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Protein

Small nuclear ribonucleoprotein Sm D2

Gene

Snrpd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_271571. mRNA Splicing - Minor Pathway.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_333207. snRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Small nuclear ribonucleoprotein Sm D2
Short name:
Sm-D2
Alternative name(s):
snRNP core protein D2
Gene namesi
Name:Snrpd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98345. Snrpd2.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Nucleus By similarity

  • Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 118117Small nuclear ribonucleoprotein Sm D2PRO_0000122208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei12 – 121PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62317.
PaxDbiP62317.
PRIDEiP62317.

PTM databases

PhosphoSiteiP62317.

Expressioni

Gene expression databases

BgeeiP62317.
CleanExiMM_SNRPD2.
ExpressionAtlasiP62317. baseline and differential.
GenevisibleiP62317. MM.

Interactioni

Subunit structurei

U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP (By similarity).By similarity

Protein-protein interaction databases

BioGridi223486. 1 interaction.
IntActiP62317. 1 interaction.
MINTiMINT-124854.
STRINGi10090.ENSMUSP00000037597.

Structurei

3D structure databases

ProteinModelPortaliP62317.
SMRiP62317. Positions 10-116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP core protein family.Curated

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00390000017608.
HOGENOMiHOG000223545.
HOVERGENiHBG054415.
InParanoidiP62317.
KOiK11096.
OMAiCRNNHKL.
OrthoDBiEOG7HB5CJ.
PhylomeDBiP62317.
TreeFamiTF319595.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR027248. Sm_D2.
[Graphical view]
PANTHERiPTHR12777. PTHR12777. 1 hit.
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P62317-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLNKPKSE MTPEELQKRE EEEFNTGPLS VLTQSVKNNT QVLINCRNNK
60 70 80 90 100
KLLGRVKAFD RHCNMVLENV KEMWTEVPKS GKGKKKSKPV NKDRYISKMF
110
LRGDSVIVVL RNPLIAGK
Length:118
Mass (Da):13,527
Last modified:July 5, 2004 - v1
Checksum:iD986059D82B7E045
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311V → M in BAC32551 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007389 mRNA. Translation: BAB25006.1.
AK045968 mRNA. Translation: BAC32551.1.
AK088105 mRNA. Translation: BAC40147.1.
BC043014 mRNA. Translation: AAH43014.1.
BC051208 mRNA. Translation: AAH51208.1.
CCDSiCCDS20892.1.
RefSeqiNP_081219.1. NM_026943.1.
UniGeneiMm.29135.

Genome annotation databases

EnsembliENSMUST00000049294; ENSMUSP00000037597; ENSMUSG00000040824.
GeneIDi107686.
KEGGimmu:107686.
UCSCiuc009fkv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007389 mRNA. Translation: BAB25006.1.
AK045968 mRNA. Translation: BAC32551.1.
AK088105 mRNA. Translation: BAC40147.1.
BC043014 mRNA. Translation: AAH43014.1.
BC051208 mRNA. Translation: AAH51208.1.
CCDSiCCDS20892.1.
RefSeqiNP_081219.1. NM_026943.1.
UniGeneiMm.29135.

3D structure databases

ProteinModelPortaliP62317.
SMRiP62317. Positions 10-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223486. 1 interaction.
IntActiP62317. 1 interaction.
MINTiMINT-124854.
STRINGi10090.ENSMUSP00000037597.

PTM databases

PhosphoSiteiP62317.

Proteomic databases

MaxQBiP62317.
PaxDbiP62317.
PRIDEiP62317.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049294; ENSMUSP00000037597; ENSMUSG00000040824.
GeneIDi107686.
KEGGimmu:107686.
UCSCiuc009fkv.1. mouse.

Organism-specific databases

CTDi6633.
MGIiMGI:98345. Snrpd2.

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00390000017608.
HOGENOMiHOG000223545.
HOVERGENiHBG054415.
InParanoidiP62317.
KOiK11096.
OMAiCRNNHKL.
OrthoDBiEOG7HB5CJ.
PhylomeDBiP62317.
TreeFamiTF319595.

Enzyme and pathway databases

ReactomeiREACT_271571. mRNA Splicing - Minor Pathway.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_333207. snRNP Assembly.

Miscellaneous databases

NextBioi359250.
PROiP62317.
SOURCEiSearch...

Gene expression databases

BgeeiP62317.
CleanExiMM_SNRPD2.
ExpressionAtlasiP62317. baseline and differential.
GenevisibleiP62317. MM.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR027248. Sm_D2.
[Graphical view]
PANTHERiPTHR12777. PTHR12777. 1 hit.
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Pancreas and Thymus.
  2. "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].
    Strain: C57BL/6.
    Tissue: Brain and Mammary gland.

Entry informationi

Entry nameiSMD2_MOUSE
AccessioniPrimary (citable) accession number: P62317
Secondary accession number(s): P43330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.