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P07108 (ACBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. 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:
Acyl-CoA-binding protein

Short name=ACBP
Alternative name(s):
Diazepam-binding inhibitor
Short name=DBI
Endozepine
Short name=EP
Gene names
Name:DBI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length87 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.

Subunit structure

Monomer.

Subcellular location

Endoplasmic reticulum. Golgi apparatus. Note: Golgi localization is dependent on ligand binding. Ref.4 Ref.14

Tissue specificity

Isoform 1 is ubiquitous, with a moderate expression level. Isoform 2 is ubiquitous with high level in liver and adipose tissue. Isoform 3 is ubiquitous with strong expression in adipose tissue and heart. Ref.3 Ref.4

Sequence similarities

Belongs to the ACBP family.

Contains 1 ACB (acyl-CoA-binding) domain.

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07108-1)

Also known as: ACBP-1a; Short;

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: P07108-2)

Also known as: ACBP-1b; Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MWGDLWLLPPASANPGTGTE
Isoform 3 (identifier: P07108-3)

Also known as: ACBP-1c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MPAF
Isoform 4 (identifier: P07108-4)

Also known as: ACBP-1a1-g;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MSQHRAGRRGGVGKRGVRGRELGGQGKYGAGCSECGTRRIAARGE
Isoform 5 (identifier: P07108-5)

Also known as: ACBP-1g;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSQ → MERWGKGLHGLEERGDSVPIPKHRAGRRGGVGKRGVRGRELGGQGKYGAGCSECGTRRIAARGE
Isoform 6 (identifier: P07108-6)

Also known as: ACBP-1e;

The sequence of this isoform differs from the canonical sequence as follows:
     43-87: ERPGMLDFTG...VEELKKKYGI → GMQSGGWKGI...YWPSPAATLY
Note: Predominantly expressed in adipose tissue and hippocampus.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10 Ref.11
Chain2 – 8786Acyl-CoA-binding protein
PRO_0000214004

Regions

Domain2 – 8786ACB
Region29 – 335Acyl-CoA binding

Sites

Binding site141Acyl-CoA
Binding site551Acyl-CoA
Binding site741Acyl-CoA

Amino acid modifications

Modified residue21N-acetylserine Ref.10 Ref.15 Ref.16 Ref.20
Modified residue81N6-acetyllysine; alternate Ref.16
Modified residue81N6-succinyllysine; alternate By similarity
Modified residue171N6-succinyllysine By similarity
Modified residue191N6-acetyllysine Ref.16
Modified residue291Phosphotyrosine Ref.17
Modified residue551N6-acetyllysine; alternate Ref.16
Modified residue551N6-malonyllysine; alternate Ref.19
Modified residue551N6-succinyllysine; alternate By similarity
Modified residue771N6-acetyllysine; alternate Ref.16
Modified residue771N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence1 – 33MSQ → MWGDLWLLPPASANPGTGTE in isoform 2.
VSP_000068
Alternative sequence1 – 33MSQ → MPAF in isoform 3.
VSP_038680
Alternative sequence1 – 33MSQ → MSQHRAGRRGGVGKRGVRGR ELGGQGKYGAGCSECGTRRI AARGE in isoform 4.
VSP_043437
Alternative sequence1 – 33MSQ → MERWGKGLHGLEERGDSVPI PKHRAGRRGGVGKRGVRGRE LGGQGKYGAGCSECGTRRIA ARGE in isoform 5.
VSP_043438
Alternative sequence43 – 8745ERPGM…KKYGI → GMQSGGWKGICSSKQAQQLR LEVPGNFTLKLPEALLFRWG MVMVPEVEKTMFRILSVSSS NRIQILVLEGLYWPSPAATL Y in isoform 6.
VSP_044114
Natural variant391D → N.
Corresponds to variant rs8192504 [ dbSNP | Ensembl ].
VAR_048160
Natural variant711M → V.
Corresponds to variant rs8192506 [ dbSNP | Ensembl ].
VAR_048161
Natural variant861G → R.
Corresponds to variant rs8192507 [ dbSNP | Ensembl ].
VAR_048162

Secondary structure

........... 87
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ACBP-1a) (Short) [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B343A309F1B1AE28

FASTA8710,044
        10         20         30         40         50         60 
MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF TGKAKWDAWN 

        70         80 
ELKGTSKEDA MKAYINKVEE LKKKYGI 

« Hide

Isoform 2 (ACBP-1b) (Long) [UniParc].

Checksum: 54D0238ABE40BCD2
Show »

FASTA10411,793
Isoform 3 (ACBP-1c) [UniParc].

Checksum: F4FFCEBA6D9D4330
Show »

FASTA8810,145
Isoform 4 (ACBP-1a1-g) [UniParc].

Checksum: A3985333C4BE1F8F
Show »

FASTA12914,367
Isoform 5 (ACBP-1g) [UniParc].

Checksum: 29F51D3DA08F300B
Show »

FASTA14816,495
Isoform 6 (ACBP-1e) [UniParc].

Checksum: 61407128B4E7B1DD
Show »

FASTA12313,911

References

« Hide 'large scale' references
[1]"Cloning and expression of cDNA for human diazepam binding inhibitor, a natural ligand of an allosteric regulatory site of the gamma-aminobutyric acid type A receptor."
Gray P.W., Glaister D., Seeburg P.H., Guidotti A., Costa E.
Proc. Natl. Acad. Sci. U.S.A. 83:7547-7551(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Bovine and human cDNA sequences encoding a putative benzodiazepine receptor ligand."
Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J., Lee D.C.
DNA 6:71-79(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Identification of new acyl-CoA binding protein transcripts in human and mouse."
Nitz I., Doering F., Schrezenmeir J., Burwinkel B.
Int. J. Biochem. Cell Biol. 37:2395-2405(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
[4]"Identification of a novel human Acyl-CoA binding protein isoform with a unique C-terminal domain."
Ludewig A.H., Nitz I., Klapper M., Doring F.
IUBMB Life 63:547-552(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Specific regulation of low-abundance transcript variants encoding human Acyl-CoA binding protein (ACBP) isoforms."
Nitz I., Kruse M.L., Klapper M., Doring F.
J. Cell. Mol. Med. 15:909-927(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE SPLICING, ALTERNATIVE PROMOTER USAGE.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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].
[8]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].
[9]"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: Brain.
[10]"Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor."
Marquardt H., Todaro G.J., Shoyab M.
J. Biol. Chem. 261:9727-9731(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-87 (ISOFORM 1), ACETYLATION AT SER-2.
Tissue: Brain.
[11]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14 (ISOFORM 1).
Tissue: Platelet.
[12]"Purification and analysis of growth regulating proteins secreted by a human melanoma cell line."
Apfel R., Lottspeich F., Hoppe J., Behl C., Duerr G., Bogdahn U.
Melanoma Res. 2:327-336(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-30 AND 72-87.
[13]"The characterization of two diazepam binding inhibitor (DBI) transcripts in humans."
Kolmer M., Rovio A., Alho H.
Biochem. J. 306:327-330(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[14]"Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and Golgi in a ligand-dependent manner in mammalian cells."
Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J.
Biochem. J. 410:463-472(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-8; LYS-19; LYS-55 AND LYS-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-55.
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand."
Taskinen J.P., van Aalten D.M., Knudsen J., Wierenga R.K.
Proteins 66:229-238(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ACYL-COENZYME A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14200 mRNA. Translation: AAA52171.1.
M15887 mRNA. Translation: AAA35788.1.
FM213123 mRNA. Translation: CAR82405.1.
FM213124 mRNA. Translation: CAR82406.1.
FM213125 mRNA. Translation: CAR82407.1.
FM213126 mRNA. Translation: CAR82408.1.
FM213127 mRNA. Translation: CAR82409.1.
FM213128 mRNA. Translation: CAR82410.1.
FM213131 mRNA. Translation: CAR82414.1.
CR456956 mRNA. Translation: CAG33237.1.
AC016736 Genomic DNA. Translation: AAY14873.1.
CH471103 Genomic DNA. Translation: EAW95214.1.
BC006466 mRNA. No translation available.
BC062996 mRNA. Translation: AAH62996.1.
AM000001 mRNA. Translation: CAJ00736.1.
PIRNZHU. B26448.
RefSeqNP_001073331.1. NM_001079862.2.
NP_001073332.1. NM_001079863.1.
NP_001171488.1. NM_001178017.1.
NP_001171512.1. NM_001178041.2.
NP_001171513.1. NM_001178042.2.
NP_001269562.1. NM_001282633.1.
NP_001269563.1. NM_001282634.1.
NP_001269564.1. NM_001282635.1.
NP_065438.1. NM_020548.7.
UniGeneHs.78888.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CB8X-ray1.40A/B1-87[»]
2FJ9X-ray1.60A2-87[»]
ProteinModelPortalP07108.
SMRP07108. Positions 2-87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107990. 10 interactions.
IntActP07108. 9 interactions.
MINTMINT-1394907.
STRING9606.ENSP00000311117.

PTM databases

PhosphoSiteP07108.

Proteomic databases

PaxDbP07108.
PRIDEP07108.

Protocols and materials databases

DNASU1622.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311521; ENSP00000311117; ENSG00000155368. [P07108-2]
ENST00000355857; ENSP00000348116; ENSG00000155368. [P07108-1]
ENST00000393103; ENSP00000376815; ENSG00000155368. [P07108-3]
ENST00000409094; ENSP00000386486; ENSG00000155368. [P07108-2]
ENST00000535617; ENSP00000442917; ENSG00000155368. [P07108-4]
ENST00000535757; ENSP00000439012; ENSG00000155368. [P07108-2]
ENST00000542275; ENSP00000440698; ENSG00000155368. [P07108-5]
GeneID1622.
KEGGhsa:1622.
UCSCuc002tlv.3. human. [P07108-1]
uc002tlw.3. human. [P07108-2]
uc002tlx.3. human. [P07108-3]
uc010yyk.2. human. [P07108-4]
uc021vnj.1. human. [P07108-5]

Organism-specific databases

CTD1622.
GeneCardsGC02P120124.
HGNCHGNC:2690. DBI.
HPACAB008595.
MIM125950. gene.
neXtProtNX_P07108.
PharmGKBPA27158.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4281.
HOVERGENHBG000398.
KOK08762.
OMAERPDNAT.
OrthoDBEOG7SN8G8.
PhylomeDBP07108.
TreeFamTF335802.

Gene expression databases

ArrayExpressP07108.
BgeeP07108.
CleanExHS_DBI.
GenevestigatorP07108.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
InterProIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamPF00887. ACBP. 1 hit.
[Graphical view]
PRINTSPR00689. ACOABINDINGP.
SUPFAMSSF47027. SSF47027. 1 hit.
PROSITEPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDBI. human.
EvolutionaryTraceP07108.
GeneWikiDiazepam_binding_inhibitor.
GenomeRNAi1622.
NextBio6658.
PROP07108.
SOURCESearch...

Entry information

Entry nameACBP_HUMAN
AccessionPrimary (citable) accession number: P07108
Secondary accession number(s): B8ZWD2 expand/collapse secondary AC list , B8ZWD6, B8ZWD7, P08869, Q4VWZ6, Q53SQ7, Q6IB48, Q9UCI8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 149 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 2

Human chromosome 2: entries, gene names and cross-references to MIM