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Q10471 (GALT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. 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:
Polypeptide N-acetylgalactosaminyltransferase 2

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 2
Short name=GalNAc-T2
Short name=pp-GaNTase 2
Protein-UDP acetylgalactosaminyltransferase 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
Gene names
Name:GALNT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. Ref.1 Ref.7 Ref.9 Ref.12

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1 Ref.12

Cofactor

Manganese. Ref.1 Ref.12

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists. Ref.8

Tissue specificity

Widely expressed. Ref.1

Domain

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding By similarity.

The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
Manganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processO-glycan processing

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

immunoglobulin biosynthetic process

Inferred from direct assay Ref.9. Source: BHF-UCL

post-translational protein modification

Traceable author statement. Source: Reactome

protein O-linked glycosylation

Inferred from direct assay Ref.12. Source: UniProtKB

protein O-linked glycosylation via serine

Inferred from direct assay Ref.9Ref.7. Source: BHF-UCL

protein O-linked glycosylation via threonine

Inferred from direct assay Ref.9Ref.7. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 9852147. Source: BHF-UCL

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

Golgi stack

Inferred from direct assay PubMed 9852147. Source: BHF-UCL

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of Golgi membrane

Non-traceable author statement PubMed 9852147. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12506059. Source: BHF-UCL

   Molecular_functionmanganese ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

polypeptide N-acetylgalactosaminyltransferase activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571Polypeptide N-acetylgalactosaminyltransferase 2
PRO_0000223391
Chain52 – 571520Polypeptide N-acetylgalactosaminyltransferase 2 soluble form
PRO_0000012265

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2418Helical; Signal-anchor for type II membrane protein; Potential
Topological domain25 – 571547Lumenal Potential
Domain443 – 566124Ricin B-type lectin
Region135 – 240106Catalytic subdomain A
Region300 – 36263Catalytic subdomain B

Sites

Metal binding2241Manganese
Metal binding2261Manganese
Metal binding3591Manganese
Binding site1431Substrate
Binding site1761Substrate
Binding site2011Substrate
Binding site2251Substrate
Binding site3311Substrate
Binding site3621Substrate
Binding site3651Substrate
Binding site3671Substrate
Site5161Not glycosylated

Amino acid modifications

Disulfide bond126 ↔ 354 Ref.12
Disulfide bond345 ↔ 423 Ref.12
Disulfide bond456 ↔ 473 Ref.12
Disulfide bond496 ↔ 513 Ref.12
Disulfide bond539 ↔ 555 Ref.12

Natural variations

Natural variant2451R → H.
Corresponds to variant rs1923950 [ dbSNP | Ensembl ].
VAR_049240
Natural variant5541V → M. Ref.2
Corresponds to variant rs2273970 [ dbSNP | Ensembl ].
VAR_019575

Experimental info

Sequence conflict701T → G AA sequence Ref.1
Sequence conflict781W → D AA sequence Ref.1
Sequence conflict931R → G AA sequence Ref.1
Sequence conflict2101R → W AA sequence Ref.1
Sequence conflict290 – 2912RR → SC AA sequence Ref.1
Sequence conflict2931R → Q AA sequence Ref.1
Sequence conflict3001P → H AA sequence Ref.1
Sequence conflict5221W → A AA sequence Ref.1
Sequence conflict5331H → M AA sequence Ref.1

Secondary structure

................................................................................................ 571
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q10471 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D9A0F5D17C55BAF2

FASTA57164,733
        10         20         30         40         50         60 
MRRRSRMLLC FAFLWVLGIA YYMYSGGGSA LAGGAGGGAG RKEDWNEIDP IKKKDLHHSN 

        70         80         90        100        110        120 
GEEKAQSMET LPPGKVRWPD FNQEAYVGGT MVRSGQDPYA RNKFNQVESD KLRMDRAIPD 

       130        140        150        160        170        180 
TRHDQCQRKQ WRVDLPATSV VITFHNEARS ALLRTVVSVL KKSPPHLIKE IILVDDYSND 

       190        200        210        220        230        240 
PEDGALLGKI EKVRVLRNDR REGLMRSRVR GADAAQAKVL TFLDSHCECN EHWLEPLLER 

       250        260        270        280        290        300 
VAEDRTRVVS PIIDVINMDN FQYVGASADL KGGFDWNLVF KWDYMTPEQR RSRQGNPVAP 

       310        320        330        340        350        360 
IKTPMIAGGL FVMDKFYFEE LGKYDMMMDV WGGENLEISF RVWQCGGSLE IIPCSRVGHV 

       370        380        390        400        410        420 
FRKQHPYTFP GGSGTVFARN TRRAAEVWMD EYKNFYYAAV PSARNVPYGN IQSRLELRKK 

       430        440        450        460        470        480 
LSCKPFKWYL ENVYPELRVP DHQDIAFGAL QQGTNCLDTL GHFADGVVGV YECHNAGGNQ 

       490        500        510        520        530        540 
EWALTKEKSV KHMDLCLTVV DRAPGSLIKL QGCRENDSRQ KWEQIEGNSK LRHVGSNLCL 

       550        560        570 
DSRTAKSGGL SVEVCGPALS QQWKFTLNLQ Q 

« Hide

References

« Hide 'large scale' references
[1]"Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
White T., Bennett E.P., Takio K., Soerensen T., Bonding N., Clausen H.
J. Biol. Chem. 270:24156-24165(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-93; 104-120; 170-182; 193-218; 303-323; 421-424 AND 510-546, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
Tissue: Gastric carcinoma.
[2]"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], VARIANT MET-554.
Tissue: Hippocampus.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
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]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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: Lymph.
[7]"Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2."
Iwasaki H., Zhang Y., Tachibana K., Gotoh M., Kikuchi N., Kwon Y.-D., Togayachi A., Kudo T., Kubota T., Narimatsu H.
J. Biol. Chem. 278:5613-5621(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"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].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2."
Fritz T.A., Raman J., Tabak L.A.
J. Biol. Chem. 281:8613-8619(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 75-571 IN COMPLEX WITH UDP; PEPTIDE SUBSTRATE AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85019 mRNA. Translation: CAA59381.1.
AK290048 mRNA. Translation: BAF82737.1.
AL078646, AL117349, AL136988 Genomic DNA. Translation: CAC00585.2.
AL117349, AL078646, AL136988 Genomic DNA. Translation: CAI22902.1.
AL136988, AL078646, AL117349 Genomic DNA. Translation: CAI23447.1.
FJ515852 Genomic DNA. Translation: ACS13744.1.
CH471098 Genomic DNA. Translation: EAW69911.1.
BC041120 mRNA. Translation: AAH41120.1.
PIRI37405.
RefSeqNP_004472.1. NM_004481.3.
UniGeneHs.743964.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FFUX-ray1.64A75-571[»]
2FFVX-ray2.75A/B75-571[»]
ProteinModelPortalQ10471.
SMRQ10471. Positions 40-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108862. 8 interactions.
MINTMINT-3026412.
STRING9606.ENSP00000355632.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ10471.

Polymorphism databases

DMDM51315838.

Proteomic databases

PaxDbQ10471.
PeptideAtlasQ10471.
PRIDEQ10471.

Protocols and materials databases

DNASU2590.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366672; ENSP00000355632; ENSG00000143641.
GeneID2590.
KEGGhsa:2590.
UCSCuc010pwa.1. human.

Organism-specific databases

CTD2590.
GeneCardsGC01P230193.
H-InvDBHIX0001682.
HGNCHGNC:4124. GALNT2.
HPAHPA011222.
MIM602274. gene.
neXtProtNX_Q10471.
PharmGKBPA28537.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239675.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ10471.
KOK00710.
OMADDYSDNP.
OrthoDBEOG7J9VP2.
PhylomeDBQ10471.
TreeFamTF313267.

Enzyme and pathway databases

BRENDA2.4.1.41. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ10471.
BgeeQ10471.
CleanExHS_GALNT2.
GenevestigatorQ10471.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT2. human.
EvolutionaryTraceQ10471.
GeneWikiGALNT2.
GenomeRNAi2590.
NextBio10245.
PROQ10471.
SOURCESearch...

Entry information

Entry nameGALT2_HUMAN
AccessionPrimary (citable) accession number: Q10471
Secondary accession number(s): A8K1Y3, C5HU00, Q9NPY4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 131 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 1

Human chromosome 1: entries, gene names and cross-references to MIM