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Q8CHT0

- AL4A1_MOUSE

UniProt

Q8CHT0 - AL4A1_MOUSE

Protein

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Gene

Aldh4a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes By similarity.By similarity

    Catalytic activityi

    L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei207 – 2071NAD
    Sitei210 – 2101Transition state stabilizerBy similarity
    Binding sitei232 – 2321NAD
    Active sitei313 – 3131Proton acceptor1 PublicationPROSITE-ProRule annotation
    Active sitei347 – 3471Nucleophile1 PublicationPROSITE-ProRule annotation
    Binding sitei446 – 4461NAD
    Binding sitei512 – 5121Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi285 – 2895NAD

    GO - Molecular functioni

    1. 1-pyrroline-5-carboxylate dehydrogenase activity Source: Ensembl
    2. oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: InterPro

    GO - Biological processi

    1. proline biosynthetic process Source: InterPro
    2. proline catabolic process to glutamate Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Proline metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00261; UER00374.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC:1.2.1.88)
    Short name:
    P5C dehydrogenase
    Alternative name(s):
    Aldehyde dehydrogenase family 4 member A1
    L-glutamate gamma-semialdehyde dehydrogenase
    Gene namesi
    Name:Aldh4a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2443883. Aldh4a1.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2323MitochondrionBy similarityAdd
    BLAST
    Chaini24 – 562539Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialPRO_0000007174Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301N6-succinyllysine1 Publication
    Modified residuei51 – 511N6-acetyllysine1 Publication
    Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
    Modified residuei92 – 921N6-succinyllysine; alternate1 Publication
    Modified residuei98 – 981N6-acetyllysine; alternate1 Publication
    Modified residuei98 – 981N6-succinyllysine; alternate1 Publication
    Modified residuei113 – 1131N6-acetyllysine; alternate1 Publication
    Modified residuei113 – 1131N6-succinyllysine; alternate1 Publication
    Modified residuei129 – 1291N6-acetyllysine; alternate1 Publication
    Modified residuei129 – 1291N6-succinyllysine; alternate1 Publication
    Modified residuei174 – 1741N6-acetyllysine; alternate1 Publication
    Modified residuei174 – 1741N6-succinyllysine; alternate1 Publication
    Modified residuei317 – 3171N6-acetyllysine1 Publication
    Modified residuei346 – 3461N6-succinyllysine1 Publication
    Modified residuei357 – 3571N6-acetyllysine; alternate1 Publication
    Modified residuei357 – 3571N6-succinyllysine; alternate1 Publication
    Modified residuei364 – 3641N6-acetyllysine1 Publication
    Modified residuei375 – 3751N6-acetyllysine1 Publication
    Modified residuei394 – 3941N6-succinyllysine1 Publication
    Modified residuei461 – 4611N6-acetyllysine1 Publication
    Modified residuei508 – 5081N6-acetyllysine; alternate1 Publication
    Modified residuei508 – 5081N6-succinyllysine; alternate1 Publication
    Modified residuei530 – 5301N6-acetyllysine1 Publication
    Modified residuei551 – 5511N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8CHT0.
    PaxDbiQ8CHT0.
    PRIDEiQ8CHT0.

    PTM databases

    PhosphoSiteiQ8CHT0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8CHT0.
    BgeeiQ8CHT0.
    CleanExiMM_ALDH4A1.
    GenevestigatoriQ8CHT0.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiQ8CHT0. 3 interactions.
    MINTiMINT-1859863.

    Structurei

    Secondary structure

    1
    562
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 5411
    Turni55 – 584
    Beta strandi65 – 673
    Beta strandi70 – 723
    Beta strandi77 – 826
    Beta strandi85 – 9410
    Helixi98 – 11720
    Helixi120 – 13516
    Turni136 – 1383
    Helixi139 – 15012
    Helixi154 – 1607
    Helixi163 – 17917
    Beta strandi190 – 1956
    Beta strandi200 – 2067
    Helixi212 – 22413
    Beta strandi229 – 2324
    Helixi235 – 2373
    Helixi238 – 25013
    Beta strandi257 – 2604
    Helixi265 – 2728
    Beta strandi278 – 2858
    Helixi287 – 29913
    Turni300 – 3034
    Beta strandi309 – 3135
    Beta strandi318 – 3225
    Helixi328 – 34013
    Helixi341 – 3444
    Beta strandi350 – 3567
    Helixi357 – 3593
    Helixi360 – 37213
    Turni379 – 3813
    Helixi393 – 40816
    Beta strandi412 – 4165
    Beta strandi423 – 4253
    Beta strandi431 – 4366
    Helixi441 – 4433
    Beta strandi449 – 4579
    Helixi459 – 4613
    Helixi462 – 47110
    Beta strandi472 – 48211
    Helixi486 – 49510
    Turni496 – 4994
    Beta strandi501 – 5077
    Turni514 – 5163
    Helixi536 – 5405
    Beta strandi544 – 5496
    Helixi559 – 5613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3V9JX-ray1.30A/B21-562[»]
    3V9KX-ray1.50A/B21-562[»]
    3V9LX-ray1.50A/B21-562[»]
    4E3XX-ray1.24A/B21-562[»]
    4LGZX-ray1.68A/B21-562[»]
    4LH0X-ray1.67A/B21-562[»]
    4LH1X-ray1.67A/B21-562[»]
    4LH2X-ray1.67A/B21-562[»]
    4LH3X-ray1.81A/B21-562[»]
    ProteinModelPortaliQ8CHT0.
    SMRiQ8CHT0. Positions 21-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    GeneTreeiENSGT00560000077335.
    HOGENOMiHOG000271511.
    HOVERGENiHBG050484.
    InParanoidiB1AXW8.
    KOiK00294.
    OMAiLRWKHTS.
    OrthoDBiEOG7T1R9D.
    TreeFamiTF300481.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR005931. P5CDH/ALDH4A1.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8CHT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPLPSLRRS LLSHAWRGAG LRWKHTSSLK VTNEPILAFS QGSPERDALQ    50
    KALKDLKGQM EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL 100
    LNRAIDAALA ARKEWDLKPM ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ 150
    GKTVIQAEID AAAELIDFFR FNAKFAVELE GEQPISVPPS TNHTVYRGLE 200
    GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA SYAVYRILRE 250
    AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN 300
    LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC 350
    SRLYVPKSLW PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK 400
    KWLEHARSSP SLSILAGGQC NESVGYYVEP CIIESKDPQE PIMKEEIFGP 450
    VLTVYVYPDD KYRETLQLVD STTSYGLTGA VFAQDKAIVQ EATRMLRNAA 500
    GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW TSPQVIKETH 550
    KPLGDWRYSY MQ 562
    Length:562
    Mass (Da):61,841
    Last modified:July 27, 2011 - v3
    Checksum:i4D8A0C9C68A99478
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181G → S in BAC32045. (PubMed:16141072)Curated
    Sequence conflicti18 – 181G → S in AAH56226. (PubMed:15489334)Curated
    Sequence conflicti18 – 181G → S in AAH39281. (PubMed:15489334)Curated
    Sequence conflicti18 – 181G → S in AAH24133. (PubMed:15489334)Curated
    Sequence conflicti32 – 321T → A in BAC32045. (PubMed:16141072)Curated
    Sequence conflicti32 – 321T → A in AAH56226. (PubMed:15489334)Curated
    Sequence conflicti32 – 321T → A in AAH39281. (PubMed:15489334)Curated
    Sequence conflicti32 – 321T → A in AAH24133. (PubMed:15489334)Curated
    Sequence conflicti47 – 471D → G in BAC32045. (PubMed:16141072)Curated
    Sequence conflicti60 – 601M → T in BAC32045. (PubMed:16141072)Curated
    Sequence conflicti60 – 601M → T in AAH56226. (PubMed:15489334)Curated
    Sequence conflicti60 – 601M → T in AAH39281. (PubMed:15489334)Curated
    Sequence conflicti60 – 601M → T in AAH24133. (PubMed:15489334)Curated
    Sequence conflicti467 – 4671Q → K in BAC32045. (PubMed:16141072)Curated
    Sequence conflicti467 – 4671Q → K in AAH56226. (PubMed:15489334)Curated
    Sequence conflicti467 – 4671Q → K in AAH39281. (PubMed:15489334)Curated
    Sequence conflicti467 – 4671Q → K in AAH24133. (PubMed:15489334)Curated
    Sequence conflicti467 – 4671Q → K in AAH26589. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK044712 mRNA. Translation: BAC32045.1.
    AL831790 Genomic DNA. Translation: CAM21310.1.
    CH466615 Genomic DNA. Translation: EDL13315.1.
    BC024133 mRNA. Translation: AAH24133.1.
    BC026589 mRNA. Translation: AAH26589.1.
    BC039281 mRNA. Translation: AAH39281.2.
    BC056226 mRNA. Translation: AAH56226.1.
    CCDSiCCDS18848.1.
    RefSeqiNP_780647.3. NM_175438.4.
    UniGeneiMm.273571.

    Genome annotation databases

    EnsembliENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737.
    GeneIDi212647.
    KEGGimmu:212647.
    UCSCiuc012dnu.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK044712 mRNA. Translation: BAC32045.1 .
    AL831790 Genomic DNA. Translation: CAM21310.1 .
    CH466615 Genomic DNA. Translation: EDL13315.1 .
    BC024133 mRNA. Translation: AAH24133.1 .
    BC026589 mRNA. Translation: AAH26589.1 .
    BC039281 mRNA. Translation: AAH39281.2 .
    BC056226 mRNA. Translation: AAH56226.1 .
    CCDSi CCDS18848.1.
    RefSeqi NP_780647.3. NM_175438.4.
    UniGenei Mm.273571.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3V9J X-ray 1.30 A/B 21-562 [» ]
    3V9K X-ray 1.50 A/B 21-562 [» ]
    3V9L X-ray 1.50 A/B 21-562 [» ]
    4E3X X-ray 1.24 A/B 21-562 [» ]
    4LGZ X-ray 1.68 A/B 21-562 [» ]
    4LH0 X-ray 1.67 A/B 21-562 [» ]
    4LH1 X-ray 1.67 A/B 21-562 [» ]
    4LH2 X-ray 1.67 A/B 21-562 [» ]
    4LH3 X-ray 1.81 A/B 21-562 [» ]
    ProteinModelPortali Q8CHT0.
    SMRi Q8CHT0. Positions 21-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8CHT0. 3 interactions.
    MINTi MINT-1859863.

    PTM databases

    PhosphoSitei Q8CHT0.

    Proteomic databases

    MaxQBi Q8CHT0.
    PaxDbi Q8CHT0.
    PRIDEi Q8CHT0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000039818 ; ENSMUSP00000043821 ; ENSMUSG00000028737 .
    GeneIDi 212647.
    KEGGi mmu:212647.
    UCSCi uc012dnu.1. mouse.

    Organism-specific databases

    CTDi 8659.
    MGIi MGI:2443883. Aldh4a1.

    Phylogenomic databases

    eggNOGi COG1012.
    GeneTreei ENSGT00560000077335.
    HOGENOMi HOG000271511.
    HOVERGENi HBG050484.
    InParanoidi B1AXW8.
    KOi K00294.
    OMAi LRWKHTS.
    OrthoDBi EOG7T1R9D.
    TreeFami TF300481.

    Enzyme and pathway databases

    UniPathwayi UPA00261 ; UER00374 .

    Miscellaneous databases

    ChiTaRSi ALDH4A1. mouse.
    NextBioi 373656.
    PROi Q8CHT0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CHT0.
    Bgeei Q8CHT0.
    CleanExi MM_ALDH4A1.
    Genevestigatori Q8CHT0.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR005931. P5CDH/ALDH4A1.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR01236. D1pyr5carbox1. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Retina.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. 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].
    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].
      Strain: FVB/N.
      Tissue: Kidney and Liver.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-346; LYS-357; LYS-394 AND LYS-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-317; LYS-357; LYS-364; LYS-375; LYS-461; LYS-508; LYS-530 AND LYS-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Proline: Mother Nature's cryoprotectant applied to protein crystallography."
      Pemberton T.A., Still B.R., Christensen E.M., Singh H., Srivastava D., Tanner J.J.
      Acta Crystallogr. D 68:1010-1018(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 21-562.
    8. "The three-dimensional structural basis of type II hyperprolinemia."
      Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F., Tanner J.J.
      J. Mol. Biol. 420:176-189(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-562 IN COMPLEXES WITH GLUTAMATE AND NAD, SUBUNIT, ACTIVE SITE.

    Entry informationi

    Entry nameiAL4A1_MOUSE
    AccessioniPrimary (citable) accession number: Q8CHT0
    Secondary accession number(s): B1AXW8
    , Q7TND0, Q8BXM3, Q8R0N1, Q8R1S2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 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