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Q9Y2H6 (FND3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Fibronectin type-III domain-containing protein 3A
Alternative name(s):
Human gene expressed in odontoblasts
Gene names
Name:FNDC3A
Synonyms:FNDC3, HUGO, KIAA0970
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1198 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates spermatid-Sertoli adhesion during spermatogenesis By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass membrane protein Potential Ref.1.

Tissue specificity

Expressed in the odontoblast and nerves in the dental pulp. Also expressed in trachea and to a lesser extent in the brain, liver, lung and kidney. Ref.1

Sequence similarities

Belongs to the FNDC3 family.

Contains 9 fibronectin type-III domains.

Sequence caution

The sequence BAA76814.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAD18784.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: Q9Y2H6-1)

Also known as: HUGO1;

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: Q9Y2H6-2)

Also known as: HUGO2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
     57-58: IT → MS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11981198Fibronectin type-III domain-containing protein 3A
PRO_0000087321

Regions

Transmembrane1177 – 119721Helical; Potential
Domain268 – 369102Fibronectin type-III 1
Domain373 – 46593Fibronectin type-III 2
Domain469 – 56294Fibronectin type-III 3
Domain566 – 66095Fibronectin type-III 4
Domain664 – 75794Fibronectin type-III 5
Domain761 – 85191Fibronectin type-III 6
Domain861 – 95090Fibronectin type-III 7
Domain951 – 104595Fibronectin type-III 8
Domain1046 – 1151106Fibronectin type-III 9
Compositional bias68 – 13366Pro-rich

Amino acid modifications

Modified residue2071Phosphoserine By similarity
Modified residue2131Phosphoserine Ref.9 Ref.10
Modified residue3841N6-acetyllysine Ref.12

Natural variations

Alternative sequence1 – 5656Missing in isoform 2.
VSP_037723
Alternative sequence57 – 582IT → MS in isoform 2.
VSP_037724
Natural variant1071S → G.
Corresponds to variant rs34539036 [ dbSNP | Ensembl ].
VAR_059655

Experimental info

Sequence conflict531Q → R in CAI45989. Ref.5
Sequence conflict3501E → G in CAE45852. Ref.5
Sequence conflict5011Y → H in CAE45852. Ref.5
Sequence conflict8391P → R in AAH60816. Ref.8
Sequence conflict8391P → R in AAH70072. Ref.8

Secondary structure

.................................................................................................. 1198
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HUGO1) [UniParc].

Last modified July 28, 2009. Version 4.
Checksum: 2809E41E89BDD095

FASTA1,198131,852
        10         20         30         40         50         60 
MAEHPPLLDT TQILSSDISL LSAPIVSADG TQQVILVQVN PGEAFTIRRE DGQFQCITGP 

        70         80         90        100        110        120 
AQVPMMSPNG SVPPIYVPPG YAPQVIEDNG VRRVVVVPQA PEFHPGSHTV LHRSPHPPLP 

       130        140        150        160        170        180 
GFIPVPTMMP PPPRHMYSPV TGAGDMTTQY MPQYQSSQVY GDVDAHSTHG RSNFRDERSS 

       190        200        210        220        230        240 
KTYERLQKKL KDRQGTQKDK MSSPPSSPQK CPSPINEHNG LIKGQIAGGI NTGSAKIKSG 

       250        260        270        280        290        300 
KGKGGTQVDT EIEEKDEETK AFEALLSNIV KPVASDIQAR TVVLTWSPPS SLINGETDES 

       310        320        330        340        350        360 
SVPELYGYEV LISSTGKDGK YKSVYVGEET NITLNDLKPA MDYHAKVQAE YNSIKGTPSE 

       370        380        390        400        410        420 
AEIFTTLSCE PDIPNPPRIA NRTKNSLTLQ WKAPSDNGSK IQNFVLEWDE GKGNGEFCQC 

       430        440        450        460        470        480 
YMGSQKQFKI TKLSPAMGCK FRLSARNDYG TSGFSEEVLY YTSGCAPSMP ASPVLTKAGI 

       490        500        510        520        530        540 
TWLSLQWSKP SGTPSDEGIS YILEMEEETS GYGFKPKYDG EDLAYTVKNL RRSTKYKFKV 

       550        560        570        580        590        600 
IAYNSEGKSN PSEVVEFTTC PDKPGIPVKP SVKGKIHSHS FKITWDPPKD NGGATINKYV 

       610        620        630        640        650        660 
VEMAEGSNGN KWEMIYSGAT REHLCDRLNP GCFYRLRVYC ISDGGQSAVS ESLLVQTPAV 

       670        680        690        700        710        720 
PPGPCLPPRL QGRPKAKEIQ LRWGPPLVDG GSPISCYSVE MSPIEKDEPR EVYQGSEVEC 

       730        740        750        760        770        780 
TVSSLLPGKT YSFRLRAANK MGFGPFSEKC DITTAPGPPD QCKPPQVTCR SATCAQVNWE 

       790        800        810        820        830        840 
VPLSNGTDVT EYRLEWGGVE GSMQICYCGP GLSYEIKGLS PATTYYCRVQ ALSVVGAGPF 

       850        860        870        880        890        900 
SEVVACVTPP SVPGIVTCLQ EISDDEIENP HYSPSTCLAI SWEKPCDHGS EILAYSIDFG 

       910        920        930        940        950        960 
DKQSLTVGKV TSYIINNLQP DTTYRIRIQA LNSLGAGPFS HMIKLKTKPL PPDPPRLECV 

       970        980        990       1000       1010       1020 
AFSHQNLKLK WGEGTPKTLS TDSIQYHLQM EDKNGRFVSL YRGPCHTYKV QRLNESTSYK 

      1030       1040       1050       1060       1070       1080 
FCIQACNEAG EGPLSQEYIF TTPKSVPAAL KAPKIEKVND HICEITWECL QPMKGDPVIY 

      1090       1100       1110       1120       1130       1140 
SLQVMLGKDS EFKQIYKGPD SSFRYSSLQL NCEYRFRVCA IRQCQDSLGH QDLVGPYSTT 

      1150       1160       1170       1180       1190 
VLFISQRTEP PASTNRDTVE STRTRRALSD EQCAAVILVL FAFFSILIAF IIQYFVIK 

« Hide

Isoform 2 (HUGO2) [UniParc].

Checksum: 2136F2F51012A73F
Show »

FASTA1,142125,822

References

« Hide 'large scale' references
[1]"HUGO (FNDC3A): a new gene overexpressed in human odontoblasts."
Carrouel F., Couble M.-L., Vanbelle C., Staquet M.-J., Magloire H., Bleicher F.
J. Dent. Res. 87:131-136(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Dental pulp and Odontoblast.
[2]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[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] (ISOFORM 2).
Tissue: Testis.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Cervix and Fetal kidney.
[6]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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 1).
Tissue: Brain, Placenta and Testis.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
[14]"Solution structure of fibronectin type III domains derived from human KIAA0970 protein."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 256-851.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ749706 mRNA. Translation: CAG44602.1.
AJ749707 mRNA. Translation: CAG44603.1.
AB023187 mRNA. Translation: BAA76814.2. Different initiation.
AK172814 mRNA. Translation: BAD18784.1. Different initiation.
AK302415 mRNA. Translation: BAG63723.1.
BX640739 mRNA. Translation: CAE45852.1.
BX648141 mRNA. Translation: CAI45989.1.
AL161421, AL137000, AL359184 Genomic DNA. Translation: CAH70653.1.
AL359184, AL137000, AL161421 Genomic DNA. Translation: CAH73933.1.
AL137000, AL161421, AL359184 Genomic DNA. Translation: CAI39727.1.
AL137000 Genomic DNA. Translation: CAI39726.2.
CH471075 Genomic DNA. Translation: EAX08804.1.
CH471075 Genomic DNA. Translation: EAX08806.1.
BC060816 mRNA. Translation: AAH60816.1.
BC070072 mRNA. Translation: AAH70072.1.
BC132812 mRNA. Translation: AAI32813.1.
BC136617 mRNA. Translation: AAI36618.1.
BC144301 mRNA. Translation: AAI44302.1.
CCDSCCDS41886.1. [Q9Y2H6-1]
CCDS9413.2. [Q9Y2H6-2]
RefSeqNP_001073141.1. NM_001079673.1. [Q9Y2H6-1]
NP_001265367.1. NM_001278438.1. [Q9Y2H6-1]
NP_055738.3. NM_014923.4. [Q9Y2H6-2]
UniGeneHs.508010.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WK0NMR-A256-379[»]
1X3DNMR-A361-465[»]
1X4XNMR-A759-851[»]
1X5XNMR-A467-562[»]
2CRMNMR-A554-660[»]
2CRZNMR-A661-757[»]
ProteinModelPortalQ9Y2H6.
SMRQ9Y2H6. Positions 256-969.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116530. 2 interactions.
IntActQ9Y2H6. 5 interactions.
MINTMINT-3084391.

PTM databases

PhosphoSiteQ9Y2H6.

Polymorphism databases

DMDM254763442.

Proteomic databases

MaxQBQ9Y2H6.
PaxDbQ9Y2H6.
PRIDEQ9Y2H6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398316; ENSP00000381362; ENSG00000102531. [Q9Y2H6-2]
ENST00000492622; ENSP00000417257; ENSG00000102531. [Q9Y2H6-1]
ENST00000541916; ENSP00000441831; ENSG00000102531. [Q9Y2H6-1]
GeneID22862.
KEGGhsa:22862.
UCSCuc001vcm.3. human. [Q9Y2H6-1]
uc001vcp.1. human. [Q9Y2H6-2]

Organism-specific databases

CTD22862.
GeneCardsGC13P049550.
H-InvDBHIX0011312.
HGNCHGNC:20296. FNDC3A.
HPAHPA008927.
HPA012825.
neXtProtNX_Q9Y2H6.
PharmGKBPA128394588.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG100680.
InParanoidQ9Y2H6.
OMANFRDERS.
OrthoDBEOG7F7W8B.
PhylomeDBQ9Y2H6.
TreeFamTF316401.

Gene expression databases

ArrayExpressQ9Y2H6.
BgeeQ9Y2H6.
CleanExHS_FNDC3A.
GenevestigatorQ9Y2H6.

Family and domain databases

Gene3D2.60.40.10. 9 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF00041. fn3. 8 hits.
[Graphical view]
SMARTSM00060. FN3. 9 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 6 hits.
PROSITEPS50853. FN3. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFNDC3A. human.
EvolutionaryTraceQ9Y2H6.
GeneWikiFNDC3A.
GenomeRNAi22862.
NextBio43369.
PROQ9Y2H6.

Entry information

Entry nameFND3A_HUMAN
AccessionPrimary (citable) accession number: Q9Y2H6
Secondary accession number(s): B4DYG1 expand/collapse secondary AC list , Q5HYC9, Q5JVF8, Q5JVF9, Q6EVH3, Q6EVH4, Q6N020, Q6P9D5, Q6ZME4, Q9H1W1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 120 of the entry and version 4 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM