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Q14995 (NR1D2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. 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:
Nuclear receptor subfamily 1 group D member 2
Alternative name(s):
Orphan nuclear hormone receptor BD73
Rev-erb alpha-related receptor
Short name=RVR
Rev-erb-beta
V-erbA-related protein 1-related
Short name=EAR-1R
Gene names
Name:NR1D2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core clock components BMAL1 and CLOCK. Also regulates genes involved in metabolic functions, including lipid metabolism and the inflammatory response. Acts as a receptor for heme which stimulates its interaction with the NCOR1/HDAC3 corepressor complex, enhancing transcriptional repression. Recognizes two classes of DNA response elements within the promoter of its target genes and can bind to DNA as either monomers or homodimers, depending on the nature of the response element. Binds as a monomer to a response element composed of the consensus half-site motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence (RevRE), or as a homodimer to a direct repeat of the core motif spaced by two nuclegotides (RevDR-2). Acts as a potent competitive repressor of ROR alpha (RORA) function and also negatively regulates the expression of NR1D1. Regulates lipid and energy homeostasis in the skeletal muscle via repression of genes involved in lipid metabolism and myogenesis including: CD36, FABP3, FABP4, UCP3, SCD1 and MSTN. Regulates hepatic lipid metabolism via the repression of APOC3. Represses gene expression at a distance in macrophages by inhibiting the transcription of enhancer-derived RNAs (eRNAs). In addition to its activity as a repressor, can also act as a transcriptional activator. Acts as a transcriptional activator of the sterol regulatory element-binding protein 1 (SREBF1) and the inflammatory mediator interleukin-6 (IL6) in the skeletal muscle. Ref.7 Ref.8

Enzyme regulation

The heme-bound form can bind gaseous signaling molecules such as CO and nitric oxide (NO) and NO can reverse its transcriptional repressor activity. Ref.13

Subunit structure

Binds DNA as a monomer or a homodimer. Interacts with NCOA5 coactivator, leading to a strong increase of transcription of target genes. Interacts (via N-terminus) with KAT5. Interacts (via C-terminus) with HDAC1. Interacts with ZNHIT1. Ref.6 Ref.7 Ref.8

Subcellular location

Nucleus Ref.7 Ref.8.

Tissue specificity

Widely expressed. Expressed at high levels in the liver, adipose tissue, skeletal muscle and brain. Expression oscillates diurnally in the suprachiasmatic nucleus (SCN) of the hypothalamus as well as in peripheral tissues.

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Post-translational modification

Deacetylated by HDAC1. Acetylation and deacetylation regulate its transcriptional regulatory activity. Ref.8

Under more reducing intracellular redox conditions, Cys-384 is in its heme-bound state, which is optimal for recruitment of the NCOR1/HDAC3 corepressor complex and repression of target genes. When subjected to oxidative stress conditions, Cys-384 undergoes oxidation to form a disulfide bridge with Cys-374, also triggering a ligand switch that results in release of bound heme and derepression of target genes.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandDNA-binding
Heme
Iron
Metal-binding
Zinc
   Molecular functionActivator
Receptor
Repressor
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

intracellular receptor signaling pathway

Traceable author statement Ref.5. Source: GOC

lipid homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of energy homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of lipid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of skeletal muscle cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement Ref.5. Source: UniProtKB

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

   Molecular_functioncore promoter sequence-specific DNA binding

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Traceable author statement Ref.5. Source: UniProtKB

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ClockO087852EBI-6144053,EBI-79859From a different organism.
PRMT6Q96LA82EBI-6144053,EBI-912440

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Nuclear receptor subfamily 1 group D member 2
PRO_0000053501

Regions

DNA binding100 – 17677Nuclear receptor
Zinc finger103 – 12321NR C4-type
Zinc finger140 – 16425NR C4-type
Region1 – 9999Modulating
Region124 – 249126Hinge
Region250 – 570321Ligand-binding
Region397 – 579183Interaction with ZNHIT1
Compositional bias13 – 208Poly-Ser
Compositional bias35 – 395Poly-Ser

Sites

Binding site3841Heme
Binding site5681Heme

Amino acid modifications

Modified residue461Phosphoserine; by GSK3-beta By similarity
Modified residue1621N6-acetyllysine; by KAT5 Ref.8
Modified residue1631N6-acetyllysine; by KAT5 Ref.8
Disulfide bond337 ↔ 343 Ref.9
Disulfide bond374 ↔ 384 Ref.9

Natural variations

Natural variant211P → H. Ref.4
Corresponds to variant rs17854365 [ dbSNP | Ensembl ].
VAR_047377
Natural variant2821Q → K. Ref.4
Corresponds to variant rs17857305 [ dbSNP | Ensembl ].
VAR_047378
Natural variant2881P → R. Ref.4
Corresponds to variant rs17857306 [ dbSNP | Ensembl ].
VAR_047379
Natural variant3861L → M. Ref.1 Ref.4 Ref.5
Corresponds to variant rs4858097 [ dbSNP | Ensembl ].
VAR_047380

Experimental info

Sequence conflict519 – 5202IE → NRK in AAA65937. Ref.5

Secondary structure

......................... 579
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14995 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 39BDDCD323BD14BF

FASTA57964,625
        10         20         30         40         50         60 
MEVNAGGVIA YISSSSSASS PASCHSEGSE NSFQSSSSSV PSSPNSSNSD TNGNPKNGDL 

        70         80         90        100        110        120 
ANIEGILKND RIDCSMKTSK SSAPGMTKSH SGVTKFSGMV LLCKVCGDVA SGFHYGVHAC 

       130        140        150        160        170        180 
EGCKGFFRRS IQQNIQYKKC LKNENCSIMR MNRNRCQQCR FKKCLSVGMS RDAVRFGRIP 

       190        200        210        220        230        240 
KREKQRMLIE MQSAMKTMMN SQFSGHLQND TLVEHHEQTA LPAQEQLRPK PQLEQENIKS 

       250        260        270        280        290        300 
SSPPSSDFAK EEVIGMVTRA HKDTFMYNQE QQENSAESMQ PQRGERIPKN MEQYNLNHDH 

       310        320        330        340        350        360 
CGNGLSSHFP CSESQQHLNG QFKGRNIMHY PNGHAICIAN GHCMNFSNAY TQRVCDRVPI 

       370        380        390        400        410        420 
DGFSQNENKN SYLCNTGGRM HLVCPLSKSP YVDPHKSGHE IWEEFSMSFT PAVKEVVEFA 

       430        440        450        460        470        480 
KRIPGFRDLS QHDQVNLLKA GTFEVLMVRF ASLFDAKERT VTFLSGKKYS VDDLHSMGAG 

       490        500        510        520        530        540 
DLLNSMFEFS EKLNALQLSD EEMSLFTAVV LVSADRSGIE NVNSVEALQE TLIRALRTLI 

       550        560        570 
MKNHPNEASI FTKLLLKLPD LRSLNNMHSE ELLAFKVHP 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a novel member of the thyroid/steroid hormone receptor superfamily from human osteoblastic osteosarcoma HOS cell."
Kamizono A., Shuichiro K., Kohei U.
Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-386.
[2]"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].
Tissue: Hippocampus.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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], VARIANTS HIS-21; LYS-282; ARG-288 AND MET-386.
Tissue: Brain.
[5]"A new orphan member of the nuclear hormone receptor superfamily closely related to Rev-Erb."
Dumas B., Harding H.P., Choi H.-S., Lehmann K.A., Chung M., Lazar M.A., Moore D.D.
Mol. Endocrinol. 8:996-1005(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-579, VARIANT MET-386.
Tissue: Peripheral blood lymphocyte.
[6]"CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant."
Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.
Mol. Cell. Biol. 21:343-353(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA5.
[7]"A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with orphan nuclear hormone receptor Rev-erbbeta and removes Rev-erbbeta-induced inhibition of apoCIII transcription."
Wang J., Li Y., Zhang M., Liu Z., Wu C., Yuan H., Li Y.Y., Zhao X., Lu H.
FEBS J. 274:5370-5381(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZNHIT1, SUBCELLULAR LOCATION.
[8]"The orphan nuclear receptor Rev-erbbeta recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter."
Wang J., Liu N., Liu Z., Li Y., Song C., Yuan H., Li Y.Y., Zhao X., Lu H.
Biochim. Biophys. Acta 1783:224-236(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KAT5 AND HDAC1, SUBCELLULAR LOCATION, ACETYLATION AT LYS-162 AND LYS-163.
[9]"Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}."
Gupta N., Ragsdale S.W.
J. Biol. Chem. 286:4392-4403(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: HEME-BINDING, DISULFIDE BONDS.
[10]"REV-ERBs: more than the sum of the individual parts."
Stratmann M., Schibler U.
Cell Metab. 15:791-793(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"REV-ERB-erating nuclear receptor functions in circadian metabolism and physiology."
Ripperger J.A., Albrecht U.
Cell Res. 22:1319-1321(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Structural insight into the constitutive repression function of the nuclear receptor Rev-erbbeta."
Woo E.-J., Jeong D.G., Lim M.-Y., Jun Kim S., Kim K.-J., Yoon S.-M., Park B.-C., Eon Ryu S.
J. Mol. Biol. 373:735-744(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 386-579.
[13]"The structural basis of gas-responsive transcription by the human nuclear hormone receptor REV-ERBbeta."
Pardee K.I., Xu X., Reinking J., Schuetz A., Dong A., Liu S., Zhang R., Tiefenbach J., Lajoie G., Plotnikov A.N., Botchkarev A., Krause H.M., Edwards A.
PLoS Biol. 7:E43-E43(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 381-579, HEME-BINDING, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16815 mRNA. Translation: BAA20088.1.
AK313464 mRNA. Translation: BAG36250.1.
AC124914 Genomic DNA. No translation available.
BC045613 mRNA. Translation: AAH45613.1.
L31785 mRNA. Translation: AAA65937.1.
PIRA57057.
RefSeqNP_005117.3. NM_005126.4.
UniGeneHs.37288.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V0VX-ray2.40A/B/C/D387-579[»]
2V7CX-ray2.40A/B387-579[»]
3CQVX-ray1.90A381-579[»]
ProteinModelPortalQ14995.
SMRQ14995. Positions 98-577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115299. 12 interactions.
IntActQ14995. 7 interactions.
MINTMINT-8417705.
STRING9606.ENSP00000310006.

Chemistry

BindingDBQ14995.
ChEMBLCHEMBL1961784.
GuidetoPHARMACOLOGY597.

PTM databases

PhosphoSiteQ14995.

Polymorphism databases

DMDM215274122.

Proteomic databases

PaxDbQ14995.
PRIDEQ14995.

Protocols and materials databases

DNASU9975.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312521; ENSP00000310006; ENSG00000174738.
GeneID9975.
KEGGhsa:9975.

Organism-specific databases

CTD9975.
GeneCardsGC03P023961.
HGNCHGNC:7963. NR1D2.
HPAHPA053868.
HPA054798.
MIM602304. gene.
neXtProtNX_Q14995.
PharmGKBPA31749.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324222.
HOGENOMHOG000261691.
HOVERGENHBG106790.
InParanoidQ14995.
KOK08531.
OMAPGMTKSH.
OrthoDBEOG776SQ0.
PhylomeDBQ14995.
TreeFamTF328382.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ14995.
BgeeQ14995.
CleanExHS_NR1D2.
GenevestigatorQ14995.

Family and domain databases

Gene3D1.10.565.10. 3 hits.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14995.
GeneWikiRev-ErbA_beta.
GenomeRNAi9975.
NextBio37672.
PROQ14995.
SOURCESearch...

Entry information

Entry nameNR1D2_HUMAN
AccessionPrimary (citable) accession number: Q14995
Secondary accession number(s): B2R8Q3, O00402, Q86XD4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 3 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 3

Human chromosome 3: entries, gene names and cross-references to MIM