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Q96QV1 (HHIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. 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:
Hedgehog-interacting protein

Short name=HHIP
Short name=HIP
Gene names
Name:HHIP
Synonyms:HIP
ORF Names:UNQ5825/PRO19644
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulates hedgehog signaling in several cell types including brain and lung through direct interaction with members of the hedgehog family. Ref.7 Ref.8

Subunit structure

Interacts with all three hedgehog family members, SHH, IHH and DHH. Ref.7 Ref.8 Ref.9

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Secreted By similarity. Note: The last 22 C-terminal amino acids may participate in cell membrane attachment.

Isoform 2: Cytoplasm Probable.

Tissue specificity

Widely expressed in fetal and adult tissues. Highest expression in adult heart, liver and pancreas, and in fetal kidney. Ref.1 Ref.2

Domain

A flexible loop interacts with the SHH zinc binding site and contributes to zinc binding.

Polymorphism

Genetic variations in HHIP define the stature quantitative trait locus 12 (STQTL12) [MIM:612226]. Adult height is an easily observable and highly heritable complex continuous trait. Because of this, it is a model trait for studying genetic influence on quantitative traits.

Sequence similarities

Belongs to the HHIP family.

Contains 2 EGF-like domains.

Sequence caution

The sequence BAB14945.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Repeat
Signal
   LigandMetal-binding
Zinc
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

dorsal/ventral pattern formation

Inferred from electronic annotation. Source: Ensembl

epithelial tube branching involved in lung morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of signal transduction

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of smoothened signaling pathway

Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL

neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of fibroblast growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

skeletal system morphogenesis

Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL

smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL

   Molecular_functionhedgehog family protein binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

quinone binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96QV1-1)

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: Q96QV1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     278-320: GGDERGLLSL...AIGPHDHILR → VGFLNFIYFC...NLAGENKGAT
     321-700: Missing.
Note: Potentially soluble form.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 700683Hedgehog-interacting protein
PRO_0000007623

Regions

Domain607 – 63428EGF-like 1
Domain635 – 66733EGF-like 2
Region376 – 38813Interaction with SHH zinc binding site
Compositional bias35 – 5420Arg-rich

Sites

Metal binding3831Zinc; shared with SHH

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Ref.9
Glycosylation4591N-linked (GlcNAc...) Potential
Disulfide bond216 ↔ 536 Ref.8 Ref.9
Disulfide bond218 ↔ 543 Ref.8 Ref.9
Disulfide bond402 ↔ 624 Ref.8 Ref.9
Disulfide bond435 ↔ 452 Ref.8 Ref.9
Disulfide bond500 ↔ 594 Ref.8 Ref.9
Disulfide bond608 ↔ 617 Ref.8 Ref.9
Disulfide bond612 ↔ 623 Ref.8 Ref.9
Disulfide bond625 ↔ 634 Ref.8 Ref.9
Disulfide bond639 ↔ 649 Ref.8 Ref.9
Disulfide bond643 ↔ 655 Ref.8 Ref.9
Disulfide bond657 ↔ 666 Ref.8 Ref.9

Natural variations

Alternative sequence278 – 32043GGDER…DHILR → VGFLNFIYFCAGYVNFILVL PSSLKVFLCNKRKNLAGENK GAT in isoform 2.
VSP_013192
Alternative sequence321 – 700380Missing in isoform 2.
VSP_013193
Natural variant3411V → I. Ref.1 Ref.4
VAR_021518

Experimental info

Mutagenesis3801E → A: Abolishes SHH binding. Ref.8
Mutagenesis3821M → A: Abolishes SHH binding. Ref.8
Mutagenesis3831D → A or R: Abolishes SHH binding. Ref.8 Ref.9
Mutagenesis3871D → A: Abolishes SHH binding. Ref.8
Sequence conflict1261P → L in BAC11154. Ref.4
Sequence conflict1351L → I in AAG34731. Ref.1
Sequence conflict1731R → G in BAC11154. Ref.4

Secondary structure

.............................................................................................................. 700
Helix Strand Turn

Details...

Sequences

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

Last modified November 28, 2006. Version 3.
Checksum: CC1CB3435E29303A

FASTA70078,851
        10         20         30         40         50         60 
MLKMLSFKLL LLAVALGFFE GDAKFGERNE GSGARRRRCL NGNPPKRLKR RDRRMMSQLE 

        70         80         90        100        110        120 
LLSGGEMLCG GFYPRLSCCL RSDSPGLGRL ENKIFSVTNN TECGKLLEEI KCALCSPHSQ 

       130        140        150        160        170        180 
SLFHSPEREV LERDLVLPLL CKDYCKEFFY TCRGHIPGFL QTTADEFCFY YARKDGGLCF 

       190        200        210        220        230        240 
PDFPRKQVRG PASNYLDQME EYDKVEEISR KHKHNCFCIQ EVVSGLRQPV GALHSGDGSQ 

       250        260        270        280        290        300 
RLFILEKEGY VKILTPEGEI FKEPYLDIHK LVQSGIKGGD ERGLLSLAFH PNYKKNGKLY 

       310        320        330        340        350        360 
VSYTTNQERW AIGPHDHILR VVEYTVSRKN PHQVDLRTAR VFLEVAELHR KHLGGQLLFG 

       370        380        390        400        410        420 
PDGFLYIILG DGMITLDDME EMDGLSDFTG SVLRLDVDTD MCNVPYSIPR SNPHFNSTNQ 

       430        440        450        460        470        480 
PPEVFAHGLH DPGRCAVDRH PTDININLTI LCSDSNGKNR SSARILQIIK GKDYESEPSL 

       490        500        510        520        530        540 
LEFKPFSNGP LVGGFVYRGC QSERLYGSYV FGDRNGNFLT LQQSPVTKQW QEKPLCLGTS 

       550        560        570        580        590        600 
GSCRGYFSGH ILGFGEDELG EVYILSSSKS MTQTHNGKLY KIVDPKRPLM PEECRATVQP 

       610        620        630        640        650        660 
AQTLTSECSR LCRNGYCTPT GKCCCSPGWE GDFCRTAKCE PACRHGGVCV RPNKCLCKKG 

       670        680        690        700 
YLGPQCEQVD RNIRRVTRAG ILDQIIDMTS YLLDLTSYIV 

« Hide

Isoform 2 [UniParc].

Checksum: 3AF86509A46A7676
Show »

FASTA32036,373

References

« Hide 'large scale' references
[1]"Determination of the chromosomal location and genomic structure of the Hedgehog-interacting protein gene, and analysis of its role in holoprosencephaly."
Huo L., Roessler E., Dutra A., Chuang P.-T., McMahon A.P., Muenke M.
Gene Funct. Dis. 1:119-127(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT ILE-341, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"The human hedgehog-interacting protein gene: structure and chromosome mapping to 4q31.21-->q31.3."
Bak M., Hansen C., Friis Henriksen K., Tommerup N.
Cytogenet. Cell Genet. 92:300-303(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Testis.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"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] (ISOFORMS 1 AND 2), VARIANT ILE-341.
Tissue: Coronary arterial endothelium and Teratocarcinoma.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Muscle.
[7]"Comparative biological responses to human Sonic, Indian, and Desert hedgehog."
Pathi S., Pagan-Westphal S., Baker D.P., Garber E.A., Rayhorn P., Bumcrot D., Tabin C.J., Blake Pepinsky R., Williams K.P.
Mech. Dev. 106:107-117(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[8]"The structure of SHH in complex with HHIP reveals a recognition role for the Shh pseudo active site in signaling."
Bosanac I., Maun H.R., Scales S.J., Wen X., Lingel A., Bazan J.F., de Sauvage F.J., Hymowitz S.G., Lazarus R.A.
Nat. Struct. Mol. Biol. 16:691-697(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 193-667 IN COMPLEX WITH SHH, INTERACTION WITH SHH, FUNCTION, MUTAGENESIS OF GLU-380; MET-382; ASP-383 AND ASP-387, DISULFIDE BONDS.
[9]"Structural insights into hedgehog ligand sequestration by the human hedgehog-interacting protein HHIP."
Bishop B., Aricescu A.R., Harlos K., O'Callaghan C.A., Jones E.Y., Siebold C.
Nat. Struct. Mol. Biol. 16:698-703(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 214-670 IN COMPLEX WITH SHH, INTERACTION WITH SHH AND DHH, DISULFIDE BONDS, MUTAGENESIS OF ASP-383, GLYCOSYLATION AT ASN-447.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY009951 mRNA. Translation: AAG34731.1.
AF326471 expand/collapse EMBL AC list , AF326459, AF326460, AF326462, AF326464, AF326466, AF326468, AF326470, AF326469, AF326467, AF326465, AF326463, AF326461 Genomic DNA. Translation: AAK18182.1.
AY009317 mRNA. Translation: AAG35411.1.
AY358747 mRNA. Translation: AAQ89107.1.
AK024645 mRNA. Translation: BAB14945.1. Different initiation.
AK074711 mRNA. Translation: BAC11154.1.
AC098588 Genomic DNA. No translation available.
BC009298 mRNA. Translation: AAH09298.1.
BC025311 mRNA. Translation: AAH25311.1.
CCDSCCDS3762.1. [Q96QV1-1]
RefSeqNP_071920.1. NM_022475.2. [Q96QV1-1]
UniGeneHs.507991.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WFTX-ray2.80A/B214-671[»]
2WFXX-ray3.20B214-670[»]
2WG3X-ray2.60C/D214-670[»]
2WG4X-ray3.15B214-670[»]
3HO3X-ray2.90A193-667[»]
3HO4X-ray3.10A/B193-667[»]
3HO5X-ray3.01A/B193-667[»]
ProteinModelPortalQ96QV1.
SMRQ96QV1. Positions 214-668.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122156. 1 interaction.
DIPDIP-48536N.
IntActQ96QV1. 1 interaction.
STRING9606.ENSP00000296575.

PTM databases

PhosphoSiteQ96QV1.

Polymorphism databases

DMDM118572655.

Proteomic databases

MaxQBQ96QV1.
PaxDbQ96QV1.
PRIDEQ96QV1.

Protocols and materials databases

DNASU64399.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296575; ENSP00000296575; ENSG00000164161. [Q96QV1-1]
ENST00000434550; ENSP00000408587; ENSG00000164161. [Q96QV1-2]
GeneID64399.
KEGGhsa:64399.
UCSCuc003ijr.2. human. [Q96QV1-2]
uc003ijs.2. human. [Q96QV1-1]

Organism-specific databases

CTD64399.
GeneCardsGC04P145567.
HGNCHGNC:14866. HHIP.
HPAHPA012616.
MIM606178. gene.
612226. phenotype.
neXtProtNX_Q96QV1.
PharmGKBPA29276.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2133.
HOGENOMHOG000008644.
HOVERGENHBG051901.
InParanoidQ96QV1.
KOK06231.
OMAFGDRNGN.
OrthoDBEOG7CZK54.
PhylomeDBQ96QV1.
TreeFamTF329059.

Enzyme and pathway databases

SignaLinkQ96QV1.

Gene expression databases

BgeeQ96QV1.
CleanExHS_HHIP.
GenevestigatorQ96QV1.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR018143. Folate_rcpt-like.
IPR012938. Glc/Sorbosone_DH.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view]
PfamPF03024. Folate_rec. 1 hit.
PF07995. GSDH. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
[Graphical view]
SUPFAMSSF50952. SSF50952. 1 hit.
PROSITEPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHHIP. human.
EvolutionaryTraceQ96QV1.
GeneWikiHHIP.
GenomeRNAi64399.
NextBio66342.
PROQ96QV1.
SOURCESearch...

Entry information

Entry nameHHIP_HUMAN
AccessionPrimary (citable) accession number: Q96QV1
Secondary accession number(s): Q6PK09 expand/collapse secondary AC list , Q8NCI7, Q9BXK3, Q9H1J4, Q9H7E7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 109 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 4

Human chromosome 4: entries, gene names and cross-references to MIM