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P49257

- LMAN1_HUMAN

UniProt

P49257 - LMAN1_HUMAN

Protein

Protein ERGIC-53

Gene

LMAN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (13 Aug 2002)
      Previous versions | rss
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    Functioni

    Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei88 – 881CarbohydratePROSITE-ProRule annotation
    Binding sitei121 – 1211CarbohydratePROSITE-ProRule annotation
    Metal bindingi152 – 1521Calcium
    Metal bindingi154 – 1541Calcium; via carbonyl oxygen
    Metal bindingi156 – 1561Calcium
    Binding sitei156 – 1561CarbohydratePROSITE-ProRule annotation
    Binding sitei178 – 1781CarbohydratePROSITE-ProRule annotation
    Metal bindingi181 – 1811Calcium
    Sitei501 – 5011Required for ER export

    GO - Molecular functioni

    1. mannose binding Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. unfolded protein binding Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: ProtInc
    2. cellular protein metabolic process Source: Reactome
    3. endoplasmic reticulum organization Source: Ensembl
    4. ER to Golgi vesicle-mediated transport Source: ProtInc
    5. Golgi organization Source: UniProtKB
    6. positive regulation of organelle organization Source: UniProtKB
    7. post-translational protein modification Source: Reactome
    8. protein folding Source: ProtInc
    9. protein N-linked glycosylation via asparagine Source: Reactome
    10. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    ER-Golgi transport, Protein transport, Transport

    Keywords - Ligandi

    Lectin, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_25046. Transport to the Golgi and subsequent modification.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein ERGIC-53
    Alternative name(s):
    ER-Golgi intermediate compartment 53 kDa protein
    Gp58
    Intracellular mannose-specific lectin MR60
    Lectin mannose-binding 1
    Gene namesi
    Name:LMAN1
    Synonyms:ERGIC53, F5F8D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6631. LMAN1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    2. endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
    3. endoplasmic reticulum membrane Source: ProtInc
    4. ER to Golgi transport vesicle membrane Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi membrane Source: ProtInc
    7. integral component of membrane Source: ProtInc
    8. membrane Source: UniProtKB
    9. sarcomere Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Factor V and factor VIII combined deficiency 1 (F5F8D1) [MIM:227300]: A blood coagulation disorder characterized by bleeding symptoms similar to those in hemophilia or parahemophilia, that are caused by single deficiency of FV or FVIII, respectively. The most common symptoms are epistaxis, menorrhagia, and excessive bleeding during or after trauma. Plasma levels of coagulation factors V and VIII are in the range of 5 to 30% of normal.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi227300. phenotype.
    Orphaneti35909. Combined deficiency of factor V and factor VIII.
    PharmGKBiPA30399.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 30303 PublicationsAdd
    BLAST
    Chaini31 – 510480Protein ERGIC-53PRO_0000017660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi190 ↔ 230
    Disulfide bondi466 – 466Interchain
    Disulfide bondi475 – 475Interchain

    Post-translational modificationi

    The N-terminal may be partly blocked.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP49257.
    PaxDbiP49257.
    PeptideAtlasiP49257.
    PRIDEiP49257.

    PTM databases

    PhosphoSiteiP49257.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiP49257.
    GenevestigatoriP49257.

    Organism-specific databases

    HPAiCAB037163.
    HPA002320.

    Interactioni

    Subunit structurei

    Exists both as a covalent disulfide-linked homohexamer, and a complex of three disulfide-linked dimers non-covalently kept together. Interacts with MCFD2.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERP44Q9BS263EBI-1057738,EBI-541644
    SURF4O152603EBI-1057738,EBI-1044848

    Protein-protein interaction databases

    BioGridi110185. 31 interactions.
    DIPiDIP-42188N.
    IntActiP49257. 8 interactions.
    MINTiMINT-4999949.

    Structurei

    Secondary structure

    1
    510
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 464
    Helixi48 – 503
    Beta strandi52 – 565
    Beta strandi67 – 715
    Beta strandi80 – 834
    Beta strandi85 – 884
    Beta strandi90 – 978
    Beta strandi102 – 11312
    Beta strandi115 – 1184
    Beta strandi122 – 1309
    Beta strandi134 – 1374
    Beta strandi145 – 1528
    Beta strandi158 – 1603
    Beta strandi164 – 17310
    Helixi178 – 1803
    Helixi183 – 1853
    Beta strandi188 – 1914
    Beta strandi201 – 2088
    Beta strandi211 – 2177
    Beta strandi219 – 2224
    Beta strandi228 – 2336
    Beta strandi240 – 24910
    Beta strandi251 – 2533
    Beta strandi256 – 26611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A4UX-ray1.84A31-285[»]
    3LCPX-ray2.45A/B32-277[»]
    3WHTX-ray1.80A31-269[»]
    3WHUX-ray2.60A31-269[»]
    3WNXX-ray2.75A31-269[»]
    4GKXX-ray2.70A/B/C/D/E/F31-270[»]
    4GKYX-ray2.42A31-270[»]
    ProteinModelPortaliP49257.
    SMRiP49257. Positions 41-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49257.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 477447LumenalSequence AnalysisAdd
    BLAST
    Topological domaini499 – 51012CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei478 – 49821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 267224L-type lectin-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni251 – 2533Carbohydrate bindingPROSITE-ProRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi509 – 5102ER export motif

    Domaini

    The FF ER export motif at the C-terminus is not sufficient to support endoplasmic reticulum exit, and needs assistance of Gln-501 for proper recognition of COPII coat components.

    Sequence similaritiesi

    Contains 1 L-type lectin-like domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG292314.
    HOVERGENiHBG052332.
    InParanoidiP49257.
    KOiK10080.
    OMAiGTVPFWA.
    OrthoDBiEOG7QC7VR.
    PhylomeDBiP49257.
    TreeFamiTF313311.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR005052. Lectin_leg.
    [Graphical view]
    PANTHERiPTHR12223. PTHR12223. 1 hit.
    PfamiPF03388. Lectin_leg-like. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS51328. L_LECTIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P49257-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGSRQRGLR ARVRPLFCAL LLSLGRFVRG DGVGGDPAVA LPHRRFEYKY    50
    SFKGPHLVQS DGTVPFWAHA GNAIPSSDQI RVAPSLKSQR GSVWTKTKAA 100
    FENWEVEVTF RVTGRGRIGA DGLAIWYAEN QGLEGPVFGS ADLWNGVGIF 150
    FDSFDNDGKK NNPAIVIIGN NGQIHYDHQN DGASQALASC QRDFRNKPYP 200
    VRAKITYYQN TLTVMINNGF TPDKNDYEFC AKVENMIIPA QGHFGISAAT 250
    GGLADDHDVL SFLTFQLTEP GKEPPTPDKE ISEKEKEKYQ EEFEHFQQEL 300
    DKKKEEFQKG HPDLQGQPAE EIFESVGDRE LRQVFEGQNR IHLEIKQLNR 350
    QLDMILDEQR RYVSSLTEEI SKRGAGMPGQ HGQITQQELD TVVKTQHEIL 400
    RQVNEMKNSM SETVRLVSGM QHPGSAGGVY ETTQHFIDIK EHLHIVKRDI 450
    DNLVQRNMPS NEKPKCPELP PFPSCLSTVH FIIFVVVQTV LFIGYIMYRS 500
    QQEAAAKKFF 510
    Length:510
    Mass (Da):57,549
    Last modified:August 13, 2002 - v2
    Checksum:iB87EF117C0CD386C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531S → T in CAA50653. (PubMed:8223692)Curated

    Mass spectrometryi

    Molecular mass is 54222.91 Da from positions 31 - 510. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141R → Q.1 Publication
    Corresponds to variant rs1043302 [ dbSNP | Ensembl ].
    VAR_013703
    Natural varianti39 – 391V → A.1 Publication
    Corresponds to variant rs33926449 [ dbSNP | Ensembl ].
    VAR_013704
    Natural varianti355 – 3551I → T.
    Corresponds to variant rs3737392 [ dbSNP | Ensembl ].
    VAR_049770
    Natural varianti410 – 4101M → L.2 Publications
    Corresponds to variant rs2298711 [ dbSNP | Ensembl ].
    VAR_013705

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71661 mRNA. Translation: CAA50653.1.
    U09716 mRNA. Translation: AAA95960.1.
    AF081866, AF081865 Genomic DNA. Translation: AAD32479.1.
    AF081867 Genomic DNA. Translation: AAD32480.1.
    AF081869, AF081868 Genomic DNA. Translation: AAD32481.1.
    AF081871, AF081870 Genomic DNA. Translation: AAD32482.1.
    AF081873, AF081872 Genomic DNA. Translation: AAD32483.1.
    AF081875, AF081874 Genomic DNA. Translation: AAD32484.1.
    AF081877, AF081876 Genomic DNA. Translation: AAD32485.1.
    AF081879, AF081878 Genomic DNA. Translation: AAD32486.1.
    AF081880 Genomic DNA. Translation: AAD32487.1.
    AF081882, AF081881 Genomic DNA. Translation: AAD32488.1.
    AF081884, AF081883 Genomic DNA. Translation: AAD32489.1.
    AF081885 Genomic DNA. Translation: AAD32490.1.
    BC032330 mRNA. Translation: AAH32330.1.
    CCDSiCCDS11974.1.
    PIRiS42626.
    RefSeqiNP_005561.1. NM_005570.3.
    UniGeneiHs.465295.

    Genome annotation databases

    EnsembliENST00000251047; ENSP00000251047; ENSG00000074695.
    GeneIDi3998.
    KEGGihsa:3998.
    UCSCiuc002lhz.3. human.

    Polymorphism databases

    DMDMi22261801.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71661 mRNA. Translation: CAA50653.1 .
    U09716 mRNA. Translation: AAA95960.1 .
    AF081866 , AF081865 Genomic DNA. Translation: AAD32479.1 .
    AF081867 Genomic DNA. Translation: AAD32480.1 .
    AF081869 , AF081868 Genomic DNA. Translation: AAD32481.1 .
    AF081871 , AF081870 Genomic DNA. Translation: AAD32482.1 .
    AF081873 , AF081872 Genomic DNA. Translation: AAD32483.1 .
    AF081875 , AF081874 Genomic DNA. Translation: AAD32484.1 .
    AF081877 , AF081876 Genomic DNA. Translation: AAD32485.1 .
    AF081879 , AF081878 Genomic DNA. Translation: AAD32486.1 .
    AF081880 Genomic DNA. Translation: AAD32487.1 .
    AF081882 , AF081881 Genomic DNA. Translation: AAD32488.1 .
    AF081884 , AF081883 Genomic DNA. Translation: AAD32489.1 .
    AF081885 Genomic DNA. Translation: AAD32490.1 .
    BC032330 mRNA. Translation: AAH32330.1 .
    CCDSi CCDS11974.1.
    PIRi S42626.
    RefSeqi NP_005561.1. NM_005570.3.
    UniGenei Hs.465295.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A4U X-ray 1.84 A 31-285 [» ]
    3LCP X-ray 2.45 A/B 32-277 [» ]
    3WHT X-ray 1.80 A 31-269 [» ]
    3WHU X-ray 2.60 A 31-269 [» ]
    3WNX X-ray 2.75 A 31-269 [» ]
    4GKX X-ray 2.70 A/B/C/D/E/F 31-270 [» ]
    4GKY X-ray 2.42 A 31-270 [» ]
    ProteinModelPortali P49257.
    SMRi P49257. Positions 41-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110185. 31 interactions.
    DIPi DIP-42188N.
    IntActi P49257. 8 interactions.
    MINTi MINT-4999949.

    Chemistry

    DrugBanki DB00025. Antihemophilic Factor.

    PTM databases

    PhosphoSitei P49257.

    Polymorphism databases

    DMDMi 22261801.

    Proteomic databases

    MaxQBi P49257.
    PaxDbi P49257.
    PeptideAtlasi P49257.
    PRIDEi P49257.

    Protocols and materials databases

    DNASUi 3998.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251047 ; ENSP00000251047 ; ENSG00000074695 .
    GeneIDi 3998.
    KEGGi hsa:3998.
    UCSCi uc002lhz.3. human.

    Organism-specific databases

    CTDi 3998.
    GeneCardsi GC18M056969.
    HGNCi HGNC:6631. LMAN1.
    HPAi CAB037163.
    HPA002320.
    MIMi 227300. phenotype.
    601567. gene.
    neXtProti NX_P49257.
    Orphaneti 35909. Combined deficiency of factor V and factor VIII.
    PharmGKBi PA30399.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292314.
    HOVERGENi HBG052332.
    InParanoidi P49257.
    KOi K10080.
    OMAi GTVPFWA.
    OrthoDBi EOG7QC7VR.
    PhylomeDBi P49257.
    TreeFami TF313311.

    Enzyme and pathway databases

    Reactomei REACT_25046. Transport to the Golgi and subsequent modification.

    Miscellaneous databases

    EvolutionaryTracei P49257.
    GeneWikii LMAN1.
    GenomeRNAii 3998.
    NextBioi 15688.
    PROi P49257.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49257.
    Genevestigatori P49257.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR005052. Lectin_leg.
    [Graphical view ]
    PANTHERi PTHR12223. PTHR12223. 1 hit.
    Pfami PF03388. Lectin_leg-like. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS51328. L_LECTIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif."
      Schindler R., Itin C., Zerial M., Lottspeich F., Hauri H.-P.
      Eur. J. Cell Biol. 61:1-9(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-59 AND 418-432.
      Tissue: Liver and Placenta.
    2. "ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells."
      Arar C., Carpentier V., Le Caer J.-P., Monsigny M., Legrand A., Roche A.-C.
      J. Biol. Chem. 270:3551-3553(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-41.
      Tissue: Peripheral blood.
    3. "ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families."
      Nichols W.C., Terry V.H., Wheatley M.A., Yang A., Zivelin A., Ciavarella N., Stefanile C., Matsushita T., Saito H., de Bosch N.B., Ruiz-Saez A., Torres A., Thompson A.R., Feinstein D.I., White G.C., Negrier C., Vinciguerra C., Aktan M.
      , Kaufman R.J., Ginsburg D., Seligsohn U.
      Blood 93:2261-2266(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-14; ALA-39 AND LEU-410, INVOLVEMENT IN F5F8D1.
    4. "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 LEU-410.
      Tissue: Brain.
    5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-44.
      Tissue: Platelet.
    6. "A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins."
      Fiedler K., Simons K.
      Cell 77:625-626(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO LEGUMINOUS LECTINS.
    7. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    8. "ER export of ERGIC-53 is controlled by cooperation of targeting determinants in all three of its domains."
      Nufer O., Kappeler F., Guldbrandsen S., Hauri H.-P.
      J. Cell Sci. 116:4429-4440(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MOTIF ER EXPORT, DISULFIDE BOND.
    9. Cited for: INTERACTION WITH MCFD2, FUNCTION.
    10. "Oligomerization and intracellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds."
      Neve E.P., Lahtinen U., Pettersson R.F.
      J. Mol. Biol. 354:556-568(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERCHAIN DISULFIDE BONDS.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII."
      Wigren E., Bourhis J.M., Kursula I., Guy J.E., Lindqvist Y.
      FEBS Lett. 584:878-882(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 32-277 IN COMPLEX WITH MCFD2 AND CALCIUM IONS, SUBUNIT, DISULFIDE BOND.
    13. "Structural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiency."
      Nishio M., Kamiya Y., Mizushima T., Wakatsuki S., Sasakawa H., Yamamoto K., Uchiyama S., Noda M., McKay A.R., Fukui K., Hauri H.P., Kato K.
      Proc. Natl. Acad. Sci. U.S.A. 107:4034-4039(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 31-285 IN COMPLEX WITH CALCIUM IONS, SUBUNIT, DISULFIDE BOND.

    Entry informationi

    Entry nameiLMAN1_HUMAN
    AccessioniPrimary (citable) accession number: P49257
    Secondary accession number(s): Q12895
    , Q8N5I7, Q9UQG1, Q9UQG2, Q9UQG3, Q9UQG4, Q9UQG5, Q9UQG6, Q9UQG7, Q9UQG8, Q9UQG9, Q9UQH0, Q9UQH1, Q9UQH2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: August 13, 2002
    Last modified: October 1, 2014
    This is version 150 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3