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Q9UQB9 (AURKC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aurora kinase C

EC=2.7.11.1
Alternative name(s):
Aurora 3
Aurora/IPL1-related kinase 3
Short name=ARK-3
Short name=Aurora-related kinase 3
Aurora/IPL1/Eg2 protein 2
Serine/threonine-protein kinase 13
Serine/threonine-protein kinase aurora-C
Gene names
Name:AURKC
Synonyms:AIE2, AIK3, AIRK3, ARK3, STK13
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'. Ref.4 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Okadaic acid, an inhibitor of protein phosphatase 1 (PP1), protein phosphatase 2A (PP2A) and protein phosphatase 5 (PP5), increases AURKC activity. AURKC is also stabilized through its interaction with INCENP, which acts also as an activator. Ref.9

Subunit structure

Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC. Interacts directly with BIRC5/survivin and INCENP. Interacts with TACC1. Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Nucleus. Chromosome. Chromosomecentromere. Cytoplasmcytoskeletonspindle. Note: Distributes in the condensed chromosomes during prophase to metaphase. After entering anaphase, there is a dissociation from separated chromosomes and a redistribution to midzone microtubules, and finally remains in the midbody during cytokinesis. Ref.1 Ref.3 Ref.4 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Tissue specificity

Isoform 1 and isoform 2 are expressed in testis. Elevated expression levels were seen only in a subset of cancer cell lines such as Hep-G2, Huh-7 and HeLa. Expression is maximum at M phase. Ref.4

Induction

Expression is cell cycle-regulated, with an increase during G2 and M phases. Ref.3 Ref.8 Ref.9

Involvement in disease

Spermatogenic failure 5 (SPGF5) [MIM:243060]: An infertility disorder caused by spermatogenesis defects. Semen from affected men show close to 100% morphologically abnormal multiflagellar spermatozoa with low motility, oversized irregular heads, and abnormal midpiece and acrosome.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.14

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Meiosis
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processattachment of spindle microtubules to kinetochore

Traceable author statement PubMed 19774610. Source: UniProtKB

cytokinesis

Traceable author statement Ref.3. Source: ProtInc

histone modification

Traceable author statement PubMed 19774610. Source: UniProtKB

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cytokinesis

Traceable author statement PubMed 19774610. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.4. Source: UniProtKB

spindle midzone assembly involved in mitosis

Traceable author statement PubMed 19774610. Source: UniProtKB

   Cellular_componentchromosome passenger complex

Traceable author statement PubMed 19774610. Source: UniProtKB

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed chromosome

Inferred from direct assay Ref.4. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.4. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle

Traceable author statement PubMed 19774610. Source: UniProtKB

spindle midzone

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Inferred from direct assay Ref.4. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine/tyrosine kinase activity

Traceable author statement PubMed 19774610. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UQB9-1)

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: Q9UQB9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.
Isoform 3 (identifier: Q9UQB9-3)

Also known as: Aurora C-SV;

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MSSPRAVVQLGKAQPAGEEL → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Aurora kinase C
PRO_0000085660

Regions

Domain43 – 293251Protein kinase
Nucleotide binding49 – 579ATP By similarity

Sites

Active site1661Proton acceptor By similarity
Binding site721ATP By similarity

Amino acid modifications

Modified residue1981Phosphothreonine; by PKA By similarity

Natural variations

Alternative sequence1 – 3434Missing in isoform 2.
VSP_004872
Alternative sequence1 – 2020MSSPR…AGEEL → M in isoform 3.
VSP_041095
Natural variant521G → E in a lung adenocarcinoma sample; somatic mutation. Ref.15
VAR_040385
Natural variant1481E → Q in a lung squamous cell carcinoma sample; somatic mutation. Ref.15
VAR_040386
Natural variant2441H → Q in a lung adenocarcinoma sample; somatic mutation. Ref.15
VAR_040387

Experimental info

Mutagenesis721K → R: Impairs kinase activity. Ref.8 Ref.9
Mutagenesis1661D → Y: Impairs kinase activity, and keeps AURKC with the chromosomes until the end of mitosis. Ref.10
Mutagenesis1981T → A: Impairs kinase activity. Ref.4 Ref.9
Sequence conflict1091Y → H in AAC25955. Ref.1
Sequence conflict1501L → V in AAC77369. Ref.2
Sequence conflict193 – 1953SLR → LPE in AAC77369. Ref.2

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 41B7DFCA91704201

FASTA30935,591
        10         20         30         40         50         60 
MSSPRAVVQL GKAQPAGEEL ATANQTAQQP SSPAMRRLTV DDFEIGRPLG KGKFGNVYLA 

        70         80         90        100        110        120 
RLKESHFIVA LKVLFKSQIE KEGLEHQLRR EIEIQAHLQH PNILRLYNYF HDARRVYLIL 

       130        140        150        160        170        180 
EYAPRGELYK ELQKSEKLDE QRTATIIEEL ADALTYCHDK KVIHRDIKPE NLLLGFRGEV 

       190        200        210        220        230        240 
KIADFGWSVH TPSLRRKTMC GTLDYLPPEM IEGRTYDEKV DLWCIGVLCY ELLVGYPPFE 

       250        260        270        280        290        300 
SASHSETYRR ILKVDVRFPL SMPLGARDLI SRLLRYQPLE RLPLAQILKH PWVQAHSRRV 


LPPCAQMAS 

« Hide

Isoform 2 [UniParc].

Checksum: 8DF2BDC1F436E266
Show »

FASTA27532,187
Isoform 3 (Aurora C-SV) [UniParc].

Checksum: D07FD6988B208140
Show »

FASTA29033,672

References

« Hide 'large scale' references
[1]"Protein kinase profile of sperm and eggs: cloning and characterization of two novel testis-specific protein kinases (AIE1, AIE2) related to yeast and fly chromosome segregation regulators."
Tseng T.-C., Chen S.-H., Hsu Y.-P.P., Tang T.K.
DNA Cell Biol. 17:823-833(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
Tissue: Testis.
[2]"Cloning of STK13, a third human protein kinase related to Drosophila aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter."
Bernard M., Sanseau P., Henry C., Couturier A., Prigent C.
Genomics 53:406-409(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[3]"Cell cycle-dependent expression and centrosome localization of a third human Aurora/Ipl1-related protein kinase, AIK3."
Kimura M., Matsuda Y., Yoshioka T., Okano Y.
J. Biol. Chem. 274:7334-7340(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION.
Tissue: Testis.
[4]"Cloning and characterization of a novel human Aurora C splicing variant."
Yan X., Wu Y., Li Q., Cao L., Liu X., Saiyin H., Yu L.
Biochem. Biophys. Res. Commun. 328:353-361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF THR-198, SUBCELLULAR LOCATION.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [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] (ISOFORM 2).
Tissue: Brain.
[8]"Aurora-C kinase is a novel chromosomal passenger protein that can complement Aurora-B kinase function in mitotic cells."
Sasai K., Katayama H., Stenoien D.L., Fujii S., Honda R., Kimura M., Okano Y., Tatsuka M., Suzuki F., Nigg E.A., Earnshaw W.C., Brinkley W.R., Sen S.
Cell Motil. Cytoskeleton 59:249-263(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INCENP, MUTAGENESIS OF LYS-72.
[9]"Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C."
Li X., Sakashita G., Matsuzaki H., Sugimoto K., Kimura K., Hanaoka F., Taniguchi H., Furukawa K., Urano T.
J. Biol. Chem. 279:47201-47211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CDC COMPLEX, SUBCELLULAR LOCATION, ENZYME REGULATION, FUNCTION, MUTAGENESIS OF LYS-72 AND THR-198.
[10]"Aurora C is directly associated with Survivin and required for cytokinesis."
Yan X., Cao L., Li Q., Wu Y., Zhang H., Saiyin H., Liu X., Zhang X., Shi Q., Yu L.
Genes Cells 10:617-626(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CDC COMPLEX, INTERACTION WITH BIRC5, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF ASP-166.
[11]"Homozygous mutation of AURKC yields large-headed polyploid spermatozoa and causes male infertility."
Dieterich K., Soto Rifo R., Faure A.K., Hennebicq S., Ben Amar B., Zahi M., Perrin J., Martinez D., Sele B., Jouk P.-S., Ohlmann T., Rousseaux S., Lunardi J., Ray P.F.
Nat. Genet. 39:661-665(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SPGF5.
[12]"Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein."
Gabillard J.C., Ulisse S., Baldini E., Sorrenti S., Cremet J.Y., Coccaro C., Prigent C., D'Armiento M., Arlot-Bonnemains Y.
Biochem. Biophys. Res. Commun. 408:647-653(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TACC1.
[13]"A role for Aurora C in the chromosomal passenger complex during human preimplantation embryo development."
Avo Santos M., van de Werken C., de Vries M., Jahr H., Vromans M.J., Laven J.S., Fauser B.C., Kops G.J., Lens S.M., Baart E.B.
Hum. Reprod. 26:1868-1881(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"A new AURKC mutation causing macrozoospermia: implications for human spermatogenesis and clinical diagnosis."
Ben Khelifa M., Zouari R., Harbuz R., Halouani L., Arnoult C., Lunardi J., Ray P.F.
Mol. Hum. Reprod. 17:762-768(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SPGF5.
[15]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-52; GLN-148 AND GLN-244.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF054621 mRNA. Translation: AAC25955.1.
AF059681 mRNA. Translation: AAC77369.1.
AB017332 mRNA. Translation: BAA76292.1.
AY661554 mRNA. Translation: AAT64422.1.
AC005261 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW72485.1.
BC075064 mRNA. Translation: AAH75064.2.
CCDSCCDS33128.1. [Q9UQB9-1]
CCDS46205.1. [Q9UQB9-3]
CCDS46206.1. [Q9UQB9-2]
RefSeqNP_001015878.1. NM_001015878.1. [Q9UQB9-1]
NP_001015879.1. NM_001015879.1. [Q9UQB9-3]
NP_003151.2. NM_003160.2. [Q9UQB9-2]
UniGeneHs.98338.

3D structure databases

ProteinModelPortalQ9UQB9.
SMRQ9UQB9. Positions 36-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112671. 14 interactions.
IntActQ9UQB9. 3 interactions.
STRING9606.ENSP00000302898.

Chemistry

BindingDBQ9UQB9.
ChEMBLCHEMBL3935.
GuidetoPHARMACOLOGY1938.

PTM databases

PhosphoSiteQ9UQB9.

Polymorphism databases

DMDM27805738.

Proteomic databases

PaxDbQ9UQB9.
PRIDEQ9UQB9.

Protocols and materials databases

DNASU6795.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302804; ENSP00000302898; ENSG00000105146. [Q9UQB9-1]
ENST00000415300; ENSP00000407162; ENSG00000105146. [Q9UQB9-3]
ENST00000448930; ENSP00000406798; ENSG00000105146. [Q9UQB9-2]
ENST00000598785; ENSP00000471830; ENSG00000105146. [Q9UQB9-2]
GeneID6795.
KEGGhsa:6795.
UCSCuc002qoc.3. human. [Q9UQB9-3]
uc002qod.3. human. [Q9UQB9-1]

Organism-specific databases

CTD6795.
GeneCardsGC19P057743.
HGNCHGNC:11391. AURKC.
HPAHPA034859.
MIM243060. phenotype.
603495. gene.
neXtProtNX_Q9UQB9.
Orphanet137893. Male infertility due to large-headed multiflagellar polyploid spermatozoa.
PharmGKBPA36200.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
HOVERGENHBG108519.
InParanoidQ9UQB9.
KOK11480.
OMAILKHPWV.
OrthoDBEOG74FF1F.
PhylomeDBQ9UQB9.
TreeFamTF105331.

Enzyme and pathway databases

SignaLinkQ9UQB9.

Gene expression databases

ArrayExpressQ9UQB9.
BgeeQ9UQB9.
CleanExHS_AURKC.
GenevestigatorQ9UQB9.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAURKC.
GenomeRNAi6795.
NextBio26545.
PROQ9UQB9.
SOURCESearch...

Entry information

Entry nameAURKC_HUMAN
AccessionPrimary (citable) accession number: Q9UQB9
Secondary accession number(s): O60681 expand/collapse secondary AC list , O75442, Q6AZY8, Q6DLZ0, Q9UPK5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 137 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

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 19

Human chromosome 19: entries, gene names and cross-references to MIM