Q8BUV6 (LSM11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
U7 snRNA-associated Sm-like protein LSm11

Gene names

Name:

Lsm11

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing. Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases. Binds specifically to the Sm-binding site of U7 snRNA. Ref.1 Ref.4 Ref.5
Subunit structure	Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts (via the Sm domains) with CLNS1A. Interacts with PRMT5, SMN, ZNF473 and WDR77. Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA By similarity. Formation of the U7 snRNP is an ATP-dependent process mediated by a specialized SMN complex containing at least the Sm protein core complex and additionally, the U7-specific LSM10 and LSM11 proteins By similarity. Interacts with LSM10 and SNRPB By similarity. Ref.1 Ref.3 Ref.4
Subcellular location	Nucleus By similarity.
Domain	The C-terminal SM 1 domain is both necessary for the binding to the Sm-binding site of U7 snRNA and U7 snRNP assembly. The N-terminal domain is essential for histone pre-mRNA cleavage By similarity. Amino acids 63-82 are sufficient to interact with ZNF473 By similarity.
Post-translational modification	Not methylated. Ref.3
Sequence similarities	Belongs to the snRNP Sm proteins family.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	S phase of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB histone mRNA 3'-end processing Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	U7 snRNP Inferred from direct assay Ref.1. Source: UniProtKB histone pre-mRNA 3'end processing complex Inferred from direct assay Ref.6. Source: UniProtKB
Molecular function	U7 snRNA binding Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	U7 snRNA-associated Sm-like protein LSm11		PRO_0000125588
Regions
	Region	172 – 205	34	SM 1
	Region	344 – 357	14	SM 2
Amino acid modifications
	Modified residue	10	1	Phosphoserine By similarity
	Modified residue	21	1	Phosphoserine By similarity
Experimental info
	Mutagenesis	33 – 35	3	PLL → AAA: Does not inhibit interaction with ZNF473. Reduces strongly histone 3' end processing.
	Mutagenesis	59 – 61	3	YES → AAA: Does not inhibit interaction with ZNF473 and histone 3'-end processing.
	Mutagenesis	108 – 110	3	PER → AAA: Does not inhibit interaction with ZNF473. Reduces weakly histone 3' end processing. Ref.4
	Mutagenesis	149 – 151	3	MPL → AAA: Does not inhibit interaction with ZNF473. Reduces weakly histone 3' end processing. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8BUV6 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 68777427AC37E10E	FASTA	361	39,907
	10 20 30 40 50 60 MEEREWGARS ARAGSPASPP SPRLDVSSYS FDPLLALYAP RLPPIPYPNA PCFNNVAEYE 70 80 90 100 110 120 SFLKGGRTGR GRARGTGEPA SAGTSTGTST GAGSSSRARR RAAPTPDPER IQRLRRLMVV 130 140 150 160 170 180 KEDTDGTAGA RRQGPGRSKK APRNVLTRMP LHEGSPLGEL HRCIREGVKV NVHIRTFKGL 190 200 210 220 230 240 RGVCTGFLVA FDKFWNMALT DVDETYRKPV LGKAYERDSS LTLTRLFDRL KLQDSSKKEA 250 260 270 280 290 300 DSKSAVEDST LSRYSQTSTW KVASVWGRGD TDRSSHRRSR SVPSSLQASA REESRSELSG 310 320 330 340 350 360 RTTRTEGSSV GGTFSRATTL SRGQSRKKKR KPKVDYQQVF TRHINQIFIR GENVLLVHLA Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing." Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U., Schuemperli D. Genes Dev. 17:2321-2333(2003) [PubMed: 12975319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN THE U7 SNRNP COMPLEX, INTERACTION WITH ZNF473.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum.
[3]	"Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes." Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D. J. Biol. Chem. 280:34435-34440(2005) [PubMed: 16087681] [Abstract] Cited for: INTERACTION WITH CLNS1A; PRMT5 AND WDR77, ABSENCE OF METHYLATION.
[4]	"U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa zinc finger processing factor (ZFP100) and a ZFP100-independent function in histone RNA 3'-end processing." Azzouz T.N., Gruber A., Schuemperli D. Nucleic Acids Res. 33:2106-2117(2005) [PubMed: 15824063] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 33-PRO--LEU-35; 59-THY--SER-61; 108-PRO--ARG-110 AND 149-MET--LEU-151, INTERACTION WITH ZNF473.
[5]	"ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S phase." Wagner E.J., Marzluff W.F. Mol. Cell. Biol. 26:6702-6712(2006) [PubMed: 16914750] [Abstract] Cited for: FUNCTION.
[6]	"Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA." Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z. Mol. Cell. Biol. 29:4045-4056(2009) [PubMed: 19470752] [Abstract] Cited for: IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF514309 mRNA. Translation: AAQ08118.1. AK082292 mRNA. Translation: BAC38456.1.
IPI	IPI00225677.
RefSeq	NP_082461.1. NM_028185.2.
UniGene	Mm.249827.
3D structure databases
ProteinModelPortal	Q8BUV6.
SMR	Q8BUV6. Positions 155-207.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8BUV6. 1 interaction.
STRING	Q8BUV6.
PTM databases
PhosphoSite	Q8BUV6.
Proteomic databases
PRIDE	Q8BUV6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000062458; ENSMUSP00000057343; ENSMUSG00000044847. ENSMUST00000129820; ENSMUSP00000117531; ENSMUSG00000044847.
GeneID	72290.
KEGG	mmu:72290.
Organism-specific databases
CTD	134353.
MGI	MGI:1919540. Lsm11.
Phylogenomic databases
HOGENOM	HBG714770.
HOVERGEN	HBG052367.
InParanoid	Q8BUV6.
OMA	IPYPNAP.
PhylomeDB	Q8BUV6.
Gene expression databases
ArrayExpress	Q8BUV6.
Bgee	Q8BUV6.
CleanEx	MM_LSM11.
Genevestigator	Q8BUV6.
GermOnline	ENSMUSG00000044847. Mus musculus.
Family and domain databases
InterPro	IPR010920. LSM-related_domain. IPR001163. LSM_domain. IPR006649. LSM_domain_euk/arc. [Graphical view]
Pfam	PF01423. LSM. 1 hit. [Graphical view]
SMART	SM00651. Sm. 1 hit. [Graphical view]
SUPFAM	SSF50182. Sm_like_riboprot. 2 hits.
ProtoNet	Search...
Other
NextBio	335924.
SOURCE	Search...

Entry information

Entry name

LSM11_MOUSE

Accession

Primary (citable) accession number: Q8BUV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program