Q14565 (DMC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Meiotic recombination protein DMC1/LIM15 homolog

Gene names

Name:	DMC1
Synonyms:	DMC1H, LIM15

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks By similarity.
Subunit structure	Interacts with the MND1-PSMC3IP heterodimer By similarity. Double stacked ring-shaped homooctamer. Interacts with BRCA2. Ref.8 Ref.9
Subcellular location	Nucleus Potential. Chromosome By similarity.
Sequence similarities	Belongs to the RecA family. DMC1 subfamily. Contains 1 HhH domain.

Ontologies

Keywords
Biological process	Cell cycle Meiosis
Cellular component	Chromosome Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	female gamete generation Traceable author statement Ref.2. Source: ProtInc male meiosis I Inferred from electronic annotation. Source: Compara oocyte maturation Inferred from electronic annotation. Source: Compara ovarian follicle development Inferred from electronic annotation. Source: Compara pachytene Inferred from electronic annotation. Source: Compara reciprocal meiotic recombination Traceable author statement Ref.2. Source: ProtInc spermatid development Inferred from electronic annotation. Source: Compara spermatogenesis Traceable author statement Ref.1. Source: ProtInc
Cellular_component	chromosome, telomeric region Inferred from electronic annotation. Source: Compara condensed nuclear chromosome Traceable author statement Ref.2. Source: ProtInc
Molecular_function	ATP binding Traceable author statement Ref.2. Source: ProtInc DNA binding Traceable author statement Ref.2. Source: ProtInc DNA-dependent ATPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 340

340

Meiotic recombination protein DMC1/LIM15 homolog

PRO_0000122918

Regions

Nucleotide binding

126 – 133

8

ATP Potential

Sites

Binding site

230

1

ssDNA or dsDNA

Binding site

233

1

ssDNA

Binding site

236

1

ssDNA or dsDNA

Binding site

242

1

ssDNA or dsDNA

Binding site

311

1

ssDNA

Natural variations

Natural variant

150

1

G → D.
Corresponds to variant rs58396845 [ dbSNP | Ensembl ].

VAR_061757

Natural variant

200

1

M → V. Ref.5
Corresponds to variant rs2227914 [ dbSNP | Ensembl ].

VAR_018960

Experimental info

Mutagenesis

258

1

E → A or Q: Decreases octamer stability. Ref.9

Sequence conflict

37

1

I → N in BAA10970. Ref.2

Sequence conflict

183

1

A → P in BAA09932. Ref.1

Secondary structure

1

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340

Helix Strand Turn

Details...

Beta strand

85 – 87

3

Helix

88 – 94

7

Helix

95 – 97

3

Helix

106 – 111

6

Beta strand

114 – 116

3

Beta strand

118 – 125

8

Helix

132 – 142

11

Turn

148 – 150

3

Beta strand

155 – 163

9

Helix

167 – 176

10

Helix

181 – 186

6

Beta strand

188 – 192

5

Helix

198 – 212

15

Beta strand

215 – 223

9

Helix

226 – 228

3

Helix

229 – 232

4

Helix

235 – 237

3

Helix

239 – 260

22

Beta strand

263 – 268

6

Turn

292 – 295

4

Beta strand

296 – 307

12

Beta strand

310 – 317

8

Beta strand

326 – 331

6

Beta strand

334 – 337

4

Sequences

	Sequence		Length	Mass (Da)
	Q14565 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: 040A6E4CF1FEBFA2	FASTA	340	37,681
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]. 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]. Tissue: Testis.
[3]	"A genome annotation-driven approach to cloning the human ORFeome." 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. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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]. Tissue: 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].
[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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D63882 mRNA. Translation: BAA09932.1.
D64108 mRNA. Translation: BAA10970.1.
CR456486 mRNA. Translation: CAG30372.1.
AK292617 mRNA. Translation: BAF85306.1.
AY520538 Genomic DNA. Translation: AAR89915.1.
AL022320 Genomic DNA. Translation: CAB45656.1.
BC125163 mRNA. Translation: AAI25164.1.
BC125164 mRNA. Translation: AAI25165.1.

IPI

IPI00031512.

PIR

S62354.

RefSeq

NP_008999.2. NM_007068.2.

UniGene

Hs.339396.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q14565.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24192N.

IntAct

Q14565. 3 interactions.

MINT

MINT-3029876.

STRING

9606.ENSP00000216024.

PTM databases

PhosphoSite

Q14565.

Polymorphism databases

DMDM

13878923.

Proteomic databases

PaxDb

Q14565.

PRIDE

Q14565.

Protocols and materials databases

DNASU

11144.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216024; ENSP00000216024; ENSG00000100206.

GeneID

11144.

KEGG

hsa:11144.

UCSC

uc003avz.1. human.

Organism-specific databases

CTD

11144.

GeneCards

GC22M038914.

HGNC

HGNC:2927. DMC1.

HPA

CAB015397.
HPA001232.

MIM

602721. gene.

neXtProt

NX_Q14565.

PharmGKB

PA27377.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0468.

HOGENOM

HOG000227426.

HOVERGEN

HBG001504.

InParanoid

Q14565.

KO

K10872.

OMA

FFQDIDL.

OrthoDB

EOG4F7NKC.

PhylomeDB

Q14565.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.

Gene expression databases

ArrayExpress

Q14565.

Bgee

Q14565.

CleanEx

HS_DMC1.

Genevestigator

Q14565.

GermOnline

ENSG00000100206. Homo sapiens.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR011940. DMC1_rcmbase.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR016467. DNA_recomb/repair_RecA-like.
IPR020588. DNA_recomb_RecA/RadB_ATP-bd.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]

Pfam

PF08423. Rad51. 1 hit.
[Graphical view]

PIRSF

PIRSF005856. Rad51. 1 hit.

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF47794. Rad51_N. 1 hit.

TIGRFAMs

TIGR02238. recomb_DMC1. 1 hit.

PROSITE

PS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q14565.

GenomeRNAi

11144.

NextBio

42364.

SOURCE

Search...

Entry information

Entry name

DMC1_HUMAN

Accession

Primary (citable) accession number: Q14565
Secondary accession number(s): A8K9A2 , Q08AI1, Q99498, Q9UH11

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 27, 2001
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.