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Q9H6U8

- ALG9_HUMAN

UniProt

Q9H6U8 - ALG9_HUMAN

Protein

Alpha-1,2-mannosyltransferase ALG9

Gene

ALG9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (30 Aug 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.2 Publications

    Catalytic activityi

    Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.
    Dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei340 – 3401Breakpoint for translocation

    GO - Molecular functioni

    1. dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC
    2. dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB-EC

    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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT22. Glycosyltransferase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-1,2-mannosyltransferase ALG9 (EC:2.4.1.259, EC:2.4.1.261)
    Alternative name(s):
    Asparagine-linked glycosylation protein 9 homolog
    Disrupted in bipolar disorder protein 1
    Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
    Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase
    Gene namesi
    Name:ALG9
    Synonyms:DIBD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:15672. ALG9.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving ALG9 is found in a family with bipolar affective disorder. Translocation t(9;11)(p24;q23). However, common variations in ALG9 do not play a major role in predisposition to bipolar affective disorder.
    Congenital disorder of glycosylation 1L (CDG1L) [MIM:608776]: 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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti287 – 2871Y → C in CDG1L; impairs activity. 1 Publication
    VAR_023410
    Natural varianti523 – 5231E → K in CDG1L; impairs activity. 1 Publication
    VAR_023413

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation

    Organism-specific databases

    MIMi608776. phenotype.
    Orphaneti79328. ALG9-CDG.
    PharmGKBiPA134887582.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 611611Alpha-1,2-mannosyltransferase ALG9PRO_0000215787Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi593 – 5931N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9H6U8.
    PaxDbiQ9H6U8.
    PRIDEiQ9H6U8.

    PTM databases

    PhosphoSiteiQ9H6U8.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed; with highest levels in heart, liver and pancreas.1 Publication

    Gene expression databases

    BgeeiQ9H6U8.
    CleanExiHS_ALG9.
    GenevestigatoriQ9H6U8.

    Organism-specific databases

    HPAiHPA038575.

    Interactioni

    Protein-protein interaction databases

    BioGridi122893. 2 interactions.
    IntActiQ9H6U8. 2 interactions.
    MINTiMINT-3068633.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H6U8.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 135135LumenalSequence AnalysisAdd
    BLAST
    Topological domaini157 – 17115CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini193 – 21321LumenalSequence AnalysisAdd
    BLAST
    Topological domaini235 – 24915CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini271 – 30434LumenalSequence AnalysisAdd
    BLAST
    Topological domaini326 – 34217CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini364 – 3707LumenalSequence Analysis
    Topological domaini392 – 40514CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini427 – 611185LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei136 – 15621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei172 – 19221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei214 – 23421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei250 – 27021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei305 – 32521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei343 – 36321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei371 – 39121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei406 – 42621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 22 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0072.
    HOVERGENiHBG062906.
    InParanoidiQ9H6U8.
    KOiK03846.
    OMAiWFHASVE.
    PhylomeDBiQ9H6U8.

    Family and domain databases

    InterProiIPR005599. GPI_mannosylTrfase.
    [Graphical view]
    PANTHERiPTHR22760. PTHR22760. 1 hit.
    PfamiPF03901. Glyco_transf_22. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H6U8-1) [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

    MASRGARQRL KGSGASSGDT APAADKLREL LGSREAGGAE HRTELSGNKA    50
    GQVWAPEGST AFKCLLSARL CAALLSNISD CDETFNYWEP THYLIYGEGF 100
    QTWEYSPAYA IRSYAYLLLH AWPAAFHARI LQTNKILVFY FLRCLLAFVS 150
    CICELYFYKA VCKKFGLHVS RMMLAFLVLS TGMFCSSSAF LPSSFCMYTT 200
    LIAMTGWYMD KTSIAVLGVA AGAILGWPFS AALGLPIAFD LLVMKHRWKS 250
    FFHWSLMALI LFLVPVVVID SYYYGKLVIA PLNIVLYNVF TPHGPDLYGT 300
    EPWYFYLING FLNFNVAFAL ALLVLPLTSL MEYLLQRFHV QNLGHPYWLT 350
    LAPMYIWFII FFIQPHKEER FLFPVYPLIC LCGAVALSAL QKCYHFVFQR 400
    YRLEHYTVTS NWLALGTVFL FGLLSFSRSV ALFRGYHGPL DLYPEFYRIA 450
    TDPTIHTVPE GRPVNVCVGK EWYRFPSSFL LPDNWQLQFI PSEFRGQLPK 500
    PFAEGPLATR IVPTDMNDQN LEEPSRYIDI SKCHYLVDLD TMRETPREPK 550
    YSSNKEEWIS LAYRPFLDAS RSSKLLRAFY VPFLSDQYTV YVNYTILKPR 600
    KAKQIRKKSG G 611
    Length:611
    Mass (Da):69,863
    Last modified:August 30, 2005 - v2
    Checksum:i51EC72DDBD866713
    GO
    Isoform 2 (identifier: Q9H6U8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-171: Missing.

    Show »
    Length:440
    Mass (Da):50,820
    Checksum:i42D3547330EA5EBB
    GO
    Isoform 3 (identifier: Q9H6U8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         391-391: Q → QHSFLYFQ

    Show »
    Length:618
    Mass (Da):70,786
    Checksum:i05790C3513BF8A4D
    GO
    Isoform 4 (identifier: Q9H6U8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-171: Missing.
         391-391: Q → QHSFLYFQ

    Note: No experimental confirmation available.

    Show »
    Length:447
    Mass (Da):51,743
    Checksum:i21DA4AC7B2DE59DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3091N → K(PubMed:12030331)Curated
    Sequence conflicti309 – 3091N → K1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti232 – 2321A → P.
    Corresponds to variant rs36111204 [ dbSNP | Ensembl ].
    VAR_049221
    Natural varianti255 – 2551S → L.
    Corresponds to variant rs17113312 [ dbSNP | Ensembl ].
    VAR_049222
    Natural varianti287 – 2871Y → C in CDG1L; impairs activity. 1 Publication
    VAR_023410
    Natural varianti289 – 2891V → I.3 Publications
    Corresponds to variant rs10502151 [ dbSNP | Ensembl ].
    VAR_023411
    Natural varianti506 – 5061P → L.1 Publication
    VAR_023412
    Natural varianti523 – 5231E → K in CDG1L; impairs activity. 1 Publication
    VAR_023413
    Natural varianti528 – 5281I → S.
    Corresponds to variant rs12575909 [ dbSNP | Ensembl ].
    VAR_049223

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 171171Missing in isoform 2 and isoform 4. 2 PublicationsVSP_015434Add
    BLAST
    Alternative sequencei391 – 3911Q → QHSFLYFQ in isoform 3 and isoform 4. 2 PublicationsVSP_015435

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF395532 mRNA. Translation: AAL25798.1.
    AF454937 mRNA. Translation: AAP97696.1.
    AL136927 mRNA. Translation: CAB66861.1.
    AK025498 mRNA. Translation: BAB15154.1.
    AK172828 mRNA. Translation: BAD18793.1.
    BC009255 mRNA. Translation: AAH09255.1.
    CCDSiCCDS41714.1. [Q9H6U8-4]
    CCDS53709.1. [Q9H6U8-2]
    RefSeqiNP_001071158.1. NM_001077690.1. [Q9H6U8-1]
    NP_001071159.1. NM_001077691.1. [Q9H6U8-4]
    NP_001071160.1. NM_001077692.1. [Q9H6U8-2]
    NP_079016.2. NM_024740.2. [Q9H6U8-3]
    UniGeneiHs.745155.

    Genome annotation databases

    EnsembliENST00000398006; ENSP00000381090; ENSG00000086848. [Q9H6U8-2]
    ENST00000531154; ENSP00000435517; ENSG00000086848. [Q9H6U8-4]
    GeneIDi79796.
    KEGGihsa:79796.
    UCSCiuc001ply.3. human. [Q9H6U8-1]
    uc001plz.3. human. [Q9H6U8-4]
    uc021qqm.1. human. [Q9H6U8-3]

    Polymorphism databases

    DMDMi73921666.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF395532 mRNA. Translation: AAL25798.1 .
    AF454937 mRNA. Translation: AAP97696.1 .
    AL136927 mRNA. Translation: CAB66861.1 .
    AK025498 mRNA. Translation: BAB15154.1 .
    AK172828 mRNA. Translation: BAD18793.1 .
    BC009255 mRNA. Translation: AAH09255.1 .
    CCDSi CCDS41714.1. [Q9H6U8-4 ]
    CCDS53709.1. [Q9H6U8-2 ]
    RefSeqi NP_001071158.1. NM_001077690.1. [Q9H6U8-1 ]
    NP_001071159.1. NM_001077691.1. [Q9H6U8-4 ]
    NP_001071160.1. NM_001077692.1. [Q9H6U8-2 ]
    NP_079016.2. NM_024740.2. [Q9H6U8-3 ]
    UniGenei Hs.745155.

    3D structure databases

    ProteinModelPortali Q9H6U8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122893. 2 interactions.
    IntActi Q9H6U8. 2 interactions.
    MINTi MINT-3068633.

    Protein family/group databases

    CAZyi GT22. Glycosyltransferase Family 22.

    PTM databases

    PhosphoSitei Q9H6U8.

    Polymorphism databases

    DMDMi 73921666.

    Proteomic databases

    MaxQBi Q9H6U8.
    PaxDbi Q9H6U8.
    PRIDEi Q9H6U8.

    Protocols and materials databases

    DNASUi 79796.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398006 ; ENSP00000381090 ; ENSG00000086848 . [Q9H6U8-2 ]
    ENST00000531154 ; ENSP00000435517 ; ENSG00000086848 . [Q9H6U8-4 ]
    GeneIDi 79796.
    KEGGi hsa:79796.
    UCSCi uc001ply.3. human. [Q9H6U8-1 ]
    uc001plz.3. human. [Q9H6U8-4 ]
    uc021qqm.1. human. [Q9H6U8-3 ]

    Organism-specific databases

    CTDi 79796.
    GeneCardsi GC11M111652.
    GeneReviewsi ALG9.
    HGNCi HGNC:15672. ALG9.
    HPAi HPA038575.
    MIMi 606941. gene.
    608776. phenotype.
    neXtProti NX_Q9H6U8.
    Orphaneti 79328. ALG9-CDG.
    PharmGKBi PA134887582.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0072.
    HOVERGENi HBG062906.
    InParanoidi Q9H6U8.
    KOi K03846.
    OMAi WFHASVE.
    PhylomeDBi Q9H6U8.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

    Miscellaneous databases

    GeneWikii ALG9.
    GenomeRNAii 79796.
    NextBioi 69332.
    PROi Q9H6U8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H6U8.
    CleanExi HS_ALG9.
    Genevestigatori Q9H6U8.

    Family and domain databases

    InterProi IPR005599. GPI_mannosylTrfase.
    [Graphical view ]
    PANTHERi PTHR22760. PTHR22760. 1 hit.
    Pfami PF03901. Glyco_transf_22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A mannosyltransferase gene at 11q23 is disrupted by a translocation breakpoint that co-segregates with bipolar affective disorder in a small family."
      Baysal B.E., Willett-Brozick J.E., Badner J.A., Corona W., Ferrell R.E., Nimgaonkar V.L., Detera-Wadleigh S.D.
      Neurogenetics 4:43-53(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION, TISSUE SPECIFICITY, VARIANTS ILE-289 AND LEU-506.
    2. Guo J.H., Yu L.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lymphoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Uterus.
    4. "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 3 AND 4), VARIANT ILE-289.
    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 3).
      Tissue: Muscle.
    6. "Identification and functional analysis of a defect in the human ALG9 gene: definition of congenital disorder of glycosylation type IL."
      Frank C.G., Grubenmann C.E., Eyaid W., Berger E.G., Aebi M., Hennet T.
      Am. J. Hum. Genet. 75:146-150(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, VARIANT CDG1L LYS-523, VARIANT ILE-289.
    7. Cited for: FUNCTION, VARIANT CDG1L CYS-287.
    8. "Common variations in ALG9 are not associated with bipolar I disorder: a family-based study."
      Baysal B.E., Willett-Brozick J.E., Bacanu S.A., Detera-Wadleigh S., Nimgaonkar V.L.
      Behav. Brain Funct. 2:25-25(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF ASSOCIATION WITH BIPOLAR AFFECTIVE DISORDERS.

    Entry informationi

    Entry nameiALG9_HUMAN
    AccessioniPrimary (citable) accession number: Q9H6U8
    Secondary accession number(s): Q6ZMD5
    , Q7Z4R4, Q96GS7, Q96PB9, Q9H068
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 108 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3