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Protein

U7 snRNA-associated Sm-like protein LSm11

Gene

LSM11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing (By similarity). 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.By similarity1 Publication

GO - Molecular functioni

  • U7 snRNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-HSA-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
U7 snRNA-associated Sm-like protein LSm11
Gene namesi
Name:LSM11
OrganismiHomo sapiens (Human)Curated
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:30860. LSM11.

Subcellular locationi

GO - Cellular componenti

  • histone pre-mRNA 3'end processing complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134983181.

Polymorphism and mutation databases

BioMutaiLSM11.
DMDMi47117879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360U7 snRNA-associated Sm-like protein LSm11PRO_0000125587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei154 – 1541PhosphoserineCombined sources
Modified residuei280 – 2801PhosphoserineCombined sources

Post-translational modificationi

Not methylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP83369.
MaxQBiP83369.
PaxDbiP83369.
PeptideAtlasiP83369.
PRIDEiP83369.

PTM databases

iPTMnetiP83369.
PhosphoSiteiP83369.

Expressioni

Gene expression databases

BgeeiENSG00000155858.
CleanExiHS_LSM11.
GenevisibleiP83369. HS.

Organism-specific databases

HPAiHPA039587.

Interactioni

Subunit structurei

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. 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. Interacts with LSM10, SMN, SNRPB and ZNF473. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By similarity). Interacts (via the Sm domains) with CLNS1A. Interacts with PRMT5 and WDR77 (By similarity).By similarity

Protein-protein interaction databases

BioGridi126394. 30 interactions.
IntActiP83369. 17 interactions.
STRINGi9606.ENSP00000286307.

Structurei

3D structure databases

ProteinModelPortaliP83369.
SMRiP83369. Positions 158-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni171 – 20434SM 1Add
BLAST
Regioni343 – 35614SM 2Add
BLAST

Domaini

The C-terminal SM 1 domain is both necessary for the binding to the Sm-binding site of U7 snRNA and U7 snRNP assembly (By similarity). The N-terminal domain is essential for histone pre-mRNA cleavage. Amino acids 63-82 are sufficient to interact with ZNF473.By similarity

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IRD3. Eukaryota.
ENOG4111F1R. LUCA.
GeneTreeiENSGT00390000012944.
HOGENOMiHOG000035131.
HOVERGENiHBG052367.
InParanoidiP83369.
OMAiCFNNLAE.
OrthoDBiEOG091G0PNU.
PhylomeDBiP83369.
TreeFamiTF326954.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 3 hits.

Sequencei

Sequence statusi: Complete.

P83369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEERERGARS AGAGSPARPP SPRLDVSSDS FDPLLALYAP RLPPIPYPNA
60 70 80 90 100
PCFNNVAEYE SFLRTGVRGG GRGRGRARGA AAGSGVPAAP GPSGRTRRRP
110 120 130 140 150
DAPAPDPERI QRLRRLMVAK EEGDGAAGAG RRGPGRSRKA PRNVLTRMPL
160 170 180 190 200
HEGSPLGELH RCIREGVKVN VHIRTFKGLR GVCTGFLVAF DKFWNMALTD
210 220 230 240 250
VDETYRKPVL GKAYERDSSL TLTRLFDRLK LQDSSKKEAD SKSAVEDSTL
260 270 280 290 300
SRYSQTSTWK LASVWGRADT GRGSHKRSRS VPSSLQASAR EESRSELSGR
310 320 330 340 350
TTRTDGSSVG GTFSRATTLS RGQSRKKKRK PKVDYQQVFT RHINQIFIRG
360
ENVLLVHLAQ
Length:360
Mass (Da):39,500
Last modified:May 10, 2004 - v2
Checksum:i3C97710C28C0DCE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK095592 mRNA. Translation: BAC04581.1.
BC051353 mRNA. Translation: AAH51353.1.
BC126449 mRNA. Translation: AAI26450.1.
CCDSiCCDS4342.1.
RefSeqiNP_775762.1. NM_173491.3.
UniGeneiHs.23648.
Hs.631954.

Genome annotation databases

EnsembliENST00000286307; ENSP00000286307; ENSG00000155858.
GeneIDi134353.
KEGGihsa:134353.
UCSCiuc003lxf.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK095592 mRNA. Translation: BAC04581.1.
BC051353 mRNA. Translation: AAH51353.1.
BC126449 mRNA. Translation: AAI26450.1.
CCDSiCCDS4342.1.
RefSeqiNP_775762.1. NM_173491.3.
UniGeneiHs.23648.
Hs.631954.

3D structure databases

ProteinModelPortaliP83369.
SMRiP83369. Positions 158-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126394. 30 interactions.
IntActiP83369. 17 interactions.
STRINGi9606.ENSP00000286307.

PTM databases

iPTMnetiP83369.
PhosphoSiteiP83369.

Polymorphism and mutation databases

BioMutaiLSM11.
DMDMi47117879.

Proteomic databases

EPDiP83369.
MaxQBiP83369.
PaxDbiP83369.
PeptideAtlasiP83369.
PRIDEiP83369.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286307; ENSP00000286307; ENSG00000155858.
GeneIDi134353.
KEGGihsa:134353.
UCSCiuc003lxf.2. human.

Organism-specific databases

CTDi134353.
GeneCardsiLSM11.
HGNCiHGNC:30860. LSM11.
HPAiHPA039587.
neXtProtiNX_P83369.
PharmGKBiPA134983181.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IRD3. Eukaryota.
ENOG4111F1R. LUCA.
GeneTreeiENSGT00390000012944.
HOGENOMiHOG000035131.
HOVERGENiHBG052367.
InParanoidiP83369.
OMAiCFNNLAE.
OrthoDBiEOG091G0PNU.
PhylomeDBiP83369.
TreeFamiTF326954.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-HSA-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.

Miscellaneous databases

GenomeRNAii134353.
PROiP83369.

Gene expression databases

BgeeiENSG00000155858.
CleanExiHS_LSM11.
GenevisibleiP83369. HS.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. LSM_dom_euk/arc.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiLSM11_HUMAN
AccessioniPrimary (citable) accession number: P83369
Secondary accession number(s): A0AVQ1, Q7Z7P0, Q8N975
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: May 10, 2004
Last modified: September 7, 2016
This is version 113 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.