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P05455

- LA_HUMAN

UniProt

P05455 - LA_HUMAN

Protein

Lupus La protein

Gene

SSB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation.2 Publications

    GO - Molecular functioni

    1. mRNA binding Source: ProtInc
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. tRNA binding Source: ProtInc

    GO - Biological processi

    1. histone mRNA metabolic process Source: ProtInc
    2. tRNA modification Source: ProtInc

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
    REACT_63. RNA Polymerase III Transcription Termination.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lupus La protein
    Alternative name(s):
    La autoantigen
    La ribonucleoprotein
    Sjoegren syndrome type B antigen
    Short name:
    SS-B
    Gene namesi
    Name:SSB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11316. SSB.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. ribonucleoprotein complex Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Systemic lupus erythematosus

    Organism-specific databases

    PharmGKBiPA36140.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 408408Lupus La proteinPRO_0000207599Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161N6-acetyllysine1 Publication
    Modified residuei128 – 1281N6-acetyllysine1 Publication
    Modified residuei328 – 3281N6-acetyllysine1 Publication
    Modified residuei341 – 3411N6-acetyllysineBy similarity
    Modified residuei360 – 3601N6-acetyllysine1 Publication
    Modified residuei366 – 3661Phosphoserine; by CK28 Publications

    Post-translational modificationi

    Phosphorylated. The phosphorylation sites are at the C-terminal part of the protein.8 Publications
    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05455.
    PaxDbiP05455.
    PeptideAtlasiP05455.
    PRIDEiP05455.

    PTM databases

    PhosphoSiteiP05455.

    Miscellaneous databases

    PMAP-CutDBP05455.

    Expressioni

    Gene expression databases

    ArrayExpressiP05455.
    BgeeiP05455.
    CleanExiHS_SSB.
    GenevestigatoriP05455.

    Organism-specific databases

    HPAiCAB004643.
    HPA012385.
    HPA017287.

    Interactioni

    Subunit structurei

    Interacts with DDX15. May interact with RUFY1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB82EBI-358037,EBI-6927928From a different organism.

    Protein-protein interaction databases

    BioGridi112619. 60 interactions.
    DIPiDIP-29750N.
    IntActiP05455. 23 interactions.
    MINTiMINT-5002383.
    STRINGi9606.ENSP00000260956.

    Structurei

    Secondary structure

    1
    408
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2414
    Turni27 – 293
    Helixi30 – 323
    Helixi34 – 429
    Turni43 – 453
    Beta strandi46 – 483
    Helixi49 – 524
    Helixi56 – 616
    Helixi65 – 739
    Beta strandi80 – 823
    Beta strandi86 – 916
    Helixi102 – 1109
    Beta strandi112 – 1165
    Helixi124 – 1318
    Helixi132 – 1343
    Beta strandi137 – 1448
    Beta strandi146 – 1483
    Beta strandi150 – 16011
    Helixi161 – 1699
    Beta strandi174 – 1774
    Beta strandi181 – 1844
    Turni185 – 1873
    Beta strandi233 – 2397
    Helixi246 – 2527
    Beta strandi259 – 2635
    Beta strandi269 – 2779
    Helixi279 – 28810
    Turni289 – 2913
    Beta strandi298 – 3047
    Helixi308 – 32619

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OWXNMR-A225-334[»]
    1S79NMR-A105-202[»]
    1S7ANMR-A1-103[»]
    1YTYX-ray2.29A/B1-194[»]
    1ZH5X-ray1.85A/B1-194[»]
    2VODX-ray2.10A/B4-194[»]
    2VONX-ray2.10A/B4-194[»]
    2VOOX-ray1.80A/B4-194[»]
    2VOPX-ray2.80A4-194[»]
    DisProtiDP00229.
    ProteinModelPortaliP05455.
    SMRiP05455. Positions 10-188, 225-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05455.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 9993HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 18777RRMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation
    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5193.
    HOGENOMiHOG000006947.
    HOVERGENiHBG001407.
    InParanoidiP05455.
    KOiK11090.
    OMAiSHGEIKW.
    PhylomeDBiP05455.
    TreeFamiTF314476.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.30.70.330. 2 hits.
    InterProiIPR002344. Lupus_La.
    IPR006630. Lupus_La_RNA-bd.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR014886. RRM_3.
    IPR000504. RRM_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF05383. La. 1 hit.
    PF00076. RRM_1. 1 hit.
    PF08777. RRM_3. 1 hit.
    [Graphical view]
    PRINTSiPR00302. LUPUSLA.
    SMARTiSM00715. LA. 1 hit.
    SM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50961. HTH_LA. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05455-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE    50
    IMIKFNRLNR LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV 100
    TDEYKNDVKN RSVYIKGFPT DATLDDIKEW LEDKGQVLNI QMRRTLHKAF 150
    KGSIFVVFDS IESAKKFVET PGQKYKETDL LILFKDDYFA KKNEERKQNK 200
    VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL DDQTCREDLH 250
    ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE 300
    VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS 350
    GKGKVQFQGK KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK 400
    TENGAGDQ 408
    Length:408
    Mass (Da):46,837
    Last modified:July 1, 1989 - v2
    Checksum:iEC153C15F9187FC4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541K → E in AAA36577. (PubMed:2452201)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481P → S.
    Corresponds to variant rs17160793 [ dbSNP | Ensembl ].
    VAR_034066

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13697 mRNA. Translation: CAA31985.1.
    J04205 mRNA. Translation: AAA51885.1.
    BT009862 mRNA. Translation: AAP88864.1.
    AB451228 mRNA. Translation: BAG70042.1.
    AC009967 Genomic DNA. Translation: AAY14868.1.
    CH471058 Genomic DNA. Translation: EAX11258.1.
    CH471058 Genomic DNA. Translation: EAX11259.1.
    BC001289 mRNA. Translation: AAH01289.1.
    BC020818 mRNA. Translation: AAH20818.1.
    M20328 mRNA. Translation: AAA36577.1.
    CCDSiCCDS2237.1.
    PIRiA31888.
    RefSeqiNP_003133.1. NM_003142.4.
    XP_005246868.1. XM_005246811.1.
    UniGeneiHs.632535.

    Genome annotation databases

    EnsembliENST00000260956; ENSP00000260956; ENSG00000138385.
    ENST00000409333; ENSP00000386636; ENSG00000138385.
    GeneIDi6741.
    KEGGihsa:6741.
    UCSCiuc002ufk.3. human.

    Polymorphism databases

    DMDMi125985.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13697 mRNA. Translation: CAA31985.1 .
    J04205 mRNA. Translation: AAA51885.1 .
    BT009862 mRNA. Translation: AAP88864.1 .
    AB451228 mRNA. Translation: BAG70042.1 .
    AC009967 Genomic DNA. Translation: AAY14868.1 .
    CH471058 Genomic DNA. Translation: EAX11258.1 .
    CH471058 Genomic DNA. Translation: EAX11259.1 .
    BC001289 mRNA. Translation: AAH01289.1 .
    BC020818 mRNA. Translation: AAH20818.1 .
    M20328 mRNA. Translation: AAA36577.1 .
    CCDSi CCDS2237.1.
    PIRi A31888.
    RefSeqi NP_003133.1. NM_003142.4.
    XP_005246868.1. XM_005246811.1.
    UniGenei Hs.632535.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OWX NMR - A 225-334 [» ]
    1S79 NMR - A 105-202 [» ]
    1S7A NMR - A 1-103 [» ]
    1YTY X-ray 2.29 A/B 1-194 [» ]
    1ZH5 X-ray 1.85 A/B 1-194 [» ]
    2VOD X-ray 2.10 A/B 4-194 [» ]
    2VON X-ray 2.10 A/B 4-194 [» ]
    2VOO X-ray 1.80 A/B 4-194 [» ]
    2VOP X-ray 2.80 A 4-194 [» ]
    DisProti DP00229.
    ProteinModelPortali P05455.
    SMRi P05455. Positions 10-188, 225-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112619. 60 interactions.
    DIPi DIP-29750N.
    IntActi P05455. 23 interactions.
    MINTi MINT-5002383.
    STRINGi 9606.ENSP00000260956.

    Chemistry

    ChEMBLi CHEMBL2040701.

    PTM databases

    PhosphoSitei P05455.

    Polymorphism databases

    DMDMi 125985.

    Proteomic databases

    MaxQBi P05455.
    PaxDbi P05455.
    PeptideAtlasi P05455.
    PRIDEi P05455.

    Protocols and materials databases

    DNASUi 6741.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260956 ; ENSP00000260956 ; ENSG00000138385 .
    ENST00000409333 ; ENSP00000386636 ; ENSG00000138385 .
    GeneIDi 6741.
    KEGGi hsa:6741.
    UCSCi uc002ufk.3. human.

    Organism-specific databases

    CTDi 6741.
    GeneCardsi GC02P170619.
    HGNCi HGNC:11316. SSB.
    HPAi CAB004643.
    HPA012385.
    HPA017287.
    MIMi 109090. gene.
    neXtProti NX_P05455.
    PharmGKBi PA36140.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5193.
    HOGENOMi HOG000006947.
    HOVERGENi HBG001407.
    InParanoidi P05455.
    KOi K11090.
    OMAi SHGEIKW.
    PhylomeDBi P05455.
    TreeFami TF314476.

    Enzyme and pathway databases

    Reactomei REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
    REACT_63. RNA Polymerase III Transcription Termination.

    Miscellaneous databases

    EvolutionaryTracei P05455.
    GeneWikii Sjogren_syndrome_antigen_B.
    GenomeRNAii 6741.
    NextBioi 26296.
    PMAP-CutDB P05455.
    PROi P05455.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05455.
    Bgeei P05455.
    CleanExi HS_SSB.
    Genevestigatori P05455.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.30.70.330. 2 hits.
    InterProi IPR002344. Lupus_La.
    IPR006630. Lupus_La_RNA-bd.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR014886. RRM_3.
    IPR000504. RRM_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF05383. La. 1 hit.
    PF00076. RRM_1. 1 hit.
    PF08777. RRM_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00302. LUPUSLA.
    SMARTi SM00715. LA. 1 hit.
    SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50961. HTH_LA. 1 hit.
    PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Ribonucleoprotein SS-B/La belongs to a protein family with consensus sequences for RNA-binding."
      Chan E.K.L., Sullivan K.F., Tan E.M.
      Nucleic Acids Res. 17:2233-2244(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genomic structure and amino acid sequence domains of the human La autoantigen."
      Chambers J.C., Kenan D., Martin B.J., Keene J.D.
      J. Biol. Chem. 263:18043-18051(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ROLE IN LUPUS ERYTHEMATOSUS.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Placenta and Skeletal muscle.
    8. "Characteristics and epitope mapping of a cloned human autoantigen La."
      Sturgess A.D., Peterson M.G., McNeilage L.J., Whittingham S., Coppel R.S.
      J. Immunol. 140:3212-3218(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-408.
    9. "Isolation and analysis of cDNA clones expressing human lupus La antigen."
      Chambers J.C., Keene J.D.
      Proc. Natl. Acad. Sci. U.S.A. 82:2115-2119(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-97.
    10. "Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III."
      Gottlieb E., Steitz J.A.
      EMBO J. 8:851-861(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes."
      Fan H., Sakulich A.L., Goodier J.L., Zhang X., Qin J., Maraie R.J.
      Cell 88:707-715(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-366.
    12. "The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a putative DEAH-box RNA helicase."
      Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S., Van Venrooij W.J., Pruijn G.J.M.
      RNA 8:1428-1443(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX15.
    13. Cited for: INTERACTION WITH RUFY1.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "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-116; LYS-128; LYS-328 AND LYS-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element."
      Jacks A., Babon J., Kelly G., Manolaridis I., Cary P.D., Curry S., Conte M.R.
      Structure 11:833-843(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 225-334.
    25. "Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein."
      Alfano C., Sanfelice D., Babon J., Kelly G., Jacks A., Curry S., Conte M.R.
      Nat. Struct. Mol. Biol. 11:323-329(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-202.
    26. "Structural basis for recognition and sequestration of UUU(OH) 3' termini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen."
      Teplova M., Yuan Y.R., Phan A.T., Malinina L., Ilin S., Teplov A., Patel D.J.
      Mol. Cell 21:75-85(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-194.
    27. "Structural analysis reveals conformational plasticity in the recognition of RNA 3' ends by the human La protein."
      Kotik-Kogan O., Valentine E.R., Sanfelice D., Conte M.R., Curry S.
      Structure 16:852-862(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-194.

    Entry informationi

    Entry nameiLA_HUMAN
    AccessioniPrimary (citable) accession number: P05455
    Secondary accession number(s): Q15367, Q53XJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 176 of the entry and version 2 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

    Miscellaneous

    Sera from patients with systemic lupus erythematosus (SLE) often contain antibodies that react with the normal cellular La protein as if this antigen was foreign.

    Keywords - Technical termi

    3D-structure, 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. 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