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O95394 (AGM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoacetylglucosamine mutase

Short name=PAGM
EC=5.4.2.3
Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase
Phosphoglucomutase-3
Short name=PGM 3
Gene names
Name:PGM3
Synonyms:AGM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interconverts GlcNAc-6-P and GlcNAc-1-P.

Catalytic activity

N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.

Tissue specificity

Found in many tissues except lung. Relatively high expression in pancreas, heart, liver, and placenta, and relatively low expression in brain, skeletal muscle and kidney.

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence caution

The sequence BAB14652.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95394-1)

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: O95394-3)

The sequence of this isoform differs from the canonical sequence as follows:
     542-542: F → YKAAETTHNINNAFGPGTANEHTVP
Note: Gene prediction based on EST data.
Isoform 3 (identifier: O95394-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGGEWGQSAICPESAQEWTYQVGQHLVDM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Phosphoacetylglucosamine mutase
PRO_0000148013

Sites

Active site641Phosphoserine intermediate
Metal binding641Magnesium; via phosphate group By similarity
Metal binding2761Magnesium By similarity
Metal binding2781Magnesium By similarity
Metal binding2801Magnesium By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10 Ref.15
Modified residue641Phosphoserine Ref.9 Ref.11 Ref.12

Natural variations

Alternative sequence11M → MGGEWGQSAICPESAQEWTY QVGQHLVDM in isoform 3.
VSP_047319
Alternative sequence5421F → YKAAETTHNINNAFGPGTAN EHTVP in isoform 2.
VSP_047320
Natural variant4661D → N in allele PGM3*2. Ref.3 Ref.7 Ref.16
Corresponds to variant rs473267 [ dbSNP | Ensembl ].
VAR_013489

Experimental info

Mutagenesis641S → A: Loss of activity.
Mutagenesis651H → A: Loss of activity.
Mutagenesis2781D → A or E: Loss of activity.
Mutagenesis2811R → A or K: Loss of activity.
Sequence conflict51A → V in BAG63306. Ref.4
Sequence conflict701D → G in BAG63306. Ref.4

Sequences

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

Last modified May 1, 1999. Version 1.
Checksum: 6A4FBCD99A2154A9

FASTA54259,852
        10         20         30         40         50         60 
MDLGAITKYS ALHAKPNGLI LQYGTAGFRT KAEHLDHVMF RMGLLAVLRS KQTKSTIGVM 

        70         80         90        100        110        120 
VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLANAEEQ DMQRVLIDIS EKEAVNLQQD 

       130        140        150        160        170        180 
AFVVIGRDTR PSSEKLSQSV IDGVTVLGGQ FHDYGLLTTP QLHYMVYCRN TGGRYGKATI 

       190        200        210        220        230        240 
EGYYQKLSKA FVELTKQASC SGDEYRSLKV DCANGIGALK LREMEHYFSQ GLSVQLFNDG 

       250        260        270        280        290        300 
SKGKLNHLCG ADFVKSHQKP PQGMEIKSNE RCCSFDGDAD RIVYYYHDAD GHFHLIDGDK 

       310        320        330        340        350        360 
IATLISSFLK ELLVEIGESL NIGVVQTAYA NGSSTRYLEE VMKVPVYCTK TGVKHLHHKA 

       370        380        390        400        410        420 
QEFDIGVYFE ANGHGTALFS TAVEMKIKQS AEQLEDKKRK AAKMLENIID LFNQAAGDAI 

       430        440        450        460        470        480 
SDMLVIEAIL ALKGLTVQQW DALYTDLPNR QLKVQVADRR VISTTDAERQ AVTPPGLQEA 

       490        500        510        520        530        540 
INDLVKKYKL SRAFVRPSGT EDVVRVYAEA DSQESADHLA HEVSLAVFQL AGGIGERPQP 


GF 

« Hide

Isoform 2 [UniParc].

Checksum: 81691708BD389ECF
Show »

FASTA56662,342
Isoform 3 [UniParc].

Checksum: 3F59B307C746CF8D
Show »

FASTA57062,941

References

« Hide 'large scale' references
[1]Matthijs G., Schollen E., Dierickx D.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning and characterization of complementary DNA encoding human N-acetylglucosamine-phosphate mutase protein."
Li C., Rodriguez M., Banerjee D.
Gene 242:97-103(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis."
Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.
Biochim. Biophys. Acta 1492:369-376(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS, VARIANT ASN-466.
[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] (ISOFORMS 1 AND 3).
Tissue: Placenta and Testis.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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), VARIANT ASN-466.
Tissue: Placenta.
[8]"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] OF 392-542 (ISOFORM 1).
Tissue: Testis.
[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-64, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Identification of human phosphoglucomutase 3 (PGM3) as N-acetylglucosamine-phosphate mutase (AGM1)."
Pang H., Koda Y., Soejima M., Kimura H.
Ann. Hum. Genet. 66:139-144(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-466.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF102265 mRNA. Translation: AAC72409.1.
AF180371 mRNA. Translation: AAD55097.1.
AB032081 mRNA. Translation: BAB00613.1.
AK023709 mRNA. Translation: BAB14652.1. Different initiation.
AK301867 mRNA. Translation: BAG63306.1.
AK314512 mRNA. Translation: BAG37112.1.
AL049699 Genomic DNA. No translation available.
AL121716 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48670.1.
CH471051 Genomic DNA. Translation: EAW48671.1.
BC001258 mRNA. Translation: AAH01258.1.
AL117443 mRNA. Translation: CAB55928.1.
CCDSCCDS4997.1. [O95394-1]
CCDS56435.1. [O95394-3]
CCDS56436.1. [O95394-4]
PIRT17238.
RefSeqNP_001186846.1. NM_001199917.1. [O95394-4]
NP_001186848.1. NM_001199919.1. [O95394-3]
NP_056414.1. NM_015599.2. [O95394-1]
XP_006715567.1. XM_006715504.1. [O95394-4]
UniGeneHs.661665.

3D structure databases

ProteinModelPortalO95394.
SMRO95394. Positions 5-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111257. 5 interactions.
MINTMINT-5000376.

PTM databases

PhosphoSiteO95394.

Proteomic databases

MaxQBO95394.
PaxDbO95394.
PRIDEO95394.

Protocols and materials databases

DNASU5238.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000506587; ENSP00000425809; ENSG00000013375. [O95394-4]
ENST00000512866; ENSP00000421565; ENSG00000013375. [O95394-3]
ENST00000513973; ENSP00000424874; ENSG00000013375. [O95394-1]
GeneID5238.
KEGGhsa:5238.
UCSCuc003pju.2. human. [O95394-1]

Organism-specific databases

CTD5238.
GeneCardsGC06M083876.
HGNCHGNC:8907. PGM3.
HPACAB004998.
HPA029759.
HPA029760.
MIM172100. gene.
neXtProtNX_O95394.
PharmGKBPA33244.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1109.
HOVERGENHBG024321.
InParanoidO95394.
KOK01836.
OMADIVRVYA.
OrthoDBEOG7W6WKJ.
PhylomeDBO95394.
TreeFamTF105670.

Enzyme and pathway databases

BioCycMetaCyc:HS00347-MONOMER.
BRENDA5.4.2.3. 2681.
ReactomeREACT_17015. Metabolism of proteins.
SABIO-RKO95394.
UniPathwayUPA00113; UER00530.

Gene expression databases

ArrayExpressO95394.
BgeeO95394.
CleanExHS_PGM3.
GenevestigatorO95394.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR016657. PAGM.
[Graphical view]
PfamPF02878. PGM_PMM_I. 2 hits.
PF02879. PGM_PMM_II. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PIRSFPIRSF016408. PAGM. 1 hit.
SUPFAMSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPhosphoglucomutase_3.
GenomeRNAi5238.
NextBio20236.
PROO95394.
SOURCESearch...

Entry information

Entry nameAGM1_HUMAN
AccessionPrimary (citable) accession number: O95394
Secondary accession number(s): B2RB65 expand/collapse secondary AC list , B4DX94, D6RF12, E1P547, E9PF86, Q5JWR4, Q96J46, Q9H8G5, Q9NS94, Q9NTT6, Q9UFV5, Q9UIY2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 150 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM