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P05455

- LA_HUMAN

UniProt

P05455 - LA_HUMAN

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Protein

Lupus La protein

Gene

SSB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. tRNA binding Source: ProtInc

GO - Biological processi

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

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-KW
  2. ribonucleoprotein complex Source: ProtInc
Complete GO annotation...

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

BgeeiP05455.
CleanExiHS_SSB.
ExpressionAtlasiP05455. baseline and differential.
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. 61 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 – 2414Combined sources
Turni27 – 293Combined sources
Helixi30 – 323Combined sources
Helixi34 – 429Combined sources
Turni43 – 453Combined sources
Beta strandi46 – 483Combined sources
Helixi49 – 524Combined sources
Helixi56 – 616Combined sources
Helixi65 – 739Combined sources
Beta strandi80 – 823Combined sources
Beta strandi86 – 916Combined sources
Helixi102 – 1109Combined sources
Beta strandi112 – 1165Combined sources
Helixi124 – 1318Combined sources
Helixi132 – 1343Combined sources
Beta strandi137 – 1448Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi150 – 16011Combined sources
Helixi161 – 1699Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi181 – 1844Combined sources
Turni185 – 1873Combined sources
Beta strandi233 – 2397Combined sources
Helixi246 – 2527Combined sources
Beta strandi259 – 2635Combined sources
Beta strandi269 – 2779Combined sources
Helixi279 – 28810Combined sources
Turni289 – 2913Combined sources
Beta strandi298 – 3047Combined sources
Helixi308 – 32619Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119379.
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

        10         20         30         40         50
MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE
60 70 80 90 100
IMIKFNRLNR LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV
110 120 130 140 150
TDEYKNDVKN RSVYIKGFPT DATLDDIKEW LEDKGQVLNI QMRRTLHKAF
160 170 180 190 200
KGSIFVVFDS IESAKKFVET PGQKYKETDL LILFKDDYFA KKNEERKQNK
210 220 230 240 250
VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL DDQTCREDLH
260 270 280 290 300
ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE
310 320 330 340 350
VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS
360 370 380 390 400
GKGKVQFQGK KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK

TENGAGDQ
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:
EMBLi
GenBanki
DDBJi
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_001281074.1. NM_001294145.1.
NP_003133.1. NM_003142.4.
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:
EMBLi
GenBanki
DDBJi
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_001281074.1. NM_001294145.1.
NP_003133.1. NM_003142.4.
UniGenei Hs.632535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 61 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 GC02P170649.
HGNCi HGNC:11316. SSB.
HPAi CAB004643.
HPA012385.
HPA017287.
MIMi 109090. gene.
neXtProti NX_P05455.
PharmGKBi PA36140.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5193.
GeneTreei ENSGT00760000119379.
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

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

Gene expression databases

Bgeei P05455.
CleanExi HS_SSB.
ExpressionAtlasi P05455. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 178 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