Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P30519

- HMOX2_HUMAN

UniProt

P30519 - HMOX2_HUMAN

Protein

Heme oxygenase 2

Gene

HMOX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.

    Catalytic activityi

    Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi45 – 451Iron (heme axial ligand)

    GO - Molecular functioni

    1. heme oxygenase (decyclizing) activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular iron ion homeostasis Source: Reactome
    2. heme catabolic process Source: Reactome
    3. heme oxidation Source: InterPro
    4. porphyrin-containing compound metabolic process Source: Reactome
    5. response to hypoxia Source: UniProtKB
    6. response to oxidative stress Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_22297. Heme degradation.
    REACT_25060. Iron uptake and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase 2 (EC:1.14.99.3)
    Short name:
    HO-2
    Gene namesi
    Name:HMOX2
    Synonyms:HO2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:5014. HMOX2.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. membrane Source: UniProtKB
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Microsome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29342.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 316315Heme oxygenase 2PRO_0000209691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30519.
    PaxDbiP30519.
    PRIDEiP30519.

    PTM databases

    PhosphoSiteiP30519.

    Miscellaneous databases

    PMAP-CutDBP30519.

    Expressioni

    Inductioni

    Heme oxygenase 2 activity is non-inducible.

    Gene expression databases

    ArrayExpressiP30519.
    BgeeiP30519.
    CleanExiHS_HMOX2.
    GenevestigatoriP30519.

    Organism-specific databases

    HPAiCAB025464.
    HPA040611.

    Interactioni

    Protein-protein interaction databases

    BioGridi109406. 32 interactions.
    DIPiDIP-53564N.
    IntActiP30519. 34 interactions.
    MINTiMINT-1384587.
    STRINGi9606.ENSP00000219700.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 408
    Helixi42 – 498
    Helixi52 – 587
    Helixi64 – 8724
    Turni88 – 903
    Turni92 – 943
    Helixi95 – 973
    Helixi100 – 1034
    Helixi106 – 11712
    Helixi121 – 1244
    Helixi129 – 14416
    Helixi146 – 1483
    Helixi149 – 17527
    Helixi185 – 1873
    Helixi195 – 20814
    Helixi213 – 23826

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Q32X-ray2.40A/B1-264[»]
    2QPPX-ray2.61A/B1-264[»]
    2RGZX-ray2.61A/B1-264[»]
    ProteinModelPortaliP30519.
    SMRiP30519. Positions 30-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30519.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati264 – 2696HRM 1
    Repeati281 – 2866HRM 2

    Sequence similaritiesi

    Belongs to the heme oxygenase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5398.
    HOGENOMiHOG000233221.
    HOVERGENiHBG005982.
    InParanoidiP30519.
    KOiK00510.
    OMAiMDRNKDH.
    PhylomeDBiP30519.
    TreeFamiTF314786.

    Family and domain databases

    Gene3Di1.20.910.10. 1 hit.
    InterProiIPR002051. Haem_Oase.
    IPR016053. Haem_Oase-like.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR018207. Haem_oxygenase_CS.
    [Graphical view]
    PANTHERiPTHR10720. PTHR10720. 1 hit.
    PfamiPF01126. Heme_oxygenase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000343. Haem_Oase. 1 hit.
    PRINTSiPR00088. HAEMOXYGNASE.
    SUPFAMiSSF48613. SSF48613. 1 hit.
    PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30519-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN    50
    TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP 100
    MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV 150
    AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ 200
    LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE 250
    DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL 300
    AAGVALAAGL LAWYYM 316
    Length:316
    Mass (Da):36,033
    Last modified:November 1, 1995 - v2
    Checksum:iBF4B6A341F1A81AC
    GO
    Isoform 2 (identifier: P30519-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: Missing.

    Show »
    Length:287
    Mass (Da):32,837
    Checksum:iE03CE816D6C72A30
    GO

    Sequence cautioni

    The sequence W38932 differs from that shown. Reason: Frameshift at position 82.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071E → T in W38932. 1 PublicationCurated
    Sequence conflicti165 – 1662QV → KC in AAC05297. 1 PublicationCurated
    Sequence conflicti222 – 2221Missing in AAB22110. (PubMed:1575508)Curated
    Sequence conflicti276 – 2761Missing in AAB22110. (PubMed:1575508)Curated
    Sequence conflicti281 – 2888SCPFRTAM → LSLPTSY in AAB22110. (PubMed:1575508)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371R → Q.1 Publication
    Corresponds to variant rs17884623 [ dbSNP | Ensembl ].
    VAR_021067
    Natural varianti146 – 1461P → L.1 Publication
    Corresponds to variant rs17880805 [ dbSNP | Ensembl ].
    VAR_021068

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_055031Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21243 mRNA. Translation: BAA04789.1.
    S34389 mRNA. Translation: AAB22110.2.
    BT019788 mRNA. Translation: AAV38591.1.
    AY771350 Genomic DNA. Translation: AAV28730.1.
    AC007606 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85299.1.
    CH471112 Genomic DNA. Translation: EAW85300.1.
    BC002396 mRNA. Translation: AAH02396.1.
    W38932 mRNA. No translation available.
    AF051306 mRNA. Translation: AAC05297.1.
    CCDSiCCDS10517.1. [P30519-1]
    CCDS66931.1. [P30519-2]
    PIRiI60119.
    S21700.
    RefSeqiNP_001120676.1. NM_001127204.1.
    NP_001120677.1. NM_001127205.1.
    NP_001120678.1. NM_001127206.2.
    NP_001273196.1. NM_001286267.1.
    NP_001273197.1. NM_001286268.1.
    NP_001273198.1. NM_001286269.1.
    NP_001273199.1. NM_001286270.1.
    NP_001273200.1. NM_001286271.1.
    NP_002125.3. NM_002134.3.
    UniGeneiHs.284279.

    Genome annotation databases

    EnsembliENST00000219700; ENSP00000219700; ENSG00000103415. [P30519-1]
    ENST00000398595; ENSP00000381595; ENSG00000103415. [P30519-1]
    ENST00000406590; ENSP00000385100; ENSG00000103415. [P30519-1]
    ENST00000414777; ENSP00000391637; ENSG00000103415. [P30519-1]
    ENST00000458134; ENSP00000394103; ENSG00000103415. [P30519-1]
    ENST00000570646; ENSP00000459214; ENSG00000103415. [P30519-1]
    ENST00000575120; ENSP00000460926; ENSG00000103415. [P30519-2]
    GeneIDi3163.
    KEGGihsa:3163.
    UCSCiuc002cwq.4. human. [P30519-1]

    Polymorphism databases

    DMDMi1170328.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21243 mRNA. Translation: BAA04789.1 .
    S34389 mRNA. Translation: AAB22110.2 .
    BT019788 mRNA. Translation: AAV38591.1 .
    AY771350 Genomic DNA. Translation: AAV28730.1 .
    AC007606 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85299.1 .
    CH471112 Genomic DNA. Translation: EAW85300.1 .
    BC002396 mRNA. Translation: AAH02396.1 .
    W38932 mRNA. No translation available.
    AF051306 mRNA. Translation: AAC05297.1 .
    CCDSi CCDS10517.1. [P30519-1 ]
    CCDS66931.1. [P30519-2 ]
    PIRi I60119.
    S21700.
    RefSeqi NP_001120676.1. NM_001127204.1.
    NP_001120677.1. NM_001127205.1.
    NP_001120678.1. NM_001127206.2.
    NP_001273196.1. NM_001286267.1.
    NP_001273197.1. NM_001286268.1.
    NP_001273198.1. NM_001286269.1.
    NP_001273199.1. NM_001286270.1.
    NP_001273200.1. NM_001286271.1.
    NP_002125.3. NM_002134.3.
    UniGenei Hs.284279.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Q32 X-ray 2.40 A/B 1-264 [» ]
    2QPP X-ray 2.61 A/B 1-264 [» ]
    2RGZ X-ray 2.61 A/B 1-264 [» ]
    ProteinModelPortali P30519.
    SMRi P30519. Positions 30-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109406. 32 interactions.
    DIPi DIP-53564N.
    IntActi P30519. 34 interactions.
    MINTi MINT-1384587.
    STRINGi 9606.ENSP00000219700.

    Chemistry

    ChEMBLi CHEMBL2546.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P30519.

    Polymorphism databases

    DMDMi 1170328.

    Proteomic databases

    MaxQBi P30519.
    PaxDbi P30519.
    PRIDEi P30519.

    Protocols and materials databases

    DNASUi 3163.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219700 ; ENSP00000219700 ; ENSG00000103415 . [P30519-1 ]
    ENST00000398595 ; ENSP00000381595 ; ENSG00000103415 . [P30519-1 ]
    ENST00000406590 ; ENSP00000385100 ; ENSG00000103415 . [P30519-1 ]
    ENST00000414777 ; ENSP00000391637 ; ENSG00000103415 . [P30519-1 ]
    ENST00000458134 ; ENSP00000394103 ; ENSG00000103415 . [P30519-1 ]
    ENST00000570646 ; ENSP00000459214 ; ENSG00000103415 . [P30519-1 ]
    ENST00000575120 ; ENSP00000460926 ; ENSG00000103415 . [P30519-2 ]
    GeneIDi 3163.
    KEGGi hsa:3163.
    UCSCi uc002cwq.4. human. [P30519-1 ]

    Organism-specific databases

    CTDi 3163.
    GeneCardsi GC16P004524.
    HGNCi HGNC:5014. HMOX2.
    HPAi CAB025464.
    HPA040611.
    MIMi 141251. gene.
    neXtProti NX_P30519.
    PharmGKBi PA29342.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5398.
    HOGENOMi HOG000233221.
    HOVERGENi HBG005982.
    InParanoidi P30519.
    KOi K00510.
    OMAi MDRNKDH.
    PhylomeDBi P30519.
    TreeFami TF314786.

    Enzyme and pathway databases

    Reactomei REACT_22297. Heme degradation.
    REACT_25060. Iron uptake and transport.

    Miscellaneous databases

    ChiTaRSi HMOX2. human.
    EvolutionaryTracei P30519.
    GeneWikii HMOX2.
    GenomeRNAii 3163.
    NextBioi 12542.
    PMAP-CutDB P30519.
    PROi P30519.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30519.
    Bgeei P30519.
    CleanExi HS_HMOX2.
    Genevestigatori P30519.

    Family and domain databases

    Gene3Di 1.20.910.10. 1 hit.
    InterProi IPR002051. Haem_Oase.
    IPR016053. Haem_Oase-like.
    IPR016084. Haem_Oase-like_multi-hlx.
    IPR018207. Haem_oxygenase_CS.
    [Graphical view ]
    PANTHERi PTHR10720. PTHR10720. 1 hit.
    Pfami PF01126. Heme_oxygenase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000343. Haem_Oase. 1 hit.
    PRINTSi PR00088. HAEMOXYGNASE.
    SUPFAMi SSF48613. SSF48613. 1 hit.
    PROSITEi PS00593. HEME_OXYGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2."
      Ishikawa K.
      J. Biol. Chem. 270:6345-6350(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal."
      McCoubrey W.K. Jr., Ewing J.F., Maines M.D.
      Arch. Biochem. Biophys. 295:13-20(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-137 AND LEU-146.
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. 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).
      Tissue: Lung.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-148 (ISOFORM 2).
    9. Bienvenut W.V., Bilsland A.E., Keith W.N.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17; 30-38; 48-59; 138-168; 206-214 AND 219-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Ovarian carcinoma.
    10. Follett J., Ahn J.-Y.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-166.
      Tissue: Intestine.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2."
      Bianchetti C.M., Yi L., Ragsdale S.W., Phillips G.N. Jr.
      J. Biol. Chem. 282:37624-37631(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264, HEME-BINDING SITE.

    Entry informationi

    Entry nameiHMOX2_HUMAN
    AccessioniPrimary (citable) accession number: P30519
    Secondary accession number(s): A8MT35
    , D3DUD5, I3L430, O60605
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3