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Q9Y4Y9

- LSM5_HUMAN

UniProt

Q9Y4Y9 - LSM5_HUMAN

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Protein

U6 snRNA-associated Sm-like protein LSm5

Gene

LSM5

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

Functioni

Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA, thereby facilitating formation of the spliceosomal U4/U6 duplex formation in vitro.

GO - Molecular functioni

  1. RNA binding Source: ProtInc

GO - Biological processi

  1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. mRNA processing Source: ProtInc
  5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  6. RNA metabolic process Source: Reactome
  7. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Names & Taxonomyi

Protein namesi
Recommended name:
U6 snRNA-associated Sm-like protein LSm5
Gene namesi
Name:LSM5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:17162. LSM5.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: ProtInc
  3. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134881171.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 9190U6 snRNA-associated Sm-like protein LSm5PRO_0000125572Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y4Y9.
PaxDbiQ9Y4Y9.
PRIDEiQ9Y4Y9.

PTM databases

PhosphoSiteiQ9Y4Y9.

Expressioni

Gene expression databases

BgeeiQ9Y4Y9.
CleanExiHS_LSM5.
ExpressionAtlasiQ9Y4Y9. baseline and differential.
GenevestigatoriQ9Y4Y9.

Organism-specific databases

HPAiHPA019054.

Interactioni

Subunit structurei

LSm subunits form a heteromer with a doughnut shape.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LSM3P623103EBI-373007,EBI-348239
LSM6P623124EBI-373007,EBI-373310
LSM7Q9UK455EBI-373007,EBI-348372

Protein-protein interaction databases

BioGridi117180. 18 interactions.
DIPiDIP-31162N.
IntActiQ9Y4Y9. 7 interactions.
MINTiMINT-3086779.
STRINGi9606.ENSP00000410758.

Structurei

3D structure databases

ProteinModelPortaliQ9Y4Y9.
SMRiQ9Y4Y9. Positions 12-86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00390000001455.
HOVERGENiHBG107310.
InParanoidiQ9Y4Y9.
KOiK12624.
OMAiCIGSKIH.
OrthoDBiEOG7NSB4W.
PhylomeDBiQ9Y4Y9.
TreeFamiTF313575.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y4Y9-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAANATTNPS QLLPLELVDK CIGSRIHIVM KSDKEIVGTL LGFDDFVNMV
60 70 80 90
LEDVTEFEIT PEGRRITKLD QILLNGNNIT MLVPGGEGPE V
Length:91
Mass (Da):9,937
Last modified:January 23, 2007 - v3
Checksum:i82B5C8830E64C992
GO
Isoform 2 (identifier: Q9Y4Y9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Show »
Length:62
Mass (Da):6,850
Checksum:i6340D862682806E2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_040991Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ238097 mRNA. Translation: CAB45868.1.
AF182291 mRNA. Translation: AAD56229.1.
AC018641 Genomic DNA. No translation available.
BC005938 mRNA. Translation: AAH05938.1.
BF701546 mRNA. No translation available.
CCDSiCCDS47571.1. [Q9Y4Y9-2]
CCDS5438.1. [Q9Y4Y9-1]
RefSeqiNP_001124182.1. NM_001130710.1. [Q9Y4Y9-2]
NP_001132971.1. NM_001139499.1. [Q9Y4Y9-2]
NP_036454.1. NM_012322.2. [Q9Y4Y9-1]
UniGeneiHs.424908.

Genome annotation databases

EnsembliENST00000409292; ENSP00000386814; ENSG00000106355. [Q9Y4Y9-2]
ENST00000409782; ENSP00000387109; ENSG00000106355. [Q9Y4Y9-2]
ENST00000409909; ENSP00000386363; ENSG00000106355. [Q9Y4Y9-2]
ENST00000409952; ENSP00000387126; ENSG00000106355. [Q9Y4Y9-2]
ENST00000410044; ENSP00000386707; ENSG00000106355. [Q9Y4Y9-2]
ENST00000450169; ENSP00000410758; ENSG00000106355. [Q9Y4Y9-1]
GeneIDi23658.
KEGGihsa:23658.
UCSCiuc003tct.2. human. [Q9Y4Y9-1]

Polymorphism databases

DMDMi10720081.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ238097 mRNA. Translation: CAB45868.1 .
AF182291 mRNA. Translation: AAD56229.1 .
AC018641 Genomic DNA. No translation available.
BC005938 mRNA. Translation: AAH05938.1 .
BF701546 mRNA. No translation available.
CCDSi CCDS47571.1. [Q9Y4Y9-2 ]
CCDS5438.1. [Q9Y4Y9-1 ]
RefSeqi NP_001124182.1. NM_001130710.1. [Q9Y4Y9-2 ]
NP_001132971.1. NM_001139499.1. [Q9Y4Y9-2 ]
NP_036454.1. NM_012322.2. [Q9Y4Y9-1 ]
UniGenei Hs.424908.

3D structure databases

ProteinModelPortali Q9Y4Y9.
SMRi Q9Y4Y9. Positions 12-86.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117180. 18 interactions.
DIPi DIP-31162N.
IntActi Q9Y4Y9. 7 interactions.
MINTi MINT-3086779.
STRINGi 9606.ENSP00000410758.

PTM databases

PhosphoSitei Q9Y4Y9.

Polymorphism databases

DMDMi 10720081.

Proteomic databases

MaxQBi Q9Y4Y9.
PaxDbi Q9Y4Y9.
PRIDEi Q9Y4Y9.

Protocols and materials databases

DNASUi 23658.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000409292 ; ENSP00000386814 ; ENSG00000106355 . [Q9Y4Y9-2 ]
ENST00000409782 ; ENSP00000387109 ; ENSG00000106355 . [Q9Y4Y9-2 ]
ENST00000409909 ; ENSP00000386363 ; ENSG00000106355 . [Q9Y4Y9-2 ]
ENST00000409952 ; ENSP00000387126 ; ENSG00000106355 . [Q9Y4Y9-2 ]
ENST00000410044 ; ENSP00000386707 ; ENSG00000106355 . [Q9Y4Y9-2 ]
ENST00000450169 ; ENSP00000410758 ; ENSG00000106355 . [Q9Y4Y9-1 ]
GeneIDi 23658.
KEGGi hsa:23658.
UCSCi uc003tct.2. human. [Q9Y4Y9-1 ]

Organism-specific databases

CTDi 23658.
GeneCardsi GC07M032524.
HGNCi HGNC:17162. LSM5.
HPAi HPA019054.
MIMi 607285. gene.
neXtProti NX_Q9Y4Y9.
PharmGKBi PA134881171.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1958.
GeneTreei ENSGT00390000001455.
HOVERGENi HBG107310.
InParanoidi Q9Y4Y9.
KOi K12624.
OMAi CIGSKIH.
OrthoDBi EOG7NSB4W.
PhylomeDBi Q9Y4Y9.
TreeFami TF313575.

Enzyme and pathway databases

Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

Miscellaneous databases

GeneWikii LSM5.
GenomeRNAii 23658.
NextBioi 46501.
PROi Q9Y4Y9.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y4Y9.
CleanExi HS_LSM5.
ExpressionAtlasi Q9Y4Y9. baseline and differential.
Genevestigatori Q9Y4Y9.

Family and domain databases

InterProi IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view ]
Pfami PF01423. LSM. 1 hit.
[Graphical view ]
SMARTi SM00651. Sm. 1 hit.
[Graphical view ]
SUPFAMi SSF50182. SSF50182. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Tissue: Placenta.
  2. "A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro."
    Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., Luehrmann R.
    EMBO J. 18:5789-5802(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Bone marrow and Brain.
  5. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLSM5_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 129 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3