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P43351 (RAD52_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD52 homolog
Gene names
Name:RAD52
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase. Ref.9

Subunit structure

The full-length protein forms heptameric rings. Interacts with ABL1. Ref.9 Ref.12

Subcellular location

Nucleus Potential.

Post-translational modification

Phosphorylated upon DNA damage by ABL1, and probably by ATM or ATR. Ref.9

Sequence similarities

Belongs to the RAD52 family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform alpha (identifier: P43351-1)

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.
Isoform beta (identifier: P43351-2)

The sequence of this isoform differs from the canonical sequence as follows:
     157-226: SFGNALGNCI...PQLQQVTSPS → LPLLGVSGRI...SGQRLPEITK
     227-418: Missing.
Note: Unable to interact with isoform alpha, may act as dominant negative.
Isoform gamma (identifier: P43351-3)

The sequence of this isoform differs from the canonical sequence as follows:
     117-139: DGSYHEDVGYGVSEGLKSKALSL → VRGWSRPAARKDQWVVGEGWFIS
     140-418: Missing.
Note: Unable to interact with isoform alpha, may act as dominant negative.
Isoform delta (identifier: P43351-4)

The sequence of this isoform differs from the canonical sequence as follows:
     94-118: DFVDLNNGKFYVGVCAFVRVQLKDG → GEYALQQWGLLHCPAPAESLLWVRR
     119-418: Missing.
Note: Unable to interact with isoform alpha, may act as dominant negative.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418DNA repair protein RAD52 homolog
PRO_0000173881

Regions

DNA binding152 – 1565 Ref.12

Amino acid modifications

Modified residue1041Phosphotyrosine; by ABL1 Ref.9
Modified residue1991Phosphoserine Ref.11
Modified residue3181Phosphothreonine Ref.10
Modified residue3351Phosphothreonine Ref.11

Natural variations

Alternative sequence94 – 11825DFVDL…QLKDG → GEYALQQWGLLHCPAPAESL LWVRR in isoform delta.
VSP_047749
Alternative sequence117 – 13923DGSYH…KALSL → VRGWSRPAARKDQWVVGEGW FIS in isoform gamma.
VSP_047750
Alternative sequence119 – 418300Missing in isoform delta.
VSP_047751
Alternative sequence140 – 418279Missing in isoform gamma.
VSP_047752
Alternative sequence157 – 22670SFGNA…VTSPS → LPLLGVSGRILYSLFSVHSV MCAGGLPTPTASAQTAPSSP CSSAVLRYAQEFWECTWKLY SGQRLPEITK in isoform beta.
VSP_047753
Alternative sequence227 – 418192Missing in isoform beta.
VSP_047754
Natural variant701R → W. Ref.6
Corresponds to variant rs11571421 [ dbSNP | Ensembl ].
VAR_019218
Natural variant2211Q → E. Ref.6
Corresponds to variant rs4987206 [ dbSNP | Ensembl ].
VAR_019219
Natural variant2871S → N. Ref.6
Corresponds to variant rs11571463 [ dbSNP | Ensembl ].
VAR_019220

Experimental info

Mutagenesis551R → A: Abolishes ssDNA-binding. Ref.12
Mutagenesis651Y → A: Moderately defective in both ss and dsDNA-binding. Ref.12
Mutagenesis1521K → A: Abolishes ssDNA-binding. Ref.12
Mutagenesis1531R → A: Moderately defective in both ss and dsDNA-binding. Ref.12
Mutagenesis1561R → A: Moderately defective in both ss and dsDNA-binding. Ref.12
Sequence conflict1001N → K in AAA87554. Ref.3
Sequence conflict4181S → SY in AAA87554. Ref.3

Secondary structure

............................... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform alpha [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7E1BBCAF0B9CD4AF

FASTA41846,169
        10         20         30         40         50         60 
MSGTEEAILG GRDSHPAAGG GSVLCFGQCQ YTAEEYQAIQ KALRQRLGPE YISSRMAGGG 

        70         80         90        100        110        120 
QKVCYIEGHR VINLANEMFG YNGWAHSITQ QNVDFVDLNN GKFYVGVCAF VRVQLKDGSY 

       130        140        150        160        170        180 
HEDVGYGVSE GLKSKALSLE KARKEAVTDG LKRALRSFGN ALGNCILDKD YLRSLNKLPR 

       190        200        210        220        230        240 
QLPLEVDLTK AKRQDLEPSV EEARYNSCRP NMALGHPQLQ QVTSPSRPSH AVIPADQDCS 

       250        260        270        280        290        300 
SRSLSSSAVE SEATHQRKLR QKQLQQQFRE RMEKQQVRVS TPSAEKSEAA PPAPPVTHST 

       310        320        330        340        350        360 
PVTVSEPLLE KDFLAGVTQE LIKTLEDNSE KWAVTPDAGD GVVKPSSRAD PAQTSDTLAL 

       370        380        390        400        410 
NNQMVTQNRT PHSVCHQKPQ AKSGSWDLQT YSADQRTTGN WESHRKSQDM KKRKYDPS 

« Hide

Isoform beta [UniParc].

Checksum: 8B0E3FC5773B46FE
Show »

FASTA22624,540
Isoform gamma [UniParc].

Checksum: DFA2F7994CACC1DF
Show »

FASTA13915,350
Isoform delta [UniParc].

Checksum: C3341B828BE835A5
Show »

FASTA11812,943

References

« Hide 'large scale' references
[1]"The human and mouse homologs of the yeast RAD52 gene: cDNA cloning, sequence analysis, assignment to human chromosome 12p12.2-p13, and mRNA expression in mouse tissues."
Shen Z., Denison K., Lobb R., Gatewood J.M., Chen D.J.
Genomics 25:199-206(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
[2]"Cloning of human and mouse genes homologous to RAD52, a yeast gene involved in DNA repair and recombination."
Muris D.F., Bezzubova O., Buerstedde J.-M., Vreeken K., Balajee A.S., Osgood C.J., Troelstra C., Hoeijmakers J.H., Ostermann K., Schmidt H., Natarajan A.T., Eeken J.C.J., Lohman P.H.M., Pastink A.
Mutat. Res. 315:295-305(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Tissue: Testis.
[3]"Expression of human RAD52 confers resistance to ionizing radiation in mammalian cells."
Park M.S.
J. Biol. Chem. 270:15467-15470(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Tissue: Spleen.
[4]"Identification of novel isoforms of human RAD52."
Kito K., Wada H., Yeh E.T., Kamitani T.
Biochim. Biophys. Acta 1489:303-314(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA; GAMMA AND DELTA), ALTERNATIVE SPLICING.
Tissue: Testis.
[5]"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. expand/collapse author list , 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 GAMMA AND DELTA).
Tissue: Amygdala and Synovium.
[6]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-70; GLU-221 AND ASN-287.
[7]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation."
Kitao H., Yuan Z.M.
J. Biol. Chem. 277:48944-48948(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-104.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND THR-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form."
Kagawa W., Kurumizaka H., Ishitani R., Fukai S., Nureki O., Shibata T., Yokoyama S.
Mol. Cell 10:359-371(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-212, SUBUNIT, DNA-BINDING REGION, MUTAGENESIS OF ARG-55; TYR-65; LYS-152; ARG-153 AND ARG-156.
[13]"Structure of the single-strand annealing domain of human RAD52 protein."
Singleton M.R., Wentzell L.M., Liu Y., West S.C., Wigley D.B.
Proc. Natl. Acad. Sci. U.S.A. 99:13492-13497(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-209.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12134 mRNA. Translation: AAA85793.1.
L33262 mRNA. Translation: AAB05203.1.
U27516 mRNA. Translation: AAA87554.1.
AF125948 mRNA. Translation: AAD24575.1.
AF125949 mRNA. Translation: AAD24576.1.
AF125950 mRNA. Translation: AAD24577.1.
AK292160 mRNA. Translation: BAF84849.1.
AK312026 mRNA. Translation: BAG34963.1.
AY527412 Genomic DNA. Translation: AAS00097.1.
AC004803 Genomic DNA. No translation available.
CH471116 Genomic DNA. Translation: EAW88943.1.
CH471116 Genomic DNA. Translation: EAW88945.1.
CH471116 Genomic DNA. Translation: EAW88946.1.
CH471116 Genomic DNA. Translation: EAW88949.1.
PIRA57518.
RefSeqNP_602296.2. NM_134424.2.
XP_005253777.1. XM_005253720.2.
XP_005253778.1. XM_005253721.1.
XP_005253784.1. XM_005253727.2.
UniGeneHs.410355.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2IX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V1-209[»]
1KN0X-ray2.85A/B/C/D/E/F/G/H/I/J/K1-212[»]
DisProtDP00437.
ProteinModelPortalP43351.
SMRP43351. Positions 24-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111830. 39 interactions.
DIPDIP-333N.
IntActP43351. 28 interactions.
MINTMINT-2803258.
STRING9606.ENSP00000351284.

Chemistry

ChEMBLCHEMBL2362978.

PTM databases

PhosphoSiteP43351.

Polymorphism databases

DMDM1172823.

Proteomic databases

PaxDbP43351.
PRIDEP43351.

Protocols and materials databases

DNASU5893.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358495; ENSP00000351284; ENSG00000002016. [P43351-1]
ENST00000430095; ENSP00000387901; ENSG00000002016. [P43351-1]
ENST00000461568; ENSP00000436008; ENSG00000002016. [P43351-3]
ENST00000468231; ENSP00000434703; ENSG00000002016. [P43351-3]
ENST00000541619; ENSP00000438965; ENSG00000002016. [P43351-4]
ENST00000544742; ENSP00000443254; ENSG00000002016. [P43351-4]
ENST00000545564; ENSP00000440268; ENSG00000002016. [P43351-2]
GeneID5893.
KEGGhsa:5893.
UCSCuc001qis.1. human. [P43351-1]

Organism-specific databases

CTD5893.
GeneCardsGC12M001021.
HGNCHGNC:9824. RAD52.
MIM600392. gene.
neXtProtNX_P43351.
PharmGKBPA34180.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5055.
HOGENOMHOG000237354.
HOVERGENHBG054676.
InParanoidP43351.
KOK10873.
OMAQARYSSC.
OrthoDBEOG74XS87.
PhylomeDBP43351.
TreeFamTF101221.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressP43351.
BgeeP43351.
CleanExHS_RAD52.
GenevestigatorP43351.

Family and domain databases

InterProIPR004585. DNA_recomb/repair_Rad52.
IPR007232. Rad52_Rad22.
[Graphical view]
PANTHERPTHR12132. PTHR12132. 1 hit.
PfamPF04098. Rad52_Rad22. 1 hit.
[Graphical view]
TIGRFAMsTIGR00607. rad52. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRAD52. human.
EvolutionaryTraceP43351.
GeneWikiRAD52.
GenomeRNAi5893.
NextBio22926.
PROP43351.
SOURCESearch...

Entry information

Entry nameRAD52_HUMAN
AccessionPrimary (citable) accession number: P43351
Secondary accession number(s): Q13205 expand/collapse secondary AC list , Q9Y5T7, Q9Y5T8, Q9Y5T9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM