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P52294 (IMA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Importin subunit alpha-5
Alternative name(s):
Karyopherin subunit alpha-1
Nucleoprotein interactor 1
Short name=NPI-1
RAG cohort protein 2
SRP1-beta

Cleaved into the following chain:

  1. Importin subunit alpha-5, N-terminally processed
Gene names
Name:KPNA1
Synonyms:RCH2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.

Subunit structure

Heterodimer; with KPNB1. Interacts with ANP32E. Interacts with ZIC3 By similarity. Interacts with NSMF; the interaction occurs in a calcium-independent manner after synaptic NMDA receptor stimulation and is required for nuclear import of NSMF but is competed by CABP1 By similarity. Interacts with the nucleoprotein of influenza A viruses. Binds to HCMV (human cytomegalovirus) UL84, HIV-1 Vpr and to ebolavirus VP24. Interacts with APEX1 and RAG1. Interacts with CTNNBL1 (via its N-terminal). Interacts with AICDA (via its NLS). Interacts with SNAI1 (via zinc fingers). Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.19

Subcellular location

Cytoplasm. Nucleus Ref.10.

Tissue specificity

Expressed ubiquitously.

Domain

Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import. Ref.9

The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins By similarity. Ref.9

The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding By similarity. Ref.9

Post-translational modification

Polyubiquitinated in the presence of RAG1 (in vitro).

Sequence similarities

Belongs to the importin alpha family.

Contains 10 ARM repeats.

Contains 1 IBB domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Protein transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Traceable author statement PubMed 7754385. Source: ProtInc

apoptotic DNA fragmentation

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

positive regulation of protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA recombination

Traceable author statement Ref.7. Source: ProtInc

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear pore

Traceable author statement Ref.7. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionnuclear localization sequence binding

Traceable author statement PubMed 7754385. Source: ProtInc

protein transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9WMX22EBI-358383,EBI-6863741From a different organism.
DCAF8Q5TAQ92EBI-358383,EBI-740686
GRM1Q132552EBI-358383,EBI-8527352

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538Importin subunit alpha-5
PRO_0000120719
Initiator methionine11Removed; alternate Ref.20
Chain2 – 538537Importin subunit alpha-5, N-terminally processed
PRO_0000424491

Regions

Domain1 – 5757IBB
Repeat77 – 11741ARM 1; truncated
Repeat118 – 16144ARM 2
Repeat162 – 20645ARM 3
Repeat207 – 24539ARM 4
Repeat246 – 29045ARM 5
Repeat291 – 33040ARM 6
Repeat331 – 37242ARM 7
Repeat373 – 41240ARM 8
Repeat413 – 45745ARM 9
Repeat460 – 50445ARM 10; atypical
Region149 – 24193NLS binding site (major) By similarity
Region245 – 437193Binding to RAG1
Region318 – 40689NLS binding site (minor) By similarity
Motif42 – 5110Nuclear localization signal By similarity
Compositional bias25 – 284Poly-Arg

Amino acid modifications

Modified residue11N-acetylmethionine Ref.20
Modified residue21N-acetylthreonine; in Importin subunit alpha-5, N-terminally processed Ref.20

Natural variations

Natural variant731S → N. Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs4678193 [ dbSNP | Ensembl ].
VAR_050002

Experimental info

Sequence conflict1421T → S in AAC60648. Ref.1
Sequence conflict1691G → R in AAC60648. Ref.1

Secondary structure

.................................................................. 538
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52294 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: E8407A3352D6051C

FASTA53860,222
        10         20         30         40         50         60 
MTTPGKENFR LKSYKNKSLN PDEMRRRREE EGLQLRKQKR EEQLFKRRNV ATAEEETEEE 

        70         80         90        100        110        120 
VMSDGGFHEA QISNMEMAPG GVITSDMIEM IFSKSPEQQL SATQKFRKLL SKEPNPPIDE 

       130        140        150        160        170        180 
VISTPGVVAR FVEFLKRKEN CTLQFESAWV LTNIASGNSL QTRIVIQAGA VPIFIELLSS 

       190        200        210        220        230        240 
EFEDVQEQAV WALGNIAGDS TMCRDYVLDC NILPPLLQLF SKQNRLTMTR NAVWALSNLC 

       250        260        270        280        290        300 
RGKSPPPEFA KVSPCLNVLS WLLFVSDTDV LADACWALSY LSDGPNDKIQ AVIDAGVCRR 

       310        320        330        340        350        360 
LVELLMHNDY KVVSPALRAV GNIVTGDDIQ TQVILNCSAL QSLLHLLSSP KESIKKEACW 

       370        380        390        400        410        420 
TISNITAGNR AQIQTVIDAN IFPALISILQ TAEFRTRKEA AWAITNATSG GSAEQIKYLV 

       430        440        450        460        470        480 
ELGCIKPLCD LLTVMDSKIV QVALNGLENI LRLGEQEAKR NGTGINPYCA LIEEAYGLDK 

       490        500        510        520        530 
IEFLQSHENQ EIYQKAFDLI EHYFGTEDED SSIAPQVDLN QQQYIFQQCE APMEGFQL 

« Hide

References

« Hide 'large scale' references
[1]"NPI-1, the human homolog of SRP-1, interacts with influenza virus nucleoprotein."
O'Neill R.E., Palese P.
Virology 206:116-125(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-73.
[3]"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], VARIANT ASN-73.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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], VARIANT ASN-73.
[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], VARIANT ASN-73.
Tissue: Lung.
[7]"RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1."
Cortes P., Ye Z.-S., Baltimore D.
Proc. Natl. Acad. Sci. U.S.A. 91:7633-7637(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAG1.
[8]"Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes."
Moroianu J., Blobel G., Radu A.
Proc. Natl. Acad. Sci. U.S.A. 92:2008-2011(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence."
Moroianu J., Blobel G., Radu A.
Proc. Natl. Acad. Sci. U.S.A. 93:6572-6576(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 481-495, DOMAINS IBB.
[10]"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins."
Moroianu J., Hijikata M., Blobel G., Radu A.
Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUBUNIT.
[11]"Viral protein R regulates nuclear import of the HIV-1 pre-integration complex."
Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L., Lane C.M., Moore M.S., Blobel G., Bukrinsky M.
EMBO J. 17:909-917(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPR.
[12]"A nonconventional nuclear localization signal within the UL84 protein of human cytomegalovirus mediates nuclear import via the importin alpha/beta pathway."
Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.
J. Virol. 77:3734-3748(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCMV UL84.
[13]"Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1)."
Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.
Nucleic Acids Res. 33:3303-3312(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APEX1.
[14]"Ebola virus VP24 binds karyopherin alpha-1 and blocks STAT1 nuclear accumulation."
Reid S.P., Leung L.W., Hartman A.L., Martinez O., Shaw M.L., Carbonnelle C., Volchkov V.E., Nichol S.T., Basler C.F.
J. Virol. 80:5156-5167(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBOLAVIRUS VP24.
[15]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase."
Simkus C., Makiya M., Jones J.M.
Mol. Immunol. 46:1319-1325(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[17]"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].
[18]"Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAI1.
[19]"CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31."
Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.
J. Biol. Chem. 286:17091-17102(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNBL1 AND AICDA.
[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 MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S75295 mRNA. Translation: AAC60648.1.
BT006959 mRNA. Translation: AAP35605.1.
CR456743 mRNA. Translation: CAG33024.1.
AC083798 Genomic DNA. No translation available.
AC096861 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79482.1.
CH471052 Genomic DNA. Translation: EAW79483.1.
BC002374 mRNA. Translation: AAH02374.1.
BC003009 mRNA. Translation: AAH03009.1.
PIRI59931.
RefSeqNP_002255.3. NM_002264.3.
XP_005247494.1. XM_005247437.2.
UniGeneHs.161008.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JDQX-ray2.20A/B66-512[»]
3TJ3X-ray2.70A/B66-512[»]
4B18X-ray2.52A66-512[»]
ProteinModelPortalP52294.
SMRP52294. Positions 10-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110034. 61 interactions.
DIPDIP-29296N.
IntActP52294. 33 interactions.
MINTMINT-240027.
STRING9606.ENSP00000343701.

PTM databases

PhosphoSiteP52294.

Polymorphism databases

DMDM296439328.

Proteomic databases

PaxDbP52294.
PRIDEP52294.

Protocols and materials databases

DNASU3836.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344337; ENSP00000343701; ENSG00000114030.
GeneID3836.
KEGGhsa:3836.
UCSCuc003efb.1. human.

Organism-specific databases

CTD3836.
GeneCardsGC03M122140.
HGNCHGNC:6394. KPNA1.
HPAHPA053627.
MIM600686. gene.
neXtProtNX_P52294.
PharmGKBPA30185.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5064.
HOGENOMHOG000167616.
HOVERGENHBG001846.
InParanoidP52294.
KOK15042.
OMAVIDAHIF.
OrthoDBEOG7VHSWV.
PhylomeDBP52294.
TreeFamTF354205.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkP52294.

Gene expression databases

ArrayExpressP52294.
BgeeP52294.
CleanExHS_KPNA1.
GenevestigatorP52294.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]
PfamPF00514. Arm. 8 hits.
PF01749. IBB. 1 hit.
[Graphical view]
PIRSFPIRSF005673. Importin_alpha. 1 hit.
SMARTSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 4 hits.
PS51214. IBB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP52294.
GeneWikiKaryopherin_alpha_1.
GenomeRNAi3836.
NextBio15079.
PMAP-CutDBP52294.
PROP52294.
SOURCESearch...

Entry information

Entry nameIMA5_HUMAN
AccessionPrimary (citable) accession number: P52294
Secondary accession number(s): D3DN93, Q6IBQ9, Q9BQ56
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 151 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

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 3

Human chromosome 3: entries, gene names and cross-references to MIM