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O75688 (PPM1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Protein phosphatase 1B

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 2C isoform beta
Short name=PP2C-beta
Gene names
Name:PPM1B
Synonyms:PP2CB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. Ref.12 Ref.15

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Subunit structure

Monomer By similarity. Interacts with PAK6. Interacts with the phosphorylated form of IKBKB/IKKB. Ref.11 Ref.12

Subcellular location

Cytoplasmcytosol. Membrane By similarity. Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization By similarity. Ref.14

Tissue specificity

Highly expressed in heart and skeletal muscle.

Post-translational modification

Isgylation negatively regulates its activity.

N-myristoylation is essential for the recognition of its substrates for dephosphorylation By similarity.

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMIsopeptide bond
Lipoprotein
Myristate
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal protein myristoylation

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of NF-kappaB import into nucleus

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of defense response to virus

Inferred from mutant phenotype Ref.15. Source: UniProtKB

negative regulation of interferon-beta production

Inferred from mutant phenotype Ref.15. Source: UniProtKB

peptidyl-threonine dephosphorylation

Inferred from direct assay PubMed 20801214. Source: UniProtKB

protein dephosphorylation

Inferred from mutant phenotype Ref.12Ref.15. Source: UniProtKB

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

manganese ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from direct assay PubMed 20801214. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Beta-1 (identifier: O75688-1)

Also known as: Beta-X; PPM1B2;

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 Beta-2 (identifier: O75688-2)

Also known as: PPM1B1;

The sequence of this isoform differs from the canonical sequence as follows:
     379-387: ASDEAEESG → GAGDLEDPW
     388-479: Missing.
Isoform Beta-X (identifier: O75688-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-287: Missing.
Isoform 4 (identifier: O75688-4)

The sequence of this isoform differs from the canonical sequence as follows:
     379-380: AS → QK
     381-387: Missing.
     388-479: Missing.
Isoform 5 (identifier: O75688-5)

The sequence of this isoform differs from the canonical sequence as follows:
     322-327: EIMEKS → GKTNAF
     328-380: Missing.
     381-387: Missing.
     388-479: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 479478Protein phosphatase 1B
PRO_0000057746

Sites

Metal binding601Manganese 1 By similarity
Metal binding601Manganese 2 By similarity
Metal binding611Manganese 1; via carbonyl oxygen By similarity
Metal binding2431Manganese 2 By similarity
Metal binding2861Manganese 2 By similarity

Amino acid modifications

Lipidation21N-myristoyl glycine By similarity
Cross-link12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) Ref.10
Cross-link142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) Ref.10

Natural variations

Alternative sequence2 – 287286Missing in isoform Beta-X.
VSP_041085
Alternative sequence322 – 3276EIMEKS → GKTNAF in isoform 5.
VSP_043641
Alternative sequence328 – 38053Missing in isoform 5.
VSP_043642
Alternative sequence379 – 3879ASDEAEESG → GAGDLEDPW in isoform Beta-2.
VSP_005087
Alternative sequence379 – 3802AS → QK in isoform 4.
VSP_043643
Alternative sequence381 – 3877Missing in isoform 4 and isoform 5.
VSP_043644
Alternative sequence388 – 47992Missing in isoform Beta-2, isoform 4 and isoform 5.
VSP_005088

Secondary structure

................................................ 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta-1 (Beta-X) (PPM1B2) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: A3A5797AD263DFBD

FASTA47952,643
        10         20         30         40         50         60 
MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD 

        70         80         90        100        110        120 
GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF 

       130        140        150        160        170        180 
SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI 

       190        200        210        220        230        240 
QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL 

       250        260        270        280        290        300 
ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK 

       310        320        330        340        350        360 
VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR 

       370        380        390        400        410        420 
NVIEAVYSRL NPHRESDGAS DEAEESGSQG KLVEALRQMR INHRGNYRQL LEEMLTSYRL 

       430        440        450        460        470 
AKVEGEESPA EPAATATSSN SDAGNPVTMQ ESHTESESGL AELDSSNEDA GTKMSGEKI 

« Hide

Isoform Beta-2 (PPM1B1) [UniParc].

Checksum: 56A644A4E5E2B12B
Show »

FASTA38742,771
Isoform Beta-X [UniParc].

Checksum: E655DD15842CA329
Show »

FASTA19320,884
Isoform 4 [UniParc].

Checksum: E5C00B5FF4278013
Show »

FASTA38042,086
Isoform 5 [UniParc].

Checksum: E38A263FCF7F1692
Show »

FASTA32736,313

References

« Hide 'large scale' references
[1]"The cloning expression and tissue distribution of human PP2Cbeta."
Marely A.E., Kline A., Crabtree G., Sullivan J.E., Beri R.K.
FEBS Lett. 431:121-124(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
Tissue: Liver.
[2]"Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2Calpha and beta2 isoforms."
Cheng A., Kaldis P., Solomon M.J.
J. Biol. Chem. 275:34744-34749(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
[3]"Protein phosphatase 1B. Cloning and characterization of two major transcripts generated by alternative use of 3' exons."
Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I., Smorodinsky N.I., Lavi S.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
[4]"The 2p21 deletion syndrome: characterization of the transcription content."
Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K., Hershkovitz E.
Genomics 86:195-211(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-2; 4 AND 5).
[5]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
Tissue: Adrenal gland.
[6]"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 BETA-1).
Tissue: Stomach.
[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.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].
[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 BETA-1 AND BETA-X).
Tissue: Brain and Urinary bladder.
[10]"Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugation."
Takeuchi T., Kobayashi T., Tamura S., Yokosawa H.
FEBS Lett. 580:4521-4526(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION AT LYS-12 AND LYS-142.
[11]"Increased PAK6 expression in prostate cancer and identification of PAK6 associated proteins."
Kaur R., Yuan X., Lu M.L., Balk S.P.
Prostate 68:1510-1516(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAK6.
[12]"PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation."
Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K., Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.
Cell. Signal. 21:95-102(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH IKBKB.
[13]"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].
[14]"Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"PPM1B negatively regulates antiviral response via dephosphorylating TBK1."
Zhao Y., Liang L., Fan Y., Sun S., An L., Shi Z., Cheng J., Jia W., Sun W., Mori-Akiyama Y., Zhang H., Fu S., Yang J.
Cell. Signal. 24:2197-2204(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Structural genomics of protein phosphatases."
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. expand/collapse author list , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.
J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005801 mRNA. Translation: CAA06704.1.
AF294792 mRNA. Translation: AAG02232.1.
AJ271832 mRNA. Translation: CAC27992.1.
AJ271835 mRNA. Translation: CAC27993.1.
DQ023508 mRNA. Translation: AAY89639.1.
DQ023509 mRNA. Translation: AAY89640.1.
DQ023510 mRNA. Translation: AAY89641.1.
AF136972 mRNA. Translation: AAG49433.1.
AL833035 mRNA. Translation: CAH56319.1.
AC013717 Genomic DNA. Translation: AAX88954.1.
AC019129 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00282.1.
CH471053 Genomic DNA. Translation: EAX00283.1.
BC012002 mRNA. Translation: AAH12002.1.
BC064381 mRNA. Translation: AAH64381.1.
CCDSCCDS1816.1. [O75688-2]
CCDS1817.1. [O75688-1]
CCDS1818.1. [O75688-3]
CCDS46271.1. [O75688-4]
CCDS46272.1. [O75688-5]
RefSeqNP_001028728.1. NM_001033556.1. [O75688-5]
NP_001028729.1. NM_001033557.1. [O75688-4]
NP_002697.1. NM_002706.4. [O75688-1]
NP_808907.1. NM_177968.2. [O75688-2]
NP_808908.1. NM_177969.2.
UniGeneHs.416769.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P8EX-ray1.82A/B2-297[»]
ProteinModelPortalO75688.
SMRO75688. Positions 4-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111490. 34 interactions.
IntActO75688. 11 interactions.
MINTMINT-2841839.
STRING9606.ENSP00000282412.

Chemistry

BindingDBO75688.
ChEMBLCHEMBL2845.

PTM databases

PhosphoSiteO75688.

Proteomic databases

MaxQBO75688.
PaxDbO75688.
PRIDEO75688.

Protocols and materials databases

DNASU5495.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282412; ENSP00000282412; ENSG00000138032. [O75688-1]
ENST00000345249; ENSP00000326089; ENSG00000138032. [O75688-3]
ENST00000378551; ENSP00000367813; ENSG00000138032. [O75688-2]
ENST00000409432; ENSP00000387287; ENSG00000138032. [O75688-4]
ENST00000409895; ENSP00000387341; ENSG00000138032. [O75688-5]
GeneID5495.
KEGGhsa:5495.
UCSCuc002rts.3. human. [O75688-5]
uc002rtt.3. human. [O75688-1]
uc002rtu.3. human. [O75688-4]
uc002rtv.3. human. [O75688-3]
uc002rtw.3. human. [O75688-2]

Organism-specific databases

CTD5495.
GeneCardsGC02P044307.
HGNCHGNC:9276. PPM1B.
HPAHPA016745.
MIM603770. gene.
neXtProtNX_O75688.
Orphanet163693. 2p21 microdeletion syndrome.
PharmGKBPA33604.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233895.
HOVERGENHBG053647.
InParanoidO75688.
KOK04461.
OMAVMISPEH.
PhylomeDBO75688.
TreeFamTF313590.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO75688.
BgeeO75688.
CleanExHS_PPM1B.
GenevestigatorO75688.

Family and domain databases

Gene3D1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO75688.
GeneWikiPPM1B.
GenomeRNAi5495.
NextBio21250.
PROO75688.
SOURCESearch...

Entry information

Entry namePPM1B_HUMAN
AccessionPrimary (citable) accession number: O75688
Secondary accession number(s): Q461Q2 expand/collapse secondary AC list , Q4J6C1, Q4J6C2, Q658R4, Q96ER6, Q9HAY8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 150 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 chromosome 2

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