LA_HUMAN
ID LA_HUMAN Reviewed; 408 AA.
AC P05455; Q15367; Q53XJ4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 240.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 ERYTHEMATOSUS.
RX PubMed=3192525; DOI=10.1016/s0021-9258(19)81321-2;
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 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., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT 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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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., Coppel R.S.;
RT "Characteristics and epitope mapping of a cloned human autoantigen 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 antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2115-2119(1985).
RN [10]
RP FUNCTION.
RX PubMed=2470590; DOI=10.1002/j.1460-2075.1989.tb03446.x;
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 putative
RT DEAH-box RNA helicase.";
RL RNA 8:1428-1443(2002).
RN [13]
RP FUNCTION.
RX PubMed=12384597; DOI=10.1093/nar/gkf583;
RA Ray P.S., Das S.;
RT "La autoantigen is required for the internal ribosome entry site-mediated
RT translation of Coxsackievirus B3 RNA.";
RL Nucleic Acids Res. 30:4500-4508(2002).
RN [14]
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 through
RT early endosomes.";
RL Mol. Biol. Cell 15:611-624(2004).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [19]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-328 AND
RP LYS-360, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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., Buerckstuemmer T.,
RA 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-94; THR-120; SER-225
RP AND SER-366, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
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 novel RNA
RT recognition motif coupled to a helical nuclear retention element.";
RL Structure 11:833-843(2003).
RN [28]
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 central
RT RRM domain of human La protein.";
RL Nat. Struct. Mol. Biol. 11:323-329(2004).
RN [29]
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' termini
RT of nascent RNA polymerase III transcripts by La, a rheumatic disease
RT autoantigen.";
RL Mol. Cell 21:75-85(2006).
RN [30]
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 recognition
RT of RNA 3' ends by the human La protein.";
RL Structure 16:852-862(2008).
CC -!- FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase
CC III transcripts, protecting them from exonuclease digestion and
CC facilitating their folding and maturation (PubMed:3192525,
CC PubMed:2470590). In case of Coxsackievirus B3 infection, binds to the
CC viral internal ribosome entry site (IRES) and stimulates the IRES-
CC mediated translation (PubMed:12384597). {ECO:0000269|PubMed:12384597,
CC ECO:0000269|PubMed:2470590, ECO:0000269|PubMed:3192525}.
CC -!- SUBUNIT: Interacts with DDX15. May interact with RUFY1.
CC {ECO:0000269|PubMed:12458796, ECO:0000269|PubMed:14617813}.
CC -!- INTERACTION:
CC P05455; P54652: HSPA2; NbExp=3; IntAct=EBI-358037, EBI-356991;
CC P05455; P42858: HTT; NbExp=3; IntAct=EBI-358037, EBI-466029;
CC P05455; O96000: NDUFB10; NbExp=3; IntAct=EBI-358037, EBI-1246371;
CC P05455; Q8WZA2: RAPGEF4; NbExp=3; IntAct=EBI-358037, EBI-948476;
CC P05455; PRO_0000045599 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-358037, EBI-6858501;
CC P05455; PRO_0000045603 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-358037, EBI-6927928;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylated. The phosphorylation sites are at the C-terminal
CC part of the protein. {ECO:0000269|PubMed:9054510}.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Sera from patients with systemic lupus erythematosus
CC (SLE) often contain antibodies that react with the normal cellular La
CC protein as if this antigen was foreign.
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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 CCDS; CCDS2237.1; -.
DR PIR; A31888; A31888.
DR RefSeq; NP_001281074.1; NM_001294145.1.
DR RefSeq; NP_003133.1; NM_003142.4.
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 AlphaFoldDB; P05455; -.
DR BMRB; P05455; -.
DR SMR; P05455; -.
DR BioGRID; 112619; 326.
DR CORUM; P05455; -.
DR DIP; DIP-29750N; -.
DR IntAct; P05455; 97.
DR MINT; P05455; -.
DR STRING; 9606.ENSP00000386636; -.
DR ChEMBL; CHEMBL2040701; -.
DR GlyGen; P05455; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P05455; -.
DR MetOSite; P05455; -.
DR PhosphoSitePlus; P05455; -.
DR SwissPalm; P05455; -.
DR BioMuta; SSB; -.
DR DMDM; 125985; -.
DR EPD; P05455; -.
DR jPOST; P05455; -.
DR MassIVE; P05455; -.
DR MaxQB; P05455; -.
DR PaxDb; P05455; -.
DR PeptideAtlas; P05455; -.
DR PRIDE; P05455; -.
DR ProteomicsDB; 51841; -.
DR Antibodypedia; 2797; 556 antibodies from 38 providers.
DR DNASU; 6741; -.
DR Ensembl; ENST00000260956.9; ENSP00000260956.4; ENSG00000138385.16.
DR Ensembl; ENST00000409333.1; ENSP00000386636.1; ENSG00000138385.16.
DR GeneID; 6741; -.
DR KEGG; hsa:6741; -.
DR MANE-Select; ENST00000260956.9; ENSP00000260956.4; NM_003142.5; NP_003133.1.
DR UCSC; uc002ufk.4; human.
DR CTD; 6741; -.
DR DisGeNET; 6741; -.
DR GeneCards; SSB; -.
DR HGNC; HGNC:11316; SSB.
DR HPA; ENSG00000138385; Low tissue specificity.
DR MIM; 109090; gene.
DR neXtProt; NX_P05455; -.
DR OpenTargets; ENSG00000138385; -.
DR PharmGKB; PA36140; -.
DR VEuPathDB; HostDB:ENSG00000138385; -.
DR eggNOG; KOG4213; Eukaryota.
DR GeneTree; ENSGT00830000128380; -.
DR HOGENOM; CLU_042341_0_0_1; -.
DR InParanoid; P05455; -.
DR OMA; QFERSIY; -.
DR OrthoDB; 882725at2759; -.
DR PhylomeDB; P05455; -.
DR TreeFam; TF314476; -.
DR PathwayCommons; P05455; -.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR SignaLink; P05455; -.
DR SIGNOR; P05455; -.
DR BioGRID-ORCS; 6741; 464 hits in 1086 CRISPR screens.
DR ChiTaRS; SSB; human.
DR EvolutionaryTrace; P05455; -.
DR GeneWiki; Sjogren_syndrome_antigen_B; -.
DR GenomeRNAi; 6741; -.
DR Pharos; P05455; Tbio.
DR PRO; PR:P05455; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P05455; protein.
DR Bgee; ENSG00000138385; Expressed in tendon of biceps brachii and 204 other tissues.
DR ExpressionAtlas; P05455; baseline and differential.
DR Genevisible; P05455; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:1990904; C:ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; IMP:CAFA.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IMP:CAFA.
DR GO; GO:0000049; F:tRNA binding; IMP:CAFA.
DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:ProtInc.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:0071045; P:nuclear histone mRNA catabolic process; IMP:CAFA.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IDA:AgBase.
DR GO; GO:0042780; P:tRNA 3'-end processing; IGI:CAFA.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IGI:CAFA.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:CAFA.
DR GO; GO:0006400; P:tRNA modification; TAS:ProtInc.
DR GO; GO:0008033; P:tRNA processing; IMP:CAFA.
DR DisProt; DP00229; -.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR014886; La_xRRM.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
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 SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51939; XRRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Systemic lupus erythematosus.
FT CHAIN 1..408
FT /note="Lupus La protein"
FT /id="PRO_0000207599"
FT DOMAIN 7..99
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 111..187
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 227..348
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 329..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 341
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32067"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 362
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 366
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9054510,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CONFLICT 54
FT /note="K -> E (in Ref. 8; AAA36577)"
FT /evidence="ECO:0000305"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:2VOO"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:2VOO"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2VOO"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2VON"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:2VOO"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2VOO"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:2VOO"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1YTY"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2VOO"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2VOP"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:2VOO"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:2VOO"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2VOD"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:2VOO"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:2VOO"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:1OWX"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1OWX"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:1OWX"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:1OWX"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:1OWX"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1OWX"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:1OWX"
FT HELIX 308..326
FT /evidence="ECO:0007829|PDB:1OWX"
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
