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Q9NWU1

- OXSM_HUMAN

UniProt

Q9NWU1 - OXSM_HUMAN

Protein

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

Gene

OXSM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.1 Publication

    Catalytic activityi

    Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

    Enzyme regulationi

    Inhibited by cerulenin.1 Publication

    Kineticsi

    The highest catalytic efficiency is observed for C10-[acyl-carrier-protein].

    1. KM=3.9 µM for C4-[acyl-carrier-protein]1 Publication
    2. KM=1.9 µM for C6-[acyl-carrier-protein]1 Publication
    3. KM=10.9 µM for C8-[acyl-carrier-protein]1 Publication
    4. KM=1.8 µM for C10-[acyl-carrier-protein]1 Publication
    5. KM=9.5 µM for C12-[acyl-carrier-protein]1 Publication
    6. KM=50.8 µM for C14-[acyl-carrier-protein]1 Publication

    Vmax=129 nmol/min/mg enzyme toward C4-[acyl-carrier-protein]1 Publication

    Vmax=241 nmol/min/mg enzyme toward C6-[acyl-carrier-protein]1 Publication

    Vmax=271 nmol/min/mg enzyme toward C8-[acyl-carrier-protein]1 Publication

    Vmax=364 nmol/min/mg enzyme toward C10-[acyl-carrier-protein]1 Publication

    Vmax=1045 nmol/min/mg enzyme toward C12-[acyl-carrier-protein]1 Publication

    Vmax=115 nmol/min/mg enzyme toward C14-[acyl-carrier-protein]1 Publication

    Pathwayi

    GO - Molecular functioni

    1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: HGNC

    GO - Biological processi

    1. acyl-CoA metabolic process Source: HGNC
    2. medium-chain fatty acid biosynthetic process Source: HGNC
    3. short-chain fatty acid biosynthetic process Source: HGNC

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    BRENDAi2.3.1.41. 2681.
    SABIO-RKQ9NWU1.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (EC:2.3.1.41)
    Alternative name(s):
    Beta-ketoacyl-ACP synthase
    Gene namesi
    Name:OXSM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:26063. OXSM.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: LIFEdb

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671214.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
    BLAST
    Chaini28 – 4594323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrialPRO_0000232660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei109 – 1091N6-acetyllysine; alternateBy similarity
    Modified residuei109 – 1091N6-succinyllysine; alternateBy similarity
    Modified residuei113 – 1131N6-succinyllysineBy similarity
    Modified residuei174 – 1741N6-acetyllysine; alternate1 Publication
    Modified residuei174 – 1741N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NWU1.
    PaxDbiQ9NWU1.
    PeptideAtlasiQ9NWU1.
    PRIDEiQ9NWU1.

    PTM databases

    PhosphoSiteiQ9NWU1.

    Expressioni

    Tissue specificityi

    Widely expressed. Higher expression in heart, skeletal muscle, liver and kidney which contain high levels of active mitochondria.1 Publication

    Gene expression databases

    ArrayExpressiQ9NWU1.
    BgeeiQ9NWU1.
    CleanExiHS_OXSM.
    GenevestigatoriQ9NWU1.

    Organism-specific databases

    HPAiHPA021293.
    HPA021300.
    HPA021337.

    Interactioni

    Protein-protein interaction databases

    BioGridi120328. 2 interactions.
    STRINGi9606.ENSP00000280701.

    Structurei

    Secondary structure

    1
    459
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 414
    Beta strandi44 – 5310
    Beta strandi56 – 583
    Helixi59 – 679
    Beta strandi73 – 753
    Helixi79 – 813
    Beta strandi88 – 903
    Beta strandi94 – 974
    Helixi103 – 1053
    Helixi109 – 1124
    Helixi117 – 13317
    Helixi140 – 1445
    Beta strandi146 – 1538
    Helixi157 – 17014
    Helixi172 – 1743
    Helixi179 – 1824
    Helixi187 – 19610
    Helixi208 – 2103
    Helixi211 – 22515
    Beta strandi229 – 2379
    Helixi242 – 2509
    Turni260 – 2623
    Beta strandi279 – 2879
    Helixi288 – 2936
    Beta strandi300 – 30910
    Beta strandi314 – 3163
    Helixi322 – 33514
    Helixi339 – 3413
    Beta strandi344 – 3463
    Helixi353 – 36715
    Helixi368 – 3725
    Beta strandi374 – 3774
    Helixi380 – 3834
    Helixi387 – 3893
    Helixi390 – 40415
    Beta strandi426 – 4283
    Beta strandi435 – 4373
    Beta strandi439 – 4468
    Turni447 – 4493
    Beta strandi450 – 4578

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C9HX-ray1.80A39-459[»]
    2IWYX-ray2.06A/B38-459[»]
    2IWZX-ray1.65A/B38-459[»]
    ProteinModelPortaliQ9NWU1.
    SMRiQ9NWU1. Positions 38-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NWU1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the beta-ketoacyl-ACP synthases family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0304.
    HOGENOMiHOG000060166.
    HOVERGENiHBG082096.
    InParanoidiQ9NWU1.
    KOiK09458.
    OMAiHAQKRNA.
    PhylomeDBiQ9NWU1.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR017568. 3-oxoacyl-ACP_synth-2.
    IPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000447. KAS_II. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR03150. fabF. 1 hit.
    PROSITEiPS00606. B_KETOACYL_SYNTHASE. 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: Q9NWU1-1) [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

    MSNCLQNFLK ITSTRLLCSR LCQQLRSKRK FFGTVPISRL HRRVVITGIG    50
    LVTPLGVGTH LVWDRLIGGE SGIVSLVGEE YKSIPCSVAA YVPRGSDEGQ 100
    FNEQNFVSKS DIKSMSSPTI MAIGAAELAM KDSGWHPQSE ADQVATGVAI 150
    GMGMIPLEVV SETALNFQTK GYNKVSPFFV PKILVNMAAG QVSIRYKLKG 200
    PNHAVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI SPLSLAGFSR 250
    ARALSTNSDP KLACRPFHPK RDGFVMGEGA AVLVLEEYEH AVQRRARIYA 300
    EVLGYGLSGD AGHITAPDPE GEGALRCMAA ALKDAGVQPE EISYINAHAT 350
    STPLGDAAEN KAIKHLFKDH AYALAVSSTK GATGHLLGAA GAVEAAFTTL 400
    ACYYQKLPPT LNLDCSEPEF DLNYVPLKAQ EWKTEKRFIG LTNSFGFGGT 450
    NATLCIAGL 459
    Length:459
    Mass (Da):48,843
    Last modified:October 1, 2000 - v1
    Checksum:iB2EF550CD354F18C
    GO
    Isoform 2 (identifier: Q9NWU1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         229-311: Missing.

    Show »
    Length:376
    Mass (Da):40,035
    Checksum:iB9470D089DE7CF7D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061F → I in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036064

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei229 – 31183Missing in isoform 2. 1 PublicationVSP_041671Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000611 mRNA. Translation: BAA91286.1.
    AK225260 mRNA. No translation available.
    AC092798 Genomic DNA. No translation available.
    BC008202 mRNA. Translation: AAH08202.1.
    CCDSiCCDS2643.1. [Q9NWU1-1]
    CCDS46780.1. [Q9NWU1-2]
    RefSeqiNP_001138863.1. NM_001145391.1. [Q9NWU1-2]
    NP_060367.1. NM_017897.2. [Q9NWU1-1]
    XP_006713279.1. XM_006713216.1. [Q9NWU1-1]
    UniGeneiHs.55781.

    Genome annotation databases

    EnsembliENST00000280701; ENSP00000280701; ENSG00000151093. [Q9NWU1-1]
    ENST00000420173; ENSP00000411303; ENSG00000151093. [Q9NWU1-2]
    GeneIDi54995.
    KEGGihsa:54995.
    UCSCiuc003cdn.3. human. [Q9NWU1-1]
    uc010hfh.3. human. [Q9NWU1-2]

    Polymorphism databases

    DMDMi74753030.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000611 mRNA. Translation: BAA91286.1 .
    AK225260 mRNA. No translation available.
    AC092798 Genomic DNA. No translation available.
    BC008202 mRNA. Translation: AAH08202.1 .
    CCDSi CCDS2643.1. [Q9NWU1-1 ]
    CCDS46780.1. [Q9NWU1-2 ]
    RefSeqi NP_001138863.1. NM_001145391.1. [Q9NWU1-2 ]
    NP_060367.1. NM_017897.2. [Q9NWU1-1 ]
    XP_006713279.1. XM_006713216.1. [Q9NWU1-1 ]
    UniGenei Hs.55781.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C9H X-ray 1.80 A 39-459 [» ]
    2IWY X-ray 2.06 A/B 38-459 [» ]
    2IWZ X-ray 1.65 A/B 38-459 [» ]
    ProteinModelPortali Q9NWU1.
    SMRi Q9NWU1. Positions 38-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120328. 2 interactions.
    STRINGi 9606.ENSP00000280701.

    PTM databases

    PhosphoSitei Q9NWU1.

    Polymorphism databases

    DMDMi 74753030.

    Proteomic databases

    MaxQBi Q9NWU1.
    PaxDbi Q9NWU1.
    PeptideAtlasi Q9NWU1.
    PRIDEi Q9NWU1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280701 ; ENSP00000280701 ; ENSG00000151093 . [Q9NWU1-1 ]
    ENST00000420173 ; ENSP00000411303 ; ENSG00000151093 . [Q9NWU1-2 ]
    GeneIDi 54995.
    KEGGi hsa:54995.
    UCSCi uc003cdn.3. human. [Q9NWU1-1 ]
    uc010hfh.3. human. [Q9NWU1-2 ]

    Organism-specific databases

    CTDi 54995.
    GeneCardsi GC03P025824.
    HGNCi HGNC:26063. OXSM.
    HPAi HPA021293.
    HPA021300.
    HPA021337.
    MIMi 610324. gene.
    neXtProti NX_Q9NWU1.
    PharmGKBi PA142671214.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0304.
    HOGENOMi HOG000060166.
    HOVERGENi HBG082096.
    InParanoidi Q9NWU1.
    KOi K09458.
    OMAi HAQKRNA.
    PhylomeDBi Q9NWU1.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BRENDAi 2.3.1.41. 2681.
    SABIO-RK Q9NWU1.

    Miscellaneous databases

    EvolutionaryTracei Q9NWU1.
    GenomeRNAii 54995.
    NextBioi 58306.
    PROi Q9NWU1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NWU1.
    Bgeei Q9NWU1.
    CleanExi HS_OXSM.
    Genevestigatori Q9NWU1.

    Family and domain databases

    Gene3Di 3.40.47.10. 2 hits.
    InterProi IPR017568. 3-oxoacyl-ACP_synth-2.
    IPR018201. Ketoacyl_synth_AS.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000447. KAS_II. 1 hit.
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR03150. fabF. 1 hit.
    PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 AND 2).
      Tissue: Carcinoma.
    2. "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].
    3. "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: Placenta.
    4. "Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain."
      Zhang L., Joshi A.K., Hofmann J., Schweizer E., Smith S.
      J. Biol. Chem. 280:12422-12429(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "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-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Structure of mitochondrial beta-ketoacyl synthase."
      Bunkoczi G., Wu X., Smee C., Gileadi O., Arrowsmith C., Edwards A., Sundstrom M., Weigelt J., von Delft F., Oppermann U.
      Submitted (DEC-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-459.
    8. "Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase."
      Christensen C.E., Kragelund B.B., von Wettstein-Knowles P., Henriksen A.
      Protein Sci. 16:261-272(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-459.
    9. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-106.

    Entry informationi

    Entry nameiOXSM_HUMAN
    AccessioniPrimary (citable) accession number: Q9NWU1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 111 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 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3