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P25490 (TYY1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional repressor protein YY1
Alternative name(s):
Delta transcription factor
INO80 complex subunit S
NF-E1
Yin and yang 1
Short name=YY-1
Gene names
Name:YY1
Synonyms:INO80S
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Ref.10 Ref.11

Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements. Ref.10 Ref.11

Subunit structure

Interacts with YAF2 through the region encompassing the first and second zinc fingers. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Interacts with EED and EZH2; the interactions are indicative for an association with the PRC2/EED-EZH2 complex. Interacts with SFMBT2. Ref.6 Ref.8 Ref.10 Ref.11 Ref.13 Ref.20 Ref.22

Subcellular location

Nucleus matrix. Note: Associated with the nuclear matrix. Ref.5 Ref.11 Ref.22

Post-translational modification

Transiently poly-ADP-ribosylated by PARP1 upon DNA damage, with the effect of decreasing affinity of YY1 to its cognate DNA binding sites.

Ubiquitinated. Ref.17

Sequence similarities

Belongs to the YY transcription factor family.

Contains 4 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processDifferentiation
DNA damage
DNA recombination
DNA repair
Spermatogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMADP-ribosylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA localization

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cellular response to UV

Inferred from mutant phenotype Ref.11. Source: UniProtKB

chromosome organization

Inferred from electronic annotation. Source: Ensembl

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 9857059. Source: MGI

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

response to UV-C

Inferred from mutant phenotype Ref.11. Source: UniProtKB

response to prostaglandin F

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentIno80 complex

Inferred from direct assay Ref.11Ref.20. Source: UniProtKB

PcG protein complex

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 21729784. Source: MGI

RNA binding

Inferred from direct assay PubMed 21729784. Source: MGI

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from sequence or structural similarity. Source: BHF-UCL

four-way junction DNA binding

Inferred from direct assay Ref.11. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.2. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.2. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.1. Source: ProtInc

transcription regulatory region DNA binding

Inferred from direct assay PubMed 9857059. Source: MGI

zinc ion binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Transcriptional repressor protein YY1
PRO_0000047190

Regions

Zinc finger296 – 32025C2H2-type 1
Zinc finger325 – 34723C2H2-type 2
Zinc finger353 – 37725C2H2-type 3
Zinc finger383 – 40725C2H2-type 4
Region257 – 34185Involved in nuclear matrix association
Region333 – 37139Involved in repression of activated transcription
Region371 – 39727Involved in masking transactivation domain
Compositional bias43 – 5311Asp/Glu-rich (acidic)
Compositional bias54 – 6916Gly-rich
Compositional bias70 – 8011Poly-His
Compositional bias159 – 17012Gly/Ser-rich

Sites

Metal binding2981Zinc 1
Metal binding3031Zinc 1
Metal binding3161Zinc 1
Metal binding3201Zinc 1
Metal binding3271Zinc 2
Metal binding3301Zinc 2
Metal binding3431Zinc 2
Metal binding3471Zinc 2
Metal binding3551Zinc 3
Metal binding3601Zinc 3
Metal binding3731Zinc 3
Metal binding3771Zinc 3
Metal binding3851Zinc 4
Metal binding3901Zinc 4
Metal binding4031Zinc 4
Metal binding4071Zinc 4

Amino acid modifications

Modified residue1181Phosphoserine Ref.16 Ref.18 Ref.21
Modified residue2471Phosphoserine Ref.12 Ref.14 Ref.16
Modified residue3781Phosphothreonine Ref.14

Natural variations

Natural variant3801D → Y De novo variant found in a patient with mental retardation. Ref.25
VAR_065086

Experimental info

Sequence conflict651H → R in AAA59926. Ref.2
Sequence conflict1961G → R in AAA59467. Ref.1

Secondary structure

........................ 414
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25490 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 058C05A0AD2D04E6

FASTA41444,713
        10         20         30         40         50         60 
MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEEEDDD DEDGGGGDHG 

        70         80         90        100        110        120 
GGGGHGHAGH HHHHHHHHHH PPMIALQPLV TDDPTQVHHH QEVILVQTRE EVVGGDDSDG 

       130        140        150        160        170        180 
LRAEDGFEDQ ILIPVPAPAG GDDDYIEQTL VTVAAAGKSG GGGSSSSGGG RVKKGGGKKS 

       190        200        210        220        230        240 
GKKSYLSGGA GAAGGGGADP GNKKWEQKQV QIKTLEGEFS VTMWSSDEKK DIDHETVVEE 

       250        260        270        280        290        300 
QIIGENSPPD YSEYMTGKKL PPGGIPGIDL SDPKQLAEFA RMKPRKIKED DAPRTIACPH 

       310        320        330        340        350        360 
KGCTKMFRDN SAMRKHLHTH GPRVHVCAEC GKAFVESSKL KRHQLVHTGE KPFQCTFEGC 

       370        380        390        400        410 
GKRFSLDFNL RTHVRIHTGD RPYVCPFDGC NKKFAQSTNL KSHILTHAKA KNNQ 

« Hide

References

« Hide 'large scale' references
[1]"Transcriptional repression by YY1, a human GLI-Kruppel-related protein, and relief of repression by adenovirus E1A protein."
Shi Y., Seto E., Chang L.-S., Shenk T.
Cell 67:377-388(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Isolation of a candidate repressor/activator, NF-E1 (YY-1, delta), that binds to the immunoglobulin kappa 3' enhancer and the immunoglobulin heavy-chain mu E1 site."
Park K., Atchison M.
Proc. Natl. Acad. Sci. U.S.A. 88:9804-9808(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Foreskin.
[3]Whitson R.H., Huang T., Dang J., Itakura K.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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].
Tissue: Brain and Lymph.
[5]"Targeting of the YY1 transcription factor to the nucleolus and the nuclear matrix in situ: the C-terminus is a principal determinant for nuclear trafficking."
McNeil S., Guo B., Stein J.L., Lian J.B., Bushmeyer S., Seto E., Atchison M.L., Penman S., van Wijnen A.J., Stein G.S.
J. Cell. Biochem. 68:500-510(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1."
Kalenik J.L., Chen D., Bradley M.E., Chen S.-J., Lee T.-C.
Nucleic Acids Res. 25:843-849(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YAF2.
[7]"Poly(ADP-ribosyl)ation of transcription factor Yin Yang 1 under conditions of DNA damage."
Oei S.L., Shi Y.
Biochem. Biophys. Res. Commun. 285:27-31(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POLY-ADP-RIBOSYLATION BY PARP1.
[8]"The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos."
Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.
Mol. Cell. Biol. 21:1360-1369(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EZH2 AND EZH2.
[9]"Transcription factor YY1: structure, function, and therapeutic implications in cancer biology."
Gordon S., Akopyan G., Garban H., Bonavida B.
Oncogene 25:1125-1142(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[10]"YY1 functions with INO80 to activate transcription."
Cai Y., Jin J., Yao T., Gottschalk A.J., Swanson S.K., Wu S., Shi Y., Washburn M.P., Florens L., Conaway R.C., Conaway J.W.
Nat. Struct. Mol. Biol. 14:872-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX.
[11]"A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR, SUBCELLULAR LOCATION, DNA-BINDING, PROTEIN INTERACTION, IDENTIFICATION IN THE INO80 COMPLEX.
[12]"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-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"YY1's longer DNA-binding motifs."
Kim J., Kim J.
Genomics 93:152-158(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING MOTIF.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Development and validation of a method for profiling post-translational modification activities using protein microarrays."
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Regulation of DU145 prostate cancer cell growth by Scm-like with four mbt domains 2."
Lee K., Na W., Maeng J.H., Wu H., Ju B.G.
J. Biosci. 38:105-112(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SFMBT2, SUBCELLULAR LOCATION.
[23]"Cocrystal structure of YY1 bound to the adeno-associated virus P5 initiator."
Houbaviy H.B., Usheva A., Shenk T., Burley S.K.
Proc. Natl. Acad. Sci. U.S.A. 93:13577-13582(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 304-414.
[24]"Design, synthesis and structure of a zinc finger with an artificial beta-turn."
Viles J.H., Patel S.U., Mitchell J.B.O., Moody C.M., Justice D.E., Uppenbrink J., Doyle P.M., Harris C.J., Sadler P.J., Thornton J.M.
J. Mol. Biol. 279:973-986(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 353-379.
[25]"A de novo paradigm for mental retardation."
Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M., de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M., van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.
Nat. Genet. 42:1109-1112(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TYR-380.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77698 mRNA. Translation: AAA59467.1.
M76541 mRNA. Translation: AAA59926.1.
Z14077 mRNA. Translation: CAA78455.1.
BC037308 mRNA. Translation: AAH37308.1.
BC065366 mRNA. Translation: AAH65366.1.
PIRA40350.
RefSeqNP_003394.1. NM_003403.4.
UniGeneHs.388927.
Hs.603118.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UBDX-ray2.50C293-414[»]
1ZNMNMR-A352-379[»]
4C5IX-ray2.59C199-228[»]
ProteinModelPortalP25490.
SMRP25490. Positions 200-227, 295-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113360. 116 interactions.
DIPDIP-150N.
IntActP25490. 41 interactions.
MINTMINT-157439.
STRING9606.ENSP00000262238.

PTM databases

PhosphoSiteP25490.

Polymorphism databases

DMDM3915889.

Proteomic databases

PaxDbP25490.
PeptideAtlasP25490.
PRIDEP25490.

Protocols and materials databases

DNASU7528.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262238; ENSP00000262238; ENSG00000100811.
GeneID7528.
KEGGhsa:7528.
UCSCuc001ygy.2. human.

Organism-specific databases

CTD7528.
GeneCardsGC14P101161.
HGNCHGNC:12856. YY1.
HPACAB009392.
HPA001119.
MIM600013. gene.
neXtProtNX_P25490.
PharmGKBPA37445.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000008232.
HOVERGENHBG006823.
InParanoidP25490.
KOK09201.
OMADIDHESV.
PhylomeDBP25490.
TreeFamTF106493.

Enzyme and pathway databases

SignaLinkP25490.

Gene expression databases

ArrayExpressP25490.
BgeeP25490.
CleanExHS_YY1.
GenevestigatorP25490.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR017114. TF_Yin_yang.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
PIRSFPIRSF037113. TF_Yin_yang. 1 hit.
SMARTSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSYY1. human.
EvolutionaryTraceP25490.
GeneWikiYY1.
GenomeRNAi7528.
NextBio29449.
PMAP-CutDBP25490.
PROP25490.
SOURCESearch...

Entry information

Entry nameTYY1_HUMAN
AccessionPrimary (citable) accession number: P25490
Secondary accession number(s): Q14935
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 164 of the entry and version 2 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 14

Human chromosome 14: entries, gene names and cross-references to MIM