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Q14565

- DMC1_HUMAN

UniProt

Q14565 - DMC1_HUMAN

Protein

Meiotic recombination protein DMC1/LIM15 homolog

Gene

DMC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    May participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei230 – 2301ssDNA or dsDNA
    Binding sitei233 – 2331ssDNA
    Binding sitei236 – 2361ssDNA or dsDNA
    Binding sitei242 – 2421ssDNA or dsDNA
    Binding sitei311 – 3111ssDNA

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi126 – 1338ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: ProtInc
    2. DNA binding Source: ProtInc
    3. DNA-dependent ATPase activity Source: InterPro
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. female gamete generation Source: ProtInc
    2. male meiosis I Source: Ensembl
    3. meiotic nuclear division Source: ProtInc
    4. oocyte maturation Source: Ensembl
    5. ovarian follicle development Source: Ensembl
    6. reciprocal meiotic recombination Source: ProtInc
    7. spermatid development Source: Ensembl
    8. spermatogenesis Source: ProtInc
    9. synapsis Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Meiosis

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_27271. Meiotic recombination.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Meiotic recombination protein DMC1/LIM15 homolog
    Gene namesi
    Name:DMC1
    Synonyms:DMC1H, LIM15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2927. DMC1.

    Subcellular locationi

    Nucleus Curated. Chromosome By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB
    2. chromosome, telomeric region Source: Ensembl
    3. condensed nuclear chromosome Source: ProtInc
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581E → A or Q: Decreases octamer stability. 1 Publication

    Organism-specific databases

    PharmGKBiPA27377.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Meiotic recombination protein DMC1/LIM15 homologPRO_0000122918Add
    BLAST

    Proteomic databases

    PaxDbiQ14565.
    PRIDEiQ14565.

    PTM databases

    PhosphoSiteiQ14565.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14565.
    BgeeiQ14565.
    CleanExiHS_DMC1.
    GenevestigatoriQ14565.

    Organism-specific databases

    HPAiCAB015397.
    HPA001232.

    Interactioni

    Subunit structurei

    Interacts with the MND1-PSMC3IP heterodimer By similarity. Double stacked ring-shaped homooctamer. Interacts with BRCA2.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA2P5158711EBI-930865,EBI-79792

    Protein-protein interaction databases

    BioGridi116316. 4 interactions.
    DIPiDIP-24192N.
    IntActiQ14565. 4 interactions.
    MINTiMINT-3029876.
    STRINGi9606.ENSP00000216024.

    Structurei

    Secondary structure

    1
    340
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi85 – 873
    Helixi88 – 958
    Helixi106 – 1116
    Beta strandi114 – 1185
    Beta strandi120 – 1278
    Helixi132 – 14211
    Helixi148 – 1503
    Beta strandi155 – 1639
    Helixi167 – 17711
    Helixi181 – 1866
    Beta strandi188 – 1925
    Helixi196 – 21217
    Beta strandi216 – 2238
    Helixi227 – 2326
    Helixi235 – 2373
    Helixi239 – 25921
    Beta strandi263 – 2686
    Beta strandi287 – 2893
    Helixi290 – 2967
    Beta strandi298 – 3058
    Beta strandi310 – 3178
    Helixi322 – 3243
    Beta strandi325 – 3317
    Beta strandi334 – 3374

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V5WX-ray3.20A/B1-340[»]
    2ZJBX-ray3.50A/B1-340[»]
    4HYYX-ray2.60A/B/C/D84-340[»]
    ProteinModelPortaliQ14565.
    SMRiQ14565. Positions 31-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14565.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RecA family. DMC1 subfamily.Curated
    Contains 1 HhH domain.Curated

    Phylogenomic databases

    eggNOGiCOG0468.
    HOGENOMiHOG000227426.
    HOVERGENiHBG001504.
    InParanoidiQ14565.
    KOiK10872.
    OMAiINMADIK.
    PhylomeDBiQ14565.
    TreeFamiTF300698.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR011940. DMC1_rcmbase.
    IPR013632. DNA_recomb/repair_Rad51_C.
    IPR016467. DNA_recomb/repair_RecA-like.
    IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
    IPR027417. P-loop_NTPase.
    IPR020588. RecA_ATP-bd.
    IPR020587. RecA_monomer-monomer_interface.
    [Graphical view]
    PfamiPF08423. Rad51. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005856. Rad51. 1 hit.
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47794. SSF47794. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR02238. recomb_DMC1. 1 hit.
    PROSITEiPS50162. RECA_2. 1 hit.
    PS50163. RECA_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14565-1) [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

    MKEDQVVAEE PGFQDEEESL FQDIDLLQKH GINVADIKKL KSVGICTIKG    50
    IQMTTRRALC NVKGLSEAKV DKIKEAANKL IEPGFLTAFE YSEKRKMVFH 100
    ITTGSQEFDK LLGGGIESMA ITEAFGEFRT GKTQLSHTLC VTAQLPGAGG 150
    YPGGKIIFID TENTFRPDRL RDIADRFNVD HDAVLDNVLY ARAYTSEHQM 200
    ELLDYVAAKF HEEAGIFKLL IIDSIMALFR VDFSGRGELA ERQQKLAQML 250
    SRLQKISEEY NVAVFVTNQM TADPGATMTF QADPKKPIGG HILAHASTTR 300
    ISLRKGRGEL RIAKIYDSPE MPENEATFAI TAGGIGDAKE 340
    Length:340
    Mass (Da):37,681
    Last modified:April 27, 2001 - v2
    Checksum:i040A6E4CF1FEBFA2
    GO
    Isoform 2 (identifier: Q14565-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         141-196: VTAQLPGAGGYPGGKIIFIDTENTFRPDRLRDIADRFNVDHDAVLDNVLYARAYTS → G

    Note: No experimental confirmation available.

    Show »
    Length:285
    Mass (Da):31,559
    Checksum:i0DDE121D137D5438
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371I → N in BAA10970. (PubMed:8602360)Curated
    Sequence conflicti183 – 1831A → P in BAA09932. (PubMed:8590282)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501G → D.
    Corresponds to variant rs58396845 [ dbSNP | Ensembl ].
    VAR_061757
    Natural varianti200 – 2001M → V.1 Publication
    Corresponds to variant rs2227914 [ dbSNP | Ensembl ].
    VAR_018960

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei141 – 19656VTAQL…RAYTS → G in isoform 2. 1 PublicationVSP_055357Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63882 mRNA. Translation: BAA09932.1.
    D64108 mRNA. Translation: BAA10970.1.
    CR456486 mRNA. Translation: CAG30372.1.
    AK292617 mRNA. Translation: BAF85306.1.
    AK297664 mRNA. Translation: BAG60028.1.
    AY520538 Genomic DNA. Translation: AAR89915.1.
    AL022320 Genomic DNA. Translation: CAB45656.1.
    BC125163 mRNA. Translation: AAI25164.1.
    BC125164 mRNA. Translation: AAI25165.1.
    CCDSiCCDS13973.1. [Q14565-1]
    CCDS63477.1. [Q14565-2]
    PIRiS62354.
    RefSeqiNP_001265137.1. NM_001278208.1.
    NP_008999.2. NM_007068.3.
    XP_006724173.1. XM_006724110.1.
    XP_006724175.1. XM_006724112.1.
    UniGeneiHs.339396.

    Genome annotation databases

    EnsembliENST00000216024; ENSP00000216024; ENSG00000100206. [Q14565-1]
    ENST00000428462; ENSP00000412703; ENSG00000100206. [Q14565-2]
    GeneIDi11144.
    KEGGihsa:11144.
    UCSCiuc003avz.2. human. [Q14565-1]

    Polymorphism databases

    DMDMi13878923.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63882 mRNA. Translation: BAA09932.1 .
    D64108 mRNA. Translation: BAA10970.1 .
    CR456486 mRNA. Translation: CAG30372.1 .
    AK292617 mRNA. Translation: BAF85306.1 .
    AK297664 mRNA. Translation: BAG60028.1 .
    AY520538 Genomic DNA. Translation: AAR89915.1 .
    AL022320 Genomic DNA. Translation: CAB45656.1 .
    BC125163 mRNA. Translation: AAI25164.1 .
    BC125164 mRNA. Translation: AAI25165.1 .
    CCDSi CCDS13973.1. [Q14565-1 ]
    CCDS63477.1. [Q14565-2 ]
    PIRi S62354.
    RefSeqi NP_001265137.1. NM_001278208.1.
    NP_008999.2. NM_007068.3.
    XP_006724173.1. XM_006724110.1.
    XP_006724175.1. XM_006724112.1.
    UniGenei Hs.339396.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V5W X-ray 3.20 A/B 1-340 [» ]
    2ZJB X-ray 3.50 A/B 1-340 [» ]
    4HYY X-ray 2.60 A/B/C/D 84-340 [» ]
    ProteinModelPortali Q14565.
    SMRi Q14565. Positions 31-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116316. 4 interactions.
    DIPi DIP-24192N.
    IntActi Q14565. 4 interactions.
    MINTi MINT-3029876.
    STRINGi 9606.ENSP00000216024.

    PTM databases

    PhosphoSitei Q14565.

    Polymorphism databases

    DMDMi 13878923.

    Proteomic databases

    PaxDbi Q14565.
    PRIDEi Q14565.

    Protocols and materials databases

    DNASUi 11144.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216024 ; ENSP00000216024 ; ENSG00000100206 . [Q14565-1 ]
    ENST00000428462 ; ENSP00000412703 ; ENSG00000100206 . [Q14565-2 ]
    GeneIDi 11144.
    KEGGi hsa:11144.
    UCSCi uc003avz.2. human. [Q14565-1 ]

    Organism-specific databases

    CTDi 11144.
    GeneCardsi GC22M038914.
    HGNCi HGNC:2927. DMC1.
    HPAi CAB015397.
    HPA001232.
    MIMi 602721. gene.
    neXtProti NX_Q14565.
    PharmGKBi PA27377.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0468.
    HOGENOMi HOG000227426.
    HOVERGENi HBG001504.
    InParanoidi Q14565.
    KOi K10872.
    OMAi INMADIK.
    PhylomeDBi Q14565.
    TreeFami TF300698.

    Enzyme and pathway databases

    Reactomei REACT_27271. Meiotic recombination.

    Miscellaneous databases

    EvolutionaryTracei Q14565.
    GeneWikii DMC1_(gene).
    GenomeRNAii 11144.
    NextBioi 35473445.
    PROi Q14565.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14565.
    Bgeei Q14565.
    CleanExi HS_DMC1.
    Genevestigatori Q14565.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR011940. DMC1_rcmbase.
    IPR013632. DNA_recomb/repair_Rad51_C.
    IPR016467. DNA_recomb/repair_RecA-like.
    IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
    IPR027417. P-loop_NTPase.
    IPR020588. RecA_ATP-bd.
    IPR020587. RecA_monomer-monomer_interface.
    [Graphical view ]
    Pfami PF08423. Rad51. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005856. Rad51. 1 hit.
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47794. SSF47794. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR02238. recomb_DMC1. 1 hit.
    PROSITEi PS50162. RECA_2. 1 hit.
    PS50163. RECA_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression profiles of a human gene identified as a structural homologue of meiosis-specific recA-like genes."
      Sato S., Seki N., Hotta Y., Tabata S.
      DNA Res. 2:183-185(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "The mouse and human homologs of DMC1, the yeast meiosis-specific homologous recombination gene, have a common unique form of exon-skipped transcript in meiosis."
      Habu T., Taki T., West A., Nishimune Y., Morita T.
      Nucleic Acids Res. 24:470-477(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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 1 AND 2).
      Tissue: Heart and Thymus.
    5. NIEHS SNPs program
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-200.
    6. "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].
    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] (ISOFORM 1).
    8. "Purified human BRCA2 stimulates RAD51-mediated recombination."
      Jensen R.B., Carreira A., Kowalczykowski S.C.
      Nature 467:678-683(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRCA2.
    9. "Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1."
      Kinebuchi T., Kagawa W., Enomoto R., Tanaka K., Miyagawa K., Shibata T., Kurumizaka H., Yokoyama S.
      Mol. Cell 14:363-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), SUBUNIT, DNA-BINDING SITES, MUTAGENESIS OF GLU-258.

    Entry informationi

    Entry nameiDMC1_HUMAN
    AccessioniPrimary (citable) accession number: Q14565
    Secondary accession number(s): A8K9A2
    , B4DMW6, Q08AI1, Q99498, Q9UH11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 137 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 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3