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Q7Z5B4 (RIC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Protein RIC-3
Alternative name(s):
Resistant to inhibitor of cholinesterase 3
Gene names
Name:RIC3
ORF Names:UNQ720/PRO1385
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes functional expression of homomeric alpha-7 and alpha-8 nicotinic acetylcholine receptors at the cell surface. May also promote functional expression of homomeric serotoninergic 5-HT3 receptors, and of heteromeric acetylcholine receptors alpha-3/beta-2, alpha-3/beta-4, alpha-4/beta-2 and alpha-4/beta-4. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subunit structure

Monomer and homodimer. Interacts with CHRNA7, CHRNA3, CHRNA4, CHRNB2, CHRNB4 and HTR3A. Ref.9 Ref.10 Ref.12

Subcellular location

Isoform 1: Endoplasmic reticulum membrane; Single-pass membrane protein Ref.10 Ref.11 Ref.13.

Isoform 2: Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein Ref.10 Ref.11 Ref.13.

Tissue specificity

Broadly expressed, with high levels in muscle, brain, heart, pancreas and testis. In the central nervous system, highest levels are detected in the cerebellum and pituitary gland. Over-expressed in brains from patients with bipolar disease or schizophrenia. Isoform 5 is predominantly expressed in the brain. Ref.1 Ref.2 Ref.14

Domain

The coiled-coil domain mediates transient homodimerization with other acetylcholine receptor-bound RIC3 molecules, promoting stepwise ACHR homomeric assembly at the membrane By similarity.

Sequence similarities

Belongs to the ric-3 family.

Sequence caution

The sequence BAB13871.1 differs from that shown. Reason: Probable cloning artifact.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z5B4-1)

Also known as: a;

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: Q7Z5B4-2)

Also known as: d;

The sequence of this isoform differs from the canonical sequence as follows:
     118-128: LSKGKTTAEDG → VSRIILIILHQ
     129-369: Missing.
Isoform 3 (identifier: Q7Z5B4-3)

Also known as: c;

The sequence of this isoform differs from the canonical sequence as follows:
     41-222: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q7Z5B4-5)

Also known as: b;

The sequence of this isoform differs from the canonical sequence as follows:
     174-174: Missing.
Isoform 5 (identifier: Q7Z5B4-6)

Also known as: e;

The sequence of this isoform differs from the canonical sequence as follows:
     143-224: TSFELAQLQE...EAPYMEDWEG → S

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 By similarity
Chain29 – 369341Protein RIC-3
PRO_0000302731

Regions

Topological domain29 – 9567Lumenal Potential
Transmembrane96 – 11621Helical; Potential
Topological domain117 – 369253Cytoplasmic Potential
Coiled coil140 – 16930 By similarity
Compositional bias81 – 9414Poly-Gly
Compositional bias269 – 2724Poly-Glu

Amino acid modifications

Modified residue2021N6-acetyllysine; alternate Ref.16
Cross-link202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.15

Natural variations

Alternative sequence41 – 222182Missing in isoform 3.
VSP_027939
Alternative sequence118 – 12811LSKGKTTAEDG → VSRIILIILHQ in isoform 2.
VSP_027940
Alternative sequence129 – 369241Missing in isoform 2.
VSP_027941
Alternative sequence143 – 22482TSFEL…EDWEG → S in isoform 5.
VSP_043786
Alternative sequence1741Missing in isoform 4.
VSP_027943
Natural variant571P → H. Ref.8
Corresponds to variant rs17855498 [ dbSNP | Ensembl ].
VAR_034943
Natural variant1301C → Y.
Corresponds to variant rs55990541 [ dbSNP | Ensembl ].
VAR_062208
Natural variant3461G → V in a colorectal cancer sample; somatic mutation. Ref.17
VAR_036391

Experimental info

Sequence conflict231Missing in AAP92163. Ref.1
Sequence conflict1651I → F in AAH22455. Ref.8
Isoform 2:
Sequence conflict1241I → T in AAP92163. Ref.1

Sequences

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

Last modified October 1, 2003. Version 1.
Checksum: 15FD70384070345D

FASTA36941,092
        10         20         30         40         50         60 
MAYSTVQRVA LASGLVLALS LLLPKAFLSR GKRQEPPPTP EGKLGRFPPM MHHHQAPSDG 

        70         80         90        100        110        120 
QTPGARFQRS HLAEAFAKAK GSGGGAGGGG SGRGLMGQII PIYGFGIFLY ILYILFKLSK 

       130        140        150        160        170        180 
GKTTAEDGKC YTAMPGNTHR KITSFELAQL QEKLKETEAA MEKLINRVGP NGESRAQTVT 

       190        200        210        220        230        240 
SDQEKRLLHQ LREITRVMKE GKFIDRFSPE KEAEEAPYME DWEGYPEETY PIYDLSDCIK 

       250        260        270        280        290        300 
RRQETILVDY PDPKELSAEE IAERMGMIEE EESDHLGWES LPTDPRAQED NSVTSCDPKP 

       310        320        330        340        350        360 
ETCSCCFHED EDPAVLAENA GFSADSYPEQ EETTKEEWSQ DFKDEGLGIS TDKAYTGSML 


RKRNPQGLE 

« Hide

Isoform 2 (d) [UniParc].

Checksum: 01D76A36CC9F0C2F
Show »

FASTA12813,663
Isoform 3 (c) [UniParc].

Checksum: C51C0B8B8F21B4B2
Show »

FASTA18720,954
Isoform 4 (b) [UniParc].

Checksum: C66CFFD8641778DA
Show »

FASTA36841,005
Isoform 5 (e) [UniParc].

Checksum: 2D0010517F3E6E20
Show »

FASTA28831,643

References

« Hide 'large scale' references
[1]"Conservation within the RIC-3 gene family. Effectors of mammalian nicotinic acetylcholine receptor expression."
Halevi S., Yassin L., Eshel M., Sala F., Sala S., Criado M., Treinin M.
J. Biol. Chem. 278:34411-34417(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, FUNCTION.
[2]"Molecular cloning and characterization of a novel human variant of RIC-3, a putative chaperone of nicotinic acetylcholine receptors."
Seredenina T., Ferraro T., Terstappen G.C., Caricasole A., Roncarati R.
Biosci. Rep. 28:299-306(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
Tissue: Hippocampus.
[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 2).
[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] (ISOFORM 4).
Tissue: Brain and Embryo.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Spinal cord.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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] (ISOFORM 4), VARIANT HIS-57.
Tissue: Brain.
[9]"Ric-3 promotes functional expression of the nicotinic acetylcholine receptor alpha7 subunit in mammalian cells."
Williams M.E., Burton B., Urrutia A., Shcherbatko A., Chavez-Noriega L.E., Cohen C.J., Aiyar J.
J. Biol. Chem. 280:1257-1263(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHRNA7.
[10]"Cell surface expression of 5-hydroxytryptamine type 3 receptors is promoted by RIC-3."
Cheng A., McDonald N.A., Connolly C.N.
J. Biol. Chem. 280:22502-22507(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HTR3A, SUBCELLULAR LOCATION.
[11]"Dual role of the RIC-3 protein in trafficking of serotonin and nicotinic acetylcholine receptors."
Castillo M., Mulet J., Gutierrez L.M., Ortiz J.A., Castelan F., Gerber S., Sala S., Sala F., Criado M.
J. Biol. Chem. 280:27062-27068(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells."
Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S.
Mol. Pharmacol. 68:1431-1438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHRNA7; CHRNA3; CHRNA4; CHRNB2 AND CHRNB4.
[13]"Differential subcellular localization of RIC-3 isoforms and their role in determining 5-HT3 receptor composition."
Cheng A., Bollan K.A., Greenwood S.M., Irving A.J., Connolly C.N.
J. Biol. Chem. 282:26158-26166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION.
[14]"Lack of RIC-3 congruence with beta2 subunit-containing nicotinic acetylcholine receptors in bipolar disorder."
Severance E.G., Yolken R.H.
Neuroscience 148:454-460(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[15]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-202.
Tissue: Mammary cancer.
[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 LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-346.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY326435 mRNA. Translation: AAP92162.1.
AY326436 mRNA. Translation: AAP92163.1.
AM422214 mRNA. Translation: CAM12309.1.
AY358475 mRNA. Translation: AAQ88839.1.
AK021670 mRNA. Translation: BAB13871.1. Sequence problems.
AK315379 mRNA. Translation: BAG37772.1.
AL832601 mRNA. Translation: CAD89943.1.
AC091013 Genomic DNA. No translation available.
AC116456 Genomic DNA. No translation available.
AC129895 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68628.1.
CH471064 Genomic DNA. Translation: EAW68630.1.
BC022455 mRNA. Translation: AAH22455.1.
CCDSCCDS44533.1. [Q7Z5B4-3]
CCDS55741.1. [Q7Z5B4-6]
CCDS55742.1. [Q7Z5B4-1]
CCDS7788.1. [Q7Z5B4-5]
RefSeqNP_001128581.1. NM_001135109.2. [Q7Z5B4-3]
NP_001193600.1. NM_001206671.2. [Q7Z5B4-1]
NP_001193601.1. NM_001206672.2. [Q7Z5B4-6]
NP_078833.3. NM_024557.4. [Q7Z5B4-5]
XP_006718381.1. XM_006718318.1. [Q7Z5B4-5]
XP_006718383.1. XM_006718320.1.
UniGeneHs.231850.
Hs.568986.

3D structure databases

ProteinModelPortalQ7Z5B4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122743. 2 interactions.
IntActQ7Z5B4. 1 interaction.
MINTMINT-8343009.
STRING9606.ENSP00000344904.

PTM databases

PhosphoSiteQ7Z5B4.

Polymorphism databases

DMDM74713638.

Proteomic databases

MaxQBQ7Z5B4.
PaxDbQ7Z5B4.
PRIDEQ7Z5B4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309737; ENSP00000308820; ENSG00000166405. [Q7Z5B4-1]
ENST00000335425; ENSP00000333988; ENSG00000166405. [Q7Z5B4-3]
ENST00000343202; ENSP00000344904; ENSG00000166405. [Q7Z5B4-5]
ENST00000419822; ENSP00000404415; ENSG00000166405. [Q7Z5B4-2]
ENST00000425599; ENSP00000395320; ENSG00000166405. [Q7Z5B4-6]
GeneID79608.
KEGGhsa:79608.
UCSCuc001mgc.2. human. [Q7Z5B4-5]
uc001mgd.2. human. [Q7Z5B4-1]
uc001mge.2. human. [Q7Z5B4-3]
uc001mgf.4. human. [Q7Z5B4-2]
uc009yfm.2. human. [Q7Z5B4-6]

Organism-specific databases

CTD79608.
GeneCardsGC11M008127.
H-InvDBHIX0009421.
HGNCHGNC:30338. RIC3.
MIM610509. gene.
neXtProtNX_Q7Z5B4.
PharmGKBPA142671066.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46432.
HOVERGENHBG106009.
InParanoidQ7Z5B4.
OMAHRKITNF.
OrthoDBEOG7MKW7H.
PhylomeDBQ7Z5B4.
TreeFamTF333291.

Gene expression databases

ArrayExpressQ7Z5B4.
BgeeQ7Z5B4.
CleanExHS_RIC3.
GenevestigatorQ7Z5B4.

Family and domain databases

InterProIPR026160. Ric3.
[Graphical view]
PANTHERPTHR21723. PTHR21723. 1 hit.
ProtoNetSearch...

Other

GeneWikiRIC3.
GenomeRNAi79608.
NextBio68650.
PROQ7Z5B4.
SOURCESearch...

Entry information

Entry nameRIC3_HUMAN
AccessionPrimary (citable) accession number: Q7Z5B4
Secondary accession number(s): B0B1U0 expand/collapse secondary AC list , B2RD25, D3DQU5, Q6UX78, Q7Z5B3, Q86T94, Q8TBJ9, Q9HAH8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 80 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

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