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Q14565

- DMC1_HUMAN

UniProt

Q14565 - DMC1_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ14565.
CleanExiHS_DMC1.
ExpressionAtlasiQ14565. baseline and differential.
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. 9 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.
GeneTreeiENSGT00760000119398.
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

        10         20         30         40         50
MKEDQVVAEE PGFQDEEESL FQDIDLLQKH GINVADIKKL KSVGICTIKG
60 70 80 90 100
IQMTTRRALC NVKGLSEAKV DKIKEAANKL IEPGFLTAFE YSEKRKMVFH
110 120 130 140 150
ITTGSQEFDK LLGGGIESMA ITEAFGEFRT GKTQLSHTLC VTAQLPGAGG
160 170 180 190 200
YPGGKIIFID TENTFRPDRL RDIADRFNVD HDAVLDNVLY ARAYTSEHQM
210 220 230 240 250
ELLDYVAAKF HEEAGIFKLL IIDSIMALFR VDFSGRGELA ERQQKLAQML
260 270 280 290 300
SRLQKISEEY NVAVFVTNQM TADPGATMTF QADPKKPIGG HILAHASTTR
310 320 330 340
ISLRKGRGEL RIAKIYDSPE MPENEATFAI TAGGIGDAKE
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. [Q14565-2]
NP_008999.2. NM_007068.3. [Q14565-1]
XP_006724173.1. XM_006724110.1. [Q14565-1]
XP_006724175.1. XM_006724112.1. [Q14565-2]
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. [Q14565-2 ]
NP_008999.2. NM_007068.3. [Q14565-1 ]
XP_006724173.1. XM_006724110.1. [Q14565-1 ]
XP_006724175.1. XM_006724112.1. [Q14565-2 ]
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. 9 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.
GeneTreei ENSGT00760000119398.
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

Bgeei Q14565.
CleanExi HS_DMC1.
ExpressionAtlasi Q14565. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 138 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