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

Q38SD2 (LRRK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich repeat serine/threonine-protein kinase 1

EC=2.7.11.1
Gene names
Name:LRRK1
Synonyms:KIAA1790
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2015 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.3

Cofactor

Magnesium or manganese. Ref.3

Enzyme regulation

Binding of GTP stimulates kinase activity. Ref.3

Subunit structure

Homodimer. Ref.6

Subcellular location

Cytoplasm Ref.3.

Sequence similarities

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

Contains 4 ANK repeats.

Contains 13 LRR (leucine-rich) repeats.

Contains 1 protein kinase domain.

Contains 1 Roc domain.

Sequence caution

The sequence AAY67799.1 differs from that shown. Reason: The cDNA contains a duplication of exon 3.

The sequence BAB15547.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC85472.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.6 (identifier: Q38SD2-1)

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.
Note: No experimental confirmation available.
Isoform 2 Ref.2 (identifier: Q38SD2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     255-264: ALRVKWSHLR → VSSHCLWSVF
     265-2015: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20152015Leucine-rich repeat serine/threonine-protein kinase 1
PRO_0000233377

Regions

Repeat86 – 11631ANK 1
Repeat119 – 14830ANK 2
Repeat152 – 18231ANK 3
Repeat193 – 22230ANK 4
Repeat279 – 30022LRR 1
Repeat303 – 32422LRR 2
Repeat330 – 35122LRR 3
Repeat353 – 37422LRR 4
Repeat381 – 40222LRR 5
Repeat405 – 42622LRR 6
Repeat427 – 44721LRR 7
Repeat451 – 47222LRR 8
Repeat474 – 49522LRR 9
Repeat498 – 51922LRR 10
Repeat549 – 57022LRR 11
Repeat572 – 59423LRR 12
Repeat596 – 61722LRR 13
Domain632 – 826195Roc
Domain1242 – 1525284Protein kinase
Nucleotide binding1248 – 12569ATP By similarity

Sites

Active site13861Proton acceptor By similarity
Binding site12701ATP By similarity

Natural variations

Alternative sequence255 – 26410ALRVKWSHLR → VSSHCLWSVF in isoform 2.
VSP_040119
Alternative sequence265 – 20151751Missing in isoform 2.
VSP_040120
Natural variant18031A → T. Ref.7
VAR_040674
Natural variant18241L → F. Ref.7
VAR_040675
Natural variant18471S → N. Ref.7
VAR_040676
Natural variant19271D → G. Ref.7
VAR_040677

Experimental info

Mutagenesis6511K → A: Loss of GTP/GDP-binding. Ref.3
Mutagenesis7461K → G: No effect on GTP-binding but reduction in subsequent stimulation of kinase activity. Ref.3
Mutagenesis10221F → C: No effect on GTP-binding but loss of subsequent stimulation of kinase activity. Ref.3
Mutagenesis12701K → W: Loss of autophosphorylation. Ref.3
Mutagenesis14121I → T: No effect on GTP-binding but reduction in subsequent stimulation of kinase activity. Ref.3
Sequence conflict2031K → R in BAC85472. Ref.4
Sequence conflict19381G → E in AAH66655. Ref.2
Sequence conflict19381G → E in BAB47419. Ref.5

Sequences

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

Last modified November 30, 2010. Version 3.
Checksum: 38E77EDC7C84583B

FASTA2,015225,393
        10         20         30         40         50         60 
MAGMSQRPPS MYWCVGPEES AVCPERAMET LNGAGDTGGK PSTRGGDPAA RSRRTEGIRA 

        70         80         90        100        110        120 
AYRRGDRGGA RDLLEEACDQ CASQLEKGQL LSIPAAYGDL EMVRYLLSKR LVELPTEPTD 

       130        140        150        160        170        180 
DNPAVVAAYF GHTAVVQELL ESLPGPCSPQ RLLNWMLALA CQRGHLGVVK LLVLTHGADP 

       190        200        210        220        230        240 
ESYAVRKNEF PVIVRLPLYA AIKSGNEDIA IFLLRHGAYF CSYILLDSPD PSKHLLRKYF 

       250        260        270        280        290        300 
IEASPLPSSY PGKTALRVKW SHLRLPWVDL DWLIDISCQI TELDLSANCL ATLPSVIPWG 

       310        320        330        340        350        360 
LINLRKLNLS DNHLGELPGV QSSDEIICSR LLEIDISSNK LSHLPPGFLH LSKLQKLTAS 

       370        380        390        400        410        420 
KNCLEKLFEE ENATNWIGLR KLQELDISDN KLTELPALFL HSFKSLNSLN VSRNNLKVFP 

       430        440        450        460        470        480 
DPWACPLKCC KASRNALECL PDKMAVFWKN HLKDVDFSEN ALKEVPLGLF QLDALMFLRL 

       490        500        510        520        530        540 
QGNQLAALPP QEKWTCRQLK TLDLSRNQLG KNEDGLKTKR IAFFTTRGRQ RSGTEAASVL 

       550        560        570        580        590        600 
EFPAFLSESL EVLCLNDNHL DTVPPSVCLL KSLSELYLGN NPGLRELPPE LGQLGNLWQL 

       610        620        630        640        650        660 
DTEDLTISNV PAEIQKEGPK AMLSYLRAQL RKAEKCKLMK MIIVGPPRQG KSTLLEILQT 

       670        680        690        700        710        720 
GRAPQVVHGE ATIRTTKWEL QRPAGSRAKV ESVEFNVWDI GGPASMATVN QCFFTDKALY 

       730        740        750        760        770        780 
VVVWNLALGE EAVANLQFWL LNIEAKAPNA VVLVVGTHLD LIEAKFRVER IATLRAYVLA 

       790        800        810        820        830        840 
LCRSPSGSRA TGFPDITFKH LHEISCKSLE GQEGLRQLIF HVTCSMKDVG STIGCQRLAG 

       850        860        870        880        890        900 
RLIPRSYLSL QEAVLAEQQR RSRDDDVQYL TDRQLEQLVE QTPDNDIKDY EDLQSAISFL 

       910        920        930        940        950        960 
IETGTLLHFP DTSHGLRNLY FLDPIWLSEC LQRIFNIKGS RSVAKNGVIR AEDLRMLLVG 

       970        980        990       1000       1010       1020 
TGFTQQTEEQ YFQFLAKFEI ALPVANDSYL LPHLLPSKPG LDTHGMRHPT ANTIQRVFKM 

      1030       1040       1050       1060       1070       1080 
SFVPVGFWQR FIARMLISLA EMDLQLFENK KNTKSRNRKV TIYSFTGNQR NRCSTFRVKR 

      1090       1100       1110       1120       1130       1140 
NQTIYWQEGL LVTFDGGYLS VESSDVNWKK KKSGGMKIVC QSEVRDFSAM AFITDHVNSL 

      1150       1160       1170       1180       1190       1200 
IDQWFPALTA TESDGTPLME QYVPCPVCET AWAQHTDPSE KSEDVQYFDM EDCVLTAIER 

      1210       1220       1230       1240       1250       1260 
DFISCPRHPD LPVPLQELVP ELFMTDFPAR LFLENSKLEH SEDEGSVLGQ GGSGTVIYRA 

      1270       1280       1290       1300       1310       1320 
RYQGQPVAVK RFHIKKFKNF ANVPADTMLR HLRATDAMKN FSEFRQEASM LHALQHPCIV 

      1330       1340       1350       1360       1370       1380 
ALIGISIHPL CFALELAPLS SLNTVLSENA RDSSFIPLGH MLTQKIAYQI ASGLAYLHKK 

      1390       1400       1410       1420       1430       1440 
NIIFCDLKSD NILVWSLDVK EHINIKLSDY GISRQSFHEG ALGVEGTPGY QAPEIRPRIV 

      1450       1460       1470       1480       1490       1500 
YDEKVDMFSY GMVLYELLSG QRPALGHHQL QIAKKLSKGI RPVLGQPEEV QFRRLQALMM 

      1510       1520       1530       1540       1550       1560 
ECWDTKPEKR PLALSVVSQM KDPTFATFMY ELCCGKQTAF FSSQGQEYTV VFWDGKEESR 

      1570       1580       1590       1600       1610       1620 
NYTVVNTEKG LMEVQRMCCP GMKVSCQLQV QRSLWTATED QKIYIYTLKG MCPLNTPQQA 

      1630       1640       1650       1660       1670       1680 
LDTPAVVTCF LAVPVIKKNS YLVLAGLADG LVAVFPVVRG TPKDSCSYLC SHTANRSKFS 

      1690       1700       1710       1720       1730       1740 
IADEDARQNP YPVKAMEVVN SGSEVWYSNG PGLLVIDCAS LEICRRLEPY MAPSMVTSVV 

      1750       1760       1770       1780       1790       1800 
CSSEGRGEEV VWCLDDKANS LVMYHSTTYQ LCARYFCGVP SPLRDMFPVR PLDTEPPAAS 

      1810       1820       1830       1840       1850       1860 
HTANPKVPEG DSIADVSIMY SEELGTQILI HQESLTDYCS MSSYSSSPPR QAARSPSSLP 

      1870       1880       1890       1900       1910       1920 
SSPASSSSVP FSTDCEDSDM LHTPGAASDR SEHDLTPMDG ETFSQHLQAV KILAVRDLIW 

      1930       1940       1950       1960       1970       1980 
VPRRGGDVIV IGLEKDSGAQ RGRVIAVLKA RELTPHGVLV DAAVVAKDTV VCTFENENTE 

      1990       2000       2010 
WCLAVWRGWG AREFDIFYQS YEELGRLEAC TRKRR 

« Hide

Isoform 2 [UniParc].

Checksum: 8E95B1F50F1DB2E4
Show »

FASTA26428,848

References

« Hide 'large scale' references
[1]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1576-2015 (ISOFORM 1).
Tissue: Pancreas and Skin.
[3]"LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain."
Korr D., Toschi L., Donner P., Pohlenz H.-P., Kreft B., Weiss B.
Cell. Signal. 18:910-920(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-2015 (ISOFORM 1), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, GTP-BINDING, MUTAGENESIS OF LYS-651; LYS-746; PHE-1022; LYS-1270 AND ILE-1412.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-364 AND 905-2015 (ISOFORM 1).
Tissue: Lung, Macrophage and Spleen.
[5]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-2015 (ISOFORM 1).
Tissue: Brain.
[6]"Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers."
Civiero L., Vancraenenbroeck R., Belluzzi E., Beilina A., Lobbestael E., Reyniers L., Gao F., Micetic I., De Maeyer M., Bubacco L., Baekelandt V., Cookson M.R., Greggio E., Taymans J.M.
PLoS ONE 7:E43472-E43472(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, LACK OF AUTOPHOSPHORYLATION.
[7]"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] THR-1803; PHE-1824; ASN-1847 AND GLY-1927.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC090907 Genomic DNA. No translation available.
BC066655 mRNA. Translation: AAH66655.1.
BC068080 mRNA. Translation: AAH68080.1.
DQ013130 mRNA. Translation: AAY67799.1. Sequence problems.
AK026772 mRNA. Translation: BAB15547.1. Different initiation.
AK130975 mRNA. Translation: BAC85472.1. Different initiation.
AK131075 mRNA. Translation: BAC85125.1.
AB058693 mRNA. Translation: BAB47419.1.
CCDSCCDS42086.1. [Q38SD2-1]
RefSeqNP_078928.3. NM_024652.3. [Q38SD2-1]
UniGeneHs.407918.

3D structure databases

ProteinModelPortalQ38SD2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122823. 32 interactions.
IntActQ38SD2. 25 interactions.
STRING9606.ENSP00000373600.

PTM databases

PhosphoSiteQ38SD2.

Polymorphism databases

DMDM313104220.

Proteomic databases

MaxQBQ38SD2.
PaxDbQ38SD2.
PRIDEQ38SD2.

Protocols and materials databases

DNASU79705.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000388948; ENSP00000373600; ENSG00000154237. [Q38SD2-1]
ENST00000532029; ENSP00000433268; ENSG00000154237. [Q38SD2-2]
GeneID79705.
KEGGhsa:79705.
UCSCuc002bwq.1. human. [Q38SD2-2]
uc002bwr.3. human. [Q38SD2-1]

Organism-specific databases

CTD79705.
GeneCardsGC15P101459.
H-InvDBHIX0012627.
HGNCHGNC:18608. LRRK1.
HPAHPA010537.
MIM610986. gene.
neXtProtNX_Q38SD2.
PharmGKBPA134892363.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOVERGENHBG081936.
KOK08843.
OMAFEEENAT.
OrthoDBEOG761BST.
PhylomeDBQ38SD2.
TreeFamTF313679.

Enzyme and pathway databases

SignaLinkQ38SD2.

Gene expression databases

ArrayExpressQ38SD2.
BgeeQ38SD2.
CleanExHS_LRRK1.
GenevestigatorQ38SD2.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
3.40.50.300. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011009. Kinase-like_dom.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR000719. Prot_kinase_dom.
IPR020859. ROC_GTPase.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
PF00560. LRR_1. 1 hit.
PF12799. LRR_4. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 1 hit.
PF08477. Miro. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 3 hits.
SM00369. LRR_TYP. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF50978. SSF50978. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS51450. LRR. 11 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS51424. ROC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiLRRK1.
GenomeRNAi79705.
NextBio69015.
PROQ38SD2.
SOURCESearch...

Entry information

Entry nameLRRK1_HUMAN
AccessionPrimary (citable) accession number: Q38SD2
Secondary accession number(s): Q6NVH5 expand/collapse secondary AC list , Q6NYC0, Q6ZNL9, Q6ZNM9, Q96JN5, Q9H5S3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 99 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

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 15

Human chromosome 15: entries, gene names and cross-references to MIM