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Q9BV10

- ALG12_HUMAN

UniProt

Q9BV10 - ALG12_HUMAN

Protein

Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase

Gene

ALG12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man7GlcNAc2) required for protein glycosylation.

    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->2)-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-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate.

    Pathwayi

    GO - Molecular functioni

    1. alpha-1,6-mannosyltransferase activity Source: UniProtKB
    2. dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. dolichol-linked oligosaccharide biosynthetic process Source: MGI
    3. mannosylation Source: GOC
    4. post-translational protein modification Source: Reactome
    5. protein folding Source: UniProtKB
    6. protein N-linked glycosylation Source: UniProtKB
    7. protein N-linked glycosylation via asparagine Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.130. 2681.
    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:
    Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC:2.4.1.260)
    Alternative name(s):
    Asparagine-linked glycosylation protein 12 homolog
    Short name:
    hALG12
    Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase
    Mannosyltransferase ALG12 homolog
    Membrane protein SB87
    Gene namesi
    Name:ALG12
    ORF Names:PP14673
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:19358. ALG12.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1G (CDG1G) [MIM:607143]: 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671T → M in CDG1G.
    VAR_017904
    Natural varianti101 – 1011G → R in CDG1G. 1 Publication
    VAR_038428
    Natural varianti142 – 1421F → V in CDG1G. 1 Publication
    Corresponds to variant rs28942090 [ dbSNP | Ensembl ].
    VAR_017905
    Natural varianti146 – 1461R → Q in CDG1G. 1 Publication
    VAR_017906
    Natural varianti158 – 1581L → P in CDG1G.
    VAR_017907

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation

    Organism-specific databases

    MIMi607143. phenotype.
    Orphaneti79324. ALG12-CDG.
    PharmGKBiPA134987771.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferasePRO_0000215781Add
    BLAST

    Proteomic databases

    MaxQBiQ9BV10.
    PaxDbiQ9BV10.
    PRIDEiQ9BV10.

    PTM databases

    PhosphoSiteiQ9BV10.

    Expressioni

    Tissue specificityi

    Expressed in fibroblasts.

    Gene expression databases

    BgeeiQ9BV10.
    CleanExiHS_ALG12.
    GenevestigatoriQ9BV10.

    Organism-specific databases

    HPAiHPA051665.

    Interactioni

    Protein-protein interaction databases

    BioGridi122535. 4 interactions.
    IntActiQ9BV10. 2 interactions.
    STRINGi9606.ENSP00000333813.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BV10.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei68 – 8821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei93 – 11321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei122 – 14221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei145 – 16521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei177 – 19721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei212 – 23221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei264 – 28421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei290 – 31021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei312 – 33221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei346 – 36621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei423 – 44321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 22 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG256776.
    HOGENOMiHOG000265945.
    HOVERGENiHBG050486.
    InParanoidiQ9BV10.
    KOiK03847.
    OMAiFHLMFYS.
    OrthoDBiEOG7ZGX2X.
    PhylomeDBiQ9BV10.
    TreeFamiTF314453.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q9BV10-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGKGSSGRR PLLLGLLVAV ATVHLVICPY TKVEESFNLQ ATHDLLYHWQ    50
    DLEQYDHLEF PGVVPRTFLG PVVIAVFSSP AVYVLSLLEM SKFYSQLIVR 100
    GVLGLGVIFG LWTLQKEVRR HFGAMVATMF CWVTAMQFHL MFYCTRTLPN 150
    VLALPVVLLA LAAWLRHEWA RFIWLSAFAI IVFRVELCLF LGLLLLLALG 200
    NRKVSVVRAL RHAVPAGILC LGLTVAVDSY FWRQLTWPEG KVLWYNTVLN 250
    KSSNWGTSPL LWYFYSALPR GLGCSLLFIP LGLVDRRTHA PTVLALGFMA 300
    LYSLLPHKEL RFIIYAFPML NITAARGCSY LLNNYKKSWL YKAGSLLVIG 350
    HLVVNAAYSA TALYVSHFNY PGGVAMQRLH QLVPPQTDVL LHIDVAAAQT 400
    GVSRFLQVNS AWRYDKREDV QPGTGMLAYT HILMEAAPGL LALYRDTHRV 450
    LASVVGTTGV SLNLTQLPPF NVHLQTKLVL LERLPRPS 488
    Length:488
    Mass (Da):54,655
    Last modified:June 1, 2001 - v1
    Checksum:i8D4F921C21CBC8B6
    GO

    Sequence cautioni

    The sequence AAM94900.1 differs from that shown. Reason: Frameshift at position 468.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti267 – 2671A → T in AAM94900. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671T → M in CDG1G.
    VAR_017904
    Natural varianti101 – 1011G → R in CDG1G. 1 Publication
    VAR_038428
    Natural varianti142 – 1421F → V in CDG1G. 1 Publication
    Corresponds to variant rs28942090 [ dbSNP | Ensembl ].
    VAR_017905
    Natural varianti146 – 1461R → Q in CDG1G. 1 Publication
    VAR_017906
    Natural varianti158 – 1581L → P in CDG1G.
    VAR_017907
    Natural varianti393 – 3931I → V.1 Publication
    Corresponds to variant rs3922872 [ dbSNP | Ensembl ].
    VAR_024466

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ290427 mRNA. Translation: CAC83681.1.
    AJ303120 mRNA. Translation: CAC67488.1.
    AF311904 mRNA. Translation: AAM94900.1. Frameshift.
    AF318343 mRNA. Translation: AAL55850.1.
    CR456369 mRNA. Translation: CAG30255.1.
    AL671710 Genomic DNA. Translation: CAO72064.1.
    CH471138 Genomic DNA. Translation: EAW73480.1.
    BC001729 mRNA. Translation: AAH01729.1.
    BC098562 mRNA. Translation: AAH98562.1.
    CCDSiCCDS14081.1.
    RefSeqiNP_077010.1. NM_024105.3.
    UniGeneiHs.526711.

    Genome annotation databases

    EnsembliENST00000330817; ENSP00000333813; ENSG00000182858.
    GeneIDi79087.
    KEGGihsa:79087.
    UCSCiuc003biy.3. human.

    Polymorphism databases

    DMDMi45476971.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ290427 mRNA. Translation: CAC83681.1 .
    AJ303120 mRNA. Translation: CAC67488.1 .
    AF311904 mRNA. Translation: AAM94900.1 . Frameshift.
    AF318343 mRNA. Translation: AAL55850.1 .
    CR456369 mRNA. Translation: CAG30255.1 .
    AL671710 Genomic DNA. Translation: CAO72064.1 .
    CH471138 Genomic DNA. Translation: EAW73480.1 .
    BC001729 mRNA. Translation: AAH01729.1 .
    BC098562 mRNA. Translation: AAH98562.1 .
    CCDSi CCDS14081.1.
    RefSeqi NP_077010.1. NM_024105.3.
    UniGenei Hs.526711.

    3D structure databases

    ProteinModelPortali Q9BV10.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122535. 4 interactions.
    IntActi Q9BV10. 2 interactions.
    STRINGi 9606.ENSP00000333813.

    Protein family/group databases

    CAZyi GT22. Glycosyltransferase Family 22.

    PTM databases

    PhosphoSitei Q9BV10.

    Polymorphism databases

    DMDMi 45476971.

    Proteomic databases

    MaxQBi Q9BV10.
    PaxDbi Q9BV10.
    PRIDEi Q9BV10.

    Protocols and materials databases

    DNASUi 79087.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330817 ; ENSP00000333813 ; ENSG00000182858 .
    GeneIDi 79087.
    KEGGi hsa:79087.
    UCSCi uc003biy.3. human.

    Organism-specific databases

    CTDi 79087.
    GeneCardsi GC22M050296.
    GeneReviewsi ALG12.
    H-InvDB HIX0175449.
    HGNCi HGNC:19358. ALG12.
    HPAi HPA051665.
    MIMi 607143. phenotype.
    607144. gene.
    neXtProti NX_Q9BV10.
    Orphaneti 79324. ALG12-CDG.
    PharmGKBi PA134987771.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256776.
    HOGENOMi HOG000265945.
    HOVERGENi HBG050486.
    InParanoidi Q9BV10.
    KOi K03847.
    OMAi FHLMFYS.
    OrthoDBi EOG7ZGX2X.
    PhylomeDBi Q9BV10.
    TreeFami TF314453.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.130. 2681.
    Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

    Miscellaneous databases

    ChiTaRSi ALG12. human.
    GeneWikii ALG12.
    GenomeRNAii 79087.
    NextBioi 67909.
    PROi Q9BV10.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BV10.
    CleanExi HS_ALG12.
    Genevestigatori Q9BV10.

    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. "Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase."
      Chantret I., Dupre T., Delenda C., Bucher S., Dancourt J., Barnier A., Charollais A., Heron D., Bader-Meunier B., Danos O., Seta N., Durand G., Oriol R., Codogno P., Moore S.E.H.
      J. Biol. Chem. 277:25815-25822(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CDG1G VAL-142.
      Tissue: Skin.
    2. "Identification of novel membrane proteins."
      Zhang W., Li N., Wan T., Cao X.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANT VAL-393.
      Tissue: Eye.
    8. "ALG12 mannosyltransferase defect in congenital disorder of glycosylation type Ig."
      Grubenmann C.E., Frank C.G., Kjaergaard S., Berger E.G., Aebi M., Hennet T.
      Hum. Mol. Genet. 11:2331-2339(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CDG1G MET-67 AND GLN-146.
    9. "Deficiency of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig."
      Thiel C., Schwarz M., Hasilik M., Grieben U., Hanefeld F., Lehle L., von Figura K., Koerner C.
      Biochem. J. 367:195-201(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT CDG1G PRO-158.
    10. "Abnormal glycosylation of red cell membrane band 3 in the congenital disorder of glycosylation Ig."
      Zdebska E., Bader-Meunier B., Schischmanoff P.-O., Dupre T., Seta N., Tchernia G., Koscielak J., Delaunay J.
      Pediatr. Res. 54:224-229(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CDG1G.
    11. "Expanding spectrum of congenital disorder of glycosylation Ig (CDG-Ig): sibs with a unique skeletal dysplasia, hypogammaglobulinemia, cardiomyopathy, genital malformations, and early lethality."
      Kranz C., Basinger A.A., Guecsavas-Calikoglu M., Sun L., Powell C.M., Henderson F.W., Aylsworth A.S., Freeze H.H.
      Am. J. Med. Genet. A 143:1371-1378(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CDG1G ARG-101 AND GLN-146.

    Entry informationi

    Entry nameiALG12_HUMAN
    AccessioniPrimary (citable) accession number: Q9BV10
    Secondary accession number(s): A6PWM1
    , Q4KMH4, Q8NG10, Q96AA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 123 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 22
      Human chromosome 22: 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