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Q15672 (TWST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Twist-related protein 1
Alternative name(s):
Class A basic helix-loop-helix protein 38
Short name=bHLHa38
H-twist
Gene names
Name:TWIST1
Synonyms:BHLHA38, TWIST
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer By similarity. Ref.8

Subunit structure

Efficient DNA binding requires dimerization with another bHLH protein. Homodimer or heterodimer with E proteins such as TCF3. ID1 binds preferentially to TCF3 but does not interact efficiently with TWIST1 so ID1 levels control the amount of TCF3 available to dimerize with TWIST1 and thus determine the type of dimer formed By similarity.

Subcellular location

Nucleus.

Tissue specificity

Subset of mesodermal cells.

Involvement in disease

Saethre-Chotzen syndrome (SCS) [MIM:101400]: A craniosynostosis syndrome characterized by coronal synostosis, brachycephaly, low frontal hairline, facial asymmetry, hypertelorism, broad halluces, and clinodactyly.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.9 Ref.10

Robinow-Sorauf syndrome (RSS) [MIM:180750]: An autosomal dominant syndrome characterized by craniosynostosis, asymmetry of orbits, flat face, hypertelorism, a thin, long, and pointed nose, shallow orbits, strabismus, and broad great toes with a duplication of the distal phalanx. RSS is clinically similar to Saethre-Chotzen syndrome, with the most characteristic additional feature in Robinow-Sorauf syndrome being a bifid or partially duplicated hallux.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Craniosynostosis 1 (CRS1) [MIM:123100]: A primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processBiological rhythms
Differentiation
Myogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseCraniosynostosis
Disease mutation
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
Repressor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaortic valve morphogenesis

Inferred from mutant phenotype PubMed 20804746. Source: BHF-UCL

cardiac neural crest cell migration involved in outflow tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell proliferation involved in heart valve development

Inferred from mutant phenotype PubMed 20804746. Source: BHF-UCL

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from mutant phenotype PubMed 18297062. Source: BHF-UCL

cranial suture morphogenesis

Traceable author statement PubMed 11001584. Source: BHF-UCL

embryonic camera-type eye formation

Inferred from mutant phenotype PubMed 17070479. Source: BHF-UCL

embryonic cranial skeleton morphogenesis

Inferred from mutant phenotype Ref.3Ref.9. Source: BHF-UCL

embryonic digit morphogenesis

Traceable author statement PubMed 11001584. Source: BHF-UCL

embryonic forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

endocardial cushion morphogenesis

Inferred from electronic annotation. Source: Ensembl

eyelid development in camera-type eye

Inferred from mutant phenotype PubMed 17070479. Source: BHF-UCL

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

mitral valve morphogenesis

Inferred from electronic annotation. Source: Ensembl

muscle organ development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype PubMed 17690110. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cellular senescence

Inferred from mutant phenotype PubMed 17690110. Source: BHF-UCL

negative regulation of double-strand break repair

Inferred from mutant phenotype PubMed 17690110. Source: BHF-UCL

negative regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone phosphorylation

Inferred from mutant phenotype PubMed 17690110. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 16888803. Source: BHF-UCL

negative regulation of oxidative phosphorylation uncoupler activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype PubMed 17003487. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17690110. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

odontogenesis

Inferred from electronic annotation. Source: Ensembl

ossification

Traceable author statement PubMed 11001584. Source: BHF-UCL

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

outer ear morphogenesis

Traceable author statement PubMed 11001584. Source: BHF-UCL

palate development

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Non-traceable author statement PubMed 17987801. Source: BHF-UCL

positive regulation of cell motility

Inferred from mutant phenotype PubMed 17332325. Source: BHF-UCL

positive regulation of endocardial cushion to mesenchymal transition involved in heart valve formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 18297062. Source: BHF-UCL

positive regulation of fatty acid beta-oxidation

Inferred from mutant phenotype PubMed 20007935. Source: BHF-UCL

positive regulation of gene expression

Inferred from mutant phenotype PubMed 17003487. Source: BHF-UCL

positive regulation of interleukin-6 secretion

Inferred from mutant phenotype PubMed 20007935. Source: BHF-UCL

positive regulation of monocyte chemotactic protein-1 production

Inferred from mutant phenotype PubMed 20007935. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17332325. Source: BHF-UCL

positive regulation of transcription regulatory region DNA binding

Inferred from mutant phenotype PubMed 12270142. Source: BHF-UCL

positive regulation of tumor necrosis factor production

Inferred from mutant phenotype PubMed 20007935. Source: BHF-UCL

regulation of bone mineralization

Inferred from mutant phenotype PubMed 19597909. Source: BHF-UCL

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17332325. Source: GOC

   Cellular_componentnucleus

Inferred from direct assay PubMed 15545268. Source: UniProtKB

   Molecular_functionE-box binding

Inferred from direct assay PubMed 17332325PubMed 20804746. Source: BHF-UCL

bHLH transcription factor binding

Inferred from physical interaction PubMed 10749989. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 18504427PubMed 18598946PubMed 21983900PubMed 22975381. Source: IntAct

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 17332325. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction PubMed 15545268. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202Twist-related protein 1
PRO_0000127483

Regions

Domain108 – 15952bHLH
Region161 – 19131Sufficient for transactivation activity By similarity
Compositional bias80 – 9819Gly-rich

Natural variations

Natural variant311S → G.
Corresponds to variant rs1800126 [ dbSNP | Ensembl ].
VAR_014821
Natural variant841G → S.
Corresponds to variant rs2234705 [ dbSNP | Ensembl ].
VAR_014822
Natural variant1191Q → P in SCS. Ref.3
VAR_004495
Natural variant1311L → P in SCS. Ref.9
VAR_004496
Natural variant1351I → IAALRKII in SCS.
VAR_004497
Natural variant1391P → PKIIPTLP in SCS.
VAR_004498
Natural variant1561I → V in SCS; variant form with features overlapping Baller-Gerold syndrome. Ref.10
VAR_015219
Natural variant1861A → T in CRS1. Ref.11
VAR_034985
Natural variant1881S → L in CRS1. Ref.11
VAR_034986

Experimental info

Sequence conflict321G → A in CAA67664. Ref.2
Sequence conflict361G → A in CAA67664. Ref.2
Sequence conflict411S → T in CAA62850. Ref.1
Sequence conflict411S → T in CAA71821. Ref.4
Sequence conflict451S → T in CAA62850. Ref.1
Sequence conflict451S → T in CAA71821. Ref.4
Sequence conflict561Missing in CAA62850. Ref.1
Sequence conflict561Missing in CAA71821. Ref.4
Sequence conflict591G → A in CAA67664. Ref.2
Sequence conflict921G → GGGGG in CAA67664. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q15672 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 9394E4351BA1D081

FASTA20220,954
        10         20         30         40         50         60 
MMQDVSSSPV SPADDSLSNS EEEPDRQQPP SGKRGGRKRR SSRRSAGGGA GPGGAAGGGV 

        70         80         90        100        110        120 
GGGDEPGSPA QGKRGKKSAG CGGGGGAGGG GGSSSGGGSP QSYEELQTQR VMANVRERQR 

       130        140        150        160        170        180 
TQSLNEAFAA LRKIIPTLPS DKLSKIQTLK LAARYIDFLY QVLQSDELDS KMASCSYVAH 

       190        200 
ERLSYAFSVW RMEGAWSMSA SH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the human twist gene: its expression is retained in adult mesodermally-derived tissues."
Wang S.M., Coljee V.W., Pignolo R.J., Rotenberg M.O., Cristofalo V.J., Sierra F.
Gene 187:83-92(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[2]"The human H-twist gene is located at 7p21 and encodes a B-HLH protein that is 96% similar to its murine M-twist counterpart."
Bourgeois P., Stoetzel C., Bolcato-Bellemin A.-L., Mattei M.-G., Perrin-Schmitt F.
Mamm. Genome 7:915-917(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"Mutations in TWIST, a basic helix-loop-helix transcription factor, in Saethre-Chotzen syndrome."
Howard T.D., Paznekas W.A., Green E.D., Chiang L.C., Ma N., Ortiz de Luna R.I., Delgado C.G., Gonzalez-Ramos M., Kline A.D., Jabs E.W.
Nat. Genet. 15:36-41(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SCS PRO-119; ALA-ALA-LEU-ARG-LYS-ILE-ILE-135 INS AND LYS-ILE-ILE-PRO-THR-LEU-PRO-139 INS.
[4]"Translocation breakpoint maps 5 kb 3-prime from TWIST in a patient affected with Saethre-Chotzen syndrome."
Krebs I., Weis I., Hudler M., Rommens J.M., Roth H., Scherer S.W., Tsui L.-C., Fuchtbauer E.-M., Grzeschik K.-H., Tsuji K., Kunz J.
Hum. Mol. Genet. 6:1079-1086(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [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].
Tissue: Brain.
[8]"Twist regulates cytokine gene expression through a negative feedback loop that represses NF-kappaB activity."
Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N.
Cell 112:169-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Mutations of the TWIST gene in the Saethre-Chotzen syndrome."
el Ghouzzi V., le Merrer M., Perrin-Schmitt F., Lajeunie E., Benit P., Renier D., Bourgeois P., Bolcato-Bellemin A.-L., Munnich A., Bonaventure J.
Nat. Genet. 15:42-46(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCS PRO-131 AND LYS-ILE-ILE-PRO-THR-LEU-PRO-139 INS.
[10]"Another TWIST on Baller-Gerold syndrome."
Seto M.L., Lee S.J., Sze R.W., Cunningham M.L.
Am. J. Med. Genet. 104:323-330(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCS VAL-156.
[11]"Isolated sagittal and coronal craniosynostosis associated with TWIST box mutations."
Seto M.L., Hing A.V., Chang J., Hu M., Kapp-Simon K.A., Patel P.K., Burton B.K., Kane A.A., Smyth M.D., Hopper R., Ellenbogen R.G., Stevenson K., Speltz M.L., Cunningham M.L.
Am. J. Med. Genet. A 143:678-686(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CRS1 THR-186 AND LEU-188.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91662 Genomic DNA. Translation: CAA62850.1.
X99268 mRNA. Translation: CAA67664.1.
U80998 Genomic DNA. Translation: AAC50930.1.
Y10871 Genomic DNA. Translation: CAA71821.1.
AC003986 Genomic DNA. Translation: AAC60381.2.
CH236948 Genomic DNA. Translation: EAL24279.1.
BC036704 mRNA. Translation: AAH36704.1.
CCDSCCDS5367.1.
PIRG01204.
RefSeqNP_000465.1. NM_000474.3.
XP_006715832.1. XM_006715769.1.
UniGeneHs.644998.
Hs.66744.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MJVNMR-A68-79[»]
ProteinModelPortalQ15672.
SMRQ15672. Positions 109-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113142. 21 interactions.
IntActQ15672. 12 interactions.
MINTMINT-8309513.
STRING9606.ENSP00000242261.

PTM databases

PhosphoSiteQ15672.

Polymorphism databases

DMDM2498009.

Proteomic databases

PaxDbQ15672.
PRIDEQ15672.

Protocols and materials databases

DNASU7291.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242261; ENSP00000242261; ENSG00000122691.
GeneID7291.
KEGGhsa:7291.
UCSCuc003sum.3. human.

Organism-specific databases

CTD7291.
GeneCardsGC07M019121.
GeneReviewsTWIST1.
HGNCHGNC:12428. TWIST1.
MIM101400. phenotype.
123100. phenotype.
180750. phenotype.
601622. gene.
neXtProtNX_Q15672.
Orphanet35099. Isolated brachycephaly.
35093. Isolated scaphocephaly.
794. Saethre-Chotzen syndrome.
PharmGKBPA37088.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258515.
HOGENOMHOG000261629.
InParanoidQ15672.
KOK09069.
OMADRQPKRC.
PhylomeDBQ15672.
TreeFamTF315153.

Enzyme and pathway databases

SignaLinkQ15672.

Gene expression databases

BgeeQ15672.
CleanExHS_TWIST1.
GenevestigatorQ15672.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
[Graphical view]
PfamPF00010. HLH. 1 hit.
[Graphical view]
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTWIST1. human.
GeneWikiTwist_transcription_factor.
GenomeRNAi7291.
NextBio28507.
PROQ15672.
SOURCESearch...

Entry information

Entry nameTWST1_HUMAN
AccessionPrimary (citable) accession number: Q15672
Secondary accession number(s): A4D128, Q92487, Q99804
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 154 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 7

Human chromosome 7: entries, gene names and cross-references to MIM