Full text data of SSB
SSB
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Lupus La protein (La autoantigen; La ribonucleoprotein; Sjoegren syndrome type B antigen; SS-B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Lupus La protein (La autoantigen; La ribonucleoprotein; Sjoegren syndrome type B antigen; SS-B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P05455
ID LA_HUMAN Reviewed; 408 AA.
AC P05455; Q15367; Q53XJ4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1989, sequence version 2.
DT 22-JAN-2014, entry version 168.
DE RecName: Full=Lupus La protein;
DE AltName: Full=La autoantigen;
DE AltName: Full=La ribonucleoprotein;
DE AltName: Full=Sjoegren syndrome type B antigen;
DE Short=SS-B;
GN Name=SSB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2468131; DOI=10.1093/nar/17.6.2233;
RA Chan E.K.L., Sullivan K.F., Tan E.M.;
RT "Ribonucleoprotein SS-B/La belongs to a protein family with consensus
RT sequences for RNA-binding.";
RL Nucleic Acids Res. 17:2233-2244(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ROLE IN LUPUS
RP ERYTHEMATOSUS.
RX PubMed=3192525;
RA Chambers J.C., Kenan D., Martin B.J., Keene J.D.;
RT "Genomic structure and amino acid sequence domains of the human La
RT autoantigen.";
RL J. Biol. Chem. 263:18043-18051(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-408.
RX PubMed=2452201;
RA Sturgess A.D., Peterson M.G., McNeilage L.J., Whittingham S.,
RA Coppel R.S.;
RT "Characteristics and epitope mapping of a cloned human autoantigen
RT La.";
RL J. Immunol. 140:3212-3218(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-97.
RX PubMed=3856888; DOI=10.1073/pnas.82.7.2115;
RA Chambers J.C., Keene J.D.;
RT "Isolation and analysis of cDNA clones expressing human lupus La
RT antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2115-2119(1985).
RN [10]
RP FUNCTION.
RX PubMed=2470590;
RA Gottlieb E., Steitz J.A.;
RT "Function of the mammalian La protein: evidence for its action in
RT transcription termination by RNA polymerase III.";
RL EMBO J. 8:851-861(1989).
RN [11]
RP PHOSPHORYLATION AT SER-366.
RX PubMed=9054510; DOI=10.1016/S0092-8674(00)81913-3;
RA Fan H., Sakulich A.L., Goodier J.L., Zhang X., Qin J., Maraie R.J.;
RT "Phosphorylation of the human La antigen on serine 366 can regulate
RT recycling of RNA polymerase III transcription complexes.";
RL Cell 88:707-715(1997).
RN [12]
RP INTERACTION WITH DDX15.
RX PubMed=12458796; DOI=10.1017/S1355838202021076;
RA Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S.,
RA Van Venrooij W.J., Pruijn G.J.M.;
RT "The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a
RT putative DEAH-box RNA helicase.";
RL RNA 8:1428-1443(2002).
RN [13]
RP INTERACTION WITH RUFY1.
RX PubMed=14617813; DOI=10.1091/mbc.E03-05-0343;
RA Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
RA van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
RT "Rabip4' is an effector of rab5 and rab4 and regulates transport
RT through early endosomes.";
RL Mol. Biol. Cell 15:611-624(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-328 AND
RP LYS-360, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP STRUCTURE BY NMR OF 225-334.
RX PubMed=12842046; DOI=10.1016/S0969-2126(03)00121-7;
RA Jacks A., Babon J., Kelly G., Manolaridis I., Cary P.D., Curry S.,
RA Conte M.R.;
RT "Structure of the C-terminal domain of human La protein reveals a
RT novel RNA recognition motif coupled to a helical nuclear retention
RT element.";
RL Structure 11:833-843(2003).
RN [25]
RP STRUCTURE BY NMR OF 1-202.
RX PubMed=15004549; DOI=10.1038/nsmb747;
RA Alfano C., Sanfelice D., Babon J., Kelly G., Jacks A., Curry S.,
RA Conte M.R.;
RT "Structural analysis of cooperative RNA binding by the La motif and
RT central RRM domain of human La protein.";
RL Nat. Struct. Mol. Biol. 11:323-329(2004).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-194.
RX PubMed=16387655; DOI=10.1016/j.molcel.2005.10.027;
RA Teplova M., Yuan Y.R., Phan A.T., Malinina L., Ilin S., Teplov A.,
RA Patel D.J.;
RT "Structural basis for recognition and sequestration of UUU(OH) 3'
RT termini of nascent RNA polymerase III transcripts by La, a rheumatic
RT disease autoantigen.";
RL Mol. Cell 21:75-85(2006).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-194.
RX PubMed=18547518; DOI=10.1016/j.str.2008.02.021;
RA Kotik-Kogan O., Valentine E.R., Sanfelice D., Conte M.R., Curry S.;
RT "Structural analysis reveals conformational plasticity in the
RT recognition of RNA 3' ends by the human La protein.";
RL Structure 16:852-862(2008).
CC -!- FUNCTION: Binds to the 3' poly(U) terminii of nascent RNA
CC polymerase III transcripts, protecting them from exonuclease
CC digestion and facilitating their folding and maturation.
CC -!- SUBUNIT: Interacts with DDX15. May interact with RUFY1.
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- PTM: Phosphorylated. The phosphorylation sites are at the C-
CC terminal part of the protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Sera from patients with systemic lupus
CC erythematosus (SLE) often contain antibodies that react with the
CC normal cellular La protein as if this antigen was foreign.
CC -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; X13697; CAA31985.1; -; mRNA.
DR EMBL; J04205; AAA51885.1; -; mRNA.
DR EMBL; BT009862; AAP88864.1; -; mRNA.
DR EMBL; AB451228; BAG70042.1; -; mRNA.
DR EMBL; AC009967; AAY14868.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11258.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11259.1; -; Genomic_DNA.
DR EMBL; BC001289; AAH01289.1; -; mRNA.
DR EMBL; BC020818; AAH20818.1; -; mRNA.
DR EMBL; M20328; AAA36577.1; -; mRNA.
DR PIR; A31888; A31888.
DR RefSeq; NP_003133.1; NM_003142.4.
DR RefSeq; XP_005246868.1; XM_005246811.1.
DR UniGene; Hs.632535; -.
DR PDB; 1OWX; NMR; -; A=225-334.
DR PDB; 1S79; NMR; -; A=105-202.
DR PDB; 1S7A; NMR; -; A=1-103.
DR PDB; 1YTY; X-ray; 2.29 A; A/B=1-194.
DR PDB; 1ZH5; X-ray; 1.85 A; A/B=1-194.
DR PDB; 2VOD; X-ray; 2.10 A; A/B=4-194.
DR PDB; 2VON; X-ray; 2.10 A; A/B=4-194.
DR PDB; 2VOO; X-ray; 1.80 A; A/B=4-194.
DR PDB; 2VOP; X-ray; 2.80 A; A=4-194.
DR PDBsum; 1OWX; -.
DR PDBsum; 1S79; -.
DR PDBsum; 1S7A; -.
DR PDBsum; 1YTY; -.
DR PDBsum; 1ZH5; -.
DR PDBsum; 2VOD; -.
DR PDBsum; 2VON; -.
DR PDBsum; 2VOO; -.
DR PDBsum; 2VOP; -.
DR DisProt; DP00229; -.
DR ProteinModelPortal; P05455; -.
DR SMR; P05455; 10-188, 225-334.
DR DIP; DIP-29750N; -.
DR IntAct; P05455; 20.
DR MINT; MINT-5002383; -.
DR STRING; 9606.ENSP00000260956; -.
DR ChEMBL; CHEMBL2040701; -.
DR PhosphoSite; P05455; -.
DR DMDM; 125985; -.
DR PaxDb; P05455; -.
DR PeptideAtlas; P05455; -.
DR PRIDE; P05455; -.
DR DNASU; 6741; -.
DR Ensembl; ENST00000260956; ENSP00000260956; ENSG00000138385.
DR Ensembl; ENST00000409333; ENSP00000386636; ENSG00000138385.
DR GeneID; 6741; -.
DR KEGG; hsa:6741; -.
DR UCSC; uc002ufk.3; human.
DR CTD; 6741; -.
DR GeneCards; GC02P170619; -.
DR HGNC; HGNC:11316; SSB.
DR HPA; CAB004643; -.
DR HPA; HPA012385; -.
DR HPA; HPA017287; -.
DR MIM; 109090; gene.
DR neXtProt; NX_P05455; -.
DR PharmGKB; PA36140; -.
DR eggNOG; COG5193; -.
DR HOGENOM; HOG000006947; -.
DR HOVERGEN; HBG001407; -.
DR InParanoid; P05455; -.
DR KO; K11090; -.
DR OMA; SHGEIKW; -.
DR PhylomeDB; P05455; -.
DR EvolutionaryTrace; P05455; -.
DR GeneWiki; Sjogren_syndrome_antigen_B; -.
DR GenomeRNAi; 6741; -.
DR NextBio; 26296; -.
DR PMAP-CutDB; P05455; -.
DR PRO; PR:P05455; -.
DR ArrayExpress; P05455; -.
DR Bgee; P05455; -.
DR CleanEx; HS_SSB; -.
DR Genevestigator; P05455; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030529; C:ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; TAS:ProtInc.
DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:ProtInc.
DR GO; GO:0006400; P:tRNA modification; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR006630; Lupus_La_RNA-bd.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR014886; RRM_3.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF05383; La; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF08777; RRM_3; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; RNA-binding;
KW Systemic lupus erythematosus.
FT CHAIN 1 408 Lupus La protein.
FT /FTId=PRO_0000207599.
FT DOMAIN 7 99 HTH La-type RNA-binding.
FT DOMAIN 111 187 RRM.
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 128 128 N6-acetyllysine.
FT MOD_RES 328 328 N6-acetyllysine.
FT MOD_RES 360 360 N6-acetyllysine.
FT MOD_RES 366 366 Phosphoserine; by CK2.
FT VARIANT 48 48 P -> S (in dbSNP:rs17160793).
FT /FTId=VAR_034066.
FT CONFLICT 54 54 K -> E (in Ref. 8; AAA36577).
FT HELIX 11 24
FT TURN 27 29
FT HELIX 30 32
FT HELIX 34 42
FT TURN 43 45
FT STRAND 46 48
FT HELIX 49 52
FT HELIX 56 61
FT HELIX 65 73
FT STRAND 80 82
FT STRAND 86 91
FT HELIX 102 110
FT STRAND 112 116
FT HELIX 124 131
FT HELIX 132 134
FT STRAND 137 144
FT STRAND 146 148
FT STRAND 150 160
FT HELIX 161 169
FT STRAND 174 177
FT STRAND 181 184
FT TURN 185 187
FT STRAND 233 239
FT HELIX 246 252
FT STRAND 259 263
FT STRAND 269 277
FT HELIX 279 288
FT TURN 289 291
FT STRAND 298 304
FT HELIX 308 326
SQ SEQUENCE 408 AA; 46837 MW; EC153C15F9187FC4 CRC64;
MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE IMIKFNRLNR
LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV TDEYKNDVKN RSVYIKGFPT
DATLDDIKEW LEDKGQVLNI QMRRTLHKAF KGSIFVVFDS IESAKKFVET PGQKYKETDL
LILFKDDYFA KKNEERKQNK VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL
DDQTCREDLH ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE
VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS GKGKVQFQGK
KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK TENGAGDQ
//
ID LA_HUMAN Reviewed; 408 AA.
AC P05455; Q15367; Q53XJ4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1989, sequence version 2.
DT 22-JAN-2014, entry version 168.
DE RecName: Full=Lupus La protein;
DE AltName: Full=La autoantigen;
DE AltName: Full=La ribonucleoprotein;
DE AltName: Full=Sjoegren syndrome type B antigen;
DE Short=SS-B;
GN Name=SSB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2468131; DOI=10.1093/nar/17.6.2233;
RA Chan E.K.L., Sullivan K.F., Tan E.M.;
RT "Ribonucleoprotein SS-B/La belongs to a protein family with consensus
RT sequences for RNA-binding.";
RL Nucleic Acids Res. 17:2233-2244(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ROLE IN LUPUS
RP ERYTHEMATOSUS.
RX PubMed=3192525;
RA Chambers J.C., Kenan D., Martin B.J., Keene J.D.;
RT "Genomic structure and amino acid sequence domains of the human La
RT autoantigen.";
RL J. Biol. Chem. 263:18043-18051(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-408.
RX PubMed=2452201;
RA Sturgess A.D., Peterson M.G., McNeilage L.J., Whittingham S.,
RA Coppel R.S.;
RT "Characteristics and epitope mapping of a cloned human autoantigen
RT La.";
RL J. Immunol. 140:3212-3218(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 54-97.
RX PubMed=3856888; DOI=10.1073/pnas.82.7.2115;
RA Chambers J.C., Keene J.D.;
RT "Isolation and analysis of cDNA clones expressing human lupus La
RT antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2115-2119(1985).
RN [10]
RP FUNCTION.
RX PubMed=2470590;
RA Gottlieb E., Steitz J.A.;
RT "Function of the mammalian La protein: evidence for its action in
RT transcription termination by RNA polymerase III.";
RL EMBO J. 8:851-861(1989).
RN [11]
RP PHOSPHORYLATION AT SER-366.
RX PubMed=9054510; DOI=10.1016/S0092-8674(00)81913-3;
RA Fan H., Sakulich A.L., Goodier J.L., Zhang X., Qin J., Maraie R.J.;
RT "Phosphorylation of the human La antigen on serine 366 can regulate
RT recycling of RNA polymerase III transcription complexes.";
RL Cell 88:707-715(1997).
RN [12]
RP INTERACTION WITH DDX15.
RX PubMed=12458796; DOI=10.1017/S1355838202021076;
RA Fouraux M.A., Kolkman M.J.M., Van der Heijden A., De Jong A.S.,
RA Van Venrooij W.J., Pruijn G.J.M.;
RT "The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a
RT putative DEAH-box RNA helicase.";
RL RNA 8:1428-1443(2002).
RN [13]
RP INTERACTION WITH RUFY1.
RX PubMed=14617813; DOI=10.1091/mbc.E03-05-0343;
RA Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J.,
RA van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M.;
RT "Rabip4' is an effector of rab5 and rab4 and regulates transport
RT through early endosomes.";
RL Mol. Biol. Cell 15:611-624(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-328 AND
RP LYS-360, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP STRUCTURE BY NMR OF 225-334.
RX PubMed=12842046; DOI=10.1016/S0969-2126(03)00121-7;
RA Jacks A., Babon J., Kelly G., Manolaridis I., Cary P.D., Curry S.,
RA Conte M.R.;
RT "Structure of the C-terminal domain of human La protein reveals a
RT novel RNA recognition motif coupled to a helical nuclear retention
RT element.";
RL Structure 11:833-843(2003).
RN [25]
RP STRUCTURE BY NMR OF 1-202.
RX PubMed=15004549; DOI=10.1038/nsmb747;
RA Alfano C., Sanfelice D., Babon J., Kelly G., Jacks A., Curry S.,
RA Conte M.R.;
RT "Structural analysis of cooperative RNA binding by the La motif and
RT central RRM domain of human La protein.";
RL Nat. Struct. Mol. Biol. 11:323-329(2004).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-194.
RX PubMed=16387655; DOI=10.1016/j.molcel.2005.10.027;
RA Teplova M., Yuan Y.R., Phan A.T., Malinina L., Ilin S., Teplov A.,
RA Patel D.J.;
RT "Structural basis for recognition and sequestration of UUU(OH) 3'
RT termini of nascent RNA polymerase III transcripts by La, a rheumatic
RT disease autoantigen.";
RL Mol. Cell 21:75-85(2006).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-194.
RX PubMed=18547518; DOI=10.1016/j.str.2008.02.021;
RA Kotik-Kogan O., Valentine E.R., Sanfelice D., Conte M.R., Curry S.;
RT "Structural analysis reveals conformational plasticity in the
RT recognition of RNA 3' ends by the human La protein.";
RL Structure 16:852-862(2008).
CC -!- FUNCTION: Binds to the 3' poly(U) terminii of nascent RNA
CC polymerase III transcripts, protecting them from exonuclease
CC digestion and facilitating their folding and maturation.
CC -!- SUBUNIT: Interacts with DDX15. May interact with RUFY1.
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- PTM: Phosphorylated. The phosphorylation sites are at the C-
CC terminal part of the protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Sera from patients with systemic lupus
CC erythematosus (SLE) often contain antibodies that react with the
CC normal cellular La protein as if this antigen was foreign.
CC -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; X13697; CAA31985.1; -; mRNA.
DR EMBL; J04205; AAA51885.1; -; mRNA.
DR EMBL; BT009862; AAP88864.1; -; mRNA.
DR EMBL; AB451228; BAG70042.1; -; mRNA.
DR EMBL; AC009967; AAY14868.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11258.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11259.1; -; Genomic_DNA.
DR EMBL; BC001289; AAH01289.1; -; mRNA.
DR EMBL; BC020818; AAH20818.1; -; mRNA.
DR EMBL; M20328; AAA36577.1; -; mRNA.
DR PIR; A31888; A31888.
DR RefSeq; NP_003133.1; NM_003142.4.
DR RefSeq; XP_005246868.1; XM_005246811.1.
DR UniGene; Hs.632535; -.
DR PDB; 1OWX; NMR; -; A=225-334.
DR PDB; 1S79; NMR; -; A=105-202.
DR PDB; 1S7A; NMR; -; A=1-103.
DR PDB; 1YTY; X-ray; 2.29 A; A/B=1-194.
DR PDB; 1ZH5; X-ray; 1.85 A; A/B=1-194.
DR PDB; 2VOD; X-ray; 2.10 A; A/B=4-194.
DR PDB; 2VON; X-ray; 2.10 A; A/B=4-194.
DR PDB; 2VOO; X-ray; 1.80 A; A/B=4-194.
DR PDB; 2VOP; X-ray; 2.80 A; A=4-194.
DR PDBsum; 1OWX; -.
DR PDBsum; 1S79; -.
DR PDBsum; 1S7A; -.
DR PDBsum; 1YTY; -.
DR PDBsum; 1ZH5; -.
DR PDBsum; 2VOD; -.
DR PDBsum; 2VON; -.
DR PDBsum; 2VOO; -.
DR PDBsum; 2VOP; -.
DR DisProt; DP00229; -.
DR ProteinModelPortal; P05455; -.
DR SMR; P05455; 10-188, 225-334.
DR DIP; DIP-29750N; -.
DR IntAct; P05455; 20.
DR MINT; MINT-5002383; -.
DR STRING; 9606.ENSP00000260956; -.
DR ChEMBL; CHEMBL2040701; -.
DR PhosphoSite; P05455; -.
DR DMDM; 125985; -.
DR PaxDb; P05455; -.
DR PeptideAtlas; P05455; -.
DR PRIDE; P05455; -.
DR DNASU; 6741; -.
DR Ensembl; ENST00000260956; ENSP00000260956; ENSG00000138385.
DR Ensembl; ENST00000409333; ENSP00000386636; ENSG00000138385.
DR GeneID; 6741; -.
DR KEGG; hsa:6741; -.
DR UCSC; uc002ufk.3; human.
DR CTD; 6741; -.
DR GeneCards; GC02P170619; -.
DR HGNC; HGNC:11316; SSB.
DR HPA; CAB004643; -.
DR HPA; HPA012385; -.
DR HPA; HPA017287; -.
DR MIM; 109090; gene.
DR neXtProt; NX_P05455; -.
DR PharmGKB; PA36140; -.
DR eggNOG; COG5193; -.
DR HOGENOM; HOG000006947; -.
DR HOVERGEN; HBG001407; -.
DR InParanoid; P05455; -.
DR KO; K11090; -.
DR OMA; SHGEIKW; -.
DR PhylomeDB; P05455; -.
DR EvolutionaryTrace; P05455; -.
DR GeneWiki; Sjogren_syndrome_antigen_B; -.
DR GenomeRNAi; 6741; -.
DR NextBio; 26296; -.
DR PMAP-CutDB; P05455; -.
DR PRO; PR:P05455; -.
DR ArrayExpress; P05455; -.
DR Bgee; P05455; -.
DR CleanEx; HS_SSB; -.
DR Genevestigator; P05455; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030529; C:ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0003729; F:mRNA binding; TAS:ProtInc.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; TAS:ProtInc.
DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:ProtInc.
DR GO; GO:0006400; P:tRNA modification; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR006630; Lupus_La_RNA-bd.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR014886; RRM_3.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF05383; La; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF08777; RRM_3; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; RNA-binding;
KW Systemic lupus erythematosus.
FT CHAIN 1 408 Lupus La protein.
FT /FTId=PRO_0000207599.
FT DOMAIN 7 99 HTH La-type RNA-binding.
FT DOMAIN 111 187 RRM.
FT MOD_RES 116 116 N6-acetyllysine.
FT MOD_RES 128 128 N6-acetyllysine.
FT MOD_RES 328 328 N6-acetyllysine.
FT MOD_RES 360 360 N6-acetyllysine.
FT MOD_RES 366 366 Phosphoserine; by CK2.
FT VARIANT 48 48 P -> S (in dbSNP:rs17160793).
FT /FTId=VAR_034066.
FT CONFLICT 54 54 K -> E (in Ref. 8; AAA36577).
FT HELIX 11 24
FT TURN 27 29
FT HELIX 30 32
FT HELIX 34 42
FT TURN 43 45
FT STRAND 46 48
FT HELIX 49 52
FT HELIX 56 61
FT HELIX 65 73
FT STRAND 80 82
FT STRAND 86 91
FT HELIX 102 110
FT STRAND 112 116
FT HELIX 124 131
FT HELIX 132 134
FT STRAND 137 144
FT STRAND 146 148
FT STRAND 150 160
FT HELIX 161 169
FT STRAND 174 177
FT STRAND 181 184
FT TURN 185 187
FT STRAND 233 239
FT HELIX 246 252
FT STRAND 259 263
FT STRAND 269 277
FT HELIX 279 288
FT TURN 289 291
FT STRAND 298 304
FT HELIX 308 326
SQ SEQUENCE 408 AA; 46837 MW; EC153C15F9187FC4 CRC64;
MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE IMIKFNRLNR
LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV TDEYKNDVKN RSVYIKGFPT
DATLDDIKEW LEDKGQVLNI QMRRTLHKAF KGSIFVVFDS IESAKKFVET PGQKYKETDL
LILFKDDYFA KKNEERKQNK VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL
DDQTCREDLH ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE
VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS GKGKVQFQGK
KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK TENGAGDQ
//
MIM
109090
*RECORD*
*FIELD* NO
109090
*FIELD* TI
*109090 SJOGREN SYNDROME ANTIGEN B; SSB
;;AUTOANTIGEN La;;
La RIBONUCLEOPROTEIN DOMAIN FAMILY, MEMBER 3; LARP3
read more*FIELD* TX
DESCRIPTION
La is involved in diverse aspects of RNA metabolism, including binding
and protecting 3-prime UUU(OH) elements of newly RNA polymerase III (see
606007)-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA
precursors, acting as an RNA chaperone, and binding viral RNAs
associated with hepatitis C virus. La protein was originally defined by
its reactivity with autoantibodies from patients with Sjogren syndrome
(270150) and systemic lupus erythematosus (SLE; 152700) (Teplova et al.,
2006).
CLONING
Chambers et al. (1988) determined the amino acid sequence of the La
protein. The cDNA sequence encodes a protein of 408 amino acids. By
immunoprecipitation and immunoblotting, it appears to be a single
phosphoprotein of 46 to 50 kD. Chambers et al. (1988) also identified at
least 3 antigenic epitopes on the La protein and predicted regions of
the protein involved in RNA binding based on structural similarities
with other RNA-binding proteins. See Bini et al. (1990).
Grolz and Bachmann (1997) stated that there are 3 La pseudogenes. They
also found that alternative splicing gives rise to 3 different mRNAs,
all of which were expressed in all tissues tested, and all of which were
translated into nuclear La protein in transfected mouse cells.
GENE FUNCTION
Histone mRNA is destabilized at the end of S phase and in cell-free mRNA
decay reaction mixtures supplemented with histone proteins, indicating
that histones might autoregulate the histone mRNA half-life. Histone
mRNA destabilization in vitro requires 3 components: polysomes,
histones, and postpolysomal supernatant (S130). Polysomes are the source
of the mRNA and mRNA-degrading enzymes. To investigate the role of the
S130 in autoregulation, McLaren et al. (1997) fractionated crude S130 by
histone-agarose affinity chromatography. They detected 2 separate
activities affecting the histone mRNA half-life. The
histone-agarose-bound fraction contained a histone mRNA destabilizer
that was activated by histone proteins; the unbound fraction contained a
histone mRNA stabilizer. The authors performed further chromatographic
fractionation of the unbound material, which revealed only a single,
approximately 52-kD stabilizer protein. McLaren et al. (1997) purified
this stabilizer to homogeneity, partially sequenced it, and identified
it as La. Addition of purified La to reaction mixtures containing
polysomes resulted in the stabilization of a histone mRNA decay
intermediate. This intermediate corresponded to histone mRNA lacking 12
nucleotides from its 3-prime end and containing an intact coding region.
Anti-La antibody blocked the stabilization effect. La had little or no
effect on several other cell cycle-regulated mRNAs. McLaren et al.
(1997) suggested that La prolongs the histone mRNA half-life during S
phase and thereby increases histone protein production.
Conversion of a nascent precursor tRNA to a mature functional species is
a multipartite process that involves the sequential actions of several
processing and modifying enzymes. La is the first protein to interact
with pre-tRNAs in eukaryotes. Intine et al. (2000) used an opal
suppressor tRNA as a functional probe to examine the activities of yeast
and human La proteins in this process in fission yeast. They found that
an RNA recognition motif and Walker motif in the metazoan-specific
C-terminal domain of human La maintain pre-tRNA in an unprocessed state
by blocking the 5-prime-processing site, impeding an early step in the
pathway. Faithful phosphorylation of human La on ser366 reverses this
block and promotes tRNA maturation. The results suggested that
regulation of tRNA maturation at the level of RNase P cleavage may occur
via phosphorylation of ser366 of human La.
BIOCHEMICAL FEATURES
Teplova et al. (2006) reported the 1.85-angstrom crystal structure of
the La N-terminal domain bound to a synthetic RNA with a UUU(OH) 3-prime
end.
GENE STRUCTURE
Chambers et al. (1988) determined that the La gene contains 11 exons.
MAPPING
By in situ hybridization and by screening a chromosome-specific library,
Chambers et al. (1988) mapped the SSB gene to chromosome 2.
*FIELD* RF
1. Bini, P.; Chu, J.-L.; Okolo, C.; Elkon, K.: Analysis of autoantibodies
to recombinant La (SS-B) peptides in systemic lupus erythematosus
and primary Sjogren's syndrome. J. Clin. Invest. 85: 325-333, 1990.
2. Chambers, J. C.; Kenan, D.; Martin, B. J.; Keene, J. D.: Genomic
structure and amino acid sequence domains of the human La autoantigen. J.
Biol. Chem. 263: 18043-18051, 1988.
3. Grolz, D.; Bachmann, M.: The nuclear autoantigen La/SS-associated
antigen B: one gene, three functional mRNAs. Biochem. J. 323: 151-158,
1997.
4. Intine, R. V. A.; Sakulich, A. L.; Koduru, S. B.; Huang, Y.; Pierstorff,
E.; Goodier, J. L.; Phan, L.; Maraia, R. J.: Control of transfer
RNA maturation by phosphorylation of the human La antigen on serine
366. Molec. Cell 6: 339-348, 2000.
5. McLaren, R. S.; Caruccio, N.; Ross, J.: Human La protein: a stabilizer
of histone mRNA. Molec. Cell. Biol. 17: 3028-3036, 1997.
6. Teplova, M.; Yuan, Y.-R.; Phan, A. T.; Malinina, L.; Ilin, S.;
Teplov, A.; Patel, D. J.: Structural basis for recognition and sequestration
of UUU(OH) 3-prime temini (sic) of nascent RNA polymerase III transcripts
by La, a rheumatic disease autoantigen. Molec. Cell 21: 75-85, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 2/9/2006
Stylianos E. Antonarakis - updated: 9/8/2000
Patti M. Sherman - updated: 6/1/2000
Rebekah S. Rasooly - updated: 4/10/1998
*FIELD* CD
Victor A. McKusick: 12/12/1989
*FIELD* ED
carol: 08/06/2007
mgross: 2/27/2006
terry: 2/9/2006
mgross: 9/8/2000
mcapotos: 6/21/2000
psherman: 6/1/2000
alopez: 4/10/1998
supermim: 3/16/1992
carol: 1/30/1991
carol: 9/7/1990
carol: 5/1/1990
supermim: 3/20/1990
supermim: 3/1/1990
*RECORD*
*FIELD* NO
109090
*FIELD* TI
*109090 SJOGREN SYNDROME ANTIGEN B; SSB
;;AUTOANTIGEN La;;
La RIBONUCLEOPROTEIN DOMAIN FAMILY, MEMBER 3; LARP3
read more*FIELD* TX
DESCRIPTION
La is involved in diverse aspects of RNA metabolism, including binding
and protecting 3-prime UUU(OH) elements of newly RNA polymerase III (see
606007)-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA
precursors, acting as an RNA chaperone, and binding viral RNAs
associated with hepatitis C virus. La protein was originally defined by
its reactivity with autoantibodies from patients with Sjogren syndrome
(270150) and systemic lupus erythematosus (SLE; 152700) (Teplova et al.,
2006).
CLONING
Chambers et al. (1988) determined the amino acid sequence of the La
protein. The cDNA sequence encodes a protein of 408 amino acids. By
immunoprecipitation and immunoblotting, it appears to be a single
phosphoprotein of 46 to 50 kD. Chambers et al. (1988) also identified at
least 3 antigenic epitopes on the La protein and predicted regions of
the protein involved in RNA binding based on structural similarities
with other RNA-binding proteins. See Bini et al. (1990).
Grolz and Bachmann (1997) stated that there are 3 La pseudogenes. They
also found that alternative splicing gives rise to 3 different mRNAs,
all of which were expressed in all tissues tested, and all of which were
translated into nuclear La protein in transfected mouse cells.
GENE FUNCTION
Histone mRNA is destabilized at the end of S phase and in cell-free mRNA
decay reaction mixtures supplemented with histone proteins, indicating
that histones might autoregulate the histone mRNA half-life. Histone
mRNA destabilization in vitro requires 3 components: polysomes,
histones, and postpolysomal supernatant (S130). Polysomes are the source
of the mRNA and mRNA-degrading enzymes. To investigate the role of the
S130 in autoregulation, McLaren et al. (1997) fractionated crude S130 by
histone-agarose affinity chromatography. They detected 2 separate
activities affecting the histone mRNA half-life. The
histone-agarose-bound fraction contained a histone mRNA destabilizer
that was activated by histone proteins; the unbound fraction contained a
histone mRNA stabilizer. The authors performed further chromatographic
fractionation of the unbound material, which revealed only a single,
approximately 52-kD stabilizer protein. McLaren et al. (1997) purified
this stabilizer to homogeneity, partially sequenced it, and identified
it as La. Addition of purified La to reaction mixtures containing
polysomes resulted in the stabilization of a histone mRNA decay
intermediate. This intermediate corresponded to histone mRNA lacking 12
nucleotides from its 3-prime end and containing an intact coding region.
Anti-La antibody blocked the stabilization effect. La had little or no
effect on several other cell cycle-regulated mRNAs. McLaren et al.
(1997) suggested that La prolongs the histone mRNA half-life during S
phase and thereby increases histone protein production.
Conversion of a nascent precursor tRNA to a mature functional species is
a multipartite process that involves the sequential actions of several
processing and modifying enzymes. La is the first protein to interact
with pre-tRNAs in eukaryotes. Intine et al. (2000) used an opal
suppressor tRNA as a functional probe to examine the activities of yeast
and human La proteins in this process in fission yeast. They found that
an RNA recognition motif and Walker motif in the metazoan-specific
C-terminal domain of human La maintain pre-tRNA in an unprocessed state
by blocking the 5-prime-processing site, impeding an early step in the
pathway. Faithful phosphorylation of human La on ser366 reverses this
block and promotes tRNA maturation. The results suggested that
regulation of tRNA maturation at the level of RNase P cleavage may occur
via phosphorylation of ser366 of human La.
BIOCHEMICAL FEATURES
Teplova et al. (2006) reported the 1.85-angstrom crystal structure of
the La N-terminal domain bound to a synthetic RNA with a UUU(OH) 3-prime
end.
GENE STRUCTURE
Chambers et al. (1988) determined that the La gene contains 11 exons.
MAPPING
By in situ hybridization and by screening a chromosome-specific library,
Chambers et al. (1988) mapped the SSB gene to chromosome 2.
*FIELD* RF
1. Bini, P.; Chu, J.-L.; Okolo, C.; Elkon, K.: Analysis of autoantibodies
to recombinant La (SS-B) peptides in systemic lupus erythematosus
and primary Sjogren's syndrome. J. Clin. Invest. 85: 325-333, 1990.
2. Chambers, J. C.; Kenan, D.; Martin, B. J.; Keene, J. D.: Genomic
structure and amino acid sequence domains of the human La autoantigen. J.
Biol. Chem. 263: 18043-18051, 1988.
3. Grolz, D.; Bachmann, M.: The nuclear autoantigen La/SS-associated
antigen B: one gene, three functional mRNAs. Biochem. J. 323: 151-158,
1997.
4. Intine, R. V. A.; Sakulich, A. L.; Koduru, S. B.; Huang, Y.; Pierstorff,
E.; Goodier, J. L.; Phan, L.; Maraia, R. J.: Control of transfer
RNA maturation by phosphorylation of the human La antigen on serine
366. Molec. Cell 6: 339-348, 2000.
5. McLaren, R. S.; Caruccio, N.; Ross, J.: Human La protein: a stabilizer
of histone mRNA. Molec. Cell. Biol. 17: 3028-3036, 1997.
6. Teplova, M.; Yuan, Y.-R.; Phan, A. T.; Malinina, L.; Ilin, S.;
Teplov, A.; Patel, D. J.: Structural basis for recognition and sequestration
of UUU(OH) 3-prime temini (sic) of nascent RNA polymerase III transcripts
by La, a rheumatic disease autoantigen. Molec. Cell 21: 75-85, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 2/9/2006
Stylianos E. Antonarakis - updated: 9/8/2000
Patti M. Sherman - updated: 6/1/2000
Rebekah S. Rasooly - updated: 4/10/1998
*FIELD* CD
Victor A. McKusick: 12/12/1989
*FIELD* ED
carol: 08/06/2007
mgross: 2/27/2006
terry: 2/9/2006
mgross: 9/8/2000
mcapotos: 6/21/2000
psherman: 6/1/2000
alopez: 4/10/1998
supermim: 3/16/1992
carol: 1/30/1991
carol: 9/7/1990
carol: 5/1/1990
supermim: 3/20/1990
supermim: 3/1/1990