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Q6PIU2

- NCEH1_HUMAN

UniProt

Q6PIU2 - NCEH1_HUMAN

Protein

Neutral cholesterol ester hydrolase 1

Gene

NCEH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 3 (12 Dec 2006)
      Previous versions | rss
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    Functioni

    Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for cholesterol ester hydrolysis in macrophages, thereby contributing to the development of atherosclerosis. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds. May contribute to cancer pathogenesis by promoting tumor cell migration.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei191 – 1911PROSITE-ProRule annotation
    Active sitei348 – 3481PROSITE-ProRule annotation
    Active sitei378 – 3781PROSITE-ProRule annotation

    GO - Molecular functioni

    1. carboxylic ester hydrolase activity Source: InterPro

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Protein family/group databases

    MEROPSiS09.992.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutral cholesterol ester hydrolase 1 (EC:3.1.1.-)
    Short name:
    NCEH
    Alternative name(s):
    Arylacetamide deacetylase-like 1
    Gene namesi
    Name:NCEH1
    Synonyms:AADACL1, KIAA1363
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:29260. NCEH1.

    Subcellular locationi

    Membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Microsome By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-KW
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165697847.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 408408Neutral cholesterol ester hydrolase 1PRO_0000265939Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi287 – 2871N-linked (GlcNAc...)2 Publications
    Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ6PIU2.
    PaxDbiQ6PIU2.
    PRIDEiQ6PIU2.

    PTM databases

    PhosphoSiteiQ6PIU2.

    Expressioni

    Tissue specificityi

    Expressed in monocyte-derived macrophages. Up-regulated in invasive melanoma and breast carcinoma cell lines.2 Publications

    Gene expression databases

    ArrayExpressiQ6PIU2.
    BgeeiQ6PIU2.
    CleanExiHS_AADACL1.
    GenevestigatoriQ6PIU2.

    Organism-specific databases

    HPAiHPA026888.

    Interactioni

    Protein-protein interaction databases

    BioGridi121608. 1 interaction.
    IntActiQ6PIU2. 1 interaction.
    STRINGi9606.ENSP00000273512.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PIU2.
    SMRiQ6PIU2. Positions 90-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini26 – 408383LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi113 – 1153Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

    Sequence similaritiesi

    Belongs to the 'GDXG' lipolytic enzyme family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0657.
    HOVERGENiHBG058974.
    InParanoidiQ6PIU2.
    KOiK14349.
    OMAiALGQQFT.
    OrthoDBiEOG7HB599.
    PhylomeDBiQ6PIU2.

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR017157. Arylacetamide_deacetylase.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 2 hits.
    [Graphical view]
    PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6PIU2-1) [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

    MRSSCVLLTA LVALAAYYVY IPLPGSVSDP WKLMLLDATF RGAQQVSNLI    50
    HYLGLSHHLL ALNFIIVSFG KKSAWSSAQV KVTDTDFDGV EVRVFEGPPK 100
    PEEPLKRSVV YIHGGGWALA SAKIRYYDEL CTAMAEELNA VIVSIEYRLV 150
    PKVYFPEQIH DVVRATKYFL KPEVLQKYMV DPGRICISGD SAGGNLAAAL 200
    GQQFTQDASL KNKLKLQALI YPVLQALDFN TPSYQQNVNT PILPRYVMVK 250
    YWVDYFKGNY DFVQAMIVNN HTSLDVEEAA AVRARLNWTS LLPASFTKNY 300
    KPVVQTTGNA RIVQELPQLL DARSAPLIAD QAVLQLLPKT YILTCEHDVL 350
    RDDGIMYAKR LESAGVEVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY 400
    IKWLDQNL 408
    Length:408
    Mass (Da):45,808
    Last modified:December 12, 2006 - v3
    Checksum:iE5754850BE9805B5
    GO
    Isoform 2 (identifier: Q6PIU2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         123-123: K → SASWSPSDE

    Show »
    Length:416
    Mass (Da):46,627
    Checksum:iA315923F59D660E7
    GO
    Isoform 3 (identifier: Q6PIU2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.

    Show »
    Length:275
    Mass (Da):31,168
    Checksum:i1D5212243D62F48B
    GO

    Sequence cautioni

    The sequence AAH28734.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH47588.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AC007919 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AC069237 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA92601.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAH13028.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAH14142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAH14802.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161A → T in BAA92601. (PubMed:10718198)Curated
    Sequence conflicti58 – 581H → R in BAH13028. (PubMed:14702039)Curated
    Sequence conflicti72 – 721K → R in BAH14802. (PubMed:14702039)Curated
    Sequence conflicti79 – 791Q → K in AAH47588. (PubMed:15489334)Curated
    Sequence conflicti254 – 2541D → G in BAH14142. (PubMed:14702039)Curated
    Sequence conflicti329 – 3291A → S in BAH14142. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191V → F.
    Corresponds to variant rs35316420 [ dbSNP | Ensembl ].
    VAR_047099
    Natural varianti71 – 711K → Q.
    Corresponds to variant rs2302815 [ dbSNP | Ensembl ].
    VAR_047100
    Natural varianti343 – 3431L → M.1 Publication
    Corresponds to variant rs17857335 [ dbSNP | Ensembl ].
    VAR_047101

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 133133Missing in isoform 3. 1 PublicationVSP_037518Add
    BLAST
    Alternative sequencei123 – 1231K → SASWSPSDE in isoform 2. 1 PublicationVSP_037519

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037784 mRNA. Translation: BAA92601.1. Different initiation.
    AK294811 mRNA. Translation: BAH11890.1.
    AK295641 mRNA. Translation: BAH12137.1.
    AK299422 mRNA. Translation: BAH13028.1. Different initiation.
    AK304253 mRNA. Translation: BAH14142.1. Different initiation.
    AK316431 mRNA. Translation: BAH14802.1. Different initiation.
    AC007919 Genomic DNA. No translation available.
    AC069237 Genomic DNA. No translation available.
    BC028734 mRNA. Translation: AAH28734.2. Different initiation.
    BC047588 mRNA. Translation: AAH47588.2. Different initiation.
    CCDSiCCDS54681.1. [Q6PIU2-3]
    RefSeqiNP_001139748.1. NM_001146276.1.
    NP_001139749.1. NM_001146277.1. [Q6PIU2-3]
    NP_001139750.1. NM_001146278.1. [Q6PIU2-3]
    NP_065843.3. NM_020792.4.
    UniGeneiHs.444099.

    Genome annotation databases

    EnsembliENST00000475381; ENSP00000418571; ENSG00000144959. [Q6PIU2-1]
    ENST00000543711; ENSP00000443227; ENSG00000144959. [Q6PIU2-3]
    GeneIDi57552.
    KEGGihsa:57552.
    UCSCiuc011bpw.2. human. [Q6PIU2-1]

    Polymorphism databases

    DMDMi74737782.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB037784 mRNA. Translation: BAA92601.1 . Different initiation.
    AK294811 mRNA. Translation: BAH11890.1 .
    AK295641 mRNA. Translation: BAH12137.1 .
    AK299422 mRNA. Translation: BAH13028.1 . Different initiation.
    AK304253 mRNA. Translation: BAH14142.1 . Different initiation.
    AK316431 mRNA. Translation: BAH14802.1 . Different initiation.
    AC007919 Genomic DNA. No translation available.
    AC069237 Genomic DNA. No translation available.
    BC028734 mRNA. Translation: AAH28734.2 . Different initiation.
    BC047588 mRNA. Translation: AAH47588.2 . Different initiation.
    CCDSi CCDS54681.1. [Q6PIU2-3 ]
    RefSeqi NP_001139748.1. NM_001146276.1.
    NP_001139749.1. NM_001146277.1. [Q6PIU2-3 ]
    NP_001139750.1. NM_001146278.1. [Q6PIU2-3 ]
    NP_065843.3. NM_020792.4.
    UniGenei Hs.444099.

    3D structure databases

    ProteinModelPortali Q6PIU2.
    SMRi Q6PIU2. Positions 90-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121608. 1 interaction.
    IntActi Q6PIU2. 1 interaction.
    STRINGi 9606.ENSP00000273512.

    Chemistry

    BindingDBi Q6PIU2.
    ChEMBLi CHEMBL5048.

    Protein family/group databases

    MEROPSi S09.992.

    PTM databases

    PhosphoSitei Q6PIU2.

    Polymorphism databases

    DMDMi 74737782.

    Proteomic databases

    MaxQBi Q6PIU2.
    PaxDbi Q6PIU2.
    PRIDEi Q6PIU2.

    Protocols and materials databases

    DNASUi 57552.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000475381 ; ENSP00000418571 ; ENSG00000144959 . [Q6PIU2-1 ]
    ENST00000543711 ; ENSP00000443227 ; ENSG00000144959 . [Q6PIU2-3 ]
    GeneIDi 57552.
    KEGGi hsa:57552.
    UCSCi uc011bpw.2. human. [Q6PIU2-1 ]

    Organism-specific databases

    CTDi 57552.
    GeneCardsi GC03M172348.
    H-InvDB HIX0003864.
    HIX0163448.
    HGNCi HGNC:29260. NCEH1.
    HPAi HPA026888.
    MIMi 613234. gene.
    neXtProti NX_Q6PIU2.
    PharmGKBi PA165697847.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0657.
    HOVERGENi HBG058974.
    InParanoidi Q6PIU2.
    KOi K14349.
    OMAi ALGQQFT.
    OrthoDBi EOG7HB599.
    PhylomeDBi Q6PIU2.

    Miscellaneous databases

    ChiTaRSi NCEH1. human.
    GeneWikii NCEH1.
    GenomeRNAii 57552.
    NextBioi 64018.
    PROi Q6PIU2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PIU2.
    Bgeei Q6PIU2.
    CleanExi HS_AADACL1.
    Genevestigatori Q6PIU2.

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR017157. Arylacetamide_deacetylase.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view ]
    Pfami PF07859. Abhydrolase_3. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF037251. Arylacetamide_deacetylase. 1 hit.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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.
      , 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; 2 AND 3).
      Tissue: Brain, Hippocampus, Testis, Tongue and Trachea.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 MET-343.
      Tissue: Brain.
    5. "Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness."
      Jessani N., Liu Y., Humphrey M., Cravatt B.F.
      Proc. Natl. Acad. Sci. U.S.A. 99:10335-10340(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
    6. "An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling."
      Chiang K.P., Niessen S., Saghatelian A., Cravatt B.F.
      Chem. Biol. 13:1041-1050(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: TISSUE SPECIFICITY.
    8. "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-287.
      Tissue: Liver.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNCEH1_HUMAN
    AccessioniPrimary (citable) accession number: Q6PIU2
    Secondary accession number(s): B7Z2K4
    , B7Z3A1, B7Z5U2, B7Z906, B7ZAW6, F5H7K4, Q86WZ1, Q9P2I4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 95 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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