missing.
         899-977: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:954
    Mass (Da):106,858
    Checksum:i5E581DED7B50EB86
    GO

    Sequence cautioni

    The sequence AAI17378.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAI17380.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB15521.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD96874.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAH14244.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAH14244.1 differs from that shown. Reason: Erroneous termination at position 424. Translated as Cys.
    The sequence CAI43016.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAM28219.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti493 – 4931Y → N in BAH14677. 1 PublicationCurated
    Sequence conflicti564 – 5641G → D in BAH13276. 1 PublicationCurated
    Sequence conflicti588 – 5881K → R in BAH14677. 1 PublicationCurated
    Sequence conflicti624 – 6241D → G in BAH13276. 1 PublicationCurated
    Sequence conflicti658 – 6581P → L in BAH13790. 1 PublicationCurated
    Sequence conflicti746 – 7483PTL → ATF in BAB15521. 1 PublicationCurated
    Sequence conflicti752 – 7521G → E in BAB15521. 1 PublicationCurated
    Sequence conflicti866 – 8661N → K in BAH14677. 1 PublicationCurated
    Sequence conflicti926 – 9261P → L in BAH14244. 1 PublicationCurated
    Sequence conflicti954 – 9541N → S in BAH14244. 1 PublicationCurated
    Sequence conflicti1018 – 10181V → A in BAH14244. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941K → E in CDG1S; there is a decrease enzyme activity at about 17% of wild-type. 1 Publication
    VAR_069218
    Natural varianti107 – 1071N → S.1 Publication
    VAR_069412

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 104104Missing in isoform 4. 3 PublicationsVSP_039298Add
    BLAST
    Alternative sequencei1 – 7878Missing in isoform 3. 1 PublicationVSP_039299Add
    BLAST
    Alternative sequencei79 – 813SHA → MFT in isoform 3. 1 PublicationVSP_039300
    Alternative sequencei128 – 16538RVLTC…DFGLL → STLPGLLQSMDLSTLKCYPP GQPEKFSAFLDKVVGLQK in isoform 2. 3 PublicationsVSP_039301Add
    BLAST
    Alternative sequencei166 – 1137972Missing in isoform 2. 3 PublicationsVSP_039302Add
    BLAST
    Alternative sequencei899 – 97779Missing in isoform 4. 3 PublicationsVSP_039303Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF220051 mRNA. Translation: AAF67644.1.
    AK026671 mRNA. Translation: BAB15521.1. Different initiation.
    AK300394 mRNA. Translation: BAH13276.1.
    AK302729 mRNA. Translation: BAH13790.1.
    AK302890 mRNA. Translation: BAH13833.1.
    AK304712 mRNA. Translation: BAH14244.1. Sequence problems.
    AK316306 mRNA. Translation: BAH14677.1.
    AK316522 mRNA. Translation: BAH14893.1.
    AK312229 mRNA. Translation: BAG35162.1.
    AL096764 Genomic DNA. Translation: CAB89277.1.
    AL049563 Genomic DNA. Translation: CAI43016.2. Sequence problems.
    AL096764, AL049563 Genomic DNA. Translation: CAM28218.1.
    AL096764, AL049563 Genomic DNA. Translation: CAM28219.1. Sequence problems.
    AL049563, AL096764 Genomic DNA. Translation: CAM28289.1.
    CH471120 Genomic DNA. Translation: EAX02635.1.
    BC005336 mRNA. Translation: AAH05336.1.
    BC117377 mRNA. Translation: AAI17378.1. Different initiation.
    BC117379 mRNA. Translation: AAI17380.1. Different initiation.
    AK223154 mRNA. Translation: BAD96874.1. Different initiation.
    CCDSiCCDS14559.1. [Q9NP73-2]
    CCDS55477.1. [Q9NP73-1]
    CCDS59173.1. [Q9NP73-4]
    RefSeqiNP_001034299.3. NM_001039210.3.
    NP_001093392.1. NM_001099922.2. [Q9NP73-1]
    NP_001161857.1. NM_001168385.1.
    NP_001244159.1. NM_001257230.1. [Q9NP73-4]
    NP_001244160.1. NM_001257231.1. [Q9NP73-3]
    NP_001244163.1. NM_001257234.1. [Q9NP73-4]
    NP_001244166.1. NM_001257237.1. [Q9NP73-4]
    NP_001244170.1. NM_001257241.1.
    NP_060936.1. NM_018466.4. [Q9NP73-2]
    UniGeneiHs.443061.

    Genome annotation databases

    EnsembliENST00000251943; ENSP00000251943; ENSG00000101901. [Q9NP73-4]
    ENST00000371979; ENSP00000361047; ENSG00000101901. [Q9NP73-2]
    ENST00000394780; ENSP00000378260; ENSG00000101901. [Q9NP73-1]
    GeneIDi79868.
    KEGGihsa:79868.
    UCSCiuc004epi.2. human. [Q9NP73-2]
    uc011msx.2. human. [Q9NP73-4]
    uc011msy.2. human. [Q9NP73-1]
    uc011msz.2. human. [Q9NP73-3]

    Polymorphism databases

    DMDMi298286785.

    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
    AF220051 mRNA. Translation: AAF67644.1 .
    AK026671 mRNA. Translation: BAB15521.1 . Different initiation.
    AK300394 mRNA. Translation: BAH13276.1 .
    AK302729 mRNA. Translation: BAH13790.1 .
    AK302890 mRNA. Translation: BAH13833.1 .
    AK304712 mRNA. Translation: BAH14244.1 . Sequence problems.
    AK316306 mRNA. Translation: BAH14677.1 .
    AK316522 mRNA. Translation: BAH14893.1 .
    AK312229 mRNA. Translation: BAG35162.1 .
    AL096764 Genomic DNA. Translation: CAB89277.1 .
    AL049563 Genomic DNA. Translation: CAI43016.2 . Sequence problems.
    AL096764 , AL049563 Genomic DNA. Translation: CAM28218.1 .
    AL096764 , AL049563 Genomic DNA. Translation: CAM28219.1 . Sequence problems.
    AL049563 , AL096764 Genomic DNA. Translation: CAM28289.1 .
    CH471120 Genomic DNA. Translation: EAX02635.1 .
    BC005336 mRNA. Translation: AAH05336.1 .
    BC117377 mRNA. Translation: AAI17378.1 . Different initiation.
    BC117379 mRNA. Translation: AAI17380.1 . Different initiation.
    AK223154 mRNA. Translation: BAD96874.1 . Different initiation.
    CCDSi CCDS14559.1. [Q9NP73-2 ]
    CCDS55477.1. [Q9NP73-1 ]
    CCDS59173.1. [Q9NP73-4 ]
    RefSeqi NP_001034299.3. NM_001039210.3.
    NP_001093392.1. NM_001099922.2. [Q9NP73-1 ]
    NP_001161857.1. NM_001168385.1.
    NP_001244159.1. NM_001257230.1. [Q9NP73-4 ]
    NP_001244160.1. NM_001257231.1. [Q9NP73-3 ]
    NP_001244163.1. NM_001257234.1. [Q9NP73-4 ]
    NP_001244166.1. NM_001257237.1. [Q9NP73-4 ]
    NP_001244170.1. NM_001257241.1.
    NP_060936.1. NM_018466.4. [Q9NP73-2 ]
    UniGenei Hs.443061.

    3D structure databases

    ProteinModelPortali Q9NP73.
    SMRi Q9NP73. Positions 2-125, 230-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122956. 6 interactions.
    IntActi Q9NP73. 5 interactions.
    MINTi MINT-2876406.
    STRINGi 9606.ENSP00000361047.

    Protein family/group databases

    CAZyi GT1. Glycosyltransferase Family 1.
    MEROPSi C85.005.

    PTM databases

    PhosphoSitei Q9NP73.

    Polymorphism databases

    DMDMi 298286785.

    Proteomic databases

    MaxQBi Q9NP73.
    PaxDbi Q9NP73.
    PeptideAtlasi Q9NP73.
    PRIDEi Q9NP73.

    Protocols and materials databases

    DNASUi 79868.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251943 ; ENSP00000251943 ; ENSG00000101901 . [Q9NP73-4 ]
    ENST00000371979 ; ENSP00000361047 ; ENSG00000101901 . [Q9NP73-2 ]
    ENST00000394780 ; ENSP00000378260 ; ENSG00000101901 . [Q9NP73-1 ]
    GeneIDi 79868.
    KEGGi hsa:79868.
    UCSCi uc004epi.2. human. [Q9NP73-2 ]
    uc011msx.2. human. [Q9NP73-4 ]
    uc011msy.2. human. [Q9NP73-1 ]
    uc011msz.2. human. [Q9NP73-3 ]

    Organism-specific databases

    CTDi 79868.
    GeneCardsi GC0XP110909.
    GeneReviewsi ALG13.
    HGNCi HGNC:30881. ALG13.
    HPAi HPA002853.
    MIMi 300776. gene.
    300884. phenotype.
    neXtProti NX_Q9NP73.
    Orphaneti 324422. ALG13-CDG.
    777. X-linked non-syndromic intellectual disability.
    PharmGKBi PA162376235.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5017.
    HOVERGENi HBG081391.
    KOi K07432.
    OMAi VPFPQFD.
    OrthoDBi EOG7RFTGJ.
    PhylomeDBi Q9NP73.
    TreeFami TF332789.

    Enzyme and pathway databases

    Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

    Miscellaneous databases

    GeneWikii ALG13.
    GenomeRNAii 79868.
    NextBioi 69622.
    PROi Q9NP73.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NP73.
    Bgeei Q9NP73.
    CleanExi HS_ALG13.
    Genevestigatori Q9NP73.

    Family and domain databases

    InterProi IPR007235. Glyco_trans_28_C.
    IPR003323. OTU.
    IPR002999. Tudor.
    [Graphical view ]
    Pfami PF04101. Glyco_tran_28_C. 1 hit.
    PF02338. OTU. 1 hit.
    [Graphical view ]
    PROSITEi PS50802. OTU. 1 hit.
    PS50304. TUDOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
      Zhao M., Gu J., Li N., Peng Y., Han Z., Chen Z.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Hematopoietic stem cell.
    2. "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 1; 2; 3 AND 4).
      Tissue: Lung, Placenta, Testis, Trachea and Uterus.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 592-1137 (ISOFORM 4).
      Tissue: Colon and Urinary bladder.
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 591-1137 (ISOFORM 4).
      Tissue: Lung.
    7. "Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation."
      Gao X.-D., Tachikawa H., Sato T., Jigami Y., Dean N.
      J. Biol. Chem. 280:36254-36262(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 2).
    8. "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
      Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
      Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: VARIANT CDG1S GLU-94.
    11. Cited for: VARIANT SER-107.

    Entry informationi

    Entry nameiALG13_HUMAN
    AccessioniPrimary (citable) accession number: Q9NP73
    Secondary accession number(s): B1AKD6
    , B1AKM1, B2R5L5, B7Z6J0, B7Z804, B7Z847, B7Z9A8, B7ZAJ1, B7ZB57, Q17RC3, Q5JXY9, Q9H5U8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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, Multifunctional enzyme, 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