P05455 (LA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lupus La protein

Alternative name(s):
La autoantigen
La ribonucleoprotein
Sjoegren syndrome type B antigen
Short name=SS-B

Gene names

Name:

SSB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to the 3' poly(U) terminii of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. Ref.2 Ref.10
Subunit structure	Interacts with DDX15. May interact with RUFY1. Ref.12 Ref.13
Subcellular location	Nucleus Probable.
Post-translational modification	Phosphorylated. The phosphorylation sites are at the C-terminal part of the protein. Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 The N-terminus is blocked.
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.
Sequence similarities	Contains 1 HTH La-type RNA-binding domain. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Systemic lupus erythematosus
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histone mRNA metabolic process Traceable author statement. Source: ProtInc tRNA modification Traceable author statement. Source: ProtInc
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Traceable author statement. Source: ProtInc
Molecular function	mRNA binding Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro tRNA binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 408

408

Lupus La protein

PRO_0000207599

Regions

Domain

7 – 99

93

HTH La-type RNA-binding

Domain

111 – 187

77

RRM

Amino acid modifications

Modified residue

116

1

N6-acetyllysine Ref.26

Modified residue

128

1

N6-acetyllysine Ref.26

Modified residue

328

1

N6-acetyllysine Ref.26

Modified residue

360

1

N6-acetyllysine Ref.26

Modified residue

362

1

Phosphothreonine Ref.23

Modified residue

366

1

Phosphoserine; by CK2 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Natural variations

Natural variant

48

1

P → S.
Corresponds to variant rs17160793 [ dbSNP | Ensembl ].

VAR_034066

Experimental info

Sequence conflict

54

1

K → E in AAA36577. Ref.8

Secondary structure

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408

Helix Strand Turn

Details...

Helix

7 – 24

18

Turn

27 – 29

3

Helix

30 – 32

3

Helix

34 – 42

9

Helix

49 – 52

4

Helix

56 – 61

6

Helix

65 – 73

9

Beta strand

80 – 82

3

Beta strand

86 – 91

6

Helix

102 – 110

9

Beta strand

112 – 116

5

Helix

124 – 131

8

Helix

132 – 134

3

Beta strand

137 – 144

8

Beta strand

150 – 160

11

Helix

161 – 169

9

Beta strand

181 – 184

4

Helix

185 – 187

3

Beta strand

233 – 239

7

Helix

246 – 252

7

Beta strand

259 – 263

5

Beta strand

269 – 277

9

Helix

279 – 288

10

Turn

289 – 291

3

Beta strand

298 – 304

7

Helix

308 – 326

19

Sequences

	Sequence		Length	Mass (Da)
	P05455 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: EC153C15F9187FC4	FASTA	408	46,837
	10 20 30 40 50 60 MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE IMIKFNRLNR 70 80 90 100 110 120 LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV TDEYKNDVKN RSVYIKGFPT 130 140 150 160 170 180 DATLDDIKEW LEDKGQVLNI QMRRTLHKAF KGSIFVVFDS IESAKKFVET PGQKYKETDL 190 200 210 220 230 240 LILFKDDYFA KKNEERKQNK VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL 250 260 270 280 290 300 DDQTCREDLH ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE 310 320 330 340 350 360 VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS GKGKVQFQGK 370 380 390 400 KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK TENGAGDQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2468131] [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: 3192525] [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: 19054851] [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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 2452201] [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: 3856888] [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: 2470590] [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: 9054510] [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: 12458796] [Abstract] Cited for: INTERACTION WITH DDX15.
[13]	"Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes." Fouraux M.A., Deneka M., Ivan V., van der Heijden A., Raymackers J., van Suylekom D., van Venrooij W.J., van der Sluijs P., Pruijn G.J.M. Mol. Biol. Cell 15:611-624(2004) [PubMed: 14617813] [Abstract] Cited for: INTERACTION WITH RUFY1.
[14]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[15]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Prostate cancer.
[17]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: T-cell.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Liver.
[22]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-362 AND SER-366, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[24]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY.
[25]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-328 AND LYS-360, MASS SPECTROMETRY.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"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: 12842046] [Abstract] Cited for: STRUCTURE BY NMR OF 225-334.
[29]	"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: 15004549] [Abstract] Cited for: STRUCTURE BY NMR OF 1-202.
[30]	"Structural basis for recognition and sequestration of UUU(OH) 3' temini 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: 16387655] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-194.
[31]	"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: 18547518] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-194.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00009032.

PIR

A31888.

RefSeq

NP_003133.1. NM_003142.4.

UniGene

Hs.632535.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P05455.

SMR

P05455. Positions 10-188, 225-334.

DisProt

DP00229.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29750N.

IntAct

P05455. 15 interactions.

MINT

MINT-5002383.

STRING

P05455.

PTM databases

PhosphoSite

P05455.

Polymorphism databases

DMDM

125985.

Proteomic databases

PeptideAtlas

P05455.

PRIDE

P05455.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260956; ENSP00000260956; ENSG00000138385.
ENST00000409333; ENSP00000386636; ENSG00000138385.

GeneID

6741.

KEGG

hsa:6741.

UCSC

uc002ufk.1. human.

Organism-specific databases

CTD

6741.

GeneCards

GC02P170619.

H-InvDB

HIX0002576.

HGNC

HGNC:11316. SSB.

HPA

CAB004643.
HPA012385.
HPA017287.

MIM

109090. gene.

neXtProt

NX_P05455.

PharmGKB

PA36140.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08885.

HOGENOM

HBG315945.

HOVERGEN

HBG001407.

InParanoid

P05455.

OMA

ENAEMKS.

OrthoDB

EOG4C2HB3.

PhylomeDB

P05455.

Gene expression databases

ArrayExpress

P05455.

Bgee

P05455.

CleanEx

HS_SSB.

Genevestigator

P05455.

GermOnline

ENSG00000138385. Homo sapiens.

Family and domain databases

InterPro

IPR002344. Lupus_La.
IPR006630. Lupus_La_RNA-bd.
IPR012677. Nucleotide-bd_a/b_plait.
IPR014886. RRM_3.
IPR000504. RRM_dom.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K11090.

Pfam

PF05383. La. 1 hit.
PF00076. RRM_1. 1 hit.
PF08777. RRM_3. 1 hit.
[Graphical view]

PRINTS

PR00302. LUPUSLA.

SMART

SM00715. LA. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50961. HTH_LA. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

26296.

PMAP-CutDB

P05455.

SOURCE

Search...

Entry information

Entry name

LA_HUMAN

Accession

Primary (citable) accession number: P05455
Secondary accession number(s): Q15367, Q53XJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	July 1, 1989
Last modified:	January 25, 2012
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.