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Reviewed, UniProtKB/Swiss-Prot P05164 (PERM_HUMAN)

Last modified November 3, 2009. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Myeloperoxidase
      Short name=MPO
    EC=1.11.1.7
Cleaved into the following 4 chains:
    1- Recommended name:
            89 kDa myeloperoxidase
    2- Recommended name:
            84 kDa myeloperoxidase
    3- Recommended name:
            Myeloperoxidase light chain
    4- Recommended name:
            Myeloperoxidase heavy chain
Gene names
Name: MPO
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O.

Cl- + H2O2 = HOCl + 2 H2O.

Cofactor

Binds 1 calcium ion per heterodimer.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer.

Subunit structure

Tetramer of two light chains and two heavy chains.

Subcellular location

Lysosome.

Involvement in disease

Defects in MPO are the cause of myeloperoxidase deficiency (MPD) [MIM:254600]. MPD is an autosomal recessive defect that results in disseminated candidiasis. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform H17 (identifier: P05164-1)

Also known as: B;

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 H14 (identifier: P05164-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-95: Missing.
Isoform H7 (identifier: P05164-3)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     182-182: N → NRCGWLGVAAGTGLREASRTPQASRCQRPVLPC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4848 Ref.12
Chain49 – 74569789 kDa myeloperoxidase
PRO_0000023651
Propeptide49 – 164116
PRO_0000023652
Chain155 – 74559184 kDa myeloperoxidase
PRO_0000023653
Chain165 – 745581Myeloperoxidase
PRO_0000023654
Chain165 – 278114Myeloperoxidase light chain
PRO_0000023655
Chain279 – 745467Myeloperoxidase heavy chain
PRO_0000023656

Sites

Active site2611Proton acceptor
Metal binding2621Calcium
Metal binding3341Calcium
Metal binding3361Calcium; via carbonyl oxygen
Metal binding3381Calcium
Metal binding3401Calcium
Metal binding5021Iron (heme axial ligand)
Binding site2601Heme (covalent; via 3 links)
Binding site4081Heme (covalent; via 3 links)
Binding site4091Heme (covalent; via 3 links)
Site4051Transition state stabilizer

Amino acid modifications

Modified residue3161Cysteine sulfenic acid (-SOH)
Glycosylation1391N-linked (GlcNAc...) Ref.16
Glycosylation3231N-linked (GlcNAc...) Ref.17
Glycosylation3551N-linked (GlcNAc...) Ref.18
Glycosylation3911N-linked (GlcNAc...) Ref.18
Glycosylation4831N-linked (GlcNAc...) Ref.16 Ref.17
CAR_000220
Disulfide bond167 ↔ 180
Disulfide bond281 ↔ 291
Disulfide bond285 ↔ 309
Disulfide bond319Interchain
Disulfide bond387 ↔ 398
Disulfide bond606 ↔ 663
Disulfide bond704 ↔ 730

Natural variations

Alternative sequence1 – 9595Missing in isoform H14.
VSP_007206
Alternative sequence1821N → NRCGWLGVAAGTGLREASRT PQASRCQRPVLPC in isoform H7.
VSP_007207
Natural variant531V → F: dbSNP rs7208693. Ref.9
VAR_023995
Natural variant1731Y → C in MPD; affects proteolytic processing and secretion. Ref.25
VAR_015377
Natural variant2511M → T in MPD. Ref.26
VAR_015378
Natural variant4471R → Q in a colorectal cancer sample; somatic mutation. Ref.27
VAR_036517
Natural variant5691R → W in MPD; suppress post-translational processing. Ref.22 Ref.23 Ref.24
VAR_015379
Natural variant6041R → C
VAR_023996
Natural variant6831E → Q
VAR_023997
Natural variant7171I → V: dbSNP rs2759. Ref.9
VAR_012066

Experimental info

Sequence conflict361L → V in CAA28565. Ref.4
Sequence conflict361L → V in CAA33438. Ref.7

Secondary structure

.............................................................................................. 745
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform H17 (B) [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 348B1CE0A11038B4

FASTA74583,869
        10         20         30         40         50         60 
MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA PAVLGEVDTS 

        70         80         90        100        110        120 
LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS YFKQPVAATR TAVRAADYLH 

       130        140        150        160        170        180 
VALDLLERKL RSLWRRPFNV TDVLTPAQLN VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC 

       190        200        210        220        230        240 
NNRRSPTLGA SNRAFVRWLP AEYEDGFSLP YGWTPGVKRN GFPVALARAV SNEIVRFPTD 

       250        260        270        280        290        300 
QLTPDQERSL MFMQWGQLLD HDLDFTPEPA ARASFVTGVN CETSCVQQPP CFPLKIPPND 

       310        320        330        340        350        360 
PRIKNQADCI PFFRSCPACP GSNITIRNQI NALTSFVDAS MVYGSEEPLA RNLRNMSNQL 

       370        380        390        400        410        420 
GLLAVNQRFQ DNGRALLPFD NLHDDPCLLT NRSARIPCFL AGDTRSSEMP ELTSMHTLLL 

       430        440        450        460        470        480 
REHNRLATEL KSLNPRWDGE RLYQEARKIV GAMVQIITYR DYLPLVLGPT AMRKYLPTYR 

       490        500        510        520        530        540 
SYNDSVDPRI ANVFTNAFRY GHTLIQPFMF RLDNRYQPME PNPRVPLSRV FFASWRVVLE 

       550        560        570        580        590        600 
GGIDPILRGL MATPAKLNRQ NQIAVDEIRE RLFEQVMRIG LDLPALNMQR SRDHGLPGYN 

       610        620        630        640        650        660 
AWRRFCGLPQ PETVGQLGTV LRNLKLARKL MEQYGTPNNI DIWMGGVSEP LKRKGRVGPL 

       670        680        690        700        710        720 
LACIIGTQFR KLRDGDRFWW ENEGVFSMQQ RQALAQISLP RIICDNTGIT TVSKNNIFMS 

       730        740 
NSYPRDFVNC STLPALNLAS WREAS 

« Hide

Isoform H14.

Checksum: 7A29F89DFE6B4916
Show »

FASTA65073,854
Isoform H7 (A).

Checksum: F15BC771A9C6F6A6
Show »

FASTA77787,248

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of cDNA for human myeloperoxidase."
Morishita K., Kubota N., Asano S., Kaziro Y., Nagata S.
J. Biol. Chem. 262:3844-3851(1987) [PubMed: 3029127] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[2]"Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor."
Morishita K., Tsuchiya M., Asano S., Kaziro Y., Nagata S.
J. Biol. Chem. 262:15208-15213(1987) [PubMed: 2444596] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase."
Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L., Degroot L.J., Rapoport B.
J. Clin. Invest. 80:1205-1208(1987) [PubMed: 3654979] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[4]"Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species."
Johnson K.R., Nauseef W.M., Care A., Wheelock M.J., Shane S., Hudson S., Koeffler H.P., Selsted M., Miller C., Rovera G.
Nucleic Acids Res. 15:2013-2028(1987) [PubMed: 3031585] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[5]"Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation."
Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.
Biochemistry 27:5906-5914(1988) [PubMed: 2903767] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS H7; H14 AND H17), PROTEIN SEQUENCE OF 165-183; 216-222; 295-304; 311-331; 464-479; 662-676 AND 766-776.
Tissue: Leukemia.
[6]Erratum
Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.
Biochemistry 27:9226-9226(1988)
[7]"Complete nucleotide sequence of the human myeloperoxidase gene."
Johnson K.R., Gemperlein I., Hudson S., Shane S., Rovera G.
Nucleic Acids Res. 17:7985-7986(1989) [PubMed: 2552418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1."
Hosokawa Y., Kawaguchi R., Hikiji K., Yamada M., Suzuki K., Nakagawa T., Yoshihara T., Yamaguchi K.
Leukemia 7:441-445(1993) [PubMed: 8383257] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[9]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-53; CYS-604; GLN-683 AND VAL-717.
[10]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].
[11]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H17).
[12]"Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures."
Yamada M., Hur S.-J., Toda H.
Biochem. Biophys. Res. Commun. 166:852-859(1990) [PubMed: 2154223] [Abstract]
Cited for: PROTEIN SEQUENCE OF 49-66.
[13]"Unique autolytic cleavage of human myeloperoxidase. Implications for the involvement of active site MET409."
Taylor K.L., Pohl J., Kinkade J.M. Jr.
J. Biol. Chem. 267:25282-25288(1992) [PubMed: 1334087] [Abstract]
Cited for: PROTEIN SEQUENCE OF 279-424.
Tissue: Leukocyte.
[14]"Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene."
Yamada M., Yoshida M., Hashinaka K.
J. Biol. Chem. 268:13479-13485(1993) [PubMed: 8390465] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-629.
[15]"Isolation and characterization of a cDNA coding for human myeloperoxidase."
Yamada M., Hur S.-J., Hashinaka K., Tsuneoka K., Saeki T., Nishio C., Sakiyama F., Tsunasawa S.
Arch. Biochem. Biophys. 255:147-155(1987) [PubMed: 2884926] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 588-745.
[16]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483, MASS SPECTROMETRY.
Tissue: Plasma.
[17]"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
J. Proteome Res. 5:1493-1503(2006) [PubMed: 16740002] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483, MASS SPECTROMETRY.
Tissue: Saliva.
[18]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-355 AND ASN-391, MASS SPECTROMETRY.
Tissue: Liver.
[19]"X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8-A resolution."
Fiedler T.J., Davey C.A., Fenna R.E.
J. Biol. Chem. 275:11964-11971(2000) [PubMed: 10766826] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744.
[20]"Structure of the green heme in myeloperoxidase."
Fenna R.E., Zeng J., Davey C.
Arch. Biochem. Biophys. 316:653-656(1995) [PubMed: 7840679] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744.
[21]"Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution."
Blair-Johnson M., Fiedler T., Fenna R.
Biochemistry 40:13990-13997(2001) [PubMed: 11705390] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744.
[22]"Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency."
Kizaki M., Miller C.W., Selsted M.E., Koeffler H.P.
Blood 83:1935-1940(1994) [PubMed: 8142659] [Abstract]
Cited for: VARIANT MPD TRP-569.
[23]"Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan."
Nauseef W.M., Brigham S., Cogley M.
J. Biol. Chem. 269:1212-1216(1994) [PubMed: 7904599] [Abstract]
Cited for: VARIANT MPD TRP-569.
[24]"Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase."
Nauseef W., Cogley M., McCormick S.
J. Biol. Chem. 271:9546-9549(1996) [PubMed: 8621627] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT MPD TRP-569.
[25]"A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation."
DeLeo F.R., Goedken M., McCormick S.J., Nauseef W.M.
J. Clin. Invest. 101:2900-2909(1998) [PubMed: 9637725] [Abstract]
Cited for: VARIANT MPD CYS-173, CHARACTERIZATION OF VARIANT MPD CYS-173.
[26]"Biochemical and molecular characterization of hereditary myeloperoxidase deficiency."
Romano M., Dri P., Dadalt L., Patriarca P., Baralle F.E.
Blood 90:4126-4134(1997) [PubMed: 9354683] [Abstract]
Cited for: VARIANT MPD THR-251.
[27]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-447.
+Additional computationally mapped references.

Web resources

MPObase

MPO mutation db

NIEHS-SNPs
Wikipedia

Myeloperoxidase entry

Cross-references

Sequence databases

J02694 mRNA. Translation: AAA59896.1.
M17176 expand/collapse EMBL AC list , M17170, M17171, M17172, M17173, M17174, M17175 Genomic DNA. Translation: AAA60346.1.
X04876 mRNA. Translation: CAA28565.1.
M19507 mRNA. Translation: AAA59863.1.
M19508 Genomic DNA. Translation: AAA59864.1.
M19508 Genomic DNA. Translation: AAA59865.1.
X15377 Genomic DNA. Translation: CAA33438.1.
S56200 mRNA. Translation: AAB25582.1.
DQ088846 Genomic DNA. Translation: AAY68218.1.
CH471109 Genomic DNA. Translation: EAW94470.1.
BC130476 mRNA. Translation: AAI30477.1.
D14466 Genomic DNA. Translation: BAA03362.1.
IPIIPI00007244.
IPI00236554.
IPI00236556.
PIROPHUM. A29467.
B28894.
D28894.
RefSeqNP_000241.1.
UniGeneHs.458272

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CXPX-ray1.80A/B167-270[»]
C/D279-744[»]
1D2VX-ray1.75A/B167-270[»]
C/D279-744[»]
1D5LX-ray1.90A/B167-270[»]
C/D279-744[»]
1D7WX-ray1.90A/B167-270[»]
C/D279-744[»]
1DNUX-ray1.85A/B167-270[»]
C/D279-744[»]
1DNWX-ray1.90A/B167-270[»]
C/D279-744[»]
1MHLX-ray2.25A/B165-272[»]
C/D279-744[»]
1MYPX-ray3.00A/B165-272[»]
C/D279-744[»]
3F9PX-ray2.93A/B165-278[»]
C/D279-745[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP05164.

Protein family/group databases

PeroxiBase3315. HsMPO.

PTM databases

GlycoSuiteDBP05164.
PhosphoSiteP05164.

Proteomic databases

PRIDEP05164.

Genome annotation databases

EnsemblENST00000225275; ENSP00000225275; ENSG00000005381; Homo sapiens. [Genome view]
ENST00000340482; ENSP00000344419; ENSG00000005381; Homo sapiens. [Genome view]
ENST00000393105; ENSP00000376817; ENSG00000005381; Homo sapiens. [Genome view]
GeneID4353.
KEGGhsa:4353.
UCSCuc002ivu.1. human.

Organism-specific databases

CTD4353.
GeneCardsGC17M053702.
H-InvDBHIX0039242.
HGNCHGNC:7218. MPO.
HPACAB000059.
HPA021147.
MIM254600. phenotype.
606989. gene.
Orphanet2587. Myeloperoxidase deficiency.
PharmGKBPA243.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP05164.
OMAKSSGCAY.

Enzyme and pathway databases

BRENDA1.11.1.7. 247.
Pathway_Interaction_DBamb2_neutrophils_pathway. amb2 Integrin signaling.
il23pathway. IL23-mediated signaling events.

Gene expression databases

ArrayExpressP05164.
BgeeP05164.
CleanExHS_MPO.
GenevestigatorP05164.
GermOnlineENSG00000005381. Homo sapiens.

Family and domain databases

InterProIPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_sg.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
Gene3DG3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. False negative.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00535. Cefdinir.
NextBio17126.
PMAP-CutDBP05164.
SOURCESearch...

Entry information

Entry namePERM_HUMAN
AccessionPrimary (citable) accession number: P05164
Secondary accession number(s): A1L4B8 expand/collapse secondary AC list , Q14862, Q4PJH5, Q9UCL7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 3, 2009
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Human chromosome 17: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents