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P11474 (ERR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Steroid hormone receptor ERR1
Alternative name(s):
Estrogen receptor-like 1
Estrogen-related receptor alpha
Short name=ERR-alpha
Nuclear receptor subfamily 3 group B member 1
Gene names
Name:ESRRA
Synonyms:ERR1, ESRL1, NR3B1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12

Subunit structure

Binds DNA as a monomer or a homodimer. Interacts (via the AF2 domain) with coactivator PPARGC1A (via the L3 motif); the interaction greatly enhances transriptional activity of genes involved in energy metabolism. Interacts with PIAS4; the interaction enhances sumoylation. Ref.6 Ref.7 Ref.9 Ref.13 Ref.14

Subcellular location

Nucleus Ref.9.

Induction

Induced by PGC1alpha in a number of specific cell types including heart, kidney and muscle. Ref.6

Post-translational modification

Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity. Ref.8 Ref.9

Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4. Sumoylation enhances repression of transcriptional activity, but has no effect on subcellular location nor on DNA binding. Ref.8 Ref.9

Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding. Ref.11

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

The sequence AAB17015.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA35778.1 differs from that shown. Reason: Frameshift at positions 345 and 354.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage development

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

intracellular receptor signaling pathway

Traceable author statement PubMed 9286700. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

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

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.12. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentintercellular bridge

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Traceable author statement PubMed 9286700. Source: ProtInc

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

Traceable author statement PubMed 9286700. Source: ProtInc

protein domain specific binding

Inferred from physical interaction PubMed 11984006. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

steroid binding

Inferred from electronic annotation. Source: InterPro

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

TRRAPQ9Y4A53EBI-372412,EBI-399128

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11474-1)

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 2 (identifier: P11474-2)

The sequence of this isoform differs from the canonical sequence as follows:
     191-191: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423Steroid hormone receptor ERR1
PRO_0000053660

Regions

DNA binding76 – 15176Nuclear receptor Ref.7
Zinc finger79 – 9921NR C4-type
Zinc finger115 – 13420NR C4-type
Region1 – 7676Repressor domain
Region206 – 402197Ligand binding domain
Region403 – 42321AF-2 domain

Sites

Site1241Required for DNA-dependent dimerization

Amino acid modifications

Modified residue191Phosphoserine Ref.8 Ref.9 Ref.10
Modified residue221Phosphoserine Ref.8 Ref.9 Ref.10
Modified residue1291N6-acetyllysine; by PCAF/KAT2B Ref.11
Modified residue1381N6-acetyllysine; by PCAF/KAT2B Ref.11
Modified residue1601N6-acetyllysine; by PCAF/KAT2B Ref.11
Modified residue1621N6-acetyllysine; by PCAF/KAT2B Ref.11
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8 Ref.9
Cross-link403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); partial Ref.8 Ref.9

Natural variations

Alternative sequence1911Missing in isoform 2.
VSP_035756

Experimental info

Mutagenesis141K → R: Some loss of sumoylation. Complete loss of sumoylation; when associated with R-403. Ref.8 Ref.9
Mutagenesis191S → A: 50% loss of phosphorylation but represses transactivation activity in the absence of coactivator. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in response to coactivator; when associated with A-22. Ref.8 Ref.9
Mutagenesis191S → D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-22. Ref.8 Ref.9
Mutagenesis221S → A: 15% loss of phosphorylation but little transactivating activity. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in the presence of coactivator; when associated with A-19. Ref.8 Ref.9
Mutagenesis221S → D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-19. Ref.8 Ref.9
Mutagenesis1181S → A: Binds DNA as a monomer or as a dimer as for wild type. No effect on interaction with PPARGC1A. Ref.7
Mutagenesis1241T → A: Binds DNA predominantly as a monomer. Loss of interaction with PPARGC1A. Ref.7
Mutagenesis1291K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-138, R-160 and R-162. Ref.11
Mutagenesis1381K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-160 and R-162. Ref.11
Mutagenesis1601K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-162. Ref.11
Mutagenesis1621K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-160. Ref.11
Mutagenesis258 – 2625MSVLQ → VSVLE: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. Ref.14
Mutagenesis2591S → H: Little effect on binding L2 of PPARGC1A. Greatly reduced binding to L3 of PPARGC1A. Ref.14
Mutagenesis3151R → A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. Ref.14
Mutagenesis3381D → A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. Ref.14
Mutagenesis3411H → A: Little effect on binding L3 of PPARGC1A. Ref.14
Mutagenesis3431E → A: No effect on binding L3 of PPARGC1A. Ref.14
Mutagenesis4031K → R: Decrease in sumoylation. No effect on transcriptional activity. Complete loss of sumoylation; when associated with R-14. Ref.8 Ref.9
Mutagenesis4131L → A: Loss of coactivation activity; when associated with A-418. Loss of increased response to coactivator; when associated with A-19 and A-418. Ref.8
Mutagenesis4181L → A: Loss of coactivation activity; when associated with A-413. Loss of increased response to coactivator activity; when associated with A-19 and A-413. Ref.8
Mutagenesis421 – 4233Missing: Greatly reduced interaction with L3 motif of PPARGC1A. Less effect on binding to L2 motif of PPARGC1A. Ref.14
Mutagenesis4231D → A: Little effect on binding L3 of PPARGC1A.

Secondary structure

................................ 423
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: BAE62DAF0BE6BA96

FASTA42345,510
        10         20         30         40         50         60 
MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVALAPG PAPTRCLPGH KEEEDGEGAG 

        70         80         90        100        110        120 
PGEQGGGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK AFFKRTIQGS IEYSCPASNE 

       130        140        150        160        170        180 
CEITKRRRKA CQACRFTKCL RVGMLKEGVR LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP 

       190        200        210        220        230        240 
LAVAGGPRKT AAPVNALVSH LLVVEPEKLY AMPDPAGPDG HLPAVATLCD LFDREIVVTI 

       250        260        270        280        290        300 
SWAKSIPGFS SLSLSDQMSV LQSVWMEVLV LGVAQRSLPL QDELAFAEDL VLDEEGARAA 

       310        320        330        340        350        360 
GLGELGAALL QLVRRLQALR LEREEYVLLK ALALANSDSV HIEDAEAVEQ LREALHEALL 

       370        380        390        400        410        420 
EYEAGRAGPG GGAERRRAGR LLLTLPLLRQ TAGKVLAHFY GVKLEGKVPM HKLFLEMLEA 


MMD 

« Hide

Isoform 2 [UniParc].

Checksum: 482E152354383842
Show »

FASTA42245,439

References

« Hide 'large scale' references
[1]"Identification of a new class of steroid hormone receptors."
Giguere V., Yang N., Segui P., Evans R.M.
Nature 331:91-94(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney.
[2]"Estrogen-related receptor, hERR1, modulates estrogen receptor-mediated response of human lactoferrin gene promoter."
Yang N., Shigeta H., Shi H., Teng C.T.
J. Biol. Chem. 271:5795-5804(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Uterus.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"SV40 early-to-late switch involves titration of cellular transcriptional repressors."
Wiley S.R., Kraus R.J., Zuo F., Murray E.E., Loritz K., Mertz J.E.
Genes Dev. 7:2206-2219(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 69-76.
[5]"The orphan nuclear receptor estrogen-related receptor alpha is a transcriptional regulator of the human medium-chain acyl coenzyme A dehydrogenase gene."
Sladek R., Bader J.-A., Giguere V.
Mol. Cell. Biol. 17:5400-5409(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor alpha (ERRalpha)."
Schreiber S.N., Knutti D., Brogli K., Uhlmann T., Kralli A.
J. Biol. Chem. 278:9013-9018(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPARGC1A, INDUCTION, FUNCTION.
[7]"A single nucleotide in an estrogen-related receptor alpha site can dictate mode of binding and peroxisome proliferator-activated receptor gamma coactivator 1alpha activation of target promoters."
Barry J.B., Laganiere J., Giguere V.
Mol. Endocrinol. 20:302-310(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING SPECIFICITY, INTERACTION WITH PPARGC1A, HOMODIMERIZATION, FUNCTION, MUTAGENESIS OF SER-118 AND THR-124.
[8]"Phosphorylation-dependent sumoylation of estrogen-related receptor alpha1."
Vu E.H., Kraus R.J., Mertz J.E.
Biochemistry 46:9795-9804(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND SER-22, FUNCTION, MUTAGENESIS OF LYS-14; SER-19; SER-22; LYS-403; LEU-413 AND LEU-418.
[9]"Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif."
Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.
Mol. Endocrinol. 22:570-584(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND SER-22, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-14; SER-19; SER-22 AND LYS-403.
[10]"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-19 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"An acetylation switch modulates the transcriptional activity of estrogen-related receptor alpha."
Wilson B.J., Tremblay A.M., Deblois G., Sylvain-Drolet G., Giguere V.
Mol. Endocrinol. 24:1349-1358(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-129; LYS-138; LYS-160 AND LYS-162 BY PCAF/KAT2B, MUTAGENESIS OF LYS-129; LYS-138; LYS-160 AND LYS-162, DEACETYLATION BY SIRT1 AND HDAC8.
[12]"Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1 (Perm1) is a tissue-specific regulator of oxidative capacity in skeletal muscle cells."
Cho Y., Hazen B.C., Russell A.P., Kralli A.
J. Biol. Chem. 288:25207-25218(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor alpha (ERRalpha): crystal structure of ERRalpha ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1alpha."
Kallen J., Schlaeppi J.-M., Bitsch F., Filipuzzi I., Schilb A., Riou V., Graham A., Strauss A., Geiser M., Fournier B.
J. Biol. Chem. 279:49330-49337(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 193-423 IN COMPLEX WITH THE L3 SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, HOMODIMERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
[14]"Communication between the ERRalpha homodimer interface and the PGC-1alpha binding surface via the helix 8-9 loop."
Greschik H., Althage M., Flaig R., Sato Y., Chavant V., Peluso-Iltis C., Choulier L., Cronet P., Rochel N., Schuele R., Stroemstedt P.E., Moras D.
J. Biol. Chem. 283:20220-20230(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 180-423 IN COMPLEX WITH THE L3 SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, INTERACTION WITH PPARGC1A, MUTAGENESIS OF 258-MET--GLN-262; SER-259; ARG-315; ASP-338; HIS-341; GLU-343 AND 421-MET--ASP-423.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51416 mRNA. Translation: CAA35778.1. Frameshift.
L38487 mRNA. Translation: AAB17015.1. Different initiation.
AP001453 Genomic DNA. No translation available.
PIRA29345.
RefSeqNP_001269379.1. NM_001282450.1.
NP_001269380.1. NM_001282451.1.
NP_004442.3. NM_004451.4.
UniGeneHs.110849.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XB7X-ray2.50A193-423[»]
2PJLX-ray2.30A/B193-423[»]
3D24X-ray2.11A/C189-423[»]
3K6PX-ray2.00A193-423[»]
ProteinModelPortalP11474.
SMRP11474. Positions 73-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108405. 42 interactions.
DIPDIP-35053N.
IntActP11474. 12 interactions.
MINTMINT-215609.
STRING9606.ENSP00000000442.

Chemistry

BindingDBP11474.
ChEMBLCHEMBL3429.
GuidetoPHARMACOLOGY622.

PTM databases

PhosphoSiteP11474.

Polymorphism databases

DMDM215274146.

Proteomic databases

PaxDbP11474.
PRIDEP11474.

Protocols and materials databases

DNASU2101.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000000442; ENSP00000000442; ENSG00000173153. [P11474-1]
ENST00000405666; ENSP00000384851; ENSG00000173153. [P11474-1]
ENST00000406310; ENSP00000385971; ENSG00000173153. [P11474-2]
GeneID2101.
KEGGhsa:2101.
UCSCuc001nzq.1. human. [P11474-1]
uc001nzr.1. human. [P11474-2]

Organism-specific databases

CTD2101.
GeneCardsGC11P064073.
HGNCHGNC:3471. ESRRA.
HPAHPA053785.
MIM601998. gene.
neXtProtNX_P11474.
PharmGKBPA27887.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282629.
HOGENOMHOG000233467.
HOVERGENHBG108344.
KOK08552.
OMAGPGEQGS.
OrthoDBEOG7288S1.
PhylomeDBP11474.
TreeFamTF323751.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP11474.

Gene expression databases

ArrayExpressP11474.
BgeeP11474.
CleanExHS_ESRRA.
GenevestigatorP11474.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR027289. Oest-rel_rcp.
IPR024178. Oest_rcpt/oest-rel_rcp.
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]
PIRSFPIRSF002527. ER-like_NR. 1 hit.
PIRSF500939. ERR1-2-3. 1 hit.
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11474.
GeneWikiEstrogen-related_receptor_alpha.
GenomeRNAi2101.
NextBio8503.
PROP11474.
SOURCESearch...

Entry information

Entry nameERR1_HUMAN
AccessionPrimary (citable) accession number: P11474
Secondary accession number(s): Q14514
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 162 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 chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM