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Q16698

- DECR_HUMAN

UniProt

Q16698 - DECR_HUMAN

Protein

2,4-dienoyl-CoA reductase, mitochondrial

Gene

DECR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.

    Catalytic activityi

    Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.1 Publication

    Kineticsi

    1. KM=7.7 µM for NADPH1 Publication
    2. KM=14.3 µM for trans-2,trans-4-hexadienoyl-CoA1 Publication

    Vmax=30.3 µmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei91 – 911NADP1 Publication
    Binding sitei91 – 911SubstrateBy similarity
    Binding sitei117 – 1171NADP1 Publication
    Binding sitei119 – 1191Substrate1 Publication
    Binding sitei149 – 1491Substrate1 Publication
    Binding sitei157 – 1571Substrate1 Publication
    Active sitei199 – 1991Proton acceptorSequence Analysis
    Binding sitei214 – 2141NADP1 Publication
    Binding sitei251 – 2511SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi66 – 716NADP1 Publication
    Nucleotide bindingi240 – 2434NADP1 Publication

    GO - Molecular functioni

    1. 2,4-dienoyl-CoA reductase (NADPH) activity Source: UniProtKB
    2. NADPH binding Source: UniProtKB
    3. oxidoreductase activity, acting on NAD(P)H Source: Reactome

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. fatty acid beta-oxidation Source: UniProtKB
    3. protein homotetramerization Source: UniProtKB
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    SABIO-RKQ16698.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,4-dienoyl-CoA reductase, mitochondrial (EC:1.3.1.34)
    Alternative name(s):
    2,4-dienoyl-CoA reductase [NADPH]
    Short name:
    4-enoyl-CoA reductase [NADPH]
    Gene namesi
    Name:DECR1
    Synonyms:DECR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2753. DECR1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: UniProtKB
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi148 – 1481N → A: Reduces enzyme activity by 97%. 1 Publication
    Mutagenesisi199 – 1991Y → A: Reduces enzyme activity by 99%. Strongly reduced affinity for substrate and for NADP. 1 Publication
    Mutagenesisi210 – 2101S → A: Reduces enzyme activity by over 99%. 1 Publication
    Mutagenesisi214 – 2141K → A: Reduces enzyme activity by over 99%. 1 Publication

    Organism-specific databases

    MIMi222745. gene+phenotype.
    PharmGKBiPA141.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3434MitochondrionBy similarityAdd
    BLAST
    Chaini35 – 3353012,4-dienoyl-CoA reductase, mitochondrialPRO_0000031965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421N6-acetyllysine; alternateBy similarity
    Modified residuei42 – 421N6-succinyllysine; alternateBy similarity
    Modified residuei49 – 491N6-acetyllysine; alternateBy similarity
    Modified residuei49 – 491N6-succinyllysine; alternateBy similarity
    Modified residuei73 – 731N6-succinyllysineBy similarity
    Modified residuei97 – 971N6-acetyllysine; alternateBy similarity
    Modified residuei97 – 971N6-succinyllysine; alternateBy similarity
    Modified residuei230 – 2301N6-acetyllysine1 Publication
    Modified residuei244 – 2441N6-acetyllysine; alternateBy similarity
    Modified residuei244 – 2441N6-succinyllysine; alternateBy similarity
    Modified residuei260 – 2601N6-acetyllysine; alternateBy similarity
    Modified residuei260 – 2601N6-succinyllysine; alternateBy similarity
    Modified residuei319 – 3191N6-acetyllysine; alternateBy similarity
    Modified residuei319 – 3191N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ16698.
    PaxDbiQ16698.
    PeptideAtlasiQ16698.
    PRIDEiQ16698.

    2D gel databases

    UCD-2DPAGEQ16698.

    PTM databases

    PhosphoSiteiQ16698.

    Expressioni

    Tissue specificityi

    Heart = liver = pancreas > kidney >> skeletal muscle = lung.1 Publication

    Gene expression databases

    ArrayExpressiQ16698.
    BgeeiQ16698.
    CleanExiHS_DECR1.
    GenevestigatoriQ16698.

    Organism-specific databases

    HPAiHPA023160.
    HPA023162.
    HPA023238.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi108030. 9 interactions.
    IntActiQ16698. 5 interactions.
    STRINGi9606.ENSP00000220764.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 438
    Turni54 – 596
    Beta strandi61 – 655
    Turni66 – 683
    Helixi70 – 8112
    Beta strandi85 – 917
    Helixi93 – 10715
    Beta strandi111 – 1155
    Helixi121 – 13414
    Beta strandi139 – 1435
    Helixi153 – 1553
    Helixi158 – 18528
    Beta strandi190 – 1956
    Helixi199 – 2024
    Helixi208 – 22821
    Helixi229 – 2313
    Beta strandi233 – 2408
    Beta strandi254 – 2563
    Helixi257 – 2637
    Helixi274 – 28411
    Helixi287 – 2893
    Beta strandi296 – 3005
    Helixi303 – 3086
    Helixi312 – 3165
    Helixi319 – 3257

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W6UX-ray1.75A/B/C/D35-335[»]
    1W73X-ray2.10A/B/C/D35-335[»]
    1W8DX-ray2.20A/B/C/D35-335[»]
    ProteinModelPortaliQ16698.
    SMRiQ16698. Positions 35-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16698.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG005465.
    InParanoidiQ16698.
    KOiK13236.
    OMAiSMAGEFN.
    PhylomeDBiQ16698.
    TreeFamiTF315256.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.

    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: Q16698-1) [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

    MKLPARVFFT LGSRLPCGLA PRRFFSYGTK ILYQNTEALQ SKFFSPLQKA    50
    MLPPNSFQGK VAFITGGGTG LGKGMTTLLS SLGAQCVIAS RKMDVLKATA 100
    EQISSQTGNK VHAIQCDVRD PDMVQNTVSE LIKVAGHPNI VINNAAGNFI 150
    SPTERLSPNA WKTITDIVLN GTAFVTLEIG KQLIKAQKGA AFLSITTIYA 200
    ETGSGFVVPS ASAKAGVEAM SKSLAAEWGK YGMRFNVIQP GPIKTKGAFS 250
    RLDPTGTFEK EMIGRIPCGR LGTVEELANL AAFLCSDYAS WINGAVIKFD 300
    GGEEVLISGE FNDLRKVTKE QWDTIEELIR KTKGS 335
    Length:335
    Mass (Da):36,068
    Last modified:November 1, 1996 - v1
    Checksum:iF04E72AACB718430
    GO
    Isoform 2 (identifier: Q16698-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MKLPARVFFTLGSRLPCGLAPRR → MSGLGKKHLLLMGE

    Note: No experimental confirmation available.

    Show »
    Length:326
    Mass (Da):34,994
    Checksum:i81B865BEAD0F75A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti287 – 2871D → G in AAB09423. 1 PublicationCurated
    Sequence conflicti292 – 2921I → V in AAB09423. 1 PublicationCurated
    Sequence conflicti303 – 3031E → G in AAB09423. 1 PublicationCurated
    Sequence conflicti311 – 3111F → G in AAB09423. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti333 – 3331K → N.
    Corresponds to variant rs15094 [ dbSNP | Ensembl ].
    VAR_012034

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323MKLPA…LAPRR → MSGLGKKHLLLMGE in isoform 2. 1 PublicationVSP_056388Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26050 mRNA. Translation: AAA67551.1.
    U49352 mRNA. Translation: AAB09423.1.
    U78302
    , U94980, U94981, U94982, U94983, U94984, U94985, U94986, U94987 Genomic DNA. Translation: AAB88724.1.
    AK300069 mRNA. Translation: BAH13204.1.
    AC004612 Genomic DNA. Translation: AAC14671.1.
    AF049895 Genomic DNA. No translation available.
    BC105080 mRNA. Translation: AAI05081.1.
    BC105082 mRNA. Translation: AAI05083.1.
    CCDSiCCDS6250.1.
    PIRiS53352.
    RefSeqiNP_001350.1. NM_001359.1.
    UniGeneiHs.492212.

    Genome annotation databases

    EnsembliENST00000220764; ENSP00000220764; ENSG00000104325.
    ENST00000522161; ENSP00000429779; ENSG00000104325.
    GeneIDi1666.
    KEGGihsa:1666.
    UCSCiuc003yek.1. human.

    Polymorphism databases

    DMDMi3913456.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26050 mRNA. Translation: AAA67551.1 .
    U49352 mRNA. Translation: AAB09423.1 .
    U78302
    , U94980 , U94981 , U94982 , U94983 , U94984 , U94985 , U94986 , U94987 Genomic DNA. Translation: AAB88724.1 .
    AK300069 mRNA. Translation: BAH13204.1 .
    AC004612 Genomic DNA. Translation: AAC14671.1 .
    AF049895 Genomic DNA. No translation available.
    BC105080 mRNA. Translation: AAI05081.1 .
    BC105082 mRNA. Translation: AAI05083.1 .
    CCDSi CCDS6250.1.
    PIRi S53352.
    RefSeqi NP_001350.1. NM_001359.1.
    UniGenei Hs.492212.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W6U X-ray 1.75 A/B/C/D 35-335 [» ]
    1W73 X-ray 2.10 A/B/C/D 35-335 [» ]
    1W8D X-ray 2.20 A/B/C/D 35-335 [» ]
    ProteinModelPortali Q16698.
    SMRi Q16698. Positions 35-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108030. 9 interactions.
    IntActi Q16698. 5 interactions.
    STRINGi 9606.ENSP00000220764.

    PTM databases

    PhosphoSitei Q16698.

    Polymorphism databases

    DMDMi 3913456.

    2D gel databases

    UCD-2DPAGE Q16698.

    Proteomic databases

    MaxQBi Q16698.
    PaxDbi Q16698.
    PeptideAtlasi Q16698.
    PRIDEi Q16698.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000220764 ; ENSP00000220764 ; ENSG00000104325 .
    ENST00000522161 ; ENSP00000429779 ; ENSG00000104325 .
    GeneIDi 1666.
    KEGGi hsa:1666.
    UCSCi uc003yek.1. human.

    Organism-specific databases

    CTDi 1666.
    GeneCardsi GC08P091082.
    HGNCi HGNC:2753. DECR1.
    HPAi HPA023160.
    HPA023162.
    HPA023238.
    MIMi 222745. gene+phenotype.
    neXtProti NX_Q16698.
    PharmGKBi PA141.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG005465.
    InParanoidi Q16698.
    KOi K13236.
    OMAi SMAGEFN.
    PhylomeDBi Q16698.
    TreeFami TF315256.

    Enzyme and pathway databases

    Reactomei REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
    SABIO-RK Q16698.

    Miscellaneous databases

    ChiTaRSi DECR1. human.
    EvolutionaryTracei Q16698.
    GenomeRNAii 1666.
    NextBioi 6856.
    PROi Q16698.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16698.
    Bgeei Q16698.
    CleanExi HS_DECR1.
    Genevestigatori Q16698.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of cDNA for human 120 kDa mitochondrial 2,4-dienoyl-coenzyme A reductase."
      Koivuranta K.T., Hakkola E.H., Hiltunen J.K.
      Biochem. J. 304:787-792(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Liver.
    2. Ding J.H., Yang B.Z., Roe C.R.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Molecular cloning and characterization of the human mitochondrial 2,4-dienoyl-CoA reductase gene (DECR)."
      Helander H.M., Koivuranta K.T., Horelli-Kuitunen N., Palvimo J.J., Palotie A., Hiltunen J.K.
      Genomics 46:112-119(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 2).
      Tissue: Pericardium.
    5. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain.
    7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase: enzyme-ligand interactions in a distinctive short-chain reductase active site."
      Alphey M.S., Yu W., Byres E., Li D., Hunter W.N.
      J. Biol. Chem. 280:3068-3077(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 35-335 IN COMPLEX WITH NADP AND SUBSTRATE, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-148; TYR-199; SER-210 AND LYS-214.

    Entry informationi

    Entry nameiDECR_HUMAN
    AccessioniPrimary (citable) accession number: Q16698
    Secondary accession number(s): B7Z6B8, Q2M304, Q93085
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 131 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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