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O00748

- EST2_HUMAN

UniProt

O00748 - EST2_HUMAN

Protein

Cocaine esterase

Gene

CES2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine.1 Publication

    Catalytic activityi

    Cocaine + H2O = ecgonine methyl ester + benzoate.1 Publication
    A carboxylic ester + H2O = an alcohol + a carboxylate.1 PublicationPROSITE-ProRule annotation
    4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate.1 Publication

    Kineticsi

    1. KM=0.39 mM for cocaine1 Publication
    2. KM=0.15 mM for 4-methylumbelliferyl acetate1 Publication
    3. KM=6.8 mM for heroin1 Publication
    4. KM=0.13 mM for 6-monoacetylmorphine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei228 – 2281Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei345 – 3451Charge relay systemBy similarity
    Active sitei457 – 4571Charge relay systemBy similarity

    GO - Molecular functioni

    1. carboxylic ester hydrolase activity Source: ProtInc
    2. methylumbelliferyl-acetate deacetylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BRENDAi3.1.1.1. 2681.
    SABIO-RKO00748.

    Protein family/group databases

    MEROPSiS09.984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cocaine esterase (EC:3.1.1.84)
    Alternative name(s):
    Carboxylesterase 2 (EC:3.1.1.1)
    Short name:
    CE-2
    Short name:
    hCE-2
    Methylumbelliferyl-acetate deacetylase 2 (EC:3.1.1.56)
    Gene namesi
    Name:CES2
    Synonyms:ICE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:1864. CES2.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: ProtInc
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA377.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 559533Cocaine esterasePRO_0000008572Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi95 ↔ 123By similarity
    Glycosylationi111 – 1111N-linked (GlcNAc...)2 Publications
    Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi280 ↔ 291By similarity

    Post-translational modificationi

    Glycosylated.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiO00748.
    PaxDbiO00748.
    PRIDEiO00748.

    PTM databases

    PhosphoSiteiO00748.

    Expressioni

    Tissue specificityi

    Preferentially expressed in intestine with moderate expression in liver. Within the intestine, highest expression is found in small intestine with lower expression in colon and rectum.1 Publication

    Gene expression databases

    ArrayExpressiO00748.
    BgeeiO00748.
    CleanExiHS_CES2.
    GenevestigatoriO00748.

    Organism-specific databases

    HPAiHPA018897.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiO00748. 1 interaction.
    STRINGi9606.ENSP00000317842.

    Structurei

    3D structure databases

    ProteinModelPortaliO00748.
    SMRiO00748. Positions 3-546.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi556 – 5594Prevents secretion from ERSequence Analysis

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2272.
    HOVERGENiHBG008839.
    InParanoidiO00748.
    KOiK03927.
    OrthoDBiEOG7RBZ7R.
    PhylomeDBiO00748.
    TreeFamiTF315470.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    [Graphical view]
    PfamiPF00135. COesterase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 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: O00748-1) [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

    MRLHRLRARL SAVACGLLLL LVRGQGQDSA SPIRTTHTGQ VLGSLVHVKG    50
    ANAGVQTFLG IPFAKPPLGP LRFAPPEPPE SWSGVRDGTT HPAMCLQDLT 100
    AVESEFLSQF NMTFPSDSMS EDCLYLSIYT PAHSHEGSNL PVMVWIHGGA 150
    LVFGMASLYD GSMLAALENV VVVIIQYRLG VLGFFSTGDK HATGNWGYLD 200
    QVAALRWVQQ NIAHFGGNPD RVTIFGESAG GTSVSSLVVS PISQGLFHGA 250
    IMESGVALLP GLIASSADVI STVVANLSAC DQVDSEALVG CLRGKSKEEI 300
    LAINKPFKMI PGVVDGVFLP RHPQELLASA DFQPVPSIVG VNNNEFGWLI 350
    PKVMRIYDTQ KEMDREASQA ALQKMLTLLM LPPTFGDLLR EEYIGDNGDP 400
    QTLQAQFQEM MADSMFVIPA LQVAHFQCSR APVYFYEFQH QPSWLKNIRP 450
    PHMKADHGDE LPFVFRSFFG GNYIKFTEEE EQLSRKMMKY WANFARNGNP 500
    NGEGLPHWPL FDQEEQYLQL NLQPAVGRAL KAHRLQFWKK ALPQKIQELE 550
    EPEERHTEL 559
    Length:559
    Mass (Da):61,807
    Last modified:July 1, 1997 - v1
    Checksum:iE2EBCABA2995339A
    GO
    Isoform 2 (identifier: O00748-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         458-474: GDELPFVFRSFFGGNYI → V

    Show »
    Length:543
    Mass (Da):59,959
    Checksum:i4F14FE06766F0F7E
    GO

    Sequence cautioni

    The sequence AAH32095.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAW29943.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAD28531.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAD98009.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 109Missing AA sequence (PubMed:9169443)Curated
    Sequence conflicti180 – 1801G → S in BAF83171. (PubMed:14702039)Curated
    Sequence conflicti239 – 2391V → M in BAF83171. (PubMed:14702039)Curated
    Sequence conflicti385 – 3851F → S in CAD98009. (PubMed:17974005)Curated
    Sequence conflicti519 – 5191Q → R in CAD98009. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341R → W.1 Publication
    VAR_018396
    Natural varianti206 – 2061R → H.1 Publication
    VAR_018397

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei458 – 47417GDELP…GGNYI → V in isoform 2. 1 PublicationVSP_010161Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09616 mRNA. Translation: CAA70831.1.
    D50579 mRNA. Translation: BAA23606.1.
    U60553 mRNA. Translation: AAB03611.1.
    AL713761 mRNA. Translation: CAD28531.1. Different initiation.
    AK290482 mRNA. Translation: BAF83171.1.
    BX538086 mRNA. Translation: CAD98009.1. Different initiation.
    AY851164 Genomic DNA. Translation: AAW29943.1. Different initiation.
    AC009084 Genomic DNA. No translation available.
    BC032095 mRNA. Translation: AAH32095.1. Different initiation.
    PIRiJC5408.
    RefSeqiNP_003860.2. NM_003869.5.
    NP_932327.1. NM_198061.2.
    UniGeneiHs.282975.

    Genome annotation databases

    EnsembliENST00000417689; ENSP00000394452; ENSG00000172831.
    GeneIDi8824.
    KEGGihsa:8824.
    UCSCiuc002eqs.3. human. [O00748-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09616 mRNA. Translation: CAA70831.1 .
    D50579 mRNA. Translation: BAA23606.1 .
    U60553 mRNA. Translation: AAB03611.1 .
    AL713761 mRNA. Translation: CAD28531.1 . Different initiation.
    AK290482 mRNA. Translation: BAF83171.1 .
    BX538086 mRNA. Translation: CAD98009.1 . Different initiation.
    AY851164 Genomic DNA. Translation: AAW29943.1 . Different initiation.
    AC009084 Genomic DNA. No translation available.
    BC032095 mRNA. Translation: AAH32095.1 . Different initiation.
    PIRi JC5408.
    RefSeqi NP_003860.2. NM_003869.5.
    NP_932327.1. NM_198061.2.
    UniGenei Hs.282975.

    3D structure databases

    ProteinModelPortali O00748.
    SMRi O00748. Positions 3-546.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O00748. 1 interaction.
    STRINGi 9606.ENSP00000317842.

    Chemistry

    BindingDBi O00748.
    ChEMBLi CHEMBL3180.

    Protein family/group databases

    MEROPSi S09.984.

    PTM databases

    PhosphoSitei O00748.

    Proteomic databases

    MaxQBi O00748.
    PaxDbi O00748.
    PRIDEi O00748.

    Protocols and materials databases

    DNASUi 8824.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000417689 ; ENSP00000394452 ; ENSG00000172831 .
    GeneIDi 8824.
    KEGGi hsa:8824.
    UCSCi uc002eqs.3. human. [O00748-1 ]

    Organism-specific databases

    CTDi 8824.
    GeneCardsi GC16P066969.
    HGNCi HGNC:1864. CES2.
    HPAi HPA018897.
    MIMi 605278. gene.
    neXtProti NX_O00748.
    PharmGKBi PA377.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2272.
    HOVERGENi HBG008839.
    InParanoidi O00748.
    KOi K03927.
    OrthoDBi EOG7RBZ7R.
    PhylomeDBi O00748.
    TreeFami TF315470.

    Enzyme and pathway databases

    BRENDAi 3.1.1.1. 2681.
    SABIO-RK O00748.

    Miscellaneous databases

    ChiTaRSi CES2. human.
    GeneWikii Carboxylesterase_2.
    GenomeRNAii 8824.
    NextBioi 33104.
    PROi O00748.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00748.
    Bgeei O00748.
    CleanExi HS_CES2.
    Genevestigatori O00748.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver."
      Schwer H., Langmann T., Daig R., Becker A., Aslanidis C., Schmitz G.
      Biochem. Biophys. Res. Commun. 233:117-120(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Small intestine.
    2. "Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin."
      Pindel E.V., Kedishvili N.Y., Abraham T.L., Brzezinski M.R., Zhang J., Dean R.A., Bosron W.F.
      J. Biol. Chem. 272:14769-14775(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 27-34; 57-70; 227-235; 300-305; 346-351; 447-454; 458-466; 535-540 AND 546-551, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Liver.
    3. "Molecular cloning and expression of a human liver cDNA encoding a novel carboxylesterase."
      Sone T., Ishida Y., Takabatake E., Wang C., Pohl L., Isobe M.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    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.
      , 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 1).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Endometrial adenocarcinoma and Testis.
    6. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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].
    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: Skin.
    9. "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] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111.
      Tissue: Liver.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population."
      Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.
      J. Hum. Genet. 48:249-270(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HIS-206.
    12. "Twelve novel single nucleotide polymorphisms in the CES2 gene encoding human carboxylesterase 2 (hCE-2)."
      Kim S.-R., Nakamura T., Saito Y., Sai K., Nakajima T., Saito H., Shirao K., Minami H., Ohtsu A., Yoshida T., Saijo N., Ozawa S., Sawada J.
      Drug Metab. Pharmacokinet. 18:327-332(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TRP-34.

    Entry informationi

    Entry nameiEST2_HUMAN
    AccessioniPrimary (citable) accession number: O00748
    Secondary accession number(s): A8K367
    , Q16859, Q5MAB8, Q7Z366, Q8IUP4, Q8TCP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3