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Q9NZN1 (IRPL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-1 receptor accessory protein-like 1

Short name=IL-1-RAPL-1
Short name=IL-1RAPL-1
Short name=IL1RAPL-1
Alternative name(s):
Oligophrenin-4
Three immunoglobulin domain-containing IL-1 receptor-related 2
Short name=TIGIRR-2
X-linked interleukin-1 receptor accessory protein-like 1
Gene names
Name:IL1RAPL1
Synonyms:OPHN4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length696 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in presynaptic and postsynaptic differentiation and dendritic spine formation in neurons. Ref.8 Ref.11

Subunit structure

Homodimer. Interacts (calcium-independent) with NCS1. Interacts (via extracellular region) with PTPRD; this interaction is required for IL1RAPL1-mediated synapse formation. Ref.8 Ref.11

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cytoplasm. Cell projectionaxon By similarity. Cell projectiondendrite By similarity. Note: May localize to the cell body and growth cones of dendrite-like processes By similarity. Ref.8

Tissue specificity

Detected at low levels in heart, skeletal muscle, ovary, skin, amygdala, caudate nucleus, corpus callosum, hippocampus, substantia nigra and thalamus. Detected at very low levels in tonsil, prostate, testis, small intestine, placenta, colon and fetal liver. Ref.1 Ref.3

Involvement in disease

Mental retardation, X-linked 21 (MRX21) [MIM:300143]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9

Sequence similarities

Belongs to the interleukin-1 receptor family.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 TIR domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from sequence or structural similarity. Source: GOC

heterophilic cell-cell adhesion

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

negative regulation of exocytosis

Inferred from direct assay Ref.8. Source: UniProtKB

neuron differentiation

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

positive regulation of dendrite morphogenesis

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

presynaptic membrane assembly

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

regulation of neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentaxon

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

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

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

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

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

postsynaptic membrane

Non-traceable author statement PubMed 21940441. Source: BHF-UCL

   Molecular_functionprotein binding

Inferred from physical interaction Ref.8PubMed 21940441. Source: UniProtKB

receptor binding

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

voltage-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced.
Isoform 1 (identifier: Q9NZN1-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 696678Interleukin-1 receptor accessory protein-like 1
PRO_0000015454

Regions

Topological domain19 – 357339Extracellular Potential
Transmembrane358 – 37821Helical; Potential
Topological domain379 – 696318Cytoplasmic Potential
Domain19 – 134116Ig-like C2-type 1
Domain143 – 23290Ig-like C2-type 2
Domain242 – 350109Ig-like C2-type 3
Domain403 – 562160TIR
Region549 – 64496Interaction with NCS1

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 118 Potential
Disulfide bond164 ↔ 216 Potential
Disulfide bond267 ↔ 334 Potential

Natural variations

Natural variant3791K → R. Ref.10
Corresponds to variant rs138267399 [ dbSNP | Ensembl ].
VAR_062263
Natural variant6181Q → H. Ref.10
VAR_062264
Natural variant6371T → S. Ref.10
VAR_062265
Natural variant6431I → V. Ref.10
VAR_062266

Secondary structure

.............................. 696
Helix Strand Turn

Details...

Sequences

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

Last modified August 22, 2003. Version 2.
Checksum: 9B7A0B503D73CCA9

FASTA69679,969
        10         20         30         40         50         60 
MKAPIPHLIL LYATFTQSLK VVTKRGSADG CTDWSIDIKK YQVLVGEPVR IKCALFYGYI 

        70         80         90        100        110        120 
RTNYSLAQSA GLSLMWYKSS GPGDFEEPIA FDGSRMSKEE DSIWFRPTLL QDSGLYACVI 

       130        140        150        160        170        180 
RNSTYCMKVS ISLTVGENDT GLCYNSKMKY FEKAELSKSK EISCRDIEDF LLPTREPEIL 

       190        200        210        220        230        240 
WYKECRTKTW RPSIVFKRDT LLIREVREDD IGNYTCELKY GGFVVRRTTE LTVTAPLTDK 

       250        260        270        280        290        300 
PPKLLYPMES KLTIQETQLG DSANLTCRAF FGYSGDVSPL IYWMKGEKFI EDLDENRVWE 

       310        320        330        340        350        360 
SDIRILKEHL GEQEVSISLI VDSVEEGDLG NYSCYVENGN GRRHASVLLH KRELMYTVEL 

       370        380        390        400        410        420 
AGGLGAILLL LVCLVTIYKC YKIEIMLFYR NHFGAEELDG DNKDYDAYLS YTKVDPDQWN 

       430        440        450        460        470        480 
QETGEEERFA LEILPDMLEK HYGYKLFIPD RDLIPTGTYI EDVARCVDQS KRLIIVMTPN 

       490        500        510        520        530        540 
YVVRRGWSIF ELETRLRNML VTGEIKVILI ECSELRGIMN YQEVEALKHT IKLLTVIKWH 

       550        560        570        580        590        600 
GPKCNKLNSK FWKRLQYEMP FKRIEPITHE QALDVSEQGP FGELQTVSAI SMAAATSTAL 

       610        620        630        640        650        660 
ATAHPDLRST FHNTYHSQMR QKHYYRSYEY DVPPTGTLPL TSIGNQHTYC NIPMTLINGQ 

       670        680        690 
RPQTKSSREQ NPDEAHTNSA ILPLLPRETS ISSVIW 

« Hide

References

« Hide 'large scale' references
[1]"A new member of the IL-1 receptor family highly expressed in hippocampus and involved in X-linked mental retardation."
Carrie A., Jun L., Bienvenu T., Vinet M.-C., McDonell N., Couvert P., Zemni R., Cardona A., Van Buggenhout G., Frints S., Hamel B.C.J., Moraine C., Ropers H.-H., Strom T., Howell G.R., Whittaker A., Ross M.T., Kahn A. expand/collapse author list , Fryns J.-P., Beldjord C., Marynen P., Chelly J.
Nat. Genet. 23:25-31(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN NONSPECIFIC XLMR, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
Tissue: Fetal brain.
[2]"Two novel members of the interleukin-1 receptor gene family, one deleted in Xp22.3-Xp21.3 mental retardation."
Jin H., Gardner R.J., Viswesvaraiah R., Muntoni F., Roberts R.G.
Eur. J. Hum. Genet. 8:87-94(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN MRX21.
[3]"Identification and characterization of two members of a novel class of the interleukin-1 receptor (IL-1R) family. Delineation of a new class of IL-1R-related proteins based on signaling."
Born T.L., Smith D.E., Garka K.E., Renshaw B.R., Bertles J.S., Sims J.E.
J. Biol. Chem. 275:29946-29954(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Brain and Testis.
[4]"Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
Kitano T., Schwarz C., Nickel B., Paeaebo S.
Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"IL1 receptor accessory protein like, a protein involved in X-linked mental retardation, interacts with Neuronal Calcium Sensor-1 and regulates exocytosis."
Bahi N., Friocourt G., Carrie A., Graham M.E., Weiss J.L., Chafey P., Fauchereau F., Burgoyne R.D., Chelly J.
Hum. Mol. Genet. 12:1415-1425(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCS1.
[9]"A truncating mutation in the IL1RAPL1 gene is responsible for X-linked mental retardation in the MRX21 family."
Tabolacci E., Pomponi M.G., Pietrobono R., Terracciano A., Chiurazzi P., Neri G.
Am. J. Med. Genet. A 140:482-487(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRX21.
[10]"Mutations in the calcium-related gene IL1RAPL1 are associated with autism."
Piton A., Michaud J.L., Peng H., Aradhya S., Gauthier J., Mottron L., Champagne N., Lafreniere R.G., Hamdan F.F., Joober R., Fombonne E., Marineau C., Cossette P., Dube M.P., Haghighi P., Drapeau P., Barker P.A., Carbonetto S., Rouleau G.A.
Hum. Mol. Genet. 17:3965-3974(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-379; HIS-618; SER-637 AND VAL-643.
[11]"Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL."
Khan J.A., Brint E.K., O'Neill L.A.J., Tong L.
J. Biol. Chem. 279:31664-31670(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 403-561, FUNCTION, DIMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ243874 mRNA. Translation: CAB56046.1.
AF181284 mRNA. Translation: AAF59411.1.
AF284435 mRNA. Translation: AAG21369.1.
AB102650 mRNA. Translation: BAC81119.1.
AL031575 expand/collapse EMBL AC list , AC005748, AC121343, AC129852, AL031466 Genomic DNA. Translation: CAI42035.1.
AL031466 expand/collapse EMBL AC list , AC005748, AC121343, AC129852, AL031575 Genomic DNA. Translation: CAI42992.1.
CH471074 Genomic DNA. Translation: EAW99046.1.
BC126345 mRNA. Translation: AAI26346.1.
BC126347 mRNA. Translation: AAI26348.1.
CCDSCCDS14218.1. [Q9NZN1-1]
RefSeqNP_055086.1. NM_014271.3. [Q9NZN1-1]
XP_005274498.1. XM_005274441.1. [Q9NZN1-1]
UniGeneHs.658912.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3GX-ray2.30A/B403-561[»]
4M92X-ray1.60B207-222[»]
ProteinModelPortalQ9NZN1.
SMRQ9NZN1. Positions 31-349, 403-561.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116313. 2 interactions.
IntActQ9NZN1. 1 interaction.
STRING9606.ENSP00000305200.

PTM databases

PhosphoSiteQ9NZN1.

Polymorphism databases

DMDM34222654.

Proteomic databases

MaxQBQ9NZN1.
PaxDbQ9NZN1.
PeptideAtlasQ9NZN1.
PRIDEQ9NZN1.

Protocols and materials databases

DNASU11141.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302196; ENSP00000305200; ENSG00000169306. [Q9NZN1-1]
ENST00000378993; ENSP00000368278; ENSG00000169306. [Q9NZN1-1]
GeneID11141.
KEGGhsa:11141.
UCSCuc004dby.2. human. [Q9NZN1-1]

Organism-specific databases

CTD11141.
GeneCardsGC0XP028605.
HGNCHGNC:5996. IL1RAPL1.
HPAHPA000564.
MIM300143. phenotype.
300206. gene.
neXtProtNX_Q9NZN1.
Orphanet777. X-linked non-syndromic intellectual disability.
PharmGKBPA29812.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41227.
HOGENOMHOG000092977.
HOVERGENHBG052148.
InParanoidQ9NZN1.
KOK05170.
OMAKLLHPLE.
OrthoDBEOG7CVPXJ.
PhylomeDBQ9NZN1.
TreeFamTF333913.

Gene expression databases

ArrayExpressQ9NZN1.
BgeeQ9NZN1.
CleanExHS_IL1RAPL1.
GenevestigatorQ9NZN1.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.40.50.10140. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR015621. IL-1_rcpt_fam.
IPR000157. TIR_dom.
[Graphical view]
PANTHERPTHR11890. PTHR11890. 1 hit.
PfamPF07679. I-set. 1 hit.
PF01582. TIR. 1 hit.
[Graphical view]
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]
SUPFAMSSF52200. SSF52200. 1 hit.
PROSITEPS50835. IG_LIKE. 3 hits.
PS50104. TIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIL1RAPL1. human.
EvolutionaryTraceQ9NZN1.
GeneWikiIL1RAPL1.
GenomeRNAi11141.
NextBio42348.
PROQ9NZN1.
SOURCESearch...

Entry information

Entry nameIRPL1_HUMAN
AccessionPrimary (citable) accession number: Q9NZN1
Secondary accession number(s): A0AVG4, Q9UJ53
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: August 22, 2003
Last modified: July 9, 2014
This is version 128 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 X

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