O15116 (LSM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
U6 snRNA-associated Sm-like protein LSm1

Alternative name(s):
Cancer-associated Sm-like
Small nuclear ribonuclear CaSm

Gene names

Name:	LSM1
Synonyms:	CASM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	133 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in replication-dependent histone mRNA degradation. Binds specifically to the 3'-terminal U-tract of U6 snRNA. Ref.6
Subunit structure	Interacts with SLBP. Interaction with SLBP occurs when histone mRNA is being rapidly degraded during the S phase. LSm subunits form a heteromer with a doughnut shape. Ref.6
Subcellular location	Nucleus Potential.
Tissue specificity	Has elevated expression in pancreatic cancer and in several cancer-derived cell lines.
Sequence similarities	Belongs to the snRNP Sm proteins family.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Nucleus
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing, via transesterification reactions Traceable author statement Ref.2. Source: UniProtKB exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Traceable author statement. Source: Reactome histone mRNA catabolic process Inferred from mutant phenotype Ref.6. Source: UniProtKB mRNA processing Traceable author statement Ref.2. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 18559850. Source: MGI ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LSM2	Q9Y333	3	EBI-347619,EBI-347416
LSM3	P62310	3	EBI-347619,EBI-348239

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 133	133	U6 snRNA-associated Sm-like protein LSm1		PRO_0000125554

Sequences

	Sequence		Length	Mass (Da)
	O15116 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: FF798CDA9447037A	FASTA	133	15,179
	10 20 30 40 50 60 MNYMPGTASL IEDIDKKHLV LLRDGRTLIG FLRSIDQFAN LVLHQTVERI HVGKKYGDIP 70 80 90 100 110 120 RGIFVVRGEN VVLLGEIDLE KESDTPLQQV SIEEILEEQR VEQQTKLEAE KLKVQALKDR 130 GLSIPRADTL DEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CaSm: an Sm-like protein that contributes to the transformed state in cancer cells." Schweinfest C.W., Graber M.W., Chapman J.M., Papas T.S., Baron P.L., Watson D.K. Cancer Res. 57:2961-2965(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin." Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B. EMBO J. 18:3451-3462(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymph node.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Substantia nigra.
[4]	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].
[5]	"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: Eye.
[6]	"Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'." Mullen T.E., Marzluff W.F. Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY, INTERACTION WITH SLBP.
[7]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF000177 mRNA. Translation: AAB62189.1. AJ238094 mRNA. Translation: CAB45865.1. AK312159 mRNA. Translation: BAG35093.1. CH471080 Genomic DNA. Translation: EAW63332.1. BC001767 mRNA. Translation: AAH01767.1.
IPI	IPI00004436.
RefSeq	NP_055277.1. NM_014462.2.
UniGene	Hs.425311.
3D structure databases
ProteinModelPortal	O15116.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31130N.
IntAct	O15116. 20 interactions.
MINT	MINT-1036791.
STRING	9606.ENSP00000310596.
PTM databases
PhosphoSite	O15116.
Proteomic databases
PaxDb	O15116.
PeptideAtlas	O15116.
PRIDE	O15116.
Protocols and materials databases
DNASU	27257.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000311351; ENSP00000310596; ENSG00000175324.
GeneID	27257.
KEGG	hsa:27257.
UCSC	uc003xkw.3. human.
Organism-specific databases
CTD	27257.
GeneCards	GC08M038020.
HGNC	HGNC:20472. LSM1.
HPA	HPA024601.
MIM	607281. gene.
neXtProt	NX_O15116.
PharmGKB	PA134864226.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236501.
HOGENOM	HOG000223544.
HOVERGEN	HBG027238.
InParanoid	O15116.
KO	K12620.
OMA	IERIHVG.
OrthoDB	EOG4BRWN3.
PhylomeDB	O15116.
Enzyme and pathway databases
Reactome	REACT_21257. Metabolism of RNA. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	O15116.
Bgee	O15116.
CleanEx	HS_LSM1.
Genevestigator	O15116.
GermOnline	ENSG00000175324. Homo sapiens.
Family and domain databases
InterPro	IPR010920. LSM_dom. IPR001163. Ribonucl_LSM. IPR006649. Ribonucl_LSM_euk/arc. [Graphical view]
Pfam	PF01423. LSM. 1 hit. [Graphical view]
SMART	SM00651. Sm. 1 hit. [Graphical view]
SUPFAM	SSF50182. Sm_like_riboprot. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	27257.
NextBio	50202.
SOURCE	Search...

Entry information

Entry name

LSM1_HUMAN

Accession

Primary (citable) accession number: O15116
Secondary accession number(s): B2R5E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 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.