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Q6UWP7

- LCLT1_HUMAN

UniProt

Q6UWP7 - LCLT1_HUMAN

Protein

Lysocardiolipin acyltransferase 1

Gene

LCLAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages.2 Publications

    Catalytic activityi

    Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

    Kineticsi

    1. KM=39 µM for arachidonoyl-CoA (20:4) for LPIAT activity1 Publication
    2. KM=289 µM for oleoyl-CoA (18:1) for LPIAT activity1 Publication
    3. KM=134 µM for linoleoyl-CoA (18:2) for LPIAT activity1 Publication
    4. KM=34 µM for stearoyl-CoA (18:0) for LPIAT activity1 Publication
    5. KM=53 µM for palmitoyl-CoA (16:0) for LPIAT activity1 Publication
    6. KM=54 µM for oleoyl-CoA (18:1) for LPGAT activity1 Publication
    7. KM=36 µM for linoleoyl-CoA (18:2) for LPGAT activity1 Publication
    8. KM=70 µM for stearoyl-CoA (18:0) for LPGAT activity1 Publication
    9. KM=34 µM for palmitoyl-CoA (16:0) for LPGAT activity1 Publication

    Vmax=3230 nmol/min/mg enzyme toward arachidonoyl-CoA (20:4) for LPIAT activity1 Publication

    Vmax=7489 nmol/min/mg enzyme toward oleoyl-CoA (18:1) for LPIAT activity1 Publication

    Vmax=4696 nmol/min/mg enzyme toward linoleoyl-CoA (18:2) for LPIAT activity1 Publication

    Vmax=1078 nmol/min/mg enzyme toward stearoyl-CoA (18:0) for LPIAT activity1 Publication

    Vmax=11203 nmol/min/mg enzyme toward palmitoyl-CoA (16:0) for LPIAT activity1 Publication

    Vmax=5514 nmol/min/mg enzyme toward oleoyl-CoA (18:1) for LPGAT activity1 Publication

    Vmax=1358 nmol/min/mg enzyme toward linoleoyl-CoA (18:2) for LPGAT activity1 Publication

    Vmax=3530 nmol/min/mg enzyme toward stearoyl-CoA (18:0) for LPGAT activity1 Publication

    Vmax=1673 nmol/min/mg enzyme toward palmitoyl-CoA (16:0) for LPGAT activity1 Publication

    Pathwayi

    GO - Molecular functioni

    1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cardiolipin acyl-chain remodeling Source: Reactome
    2. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
    3. cellular lipid metabolic process Source: Reactome
    4. glycerophospholipid biosynthetic process Source: Reactome
    5. multicellular organismal development Source: UniProtKB-KW
    6. phosphatidic acid biosynthetic process Source: Reactome
    7. phospholipid metabolic process Source: Reactome
    8. small molecule metabolic process Source: Reactome
    9. triglyceride biosynthetic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Developmental protein, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_1190. Triglyceride Biosynthesis.
    REACT_120906. Synthesis of PA.
    REACT_121006. Acyl chain remodeling of CL.
    UniPathwayiUPA00557; UER00613.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysocardiolipin acyltransferase 1 (EC:2.3.1.-, EC:2.3.1.51)
    Alternative name(s):
    1-acylglycerol-3-phosphate O-acyltransferase 8
    Short name:
    1-AGP acyltransferase 8
    Short name:
    1-AGPAT 8
    Acyl-CoA:lysocardiolipin acyltransferase 1
    Gene namesi
    Name:LCLAT1
    Synonyms:AGPAT8, ALCAT1, LYCAT
    ORF Names:UNQ1849/PRO3579
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:26756. LCLAT1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi206 – 2061D → C: Abolishes LPIAT and LPGAT activities. 2 Publications
    Mutagenesisi206 – 2061D → R: Does not increase enzyme activity. 2 Publications
    Mutagenesisi207 – 2071L → T: Abolishes LPIAT activity. No effect on LPGAT activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA164722072.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 414414Lysocardiolipin acyltransferase 1PRO_0000291577Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei221 – 2211N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ6UWP7.
    PaxDbiQ6UWP7.
    PRIDEiQ6UWP7.

    PTM databases

    PhosphoSiteiQ6UWP7.

    Expressioni

    Tissue specificityi

    Expressed at higher level in heart, kidney and pancreas than in brain, spleen, liver, lung, small intestine and placenta.2 Publications

    Gene expression databases

    ArrayExpressiQ6UWP7.
    BgeeiQ6UWP7.
    CleanExiHS_LCLAT1.
    GenevestigatoriQ6UWP7.

    Organism-specific databases

    HPAiHPA031880.
    HPA049217.

    Interactioni

    Protein-protein interaction databases

    BioGridi128972. 3 interactions.
    STRINGi9606.ENSP00000310551.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6UWP7.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei47 – 6721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei86 – 10621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei340 – 36021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei362 – 38221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi123 – 1286HXXXXD motif

    Domaini

    The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0204.
    HOGENOMiHOG000290725.
    HOVERGENiHBG055624.
    InParanoidiQ6UWP7.
    KOiK13513.
    OMAiYREIGHT.
    PhylomeDBiQ6UWP7.
    TreeFamiTF314346.

    Family and domain databases

    InterProiIPR002123. Plipid/glycerol_acylTrfase.
    [Graphical view]
    PfamiPF01553. Acyltransferase. 1 hit.
    [Graphical view]
    SMARTiSM00563. PlsC. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6UWP7-1) [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

    MHSRGREIVV LLNPWSINEA VSSYCTYFIK QDSKSFGIMV SWKGIYFILT    50
    LFWGSFFGSI FMLSPFLPLM FVNPSWYRWI NNRLVATWLT LPVALLETMF 100
    GVKVIITGDA FVPGERSVII MNHRTRMDWM FLWNCLMRYS YLRLEKICLK 150
    ASLKGVPGFG WAMQAAAYIF IHRKWKDDKS HFEDMIDYFC DIHEPLQLLI 200
    FPEGTDLTEN SKSRSNAFAE KNGLQKYEYV LHPRTTGFTF VVDRLREGKN 250
    LDAVHDITVA YPHNIPQSEK HLLQGDFPRE IHFHVHRYPI DTLPTSKEDL 300
    QLWCHKRWEE KEERLRSFYQ GEKNFYFTGQ SVIPPCKSEL RVLVVKLLSI 350
    LYWTLFSPAM CLLIYLYSLV KWYFIITIVI FVLQERIFGG LEIIELACYR 400
    LLHKQPHLNS KKNE 414
    Length:414
    Mass (Da):48,920
    Last modified:July 5, 2004 - v1
    Checksum:iF83A1911CC19F959
    GO
    Isoform 2 (identifier: Q6UWP7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         249-308: KNLDAVHDIT...DLQLWCHKRW → RRQSEGSKGP...SNLQIQCYSH
         309-414: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:308
    Mass (Da):36,045
    Checksum:i6325F89469A35016
    GO
    Isoform 3 (identifier: Q6UWP7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: Missing.

    Show »
    Length:376
    Mass (Da):44,561
    Checksum:iFB658F500239F789
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti290 – 2901I → V.
    Corresponds to variant rs12471868 [ dbSNP | Ensembl ].
    VAR_032830

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3838Missing in isoform 3. 1 PublicationVSP_044307Add
    BLAST
    Alternative sequencei249 – 30860KNLDA…CHKRW → RRQSEGSKGPLQGELQITAQ GNQRGHKQMEKHSMLMDWKN QYREIGHTAQSNLQIQCYSH in isoform 2. 1 PublicationVSP_026181Add
    BLAST
    Alternative sequencei309 – 414106Missing in isoform 2. 1 PublicationVSP_026182Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358702 mRNA. Translation: AAQ89065.1.
    AK095284 mRNA. Translation: BAC04522.1.
    AC073255 Genomic DNA. No translation available.
    AC132154 Genomic DNA. No translation available.
    BC146817 mRNA. Translation: AAI46818.1.
    CCDSiCCDS1772.1. [Q6UWP7-1]
    CCDS42670.1. [Q6UWP7-3]
    RefSeqiNP_001002257.1. NM_001002257.1. [Q6UWP7-3]
    NP_872357.2. NM_182551.3. [Q6UWP7-1]
    XP_005264301.1. XM_005264244.1. [Q6UWP7-1]
    XP_005264302.1. XM_005264245.1. [Q6UWP7-3]
    XP_006712044.1. XM_006711981.1. [Q6UWP7-3]
    UniGeneiHs.468048.
    Hs.662770.

    Genome annotation databases

    EnsembliENST00000309052; ENSP00000310551; ENSG00000172954. [Q6UWP7-1]
    ENST00000319406; ENSP00000368826; ENSG00000172954. [Q6UWP7-2]
    ENST00000379509; ENSP00000368823; ENSG00000172954. [Q6UWP7-3]
    GeneIDi253558.
    KEGGihsa:253558.
    UCSCiuc002rnj.3. human. [Q6UWP7-1]
    uc002rnk.1. human. [Q6UWP7-2]

    Polymorphism databases

    DMDMi74749398.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358702 mRNA. Translation: AAQ89065.1 .
    AK095284 mRNA. Translation: BAC04522.1 .
    AC073255 Genomic DNA. No translation available.
    AC132154 Genomic DNA. No translation available.
    BC146817 mRNA. Translation: AAI46818.1 .
    CCDSi CCDS1772.1. [Q6UWP7-1 ]
    CCDS42670.1. [Q6UWP7-3 ]
    RefSeqi NP_001002257.1. NM_001002257.1. [Q6UWP7-3 ]
    NP_872357.2. NM_182551.3. [Q6UWP7-1 ]
    XP_005264301.1. XM_005264244.1. [Q6UWP7-1 ]
    XP_005264302.1. XM_005264245.1. [Q6UWP7-3 ]
    XP_006712044.1. XM_006711981.1. [Q6UWP7-3 ]
    UniGenei Hs.468048.
    Hs.662770.

    3D structure databases

    ProteinModelPortali Q6UWP7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128972. 3 interactions.
    STRINGi 9606.ENSP00000310551.

    PTM databases

    PhosphoSitei Q6UWP7.

    Polymorphism databases

    DMDMi 74749398.

    Proteomic databases

    MaxQBi Q6UWP7.
    PaxDbi Q6UWP7.
    PRIDEi Q6UWP7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309052 ; ENSP00000310551 ; ENSG00000172954 . [Q6UWP7-1 ]
    ENST00000319406 ; ENSP00000368826 ; ENSG00000172954 . [Q6UWP7-2 ]
    ENST00000379509 ; ENSP00000368823 ; ENSG00000172954 . [Q6UWP7-3 ]
    GeneIDi 253558.
    KEGGi hsa:253558.
    UCSCi uc002rnj.3. human. [Q6UWP7-1 ]
    uc002rnk.1. human. [Q6UWP7-2 ]

    Organism-specific databases

    CTDi 253558.
    GeneCardsi GC02P030670.
    HGNCi HGNC:26756. LCLAT1.
    HPAi HPA031880.
    HPA049217.
    neXtProti NX_Q6UWP7.
    PharmGKBi PA164722072.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0204.
    HOGENOMi HOG000290725.
    HOVERGENi HBG055624.
    InParanoidi Q6UWP7.
    KOi K13513.
    OMAi YREIGHT.
    PhylomeDBi Q6UWP7.
    TreeFami TF314346.

    Enzyme and pathway databases

    UniPathwayi UPA00557 ; UER00613 .
    Reactomei REACT_1190. Triglyceride Biosynthesis.
    REACT_120906. Synthesis of PA.
    REACT_121006. Acyl chain remodeling of CL.

    Miscellaneous databases

    GenomeRNAii 253558.
    NextBioi 92116.
    PROi Q6UWP7.

    Gene expression databases

    ArrayExpressi Q6UWP7.
    Bgeei Q6UWP7.
    CleanExi HS_LCLAT1.
    Genevestigatori Q6UWP7.

    Family and domain databases

    InterProi IPR002123. Plipid/glycerol_acylTrfase.
    [Graphical view ]
    Pfami PF01553. Acyltransferase. 1 hit.
    [Graphical view ]
    SMARTi SM00563. PlsC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 2).
      Tissue: Tongue.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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 3).
    5. "Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity."
      Agarwal A.K., Barnes R.I., Garg A.
      Arch. Biochem. Biophys. 449:64-76(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-206.
    6. "The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids."
      Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.
      J. Lipid Res. 50:945-956(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-206 AND LEU-207.
    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-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLCLT1_HUMAN
    AccessioniPrimary (citable) accession number: Q6UWP7
    Secondary accession number(s): A6H8Z7, Q8N1Q7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 91 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3