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Q9UQF2 (JIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. 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:
C-Jun-amino-terminal kinase-interacting protein 1

Short name=JIP-1
Short name=JNK-interacting protein 1
Alternative name(s):
Islet-brain 1
Short name=IB-1
JNK MAP kinase scaffold protein 1
Mitogen-activated protein kinase 8-interacting protein 1
Gene names
Name:MAPK8IP1
Synonyms:IB1, JIP1, PRKM8IP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins By similarity. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response.

Subunit structure

Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely, MAPK8, MAPK9, MAPK10, MAPKK7, MLK2, MLK3, MAP3K12 and MAP3K13. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2). Interacts, via the PID domain, with ARHGEF28. Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of KNS2, then the pre-assembled MAPK8IP1 scaffolding complexes are transported as a cargo of kinesin, to the required subcellular location. Interacts with the cytoplasmic domain of APP. Interacts with DCLK2 By similarity. Interacts with MAP3K7. Interacts with isoform 1and isoform 2of VRK2. Ref.4 Ref.5 Ref.6 Ref.7 Ref.13 Ref.14

Subcellular location

Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Nucleus By similarity. Endoplasmic reticulum membrane. Mitochondrion membrane. Note: Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus By similarity. Ref.4 Ref.14

Tissue specificity

Highly expressed in brain. Expressed in neurons, localizing to neurite tips in differentiating cells. Also expressed in the pancreas, testis and prostate. Low levels in heart, ovary and small intestine. Decreased levels in pancreatic beta cells sensitize cells to IL-1-beta-induced apoptosis.

Domain

The destruction boxes (D-box) may act as recognition signals for degradation via the ubiquitin-proteasome pathway.

A minimal inhibitory domain prevents pancreatic beta cell apoptosis in vitro, and prevents activation of c-jun by MAPK8, MAPK9 and MAPK10.

The SH3 domain mediates homodimerization By similarity.

Post-translational modification

Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-103 is also necessary for the dissociation and activation of MAP3K12. Phosphorylated by isoform 1and isoform 2of VRK2. Hyperphosphorylated during mitosis following activation of stress-activated and MAP kinases. Ref.8 Ref.12 Ref.14

Ubiquitinated. Two preliminary events are required to prime for ubiquitination; phosphorylation and an increased in intracellular calcium concentration. Then, the calcium influx initiates ubiquitination and degradation by the ubiquitin-proteasome pathway. Ref.10

Involvement in disease

Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.15

Miscellaneous

A chemically synthesized cell-permeable peptide of the minimal inhibitory domain decreases brain lesions in both transient and permanent ischemia. The level of protection is still high when administered 6 or 12 hours after ischemia.

Sequence similarities

Belongs to the JIP scaffold family.

Contains 1 PID domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDiabetes mellitus
Disease mutation
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJUN phosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of signal transduction

Inferred from physical interaction Ref.5. Source: GOC

regulation of JNK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxonal growth cone

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.4. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

dendritic growth cone

Inferred from electronic annotation. Source: Ensembl

dentate gyrus mossy fiber

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionMAP-kinase scaffold activity

Inferred from physical interaction Ref.5. Source: UniProtKB

kinesin binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein kinase inhibitor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 711711C-Jun-amino-terminal kinase-interacting protein 1
PRO_0000220628

Regions

Domain488 – 54962SH3
Domain561 – 700140PID
Region127 – 285159JNK-binding domain (JBD)
Region157 – 17620Minimal inhibitory domain (MID)
Region283 – 471189Interaction with MAP3K7
Region471 – 660190Interaction with VRK2
Motif353 – 3608D-box 1
Motif364 – 3729D-box 2
Compositional bias42 – 487Asp/Glu-rich (acidic)
Compositional bias79 – 846Poly-Gly
Compositional bias107 – 11610Asp/Glu-rich (acidic)
Compositional bias331 – 3344Poly-Glu
Compositional bias359 – 3635Poly-Pro

Amino acid modifications

Modified residue401Phosphoserine Ref.12
Modified residue1031Phosphothreonine; by MAPK8, MAPK9 and MAPK10 Ref.8
Modified residue1521Phosphoserine
Modified residue1811Phosphoserine Ref.12
Modified residue1871Phosphoserine Ref.12
Modified residue1931Phosphoserine Ref.12
Modified residue1951Phosphoserine Ref.12
Modified residue1961Phosphoserine Ref.12
Modified residue2051Phosphothreonine; by MAPK8, MAPK9 and MAPK10 Ref.8
Modified residue2141Phosphoserine Ref.12
Modified residue3111Phosphoserine Ref.12
Modified residue3281Phosphoserine Ref.12
Modified residue3301Phosphoserine Ref.12
Modified residue3401Phosphoserine Ref.12
Modified residue3551Phosphoserine Ref.12
Modified residue3661Phosphoserine Ref.12
Modified residue3691Phosphoserine Ref.12
Modified residue4071Phosphoserine Ref.12
Modified residue4091Phosphoserine Ref.12
Modified residue4111Phosphothreonine Ref.12
Modified residue4441Phosphoserine Ref.12
Modified residue4471Phosphoserine Ref.12
Modified residue4481Phosphothreonine Ref.12
Modified residue4691Phosphoserine Ref.12
Modified residue4711Phosphoserine Ref.12
Modified residue4721Phosphoserine Ref.12
Modified residue4731Phosphoserine Ref.12

Natural variations

Natural variant591S → N in NIDDM. Ref.15
VAR_012243
Natural variant3221A → V.
Corresponds to variant rs34420676 [ dbSNP | Ensembl ].
VAR_049664
Natural variant3531R → Q.
Corresponds to variant rs12295161 [ dbSNP | Ensembl ].
VAR_049665

Experimental info

Mutagenesis1601R → G: Abolishes MAPK9 interaction. Ref.8
Mutagenesis1611P → G: Abolishes MAPK9 interaction. Ref.8
Mutagenesis7041P → A: No effect on KNS2 binding.
Mutagenesis7091Y → A: Abolishes KNS2 binding.

Sequences

Sequence LengthMass (Da)Tools
Q9UQF2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 55EA53B30080A751

FASTA71177,524
        10         20         30         40         50         60 
MAERESGGLG GGAASPPAAS PFLGLHIASP PNFRLTHDIS LEEFEDEDLS EITDECGISL 

        70         80         90        100        110        120 
QCKDTLSLRP PRAGLLSAGG GGAGSRLQAE MLQMDLIDAT GDTPGAEDDE EDDDEERAAR 

       130        140        150        160        170        180 
RPGAGPPKAE SGQEPASRGQ GQSQGQSQGP GSGDTYRPKR PTTLNLFPQV PRSQDTLNNN 

       190        200        210        220        230        240 
SLGKKHSWQD RVSRSSSPLK TGEQTPPHEH ICLSDELPPQ SGPAPTTDRG TSTDSPCRRS 

       250        260        270        280        290        300 
TATQMAPPGG PPAAPPGGRG HSHRDRIHYQ ADVRLEATEE IYLTPVQRPP DAAEPTSAFL 

       310        320        330        340        350        360 
PPTESRMSVS SDPDPAAYPS TAGRPHPSIS EEEEGFDCLS SPERAEPPGG GWRGSLGEPP 

       370        380        390        400        410        420 
PPPRASLSSD TSALSYDSVK YTLVVDEHAQ LELVSLRPCF GDYSDESDSA TVYDNCASVS 

       430        440        450        460        470        480 
SPYESAIGEE YEEAPRPQPP ACLSEDSTPD EPDVHFSKKF LNVFMSGRSR SSSAESFGLF 

       490        500        510        520        530        540 
SCIINGEEQE QTHRAIFRFV PRHEDELELE VDDPLLVELQ AEDYWYEAYN MRTGARGVFP 

       550        560        570        580        590        600 
AYYAIEVTKE PEHMAALAKN SDWVDQFRVK FLGSVQVPYH KGNDVLCAAM QKIATTRRLT 

       610        620        630        640        650        660 
VHFNPPSSCV LEISVRGVKI GVKADDSQEA KGNKCSHFFQ LKNISFCGYH PKNNKYFGFI 

       670        680        690        700        710 
TKHPADHRFA CHVFVSEDST KALAESVGRA FQQFYKQFVE YTCPTEDIYL E 

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization, fine-mapping, and expression of the human islet-brain 1 (IB1)/C-jun-amino-terminal kinase interacting protein-1 (JIP-1) gene."
Mooser V., Maillard A., Bonny C., Steinmann M., Shaw P., Yarnall D.P., Burns D.K., Schorderet D.F., Nicod P., Waeber G.
Genomics 55:202-208(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Insulinoma.
[2]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Yu W., Sarginson J., Gibbs R.A.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 468-711.
Tissue: Brain.
[4]"Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons."
Meyer D., Liu A., Margolis B.
J. Biol. Chem. 274:35113-35118(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF28, SUBCELLULAR LOCATION.
[5]"Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules."
Verhey K.J., Meyer D., Deehan R., Blenis J., Schnapp B.J., Rapoport T.A., Margolis B.
J. Cell Biol. 152:959-970(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, INTERACTION WITH KINESIN.
[6]"Mixed lineage kinase LZK forms a functional signaling complex with JIP-1, a scaffold protein of the c-Jun NH(2)-terminal kinase pathway."
Ikeda A., Hasegawa K., Masaki M., Moriguchi T., Nishida E., Kozutsumi Y., Oka S., Kawasaki T.
J. Biochem. 130:773-781(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP3K13.
[7]"Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade."
Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.
J. Biol. Chem. 277:20070-20078(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APP.
[8]"Recruitment of JNK to JIP1 and JNK-dependent JIP1 phosphorylation regulates JNK module dynamics and activation."
Nihalani D., Wong H.N., Holzman L.B.
J. Biol. Chem. 278:28694-28702(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-103 AND THR-205, MUTAGENESIS OF ARG-160 AND PRO-161.
[9]"Cell-permeable peptide inhibitors of JNK: novel blockers of beta-cell death."
Bonny C., Oberson A., Negri S., Sauser C., Schorderet D.F.
Diabetes 50:77-82(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PEPTIDE INHIBITORS OF JNK.
[10]"Calcium- and proteasome-dependent degradation of the JNK scaffold protein islet-brain 1."
Allaman-Pillet N., Storling J., Oberson A., Roduit R., Negri S., Sauser C., Nicod P., Beckmann J.S., Schorderet D.F., Mandrup-Poulsen T., Bonny C.
J. Biol. Chem. 278:48720-48726(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM- AND PROTEASOME-DEPENDENT DEGRADATION.
[11]"A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia."
Borsello T., Clarke P.G., Hirt L., Vercelli A., Repici M., Schorderet D.F., Bogousslavsky J., Bonny C.
Nat. Med. 9:1180-1186(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTECTION AGAINST EXCITOTOXICITY AND CEREBRAL ISCHEMIA.
[12]"Hyperphosphorylation of JNK-interacting protein 1, a protein associated with Alzheimer disease."
D'Ambrosio C., Arena S., Fulcoli G., Scheinfeld M.H., Zhou D., D'Adamio L., Scaloni A.
Mol. Cell. Proteomics 5:97-113(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-40; SER-181; SER-187; SER-193; SER-195; SER-196; SER-214; SER-311; SER-328; SER-330; SER-340; SER-355; SER-366; SER-369; SER-407; SER-409; THR-411; SER-444; SER-447; SER-444; THR-448; SER-469; SER-471; SER-472 AND SER-473.
[13]"Vaccinia-related kinase 2 modulates the stress response to hypoxia mediated by TAK1."
Blanco S., Santos C., Lazo P.A.
Mol. Cell. Biol. 27:7273-7283(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP3K7.
[14]"Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein."
Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.
PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VRK2, PHOSPHORYLATION.
[15]"The gene, MAPK8IP1, encoding islet-brain-1, is a candidate for type 2 diabetes."
Waeber G., Delplanque J., Bonny C., Mooser V., Steinmann M., Widmann C., Maillard A., Miklossy J., Dina C., Hani E.H., Vionnet N., Nicod P., Boutin P., Froguel P.
Nat. Genet. 24:291-295(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NIDDM ASN-59.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF074091 mRNA. Translation: AAD20443.1.
CH471064 Genomic DNA. Translation: EAW68027.1.
CH471064 Genomic DNA. Translation: EAW68028.1.
AF007134 mRNA. Translation: AAC19150.1.
RefSeqNP_005447.1. NM_005456.3.
UniGeneHs.234249.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G01X-ray3.50F/G157-167[»]
2GMXX-ray3.50F/G157-167[»]
2H96X-ray3.00F/G157-167[»]
3OXIX-ray2.20J158-167[»]
3PTGX-ray2.43J157-167[»]
3VUDX-ray3.50F157-167[»]
3VUGX-ray3.24F157-167[»]
3VUHX-ray2.70F157-167[»]
3VUIX-ray2.80F157-167[»]
3VUKX-ray2.95F157-167[»]
3VULX-ray2.81F157-167[»]
3VUMX-ray2.69F157-167[»]
4E73X-ray2.27B158-167[»]
4G1WX-ray2.45B157-167[»]
4H39X-ray1.99B158-167[»]
4HYSX-ray2.42B157-167[»]
4HYUX-ray2.15B157-167[»]
4IZYX-ray2.30B157-167[»]
ProteinModelPortalQ9UQF2.
SMRQ9UQF2. Positions 490-549, 565-697.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114864. 26 interactions.
IntActQ9UQF2. 14 interactions.
MINTMINT-111691.
STRING9606.ENSP00000241014.

PTM databases

PhosphoSiteQ9UQF2.

Polymorphism databases

DMDM17433093.

Proteomic databases

PaxDbQ9UQF2.
PRIDEQ9UQF2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241014; ENSP00000241014; ENSG00000121653.
GeneID9479.
KEGGhsa:9479.
UCSCuc001nbr.3. human.

Organism-specific databases

CTD9479.
GeneCardsGC11P045908.
HGNCHGNC:6882. MAPK8IP1.
HPACAB013289.
MIM125853. phenotype.
604641. gene.
neXtProtNX_Q9UQF2.
PharmGKBPA30626.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266073.
HOGENOMHOG000231470.
HOVERGENHBG018568.
InParanoidQ9UQF2.
KOK04434.
OMASPCRRSA.
OrthoDBEOG74J97M.
PhylomeDBQ9UQF2.
TreeFamTF325073.

Enzyme and pathway databases

SignaLinkQ9UQF2.

Gene expression databases

ArrayExpressQ9UQF2.
BgeeQ9UQF2.
CleanExHS_MAPK8IP1.
GenevestigatorQ9UQF2.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00640. PID. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
PROSITEPS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAPK8IP1. human.
EvolutionaryTraceQ9UQF2.
GeneWikiMAPK8IP1.
GenomeRNAi9479.
NextBio35528.
PROQ9UQF2.
SOURCESearch...

Entry information

Entry nameJIP1_HUMAN
AccessionPrimary (citable) accession number: Q9UQF2
Secondary accession number(s): D3DQP4, O43407
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 138 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 11

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