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O75604 (UBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 2

EC=3.4.19.12
Alternative name(s):
41 kDa ubiquitin-specific protease
Deubiquitinating enzyme 2
Ubiquitin thioesterase 2
Ubiquitin-specific-processing protease 2
Gene names
Name:USP2
Synonyms:UBP41
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities. Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity. Has no deubiquitinase activity against p53/TP53. Prevents MDM2-mediated degradation of MDM4. Plays a role in the G1/S cell-cycle progression in normal and cancer cells. Plays a role in the regulation of myogenic differentiation of embryonic muscle cells. Ref.8 Ref.9 Ref.10

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Cofactor

Binds 1 zinc ion.

Enzyme regulation

Cleavage is inhibited by ubiquitin in a dosage-dependent manner. Cleavage is blocked by ubiquitin aldehyde. Ref.13

Subunit structure

Homooligomer By similarity. Found in trimeric complex with MDM2 and MDM4 and UPB2. Interacts with CCND1; the interaction is direct and promotes its stabilization by antagonizing ubiquitin-dependent degradation. Interacts (via N-terminus and C-terminus) with MDM2. Interacts with MDM4. Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Note: Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane By similarity.

Isoform 4: Nucleus By similarity.

Tissue specificity

Expressed in mesangial cells of the kidney and in different types of glomerulonephritides (at protein level). Ref.11

Induction

Down-regulated by cisplatin (at protein level). Ref.10 Ref.13

Domain

The different N-terminus extensions of isoform 1 and isoform 4 determine their respective subcellular localization and differentiel effect on myoblast fusion and accumulation of muscle-specific proteins. The different N-terminus extensions of isoform 1 and isoform 4 are not essential for their catalytic activity By similarity.

Sequence similarities

Belongs to the peptidase C19 family. USP2 subfamily.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processCell cycle
Myogenesis
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

muscle organ development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

protein deubiquitination

Inferred from direct assay Ref.10Ref.9. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.8. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclin binding

Inferred from physical interaction Ref.9. Source: UniProtKB

cysteine-type endopeptidase activity

Traceable author statement PubMed 9827704. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin protein ligase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from direct assay Ref.8. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.8. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KRT15P190122EBI-743272,EBI-739566
MDM2Q009874EBI-743272,EBI-389668

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75604-1)

Also known as: USP2a; USP2-69;

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: O75604-2)

Also known as: USP2b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.
     253-258: PGRDGM → MLNKAK
Note: No experimental confirmation available.
Isoform 3 (identifier: O75604-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-258: MSQLSSTLKR...RSSSPGRDGM → MLVPGSTRPYSKKRQ
Isoform 4 (identifier: O75604-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-258: MSQLSSTLKR...RSSSPGRDGM → MRTSYTVTLP...FVGLLLNKAK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Ubiquitin carboxyl-terminal hydrolase 2
PRO_0000080616

Regions

Domain267 – 599333USP
Region1 – 200200Necessary for interaction with MDM4
Region403 – 503101Necessary for interaction with MDM4

Sites

Active site2761Nucleophile
Active site5571Proton acceptor By similarity
Metal binding4251Zinc Potential
Metal binding4281Zinc
Metal binding4761Zinc
Metal binding4791Zinc

Natural variations

Alternative sequence1 – 258258MSQLS…GRDGM → MLVPGSTRPYSKKRQ in isoform 3.
VSP_039559
Alternative sequence1 – 258258MSQLS…GRDGM → MRTSYTVTLPEDPPAAPFPA LAKELRPRSPLSPSLLLSTF VGLLLNKAK in isoform 4.
VSP_039560
Alternative sequence1 – 252252Missing in isoform 2.
VSP_005256
Alternative sequence253 – 2586PGRDGM → MLNKAK in isoform 2.
VSP_005257
Natural variant1741R → Q.
Corresponds to variant rs33929148 [ dbSNP | Ensembl ].
VAR_051519
Natural variant3831N → S.
Corresponds to variant rs45533837 [ dbSNP | Ensembl ].
VAR_051520

Experimental info

Mutagenesis2761C → A: Loss of enzymatic activity. Increases the steady-state level of CCND1. Ref.9
Mutagenesis5491H → A: Loss of enzymatic activity. Increases the steady-state level of MDM2 and MDM4 that leads to attenuation of MDM2-mediated degradation of p53/TP53 and MDM4. Increases the level of p53/TP53 and MDM4 ubiquitin conjugates. Ref.8 Ref.10
Sequence conflict4211S → G in BAB71388. Ref.3
Sequence conflict5011H → R in BAB71388. Ref.3
Sequence conflict5941L → H in AAC28392. Ref.1
Sequence conflict602 – 6054PSRM → TSPI in AAC28392. Ref.1
Isoform 3:
Sequence conflict101Y → S in AAH41366. Ref.7

Secondary structure

......................................................... 605
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (USP2a) (USP2-69) [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: AFF4DA9344D21812

FASTA60568,072
        10         20         30         40         50         60 
MSQLSSTLKR YTESARYTDA HYAKSGYGAY TPSSYGANLA ASLLEKEKLG FKPVPTSSFL 

        70         80         90        100        110        120 
TRPRTYGPSS LLDYDRGRPL LRPDITGGGK RAESQTRGTE RPLGSGLSGG SGFPYGVTNN 

       130        140        150        160        170        180 
CLSYLPINAY DQGVTLTQKL DSQSDLARDF SSLRTSDSYR IDPRNLGRSP MLARTRKELC 

       190        200        210        220        230        240 
TLQGLYQTAS CPEYLVDYLE NYGRKGSASQ VPSQAPPSRV PEIISPTYRP IGRYTLWETG 

       250        260        270        280        290        300 
KGQAPGPSRS SSPGRDGMNS KSAQGLAGLR NLGNTCFMNS ILQCLSNTRE LRDYCLQRLY 

       310        320        330        340        350        360 
MRDLHHGSNA HTALVEEFAK LIQTIWTSSP NDVVSPSEFK TQIQRYAPRF VGYNQQDAQE 

       370        380        390        400        410        420 
FLRFLLDGLH NEVNRVTLRP KSNPENLDHL PDDEKGRQMW RKYLEREDSR IGDLFVGQLK 

       430        440        450        460        470        480 
SSLTCTDCGY CSTVFDPFWD LSLPIAKRGY PEVTLMDCMR LFTKEDVLDG DEKPTCCRCR 

       490        500        510        520        530        540 
GRKRCIKKFS IQRFPKILVL HLKRFSESRI RTSKLTTFVN FPLRDLDLRE FASENTNHAV 

       550        560        570        580        590        600 
YNLYAVSNHS GTTMGGHYTA YCRSPGTGEW HTFNDSSVTP MSSSQVRTSD AYLLFYELAS 


PPSRM 

« Hide

Isoform 2 (USP2b) [UniParc].

Checksum: 7CDF2F9A300B864F
Show »

FASTA35340,638
Isoform 3 [UniParc].

Checksum: 5C93CA5F03D43293
Show »

FASTA36241,682
Isoform 4 [UniParc].

Checksum: 2A5B0403419F0655
Show »

FASTA39645,241

References

« Hide 'large scale' references
[1]"Cloning and expression of the human and mouse UBP41."
Gong L., Yeh E.T.H.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[2]"Molecular cloning and characterization of USP2b in the human prostate cancer cell line LNCaP."
Rossi S., Graner E., Weinstein L.J., Loda M.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Prostate cancer.
[3]"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 4).
Tissue: Testis.
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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].
[6]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 (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] (ISOFORMS 1 AND 3).
Tissue: Lymph and Testis.
[8]"The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2."
Stevenson L.F., Sparks A., Allende-Vega N., Xirodimas D.P., Lane D.P., Saville M.K.
EMBO J. 26:976-986(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2, MUTAGENESIS OF HIS-549.
[9]"Suppression of cancer cell growth by promoting cyclin D1 degradation."
Shan J., Zhao W., Gu W.
Mol. Cell 36:469-476(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CCND1, MUTAGENESIS OF CYS-276.
[10]"MdmX is a substrate for the deubiquitinating enzyme USP2a."
Allende-Vega N., Sparks A., Lane D.P., Saville M.K.
Oncogene 29:432-441(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDM2 AND MDM4, INDUCTION, MUTAGENESIS OF HIS-549.
[11]"Expression of USP2-69 in mesangial cells in vivo and in vitro."
Wang S., Wu H., Liu Y., Sun J., Zhao Z., Chen Q., Guo M., Ma D., Zhang Z.
Pathol. Int. 60:184-192(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Covalent ubiquitin-usp2 complex."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 251-605.
[13]"Structural basis of ubiquitin recognition by the deubiquitinating protease USP2."
Renatus M., Parrado S.G., D'Arcy A., Eidhoff U., Gerhartz B., Hassiepen U., Pierrat B., Riedl R., Vinzenz D., Worpenberg S., Kroemer M.
Structure 14:1293-1302(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 258-605 IN COMPLEX WITH UBIQUITIN AND ZINC-BINDING, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF079564 mRNA. Translation: AAC28392.1.
AF440755 mRNA. Translation: AAN65363.1.
AK057225 mRNA. Translation: BAB71388.1.
AK292255 mRNA. Translation: BAF84944.1.
EF445044 Genomic DNA. Translation: ACA06096.1.
EF445044 Genomic DNA. Translation: ACA06097.1.
AP003396 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67484.1.
CH471065 Genomic DNA. Translation: EAW67485.1.
CH471065 Genomic DNA. Translation: EAW67486.1.
BC002854 mRNA. Translation: AAH02854.1.
BC002955 mRNA. Translation: AAH02955.1.
BC041366 mRNA. Translation: AAH41366.1.
RefSeqNP_001230688.1. NM_001243759.1.
NP_004196.4. NM_004205.4.
NP_741994.1. NM_171997.2.
XP_005271778.1. XM_005271721.2.
XP_005271779.1. XM_005271722.1.
UniGeneHs.524085.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HD5X-ray1.85A258-605[»]
2IBIX-ray2.20A251-605[»]
3NHEX-ray1.26A258-605[»]
3V6CX-ray1.70A258-605[»]
3V6EX-ray2.10A258-605[»]
ProteinModelPortalO75604.
SMRO75604. Positions 263-600.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114553. 70 interactions.
DIPDIP-29134N.
IntActO75604. 10 interactions.
MINTMINT-4304073.
STRING9606.ENSP00000260187.

Chemistry

ChEMBLCHEMBL1293227.

Protein family/group databases

MEROPSC19.013.

PTM databases

PhosphoSiteO75604.

Proteomic databases

PaxDbO75604.
PRIDEO75604.

Protocols and materials databases

DNASU9099.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260187; ENSP00000260187; ENSG00000036672. [O75604-1]
ENST00000455332; ENSP00000407842; ENSG00000036672.
ENST00000525735; ENSP00000436952; ENSG00000036672. [O75604-4]
GeneID9099.
KEGGhsa:9099.
UCSCuc001pwl.4. human. [O75604-4]
uc001pwm.4. human. [O75604-1]

Organism-specific databases

CTD9099.
GeneCardsGC11M119259.
HGNCHGNC:12618. USP2.
HPAHPA006777.
HPA007222.
MIM604725. gene.
neXtProtNX_O75604.
PharmGKBPA37244.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000231498.
HOVERGENHBG011164.
InParanoidO75604.
KOK11833.
OMASASHRSY.
OrthoDBEOG7FR7GN.
PhylomeDBO75604.
TreeFamTF106277.

Gene expression databases

ArrayExpressO75604.
BgeeO75604.
CleanExHS_USP2.
GenevestigatorO75604.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP2. human.
EvolutionaryTraceO75604.
GeneWikiUSP2.
GenomeRNAi9099.
NextBio34107.
PROO75604.
SOURCESearch...

Entry information

Entry nameUBP2_HUMAN
AccessionPrimary (citable) accession number: O75604
Secondary accession number(s): B0YJB8 expand/collapse secondary AC list , E9PPM2, Q8IUM2, Q8IW04, Q96MB9, Q9BQ21
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 27, 2002
Last modified: April 16, 2014
This is version 129 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

Peptidase families

Classification of peptidase families and list of entries

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