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O94806 (KPCD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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:
Serine/threonine-protein kinase D3

EC=2.7.11.13
Alternative name(s):
Protein kinase C nu type
Protein kinase EPK2
nPKC-nu
Gene names
Name:PRKD3
Synonyms:EPK2, PRKCN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length890 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains 1 and 2 bind both DAG and phorbol ester with high affinity and mediate translocation to the cell membrane. Autophosphorylation of Ser-735 and phosphorylation of Ser-731 by PKC relieves auto-inhibition by the PH domain. Ref.7

Subcellular location

Cytoplasm. Membrane. Note: Translocation to the cell membrane is required for kinase activation. Ref.7

Tissue specificity

Ubiquitous.

Sequence similarities

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

Contains 1 PH domain.

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

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VAMP2P630277EBI-1255366,EBI-520113

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O94806-1)

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: O94806-2)

The sequence of this isoform differs from the canonical sequence as follows:
     595-611: HRKTGRDVAIKVIDKMR → QLQPFAYCTHYFKNWKM
     612-890: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 890890Serine/threonine-protein kinase D3
PRO_0000055717

Regions

Domain416 – 532117PH
Domain576 – 832257Protein kinase
Zinc finger154 – 20451Phorbol-ester/DAG-type 1
Zinc finger271 – 32151Phorbol-ester/DAG-type 2
Nucleotide binding582 – 5909ATP By similarity

Sites

Active site6991Proton acceptor By similarity
Binding site6051ATP By similarity

Amino acid modifications

Modified residue61Phosphoserine Ref.8
Modified residue271Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12
Modified residue371Phosphoserine Ref.8
Modified residue411Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12
Modified residue441Phosphoserine Ref.9 Ref.12
Modified residue2131Phosphoserine Ref.8 Ref.11
Modified residue2161Phosphoserine Ref.8 Ref.11
Modified residue3641Phosphoserine Ref.6 Ref.8 Ref.9 Ref.11
Modified residue5351Phosphothreonine Ref.8 Ref.11
Modified residue7311Phosphoserine; by PKC
Modified residue7351Phosphoserine; by autocatalysis

Natural variations

Alternative sequence595 – 61117HRKTG…IDKMR → QLQPFAYCTHYFKNWKM in isoform 2.
VSP_029405
Alternative sequence612 – 890279Missing in isoform 2.
VSP_029406
Natural variant421N → D.
Corresponds to variant rs11896614 [ dbSNP | Ensembl ].
VAR_037147
Natural variant1281A → T. Ref.5
Corresponds to variant rs17852819 [ dbSNP | Ensembl ].
VAR_037148
Natural variant2251P → S.
Corresponds to variant rs34280934 [ dbSNP | Ensembl ].
VAR_050561
Natural variant4451L → I.
Corresponds to variant rs55912911 [ dbSNP | Ensembl ].
VAR_061532
Natural variant5461Q → R. Ref.5
Corresponds to variant rs17856887 [ dbSNP | Ensembl ].
VAR_037149
Natural variant7161V → M in a glioblastoma multiforme sample; somatic mutation. Ref.14
VAR_042336

Experimental info

Mutagenesis1561T → A: Slight loss in ability to bind DAG and phorbol-ester; when associated with F-158. Ref.7
Mutagenesis1581Y → F: Slight loss in ability to bind DAG and phorbol-ester; when associated with A-156. Ref.7
Mutagenesis1651P → G: No effect on ability to bind phorbol ester, loss of ability to bind DAG, reduced DAG-induced membrane translocation. Ref.7
Mutagenesis1661T → A: Slight loss in ability to bind DAG and phorbol-ester. Ref.7
Mutagenesis1701Y → F: Slight loss in ability to bind DAG and phorbol-ester. Ref.7
Mutagenesis2821P → G: No effect on ability to bind phorbol ester, increase in ability to bind DAG. Ref.7
Mutagenesis2841I → V: Slight increase in ability to bind DAG, no effect on phorbol-ester binding.
Mutagenesis2931K → W: Increased ability to bind DAG, no effect on phorbol-ester binding. Ref.7

Secondary structure

................... 890
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 1999. Version 1.
Checksum: 66D5E7E7235064F5

FASTA890100,471
        10         20         30         40         50         60 
MSANNSPPSA QKSVLPTAIP AVLPAASPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV 

        70         80         90        100        110        120 
SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN 

       130        140        150        160        170        180 
ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHTLYVH SYKAPTFCDY CGEMLWGLVR 

       190        200        210        220        230        240 
QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP EYVALPSEES 

       250        260        270        280        290        300 
HVHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYT RPTICQYCKR LLKGLFRQGM 

       310        320        330        340        350        360 
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PSSLGTDTDI PMDIDNNDIN SDSSRGLDDT 

       370        380        390        400        410        420 
EEPSPPEDKM FFLDPSDLDV ERDEEAVKTI SPSTSNNIPL MRVVQSIKHT KRKSSTMVKE 

       430        440        450        460        470        480 
GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRISS PRDFTNISQG 

       490        500        510        520        530        540 
SNPHCFEIIT DTMVYFVGEN NGDSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV 

       550        560        570        580        590        600 
CTSPGQGKDH KDLSTSISVS NCQIQENVDI STVYQIFADE VLGSGQFGIV YGGKHRKTGR 

       610        620        630        640        650        660 
DVAIKVIDKM RFPTKQESQL RNEVAILQNL HHPGIVNLEC MFETPERVFV VMEKLHGDML 

       670        680        690        700        710        720 
EMILSSEKSR LPERITKFMV TQILVALRNL HFKNIVHCDL KPENVLLASA EPFPQVKLCD 

       730        740        750        760        770        780 
FGFARIIGEK SFRRSVVGTP AYLAPEVLRS KGYNRSLDMW SVGVIIYVSL SGTFPFNEDE 

       790        800        810        820        830        840 
DINDQIQNAA FMYPPNPWRE ISGEAIDLIN NLLQVKMRKR YSVDKSLSHP WLQDYQTWLD 

       850        860        870        880        890 
LREFETRIGE RYITHESDDA RWEIHAYTHN LVYPKHFIMA PNPDDMEEDP 

« Hide

Isoform 2 [UniParc].

Checksum: 1714FAD7DA82C942
Show »

FASTA61168,123

References

« Hide 'large scale' references
[1]"PKCnu, a new member of the protein kinase C family, composes a fourth subfamily with PKCmu."
Hayashi A., Seki N., Hattori A., Kozuma S., Saito T.
Biochim. Biophys. Acta 1450:99-106(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryo.
[2]"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].
[3]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].
[4]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].
[5]"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), VARIANTS THR-128 AND ARG-546.
Tissue: Testis.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family."
Chen J., Deng F., Li J., Wang Q.J.
Biochem. J. 411:333-342(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, PHORBOL-ESTER BINDING, MUTAGENESIS OF THR-156; TYR-158; PRO-165; THR-166; TYR-170; PRO-282 AND LYS-293.
[8]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-27; SER-37; SER-41; SER-213; SER-216; SER-364 AND THR-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-44 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-213; SER-216; SER-364 AND THR-535, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41 AND SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Solution structure of the PH domain of protein kinase C, nu type from human."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 414-532.
[14]"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: VARIANT [LARGE SCALE ANALYSIS] MET-716.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015982 mRNA. Translation: BAA36514.1.
AC007390 Genomic DNA. Translation: AAY14817.1.
CH471053 Genomic DNA. Translation: EAX00398.1.
CH471053 Genomic DNA. Translation: EAX00399.1.
BC030706 mRNA. Translation: AAH30706.1.
RefSeqNP_005804.1. NM_005813.3.
XP_005264294.1. XM_005264237.1.
UniGeneHs.660757.
Hs.716034.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9ZNMR-A417-532[»]
ProteinModelPortalO94806.
SMRO94806. Positions 155-204, 241-321, 414-532, 537-852.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117199. 8 interactions.
IntActO94806. 9 interactions.
MINTMINT-5003932.
STRING9606.ENSP00000234179.

Chemistry

BindingDBO94806.
ChEMBLCHEMBL2096620.
GuidetoPHARMACOLOGY2174.

PTM databases

PhosphoSiteO94806.

Proteomic databases

PaxDbO94806.
PRIDEO94806.

Protocols and materials databases

DNASU23683.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234179; ENSP00000234179; ENSG00000115825. [O94806-1]
ENST00000379066; ENSP00000368356; ENSG00000115825. [O94806-1]
GeneID23683.
KEGGhsa:23683.
UCSCuc002rqd.3. human. [O94806-1]
uc002rqf.1. human. [O94806-2]

Organism-specific databases

CTD23683.
GeneCardsGC02M037477.
H-InvDBHIX0030377.
HGNCHGNC:9408. PRKD3.
HPAHPA029529.
MIM607077. gene.
neXtProtNX_O94806.
PharmGKBPA33772.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000015135.
HOVERGENHBG003564.
InParanoidO94806.
KOK06070.
OMAFRHDLNS.
OrthoDBEOG75B84N.
PhylomeDBO94806.
TreeFamTF314320.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
SignaLinkO94806.

Gene expression databases

ArrayExpressO94806.
BgeeO94806.
CleanExHS_PRKD3.
GenevestigatorO94806.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR015727. Protein_Kinase_C_mu-related.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR22968. PTHR22968. 1 hit.
PfamPF00130. C1_1. 2 hits.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000552. PKC_mu_nu_D2. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00233. PH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50003. PH_DOMAIN. 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

EvolutionaryTraceO94806.
GeneWikiPRKD3.
GenomeRNAi23683.
NextBio46561.
PROO94806.
SOURCESearch...

Entry information

Entry nameKPCD3_HUMAN
AccessionPrimary (citable) accession number: O94806
Secondary accession number(s): D6W587, Q53TR7, Q8NEL8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 134 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

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 2

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