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Q9Y2U8

- MAN1_HUMAN

UniProt

Q9Y2U8 - MAN1_HUMAN

Protein

Inner nuclear membrane protein Man1

Gene

LEMD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi707 – 72620Add
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. nucleotide binding Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of activin receptor signaling pathway Source: UniProtKB
    2. negative regulation of BMP signaling pathway Source: UniProtKB
    3. negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    4. regulation of cell cycle Source: Ensembl
    5. skeletal muscle cell differentiation Source: Ensembl

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_200828. Depolymerisation of the Nuclear Lamina.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inner nuclear membrane protein Man1
    Alternative name(s):
    LEM domain-containing protein 3
    Gene namesi
    Name:LEMD3
    Synonyms:MAN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:28887. LEMD3.

    Subcellular locationi

    Nucleus inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: MGI
    2. integral component of nuclear inner membrane Source: ProtInc
    3. membrane Source: ProtInc
    4. nuclear inner membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Buschke-Ollendorff syndrome (BOS) [MIM:166700]: A disease characterized by osteopoikilosis and disseminated connective-tissue nevi. Osteopoikilosis is a skeletal dysplasia characterized by a symmetric but unequal distribution of multiple hyperostotic areas in different parts of the skeleton. Elastic-type nevi (juvenile elastoma) and collagen-type nevi (dermatofibrosis lenticularis disseminata) have been described in BOS. Skin or bony lesions can be absent in some family members, whereas other relatives may have both.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Melorheostosis (MEL) [MIM:155950]: Rare mesenchymal dysplasia and one of the sclerosing bone disorders. It is caused by a developmental error, with a sclerotomal distribution, frequently involving one limb. It may be asymptomatic, but pain, stiffness with limitation of motion, leg-length discrepancy and limb deformity may occur.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi703 – 7042LI → ED: Impairs binding to SMAD1. Loss of ability to repress transcriptional activation in response to TGF-beta, BMP2 and activin signaling. 1 Publication
    Mutagenesisi835 – 8362YV → DD: Impairs binding to SMAD1. 1 Publication

    Organism-specific databases

    MIMi155950. phenotype.
    166700. phenotype.
    Orphaneti94063. 12q14 microdeletion syndrome.
    1306. Buschke-Ollendorff syndrome.
    166119. Isolated osteopoikilosis.
    1879. Melorheostosis with osteopoikilosis.
    PharmGKBiPA134907442.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 911910Inner nuclear membrane protein Man1PRO_0000206149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei140 – 1401Phosphoserine1 Publication
    Modified residuei141 – 1411Phosphoserine1 Publication
    Modified residuei144 – 1441Phosphoserine2 Publications
    Modified residuei185 – 1851Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphoserine2 Publications
    Modified residuei259 – 2591Phosphoserine2 Publications
    Modified residuei261 – 2611Phosphoserine3 Publications
    Modified residuei280 – 2801Phosphoserine1 Publication
    Modified residuei352 – 3521Phosphoserine1 Publication
    Modified residuei365 – 3651Phosphothreonine1 Publication
    Modified residuei402 – 4021Phosphoserine2 Publications
    Modified residuei777 – 7771Phosphoserine1 Publication
    Modified residuei883 – 8831Phosphothreonine1 Publication
    Modified residuei911 – 9111Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2U8.
    PaxDbiQ9Y2U8.
    PeptideAtlasiQ9Y2U8.
    PRIDEiQ9Y2U8.

    PTM databases

    PhosphoSiteiQ9Y2U8.

    Expressioni

    Tissue specificityi

    Heart, brain, placenta, lung, liver and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ9Y2U8.
    BgeeiQ9Y2U8.
    CleanExiHS_LEMD3.
    GenevestigatoriQ9Y2U8.

    Organism-specific databases

    HPAiHPA025078.

    Interactioni

    Subunit structurei

    Interacts with SMAD1, SMAD2, SMAD3 and SMAD5. Binds to both phosphorylated and unphosphorylated R-SMADS.2 Publications

    Protein-protein interaction databases

    BioGridi117127. 9 interactions.
    IntActiQ9Y2U8. 7 interactions.
    MINTiMINT-1199446.
    STRINGi9606.ENSP00000308369.

    Structurei

    Secondary structure

    1
    911
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi659 – 6635
    Turni664 – 6696
    Helixi670 – 68415
    Helixi696 – 7016
    Helixi709 – 7124
    Helixi713 – 72311
    Turni724 – 7263
    Beta strandi730 – 7378
    Beta strandi740 – 7467
    Beta strandi751 – 7533
    Beta strandi765 – 7684
    Beta strandi771 – 7744

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CH0NMR-A655-775[»]
    ProteinModelPortaliQ9Y2U8.
    SMRiQ9Y2U8. Positions 9-49, 653-780, 783-888.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2U8.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei475 – 49521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei628 – 64821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 5045LEMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni699 – 911213Interaction with SMAD1, SMAD2, SMAD3 and SMAD5Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi65 – 706Poly-Asn
    Compositional biasi72 – 8716Ala-richAdd
    BLAST
    Compositional biasi82 – 876Poly-Ala
    Compositional biasi155 – 1584Poly-Gly
    Compositional biasi265 – 2684Poly-Asp
    Compositional biasi312 – 3154Poly-Gly
    Compositional biasi322 – 3254Poly-Ala
    Compositional biasi337 – 3404Poly-Ala
    Compositional biasi635 – 6406Poly-Leu
    Compositional biasi659 – 6624Poly-Glu

    Sequence similaritiesi

    Contains 1 LEM domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG70255.
    HOGENOMiHOG000063699.
    HOVERGENiHBG006319.
    InParanoidiQ9Y2U8.
    OMAiSPIPRYR.
    OrthoDBiEOG75J0MP.
    PhylomeDBiQ9Y2U8.
    TreeFamiTF315385.

    Family and domain databases

    Gene3Di1.10.720.40. 1 hit.
    3.30.70.330. 1 hit.
    InterProiIPR018996. Inner-Nucl-membr_MAN1.
    IPR011015. LEM/LEM-like_dom.
    IPR003887. LEM_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    [Graphical view]
    PfamiPF03020. LEM. 1 hit.
    PF09402. MSC. 1 hit.
    [Graphical view]
    SMARTiSM00540. LEM. 1 hit.
    [Graphical view]
    SUPFAMiSSF63451. SSF63451. 1 hit.
    PROSITEiPS50954. LEM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Y2U8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAAASAPQ QLSDEELFSQ LRRYGLSPGP VTESTRPVYL KKLKKLREEE    50
    QQQHRSGGRG NKTRNSNNNN TAAATVAAAG PAAAAAAGMG VRPVSGDLSY 100
    LRTPGGLCRI SASGPESLLG GPGGASAAPA AGSKVLLGFS SDESDVEASP 150
    RDQAGGGGRK DRASLQYRGL KAPPAPLAAS EVTNSNSAER RKPHSWWGAR 200
    RPAGPELQTP PGKDGAVEDE EGEGEDGEER DPETEEPLWA SRTVNGSRLV 250
    PYSCRENYSD SEEEDDDDVA SSRQVLKDDS LSRHRPRRTH SKPLPPLTAK 300
    SAGGRLETSV QGGGGLAMND RAAAAGSLDR SRNLEEAAAA EQGGGCDQVD 350
    SSPVPRYRVN AKKLTPLLPP PLTDMDSTLD SSTGSLLKTN NHIGGGAFSV 400
    DSPRIYSNSL PPSAAVAASS SLRINHANHT GSNHTYLKNT YNKPKLSEPE 450
    EELLQQFKRE EVSPTGSFSA HYLSMFLLTA ACLFFLILGL TYLGMRGTGV 500
    SEDGELSIEN PFGETFGKIQ ESEKTLMMNT LYKLHDRLAQ LAGDHECGSS 550
    SQRTLSVQEA AAYLKDLGPE YEGIFNTSLQ WILENGKDVG IRCVGFGPEE 600
    ELTNITDVQF LQSTRPLMSF WCRFRRAFVT VTHRLLLLCL GVVMVCVVLR 650
    YMKYRWTKEE EETRQMYDMV VKIIDVLRSH NEACQENKDL QPYMPIPHVR 700
    DSLIQPHDRK KMKKVWDRAV DFLAANESRV RTETRRIGGA DFLVWRWIQP 750
    SASCDKILVI PSKVWQGQAF HLDRRNSPPN SLTPCLKIRN MFDPVMEIGD 800
    QWHLAIQEAI LEKCSDNDGI VHIAVDKNSR EGCVYVKCLS PEYAGKAFKA 850
    LHGSWFDGKL VTVKYLRLDR YHHRFPQALT SNTPLKPSNK HMNSMSHLRL 900
    RTGLTNSQGS S 911
    Length:911
    Mass (Da):99,997
    Last modified:October 1, 2000 - v2
    Checksum:i21D1E6BB0D499131
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti508 – 5092IE → K in AAF73293. (PubMed:10671519)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti260 – 2601D → Y.
    Corresponds to variant rs7487311 [ dbSNP | Ensembl ].
    VAR_034605

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF112299 mRNA. Translation: AAD31593.2.
    AF263918
    , AF180135, AF180136, AF180137, AF180138, AF180139, AF180140, AF180141, AF180142 Genomic DNA. Translation: AAF73293.1.
    AL137533 mRNA. Translation: CAB70796.1. Sequence problems.
    CCDSiCCDS8972.1.
    PIRiT46377.
    RefSeqiNP_001161086.1. NM_001167614.1.
    NP_055134.2. NM_014319.4.
    UniGeneiHs.744150.

    Genome annotation databases

    EnsembliENST00000308330; ENSP00000308369; ENSG00000174106.
    GeneIDi23592.
    KEGGihsa:23592.
    UCSCiuc001ssl.2. human.

    Polymorphism databases

    DMDMi13629600.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF112299 mRNA. Translation: AAD31593.2 .
    AF263918
    , AF180135 , AF180136 , AF180137 , AF180138 , AF180139 , AF180140 , AF180141 , AF180142 Genomic DNA. Translation: AAF73293.1 .
    AL137533 mRNA. Translation: CAB70796.1 . Sequence problems.
    CCDSi CCDS8972.1.
    PIRi T46377.
    RefSeqi NP_001161086.1. NM_001167614.1.
    NP_055134.2. NM_014319.4.
    UniGenei Hs.744150.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CH0 NMR - A 655-775 [» ]
    ProteinModelPortali Q9Y2U8.
    SMRi Q9Y2U8. Positions 9-49, 653-780, 783-888.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117127. 9 interactions.
    IntActi Q9Y2U8. 7 interactions.
    MINTi MINT-1199446.
    STRINGi 9606.ENSP00000308369.

    PTM databases

    PhosphoSitei Q9Y2U8.

    Polymorphism databases

    DMDMi 13629600.

    Proteomic databases

    MaxQBi Q9Y2U8.
    PaxDbi Q9Y2U8.
    PeptideAtlasi Q9Y2U8.
    PRIDEi Q9Y2U8.

    Protocols and materials databases

    DNASUi 23592.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308330 ; ENSP00000308369 ; ENSG00000174106 .
    GeneIDi 23592.
    KEGGi hsa:23592.
    UCSCi uc001ssl.2. human.

    Organism-specific databases

    CTDi 23592.
    GeneCardsi GC12P065563.
    HGNCi HGNC:28887. LEMD3.
    HPAi HPA025078.
    MIMi 155950. phenotype.
    166700. phenotype.
    607844. gene.
    neXtProti NX_Q9Y2U8.
    Orphaneti 94063. 12q14 microdeletion syndrome.
    1306. Buschke-Ollendorff syndrome.
    166119. Isolated osteopoikilosis.
    1879. Melorheostosis with osteopoikilosis.
    PharmGKBi PA134907442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70255.
    HOGENOMi HOG000063699.
    HOVERGENi HBG006319.
    InParanoidi Q9Y2U8.
    OMAi SPIPRYR.
    OrthoDBi EOG75J0MP.
    PhylomeDBi Q9Y2U8.
    TreeFami TF315385.

    Enzyme and pathway databases

    Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_200828. Depolymerisation of the Nuclear Lamina.

    Miscellaneous databases

    EvolutionaryTracei Q9Y2U8.
    GenomeRNAii 23592.
    NextBioi 46240.
    PROi Q9Y2U8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2U8.
    Bgeei Q9Y2U8.
    CleanExi HS_LEMD3.
    Genevestigatori Q9Y2U8.

    Family and domain databases

    Gene3Di 1.10.720.40. 1 hit.
    3.30.70.330. 1 hit.
    InterProi IPR018996. Inner-Nucl-membr_MAN1.
    IPR011015. LEM/LEM-like_dom.
    IPR003887. LEM_dom.
    IPR012677. Nucleotide-bd_a/b_plait.
    [Graphical view ]
    Pfami PF03020. LEM. 1 hit.
    PF09402. MSC. 1 hit.
    [Graphical view ]
    SMARTi SM00540. LEM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63451. SSF63451. 1 hit.
    PROSITEi PS50954. LEM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin."
      Lin F., Blake D.L., Callebaut I., Skerjanc I.S., Holmer L., McBurney M.W., Paulin-Levasseur M., Worman H.J.
      J. Biol. Chem. 275:4840-4847(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-911.
      Tissue: Testis.
    3. Cited for: INVOLVEMENT IN BOS AND MEL.
    4. "MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling."
      Lin F., Morrison J.M., Wu W., Worman H.J.
      Hum. Mol. Genet. 14:437-445(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD2 AND SMAD3.
    5. "The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines."
      Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K.
      J. Biol. Chem. 280:15992-16001(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMAD1; SMAD2; SMAD3 AND SMAD5, MUTAGENESIS OF 703-LEU-ILE-704 AND 835-TYR-VAL-836.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-187; SER-259; SER-261; SER-280; SER-352; THR-365; SER-402; SER-777 AND SER-911, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-141; SER-144 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-187 AND THR-883, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain."
      Caputo S., Couprie J., Duband-Goulet I., Konde E., Lin F., Braud S., Gondry M., Gilquin B., Worman H.J., Zinn-Justin S.
      J. Biol. Chem. 281:18208-18215(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 655-775, DNA-BINDING.

    Entry informationi

    Entry nameiMAN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2U8
    Secondary accession number(s): Q9NT47, Q9NYA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 131 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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