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UniProtKB/Swiss-Prot entry Q14565


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DMC1_HUMAN
Primary accession number Q14565
Secondary accession numbers A8K9A2 Q08AI1 Q99498 Q9UH11
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on April 27, 2001 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 84)
Name and origin of the protein
Protein name Meiotic recombination protein DMC1/LIM15 homolog
Synonyms None
Gene name
Name: DMC1
Synonyms: DMC1H, LIM15
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1093/dnares/2.4.183; PubMed=8590282 [NCBI, ExPASy, EBI, Israel, Japan]
Sato S., Seki N., Hotta Y., Tabata S.;
"Expression profiles of a human gene identified as a structural homologue of meiosis-specific recA-like genes.";
DNA Res. 2:183-185(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1093/nar/24.3.470; PubMed=8602360 [NCBI, ExPASy, EBI, Israel, Japan]
Habu T., Taki T., West A., Nishimune Y., Morita T.;
"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.";
Nucleic Acids Res. 24:470-477(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-200.
NIEHS SNPs program;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), SUBUNIT, DNA-BINDING SITES, AND MUTAGENESIS OF GLU-258.
DOI=10.1016/S1097-2765(04)00218-7; PubMed=15125839 [NCBI, ExPASy, EBI, Israel, Japan]
Kinebuchi T., Kagawa W., Enomoto R., Tanaka K., Miyagawa K., Shibata T., Kurumizaka H., Yokoyama S.;
"Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1.";
Mol. Cell 14:363-374(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D63882; BAA09932.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D64108; BAA10970.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456486; CAG30372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK292617; BAF85306.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY520538; AAR89915.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022320; CAB45656.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC125163; AAI25164.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC125164; AAI25165.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00031512; -.
PIR S62354; S62354.
RefSeq NP_008999.2; -.
UniGene Hs.339396
3D structure databases
PDB
1V5W; X-ray; 3.20 A; A/B=1-340.[ExPASy / RCSB / EBI]
2ZJB; X-ray; 3.50 A; A/B=1-340.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1V5W; -.
2ZJB; -.
ModBase Q14565.
Protein-protein interaction databases
DIP DIP:24192N; -.
IntAct Q14565; 2.
Organism-specific databases
GeneCards GC22M037239; -.
H-InvDB HIX0027858; -.
HGNC HGNC:2927; DMC1.
GenAtlas DMC1.
HPA CAB015397; -.
HPA001232; -.
MIM 602721; gene. [NCBI / EBI]
PharmGKB PA27377; -.
Gene expression databases
ArrayExpress Q14565; -.
Bgee Q14565; -.
CleanEx HS_DMC1; -.
GermOnline ENSG00000100206; Homo sapiens.
Ontologies
GO
GO:0000794; Cellular component: condensed nuclear chromosome (traceable author statement from ProtInc).
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005524; Molecular function: ATP binding (traceable author statement from ProtInc).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0008094; Molecular function: DNA-dependent ATPase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0007131; Biological process: reciprocal meiotic recombination (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003593; ATPase_AAA+_core.
IPR011940; DMC1_rcmbase.
IPR016467; DNA_repair_recomb_RecA-like.
IPR000445; HhH_motif.
IPR013632; Rad51_C.
IPR001553; RecA_bac.
Graphical view of domain structure.
Pfam PF00633; HHH; 1.
PF08423; Rad51; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005856; Rad51; 1.
SMART SM00382; AAA; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR02238; recomb_DMC1; 1.
PROSITE PS50162; RECA_2; 1.
PS50163; RECA_3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q14565; -.
Genome annotation databases
Ensembl ENSG00000100206; Homo sapiens. [Contig view]
GeneID 11144; -.
KEGG hsa:11144; -.
NMPDR fig|9606.3.peg.21711; -.
Phylogenomic databases
HOGENOM Q14565; -.
HOVERGEN Q14565; -.
OMA Q14565; QLPKEMG.
Other
NextBio 42364; -.
SOURCE DMC1; Homo sapiens.
ProtoNet Q14565.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cell cycle; DNA-binding; Meiosis; Nucleotide-binding; Nucleus; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   340  340     Meiotic recombination protein DMC1/LIM15 homolog. PRO_0000122918
NP_BIND   126   133  8     ATP (Potential). 
BINDING   230   230        ssDNA or dsDNA. 
BINDING   233   233        ssDNA. 
BINDING   236   236        ssDNA or dsDNA. 
BINDING   242   242        ssDNA or dsDNA. 
BINDING   311   311        ssDNA. 
VARIANT   200   200  1     M -> V (in dbSNP:rs2227914 [NCBI]). VAR_018960 
MUTAGEN   258   258        E->A,Q: Decreases octamer stability. 
CONFLICT   37    37        I -> N (in Ref. 2; BAA10970). 
CONFLICT   183   183        A -> P (in Ref. 1; BAA09932). 
STRAND   85    87  3      
HELIX   88    94  7      
HELIX   95    97  3      
HELIX   106   111  6      
STRAND   114   116  3      
STRAND   118   125  8      
HELIX   132   142  11      
TURN   148   150  3      
STRAND   155   163  9      
HELIX   167   176  10      
HELIX   181   186  6      
STRAND   188   192  5      
HELIX   198   212  15      
STRAND   215   223  9      
HELIX   226   228  3      
HELIX   229   232  4      
HELIX   235   237  3      
HELIX   239   260  22      
STRAND   263   268  6      
TURN   292   295  4      
STRAND   296   307  12      
STRAND   310   317  8      
STRAND   326   331  6      
STRAND   334   337  4      
Sequence information
Length: 340 AA [This is the length of the unprocessed precursor] Molecular weight: 37681 Da [This is the MW of the unprocessed precursor] CRC64: 040A6E4CF1FEBFA2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKEDQVVAEE PGFQDEEESL FQDIDLLQKH GINVADIKKL KSVGICTIKG IQMTTRRALC 

        70         80         90        100        110        120 
NVKGLSEAKV DKIKEAANKL IEPGFLTAFE YSEKRKMVFH ITTGSQEFDK LLGGGIESMA 

       130        140        150        160        170        180 
ITEAFGEFRT GKTQLSHTLC VTAQLPGAGG YPGGKIIFID TENTFRPDRL RDIADRFNVD 

       190        200        210        220        230        240 
HDAVLDNVLY ARAYTSEHQM ELLDYVAAKF HEEAGIFKLL IIDSIMALFR VDFSGRGELA 

       250        260        270        280        290        300 
ERQQKLAQML SRLQKISEEY NVAVFVTNQM TADPGATMTF QADPKKPIGG HILAHASTTR 

       310        320        330        340 
ISLRKGRGEL RIAKIYDSPE MPENEATFAI TAGGIGDAKE 

Q14565 in FASTA format

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