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Q9Y5K5 (UCHL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. 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 isozyme L5

Short name=UCH-L5
EC=3.4.19.12
Alternative name(s):
Ubiquitin C-terminal hydrolase UCH37
Ubiquitin thioesterase L5
Gene names
Name:UCHL5
Synonyms:UCH37
ORF Names:AD-019, CGI-70
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1. Ref.1 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).

Enzyme regulation

Activated by ADRM1. Inhibited by interaction with NFRKB. Ref.1 Ref.8 Ref.10

Subunit structure

Component of the 19S (PA700) regulatory complex of the 26S proteasome. Interacts with ADRM1 and NFRKB; in vitro ADRM1 and NFRKB compete for interaction with UCHL5. Component of the INO80 complex; specifically part of a complex module associated with N-terminus of INO80. Ref.1 Ref.7 Ref.8 Ref.10 Ref.13

Subcellular location

Cytoplasm. Nucleus. Note: Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus. Ref.10

Sequence similarities

Belongs to the peptidase C12 family.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

forebrain morphogenesis

Inferred from electronic annotation. Source: Ensembl

lateral ventricle development

Inferred from electronic annotation. Source: Ensembl

midbrain development

Inferred from electronic annotation. Source: Ensembl

negative regulation of endopeptidase activity

Inferred from mutant phenotype PubMed 18162577. Source: GOC

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

protein deubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of proteasomal protein catabolic process

Inferred from mutant phenotype PubMed 18162577. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentIno80 complex

Inferred from direct assay Ref.13. Source: UniProtKB

cytosol

Inferred from direct assay Ref.10. Source: UniProtKB

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

proteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionendopeptidase inhibitor activity

Inferred from mutant phenotype PubMed 18162577. Source: UniProtKB

omega peptidase activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

proteasome binding

Inferred from direct assay PubMed 18162577Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11163772Ref.10. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q9Y5K5-1)

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: Q9Y5K5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     246-246: Missing.
     316-329: AKEKQNAKKAQETK → GK
Isoform 3 (identifier: Q9Y5K5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     246-246: Missing.
Isoform 4 (identifier: Q9Y5K5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     246-246: Missing.
     316-329: AKEKQNAKKAQETK → FEKHFEKTLLGK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Ubiquitin carboxyl-terminal hydrolase isozyme L5
PRO_0000211066

Regions

Region313 – 32917Interaction with ADRM1

Sites

Active site881Nucleophile Probable
Active site1641Proton donor By similarity
Site1791Important for enzyme activity By similarity

Amino acid modifications

Modified residue471N6-succinyllysine By similarity
Modified residue1581N6-acetyllysine Ref.11
Modified residue2891N6-succinyllysine By similarity

Natural variations

Alternative sequence2461Missing in isoform 2, isoform 3 and isoform 4.
VSP_005253
Alternative sequence316 – 32914AKEKQ…AQETK → GK in isoform 2.
VSP_005254
Alternative sequence316 – 32914AKEKQ…AQETK → FEKHFEKTLLGK in isoform 4.
VSP_017062
Natural variant1971I → F. Ref.2 Ref.3
VAR_011613

Experimental info

Mutagenesis881C → A: Abolishes enzymatic activity. Ref.1
Sequence conflict61G → V in AAD34065. Ref.2

Secondary structure

.............................................. 329
Helix Strand Turn

Details...

Sequences

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

Last modified May 30, 2006. Version 3.
Checksum: DF307347D48C9D0F

FASTA32937,607
        10         20         30         40         50         60 
MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP 

        70         80         90        100        110        120 
GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS 

       130        140        150        160        170        180 
FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG 

       190        200        210        220        230        240 
LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR 

       250        260        270        280        290        300 
QLAEEEPMDT DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL 

       310        320 
KTLAEHQQLI PLVEKAKEKQ NAKKAQETK 

« Hide

Isoform 2 [UniParc].

Checksum: 2552C52F2CFC1E9C
Show »

FASTA31636,079
Isoform 3 [UniParc].

Checksum: 2ECFB3AB11D07E72
Show »

FASTA32837,478
Isoform 4 [UniParc].

Checksum: A3570094A7EC96CB
Show »

FASTA32637,353

References

« Hide 'large scale' references
[1]"Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1."
Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.
Nat. Cell Biol. 8:994-1002(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, MUTAGENESIS OF CYS-88, INTERACTION WITH ADRM1.
[2]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PHE-197.
[3]"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 2), VARIANT PHE-197.
Tissue: Adrenal gland.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [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 3 AND 4).
Tissue: Lung and Uterus.
[7]"A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes."
Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.
EMBO J. 25:4524-4536(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADRM1, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37."
Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.
EMBO J. 25:5742-5753(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADRM1, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN THE INO80 COMPLEX, INTERACTION WITH NFRKB AND ADRM1, ENZYME REGULATION.
[11]"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-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
[14]"Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain."
Nishio K., Kim S.W., Kawai K., Mizushima T., Yamane T., Hamazaki J., Murata S., Tanaka K., Morimoto Y.
Biochem. Biophys. Res. Commun. 390:855-860(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-228.
[15]"Crystal structure of UCH37."
Center for eukaryotic structural genomics (CESG)
Submitted (AUG-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 2-328.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF147717 mRNA. Translation: AAD31528.1.
AF151828 mRNA. Translation: AAD34065.1.
AF157320 mRNA. Translation: AAF67486.1.
BT006790 mRNA. Translation: AAP35436.1.
AL136370 Genomic DNA. Translation: CAI10829.1.
AL136370 Genomic DNA. Translation: CAI10830.1.
AL136370 Genomic DNA. Translation: CAI10831.1.
AL136370 Genomic DNA. Translation: CAI10833.1.
BC015521 mRNA. Translation: AAH15521.1.
BC025369 mRNA. Translation: AAH25369.1.
CCDSCCDS1378.1. [Q9Y5K5-1]
CCDS55668.1. [Q9Y5K5-3]
CCDS55669.1. [Q9Y5K5-2]
CCDS55670.1. [Q9Y5K5-4]
RefSeqNP_001186190.1. NM_001199261.1. [Q9Y5K5-3]
NP_001186191.1. NM_001199262.1. [Q9Y5K5-4]
NP_001186192.1. NM_001199263.1. [Q9Y5K5-2]
NP_057068.1. NM_015984.3. [Q9Y5K5-1]
UniGeneHs.145469.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7SX-ray2.20A1-228[»]
3IHRX-ray2.95A1-329[»]
3RIIX-ray2.00A/B1-228[»]
3RISX-ray2.40A/B/C/D1-240[»]
3TB3X-ray2.30A/B1-227[»]
ProteinModelPortalQ9Y5K5.
SMRQ9Y5K5. Positions 7-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119509. 185 interactions.
DIPDIP-42671N.
IntActQ9Y5K5. 58 interactions.
MINTMINT-2823912.
STRING9606.ENSP00000356425.

Protein family/group databases

MEROPSC12.005.

PTM databases

PhosphoSiteQ9Y5K5.

Polymorphism databases

DMDM108936023.

Proteomic databases

MaxQBQ9Y5K5.
PaxDbQ9Y5K5.
PRIDEQ9Y5K5.

Protocols and materials databases

DNASU51377.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367448; ENSP00000356418; ENSG00000116750. [Q9Y5K5-4]
ENST00000367449; ENSP00000356419; ENSG00000116750. [Q9Y5K5-2]
ENST00000367454; ENSP00000356424; ENSG00000116750. [Q9Y5K5-3]
ENST00000367455; ENSP00000356425; ENSG00000116750. [Q9Y5K5-1]
GeneID51377.
KEGGhsa:51377.
UCSCuc001gsm.3. human. [Q9Y5K5-1]
uc001gso.3. human. [Q9Y5K5-3]
uc001gsp.3. human. [Q9Y5K5-4]
uc001gsq.3. human. [Q9Y5K5-2]

Organism-specific databases

CTD51377.
GeneCardsGC01M192984.
HGNCHGNC:19678. UCHL5.
HPAHPA005908.
MIM610667. gene.
neXtProtNX_Q9Y5K5.
PharmGKBPA134916228.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321645.
HOVERGENHBG056021.
KOK05610.
PhylomeDBQ9Y5K5.
TreeFamTF313976.

Enzyme and pathway databases

BRENDA3.4.19.12. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkQ9Y5K5.

Gene expression databases

ArrayExpressQ9Y5K5.
BgeeQ9Y5K5.
CleanExHS_UCHL5.
GenevestigatorQ9Y5K5.

Family and domain databases

Gene3D3.40.532.10. 1 hit.
InterProIPR001578. Peptidase_C12_UCH.
IPR017390. Ubiquitinyl_hydrolase_UCH37.
[Graphical view]
PANTHERPTHR10589. PTHR10589. 1 hit.
PfamPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PIRSFPIRSF038120. Ubiquitinyl_hydrolase_UCH37. 1 hit.
PRINTSPR00707. UBCTHYDRLASE.
ProtoNetSearch...

Other

ChiTaRSUCHL5. human.
EvolutionaryTraceQ9Y5K5.
GeneWikiUbiquitin_carboxyl-terminal_hydrolase_L5.
GenomeRNAi51377.
NextBio54875.
PROQ9Y5K5.
SOURCESearch...

Entry information

Entry nameUCHL5_HUMAN
AccessionPrimary (citable) accession number: Q9Y5K5
Secondary accession number(s): Q5LJA6 expand/collapse secondary AC list , Q5LJA7, Q8TBS4, Q96BJ9, Q9H1W5, Q9P0I3, Q9UQN2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 30, 2006
Last modified: July 9, 2014
This is version 126 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM