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P00860

- DCOR_MOUSE

UniProt

P00860 - DCOR_MOUSE

Protein

Ornithine decarboxylase

Gene

Odc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Key enzyme of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine.2 Publications

    Catalytic activityi

    L-ornithine = putrescine + CO2.

    Cofactori

    Pyridoxal phosphate.

    Enzyme regulationi

    Inhibited by S-nitrosylation. Inhibited by antizyme OAZ1, OAZ2 and OAZ3 By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei360 – 3601Proton donor; shared with dimeric partner2 Publications

    GO - Molecular functioni

    1. ornithine decarboxylase activity Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. kidney development Source: MGI
    2. positive regulation of cell proliferation Source: MGI
    3. putrescine biosynthetic process from ornithine Source: UniProtKB
    4. regulation of protein catabolic process Source: UniProtKB
    5. response to virus Source: Ensembl

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi4.1.1.17. 3474.
    UniPathwayiUPA00535; UER00288.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ornithine decarboxylase (EC:4.1.1.17)
    Short name:
    ODC
    Gene namesi
    Name:Odc1
    Synonyms:Odc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:97402. Odc1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: MGI
    3. perinuclear region of cytoplasm Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi387 – 3871G → A: Partial loss of activity. 1 Publication
    Mutagenesisi387 – 3871G → C, D, E, F, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Ornithine decarboxylasePRO_0000149892Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-(pyridoxal phosphate)lysine
    Modified residuei303 – 3031Phosphoserine; by CK21 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP00860.

    PTM databases

    PhosphoSiteiP00860.

    Expressioni

    Tissue specificityi

    Expressed during testis development in the outer part of the seminiferous tubules.1 Publication

    Gene expression databases

    BgeeiP00860.
    CleanExiMM_ODC1.
    GenevestigatoriP00860.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Does not form an heterodimer with AZIN2.1 Publication

    Protein-protein interaction databases

    IntActiP00860. 1 interaction.

    Structurei

    Secondary structure

    1
    461
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi9 – 146
    Helixi20 – 289
    Beta strandi40 – 445
    Helixi45 – 5814
    Beta strandi62 – 676
    Helixi68 – 703
    Helixi74 – 8310
    Beta strandi86 – 894
    Helixi92 – 1009
    Helixi105 – 1073
    Beta strandi108 – 1103
    Helixi117 – 1259
    Beta strandi130 – 1334
    Helixi136 – 14510
    Beta strandi150 – 1556
    Helixi174 – 18613
    Beta strandi190 – 1956
    Helixi206 – 22520
    Beta strandi231 – 2333
    Beta strandi241 – 2466
    Helixi248 – 26215
    Helixi265 – 2673
    Beta strandi270 – 2734
    Helixi277 – 2804
    Helixi281 – 2833
    Beta strandi284 – 29613
    Beta strandi313 – 3197
    Turni322 – 3265
    Helixi327 – 3315
    Beta strandi339 – 3424
    Beta strandi350 – 3567
    Beta strandi358 – 3603
    Beta strandi365 – 3739
    Beta strandi380 – 3834
    Beta strandi388 – 3903
    Helixi391 – 3933
    Helixi397 – 3993
    Beta strandi404 – 4107
    Helixi411 – 4177

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    7ODCX-ray1.60A1-424[»]
    ProteinModelPortaliP00860.
    SMRiP00860. Positions 2-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00860.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0019.
    GeneTreeiENSGT00390000011560.
    HOGENOMiHOG000274133.
    HOVERGENiHBG005456.
    InParanoidiQ6PB87.
    KOiK01581.
    OMAiTIHYVMS.
    OrthoDBiEOG73Z2T6.
    TreeFamiTF300760.

    Family and domain databases

    Gene3Di2.40.37.10. 1 hit.
    3.20.20.10. 1 hit.
    InterProiIPR009006. Ala_racemase/Decarboxylase_C.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR002433. Orn_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view]
    PfamiPF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view]
    PRINTSiPR01179. ODADCRBXLASE.
    PR01182. ORNDCRBXLASE.
    SUPFAMiSSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    PROSITEiPS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00860-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSFTKDEFD CHILDEGFTA KDILDQKINE VSSSDDKDAF YVADLGDILK    50
    KHLRWLKALP RVTPFYAVKC NDSRAIVSTL AAIGTGFDCA SKTEIQLVQG 100
    LGVPAERVIY ANPCKQVSQI KYAASNGVQM MTFDSEIELM KVARAHPKAK 150
    LVLRIATDDS KAVCRLSVKF GATLKTSRLL LERAKELNID VIGVSFHVGS 200
    GCTDPETFVQ AVSDARCVFD MATEVGFSMH LLDIGGGFPG SEDTKLKFEE 250
    ITSVINPALD KYFPSDSGVR IIAEPGRYYV ASAFTLAVNI IAKKTVWKEQ 300
    PGSDDEDESN EQTFMYYVND GVYGSFNCIL YDHAHVKALL QKRPKPDEKY 350
    YSSSIWGPTC DGLDRIVERC NLPEMHVGDW MLFENMGAYT VAAASTFNGF 400
    QRPNIYYVMS RPMWQLMKQI QSHGFPPEVE EQDDGTLPMS CAQESGMDRH 450
    PAACASARIN V 461
    Length:461
    Mass (Da):51,177
    Last modified:July 27, 2011 - v2
    Checksum:iB581753F57AC0A30
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781R → W in AAA39846. (PubMed:3456155)Curated
    Sequence conflicti206 – 2061E → D in AAA51638. (PubMed:2982844)Curated
    Sequence conflicti206 – 2061E → D in AAA39845. (PubMed:3856848)Curated
    Sequence conflicti206 – 2061E → D in CAA30301. (PubMed:3362685)Curated
    Sequence conflicti206 – 2061E → D in AAA39849. (PubMed:3372502)Curated
    Sequence conflicti206 – 2061E → D in AAB27809. (PubMed:8350350)Curated
    Sequence conflicti350 – 3501Y → H in AAA39848. (PubMed:3456155)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20617 mRNA. Translation: AAA51638.1.
    M10624 mRNA. Translation: AAA39845.1.
    X07392 Genomic DNA. Translation: CAA30301.1.
    J03733 Genomic DNA. Translation: AAA39849.1.
    S64539 mRNA. Translation: AAB27809.1.
    EU684749 mRNA. Translation: ACD81645.1.
    AK139610 mRNA. Translation: BAE24082.1.
    CH466582 Genomic DNA. Translation: EDK98494.1.
    BC059826 mRNA. Translation: AAH59826.1.
    BC083122 mRNA. Translation: AAH83122.1.
    M12330 mRNA. Translation: AAA39846.1.
    M12331 mRNA. Translation: AAA39848.1.
    CCDSiCCDS25829.1.
    PIRiA01077. DCMSO.
    I56477.
    RefSeqiNP_038642.2. NM_013614.2.
    UniGeneiMm.34102.
    Mm.472891.

    Genome annotation databases

    EnsembliENSMUST00000171737; ENSMUSP00000128661; ENSMUSG00000011179.
    GeneIDi18263.
    KEGGimmu:18263.
    UCSCiuc007ncv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20617 mRNA. Translation: AAA51638.1 .
    M10624 mRNA. Translation: AAA39845.1 .
    X07392 Genomic DNA. Translation: CAA30301.1 .
    J03733 Genomic DNA. Translation: AAA39849.1 .
    S64539 mRNA. Translation: AAB27809.1 .
    EU684749 mRNA. Translation: ACD81645.1 .
    AK139610 mRNA. Translation: BAE24082.1 .
    CH466582 Genomic DNA. Translation: EDK98494.1 .
    BC059826 mRNA. Translation: AAH59826.1 .
    BC083122 mRNA. Translation: AAH83122.1 .
    M12330 mRNA. Translation: AAA39846.1 .
    M12331 mRNA. Translation: AAA39848.1 .
    CCDSi CCDS25829.1.
    PIRi A01077. DCMSO.
    I56477.
    RefSeqi NP_038642.2. NM_013614.2.
    UniGenei Mm.34102.
    Mm.472891.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    7ODC X-ray 1.60 A 1-424 [» ]
    ProteinModelPortali P00860.
    SMRi P00860. Positions 2-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00860. 1 interaction.

    Chemistry

    ChEMBLi CHEMBL2840.

    PTM databases

    PhosphoSitei P00860.

    Proteomic databases

    PRIDEi P00860.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000171737 ; ENSMUSP00000128661 ; ENSMUSG00000011179 .
    GeneIDi 18263.
    KEGGi mmu:18263.
    UCSCi uc007ncv.1. mouse.

    Organism-specific databases

    CTDi 4953.
    MGIi MGI:97402. Odc1.

    Phylogenomic databases

    eggNOGi COG0019.
    GeneTreei ENSGT00390000011560.
    HOGENOMi HOG000274133.
    HOVERGENi HBG005456.
    InParanoidi Q6PB87.
    KOi K01581.
    OMAi TIHYVMS.
    OrthoDBi EOG73Z2T6.
    TreeFami TF300760.

    Enzyme and pathway databases

    UniPathwayi UPA00535 ; UER00288 .
    BRENDAi 4.1.1.17. 3474.

    Miscellaneous databases

    EvolutionaryTracei P00860.
    NextBioi 293712.
    PROi P00860.
    SOURCEi Search...

    Gene expression databases

    Bgeei P00860.
    CleanExi MM_ODC1.
    Genevestigatori P00860.

    Family and domain databases

    Gene3Di 2.40.37.10. 1 hit.
    3.20.20.10. 1 hit.
    InterProi IPR009006. Ala_racemase/Decarboxylase_C.
    IPR022643. De-COase2_C.
    IPR022657. De-COase2_CS.
    IPR022644. De-COase2_N.
    IPR022653. De-COase2_pyr-phos_BS.
    IPR000183. Orn/DAP/Arg_de-COase.
    IPR002433. Orn_de-COase.
    IPR029066. PLP-binding_barrel.
    [Graphical view ]
    Pfami PF02784. Orn_Arg_deC_N. 1 hit.
    PF00278. Orn_DAP_Arg_deC. 1 hit.
    [Graphical view ]
    PRINTSi PR01179. ODADCRBXLASE.
    PR01182. ORNDCRBXLASE.
    SUPFAMi SSF50621. SSF50621. 1 hit.
    SSF51419. SSF51419. 1 hit.
    PROSITEi PS00878. ODR_DC_2_1. 1 hit.
    PS00879. ODR_DC_2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse ornithine decarboxylase. Complete amino acid sequence deduced from cDNA."
      Gupta M., Coffino P.
      J. Biol. Chem. 260:2941-2944(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Nucleotide sequence of murine ornithine decarboxylase mRNA."
      Kahana C., Nathans D.
      Proc. Natl. Acad. Sci. U.S.A. 82:1673-1677(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Nucleotide sequence of the mouse ornithine decarboxylase gene."
      Coffino P., Chen E.L.
      Nucleic Acids Res. 16:2731-2731(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
    4. "Isolation and characterization of the mouse ornithine decarboxylase gene."
      Katz A., Kahana C.
      J. Biol. Chem. 263:7604-7609(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Domains within the mammalian ornithine decarboxylase messenger RNA have evolved independently and episodically."
      Johannes G.J., Berger F.G.
      J. Mol. Evol. 36:555-567(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. Yu Y., Luo X.
      Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Kunming.
    7. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Egg.
    8. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Strain: C57BL/6.
      Tissue: Brain and Embryo.
    10. "Two ornithine decarboxylase mRNA species in mouse kidney arise from size heterogeneity at their 3' termini."
      Hickok N.J., Seppaenen P.J., Kontula K.K., Jaenne P.A., Bardin C.W., Jaenne O.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:594-598(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-461.
    11. "Mouse ornithine decarboxylase is phosphorylated by casein kinase-II at a predominant single location (serine 303)."
      Rosenberg-Hasson Y., Strumpf D., Kahana C.
      Eur. J. Biochem. 197:419-424(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-303 BY CKII.
    12. "Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites."
      Poulin R., Lu L., Ackermann B., Bey P., Pegg A.E.
      J. Biol. Chem. 267:150-158(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, PYRIDOXAL PHOSPHATE AT LYS-69.
    13. "Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants."
      Tobias K.E., Kahana C.
      Biochemistry 32:5842-5847(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    14. "Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers."
      Tobias K.E., Mamroud-Kidron E., Kahana C.
      Eur. J. Biochem. 218:245-250(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-387.
    15. "Expression of antizyme inhibitor 2 in male haploid germinal cells suggests a role in spermiogenesis."
      Lopez-Contreras A.J., Ramos-Molina B., Martinez-de-la-Torre M., Penafiel-Verdu C., Puelles L., Cremades A., Penafiel R.
      Int. J. Biochem. Cell Biol. 41:1070-1078(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    16. "Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2."
      Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Kasprzak J.M., Czerwoniec A., Bujnicki J.M., Cremades A., Penafiel R.
      FEBS Open Bio 4:510-521(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    17. "Structure of mammalian ornithine decarboxylase at 1.6-A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases."
      Kern A.D., Oliveira M.A., Coffino P., Hackert M.L.
      Structure 7:567-581(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

    Entry informationi

    Entry nameiDCOR_MOUSE
    AccessioniPrimary (citable) accession number: P00860
    Secondary accession number(s): Q61997, Q61998, Q6PB87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3