Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05129 (KPCG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C gamma type

Short name=PKC-gamma
EC=2.7.11.13
Gene names
Name:PRKCG
Synonyms:PKCG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length697 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress By similarity. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Binds 3 calcium ions per subunit. The ions are bound to the C2 domain.

Enzyme regulation

Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-514 (activation loop of the kinase domain), Thr-655 (turn motif) and Thr-674 (hydrophobic region), need to be phosphorylated for its full activation.

Subunit structure

Interacts with GRIA4 By similarity. Interacts with CDCP1. Interacts with TP53INP1 and p53/TP53. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Cell membrane; Peripheral membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectiondendrite By similarity. Note: Translocates to synaptic membranes on stimulation By similarity.

Tissue specificity

Expressed in Purkinje cells of the cerebellar cortex. Ref.15

Post-translational modification

Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4 By similarity.

Ubiquitinated. Ref.10

Involvement in disease

Spinocerebellar ataxia 14 (SCA14) [MIM:605361]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA14 is an autosomal dominant cerebellar ataxia (ADCA).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Sequence similarities

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

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Synapse
Synaptosome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Neurodegeneration
Spinocerebellar ataxia
   DomainRepeat
Zinc-finger
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of phospholipase C activity

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

chemosensory behavior

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

innervation

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

learning or memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein catabolic process

Inferred from direct assay PubMed 15808853. Source: HGNC

negative regulation of protein ubiquitination

Inferred from direct assay PubMed 15808853. Source: HGNC

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphorylation

Inferred from direct assay PubMed 15808853. Source: HGNC

platelet activation

Traceable author statement. Source: Reactome

positive regulation of mismatch repair

Inferred from direct assay PubMed 15808853. Source: HGNC

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement Ref.3. Source: ProtInc

response to morphine

Inferred from sequence or structural similarity. Source: UniProtKB

response to pain

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-dependent protein kinase C activity

Inferred from electronic annotation. Source: Ensembl

protein kinase C activity

Traceable author statement Ref.3. Source: ProtInc

protein kinase activity

Inferred from direct assay PubMed 15808853. Source: HGNC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 697697Protein kinase C gamma type
PRO_0000055689

Regions

Domain170 – 26091C2
Domain351 – 614264Protein kinase
Domain615 – 68571AGC-kinase C-terminal
Zinc finger35 – 8551Phorbol-ester/DAG-type 1
Zinc finger100 – 15051Phorbol-ester/DAG-type 2
Nucleotide binding357 – 3659ATP By similarity

Sites

Active site4801Proton acceptor By similarity
Metal binding1861Calcium 1; via carbonyl oxygen
Metal binding1871Calcium 1
Metal binding1871Calcium 2
Metal binding1931Calcium 2
Metal binding2461Calcium 1
Metal binding2461Calcium 2
Metal binding2471Calcium 2; via carbonyl oxygen
Metal binding2481Calcium 1
Metal binding2481Calcium 2
Metal binding2481Calcium 3
Metal binding2511Calcium 3
Metal binding2521Calcium 3; via carbonyl oxygen
Metal binding2541Calcium 1
Metal binding2541Calcium 3
Binding site3801ATP By similarity

Amino acid modifications

Modified residue2501Phosphothreonine; by autocatalysis By similarity
Modified residue5141Phosphothreonine; by PDPK1 Probable
Modified residue6481Phosphothreonine; by autocatalysis Potential
Modified residue6551Phosphothreonine; by autocatalysis By similarity
Modified residue6741Phosphothreonine; by autocatalysis By similarity
Modified residue6751Phosphotyrosine; by SYK By similarity

Natural variations

Natural variant1011H → Y in SCA14. Ref.15
VAR_017060
Natural variant1191S → P in SCA14. Ref.15
VAR_017061
Natural variant1281G → D in SCA14. Ref.15
VAR_017062
Natural variant1411R → C. Ref.13
VAR_008755
Natural variant4151H → Q. Ref.13
VAR_008756
Natural variant5231A → D. Ref.13
VAR_008757
Natural variant6591R → S. Ref.13
VAR_008758

Experimental info

Sequence conflict314 – 3174RVRM → VSRT in AAA60102. Ref.3

Secondary structure

................................ 697
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05129 [UniParc].

Last modified February 1, 1994. Version 3.
Checksum: 3F911B5BEF713C41

FASTA69778,448
        10         20         30         40         50         60 
MAGLGPGVGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS HCTDFIWGIG 

        70         80         90        100        110        120 
KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK HKFRLHSYSS PTFCDHCGSL 

       130        140        150        160        170        180 
LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC GVDHTERRGR LQLEIRAPTA DEIHVTVGEA 

       190        200        210        220        230        240 
RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTRTVKATLN PVWNETFVFN LKPGDVERRL 

       250        260        270        280        290        300 
SVEVWDWDRT SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ 

       310        320        330        340        350        360 
KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDPKRCFFG ASPGRLHISD FSFLMVLGKG 

       370        380        390        400        410        420 
SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP GGRPHFLTQL 

       430        440        450        460        470        480 
HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD 

       490        500        510        520        530        540 
LKLDNVMLDA EGHIKITDFG MCKENVFPGT TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS 

       550        560        570        580        590        600 
FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS 

       610        620        630        640        650        660 
GPDGEPTIRA HGFFRWIDWE RLERLEIPPP FRPRPCGRSG ENFDKFFTRA APALTPPDRL 

       670        680        690 
VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM 

« Hide

References

« Hide 'large scale' references
[1]Cui W.C., Yu L., Chu Y.Y., Wang J., Zheng L.H., Zhou G.J., Zhao S.Y.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Brain.
[3]"Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways."
Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.
Science 233:859-866(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-317.
Tissue: Brain.
[4]"Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes."
Kochs G., Hummel R., Meyer D., Hug H., Marme D., Sarre T.F.
Eur. J. Biochem. 216:597-606(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-697.
Tissue: Hippocampus.
[5]"The C2 domain of PKCdelta is a phosphotyrosine binding domain."
Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P.
Cell 121:271-280(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDCP1.
[6]"Protein kinase C delta regulates Ser46 phosphorylation of p53 tumor suppressor in the apoptotic response to DNA damage."
Yoshida K., Liu H., Miki Y.
J. Biol. Chem. 281:5734-5740(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53INP1 AND P53/TP53.
[7]"Protein kinase C gamma (PKC gamma): function of neuron specific isotype."
Saito N., Shirai Y.
J. Biochem. 132:683-687(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[8]"Protein kinase C as a stress sensor."
Barnett M.E., Madgwick D.K., Takemoto D.J.
Cell. Signal. 19:1820-1829(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Development and validation of a method for profiling post-translational modification activities using protein microarrays."
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[11]"Solution structure of the phorbol esters/diacylglycerol binding domain of protein kinase C gamma."
RIKEN structural genomics initiative (RSGI)
Submitted (DEC-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 36-105.
[12]"Crystal structure of C2 domain of protein kinase C gamma."
Pike A.C.W., Amos A., Johansson C., Sobott F., Savitsky P., Berridge G., Fedorov O., Umeano C., Gorrec F., Bunkoczi G., Debreczeni J., Von Delft F., Arrowsmith C.H., Edwards A., Weigelt J., Sundstrom M., Knapp S.
Submitted (APR-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 154-295 IN COMPLEX WITH CALCIUM IONS.
[13]"Segregation of a PRKCG mutation in two RP11 families."
Al-Maghtheh M., Vithana E.N., Inglehearn C.F., Moore T., Bird A.C., Bhattacharya S.S.
Am. J. Hum. Genet. 62:1248-1252(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-141; GLN-415; ASP-523 AND SER-659.
[14]"No mutations in the coding region of the PRKCG gene in three families with retinitis pigmentosa linked to the RP11 locus on chromosome 19q."
Dryja T.P., McEvoy J., McGee T.L., Berson E.L.
Am. J. Hum. Genet. 65:926-928(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT THE VARIANTS ARE NOT A CAUSE OF RP11.
[15]"Missense mutations in the regulatory domain of PKC gamma: a new mechanism for dominant nonepisodic cerebellar ataxia."
Chen D.-H., Brkanac Z., Verlinde C.L.M.J., Tan X.-J., Bylenok L., Nochlin D., Matsushita M., Lipe H., Wolff J., Fernandez M., Cimino P.J., Bird T.D., Raskind W.H.
Am. J. Hum. Genet. 72:839-849(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, VARIANTS SCA14 TYR-101; PRO-119 AND ASP-128.
+Additional computationally mapped references.

Web resources

Mutations of the PRKCG gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF345987 mRNA. Translation: AAK13533.1.
BC047876 mRNA. Translation: AAH47876.1.
M13977 mRNA. Translation: AAA60102.1.
Z15114 mRNA. Translation: CAA78820.1.
CCDSCCDS12867.1.
PIRD24664.
RefSeqNP_002730.1. NM_002739.3.
UniGeneHs.631564.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E73NMR-A36-105[»]
2UZPX-ray2.00A/B/C154-295[»]
ProteinModelPortalP05129.
SMRP05129. Positions 36-683.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111568. 24 interactions.
DIPDIP-39795N.
IntActP05129. 7 interactions.
MINTMINT-222801.
STRING9606.ENSP00000263431.

Chemistry

BindingDBP05129.
ChEMBLCHEMBL2093867.
GuidetoPHARMACOLOGY1484.

PTM databases

PhosphoSiteP05129.

Polymorphism databases

DMDM462455.

Proteomic databases

PaxDbP05129.
PeptideAtlasP05129.
PRIDEP05129.

Protocols and materials databases

DNASU5582.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263431; ENSP00000263431; ENSG00000126583.
GeneID5582.
KEGGhsa:5582.
UCSCuc002qcq.1. human.

Organism-specific databases

CTD5582.
GeneCardsGC19P054382.
GeneReviewsPRKCG.
HGNCHGNC:9402. PRKCG.
HPACAB013051.
MIM176980. gene.
605361. phenotype.
neXtProtNX_P05129.
Orphanet98763. Spinocerebellar ataxia type 14.
PharmGKBPA33766.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108317.
InParanoidP05129.
KOK02677.
OrthoDBEOG77M8QM.
PhylomeDBP05129.
TreeFamTF351133.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP05129.

Gene expression databases

ArrayExpressP05129.
BgeeP05129.
CleanExHS_PRKCG.
GenevestigatorP05129.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000550. PKC_alpha. 1 hit.
PRINTSPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05129.
GeneWikiPRKCG.
GenomeRNAi5582.
NextBio21648.
PMAP-CutDBP05129.
PROP05129.
SOURCESearch...

Entry information

Entry nameKPCG_HUMAN
AccessionPrimary (citable) accession number: P05129
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 172 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

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 19

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