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Protein

Small nuclear ribonucleoprotein Sm D3

Gene

SNRPD3

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

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. As part of the U7 snRNP it is involved in histone 3'-end processing.2 Publications

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • histone pre-mRNA DCP binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Small nuclear ribonucleoprotein Sm D3
Short name:
Sm-D3
Alternative name(s):
snRNP core protein D3
Gene namesi
Name:SNRPD3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11160. SNRPD3.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • methylosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • pICln-Sm protein complex Source: UniProtKB
  • small nuclear ribonucleoprotein complex Source: ProtInc
  • SMN-Sm protein complex Source: UniProtKB
  • spliceosomal complex Source: ProtInc
  • U12-type spliceosomal complex Source: UniProtKB
  • U1 snRNP Source: UniProtKB
  • U4 snRNP Source: UniProtKB
  • U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36001.

Polymorphism and mutation databases

DMDMi51338667.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 126125Small nuclear ribonucleoprotein Sm D3PRO_0000122214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Post-translational modificationi

Methylated on arginine residues by PRMT5 and PRMT7; probable asymmetric dimethylation which is required for assembly and biogenesis of snRNPs.2 Publications

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiP62318.
PaxDbiP62318.
PeptideAtlasiP62318.
PRIDEiP62318.

PTM databases

PhosphoSiteiP62318.

Expressioni

Gene expression databases

BgeeiP62318.
CleanExiHS_SNRPD3.
ExpressionAtlasiP62318. baseline and differential.
GenevisibleiP62318. HS.

Organism-specific databases

HPAiHPA001170.

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. Component of the U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. 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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLNS1AP541056EBI-372789,EBI-724693
LSM7Q9UK453EBI-372789,EBI-348372
SNRPBP146782EBI-372789,EBI-372458

Protein-protein interaction databases

BioGridi112518. 95 interactions.
DIPiDIP-31216N.
IntActiP62318. 39 interactions.
MINTiMINT-5002679.
STRINGi9606.ENSP00000215829.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127Combined sources
Turni13 – 153Combined sources
Beta strandi16 – 227Combined sources
Beta strandi27 – 359Combined sources
Beta strandi37 – 393Combined sources
Beta strandi41 – 499Combined sources
Beta strandi55 – 639Combined sources
Helixi65 – 673Combined sources
Beta strandi68 – 736Combined sources
Helixi75 – 795Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3BX-ray2.00A/C/E/G/I/K1-75[»]
3CW1X-ray5.49D/S/T/U1-126[»]
3PGWX-ray4.40W/Z1-126[»]
3VRIX-ray1.60C54-63[»]
4PJOX-ray3.30A/O/a/o1-126[»]
4WZJX-ray3.60AD/AK/AR/BD/BK/BR/CD/CK/CR/DD/DK/DR1-126[»]
ProteinModelPortaliP62318.
SMRiP62318. Positions 1-84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62318.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati110 – 11121
Repeati112 – 11322
Repeati114 – 11523
Repeati116 – 11724
Repeati118 – 11925

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni110 – 119105 X 2 AA tandem repeats of [RM]-G

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi84 – 12643Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the snRNP core protein family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00610000086153.
HOGENOMiHOG000182712.
HOVERGENiHBG105305.
InParanoidiP62318.
KOiK11088.
OMAiIMRANAR.
OrthoDBiEOG7VTDQF.
PhylomeDBiP62318.
TreeFamiTF354302.

Family and domain databases

InterProiIPR027141. LSm4/Sm_D1/D3.
IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PANTHERiPTHR23338. PTHR23338. 1 hit.
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. AlignAdd to basket

Isoform 1 (identifier: P62318-1) [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
MSIGVPIKVL HEAEGHIVTC ETNTGEVYRG KLIEAEDNMN CQMSNITVTY
60 70 80 90 100
RDGRVAQLEQ VYIRGSKIRF LILPDMLKNA PMLKSMKNKN QGSGAGRGKA
110 120
AILKAQVAAR GRGRGMGRGN IFQKRR
Length:126
Mass (Da):13,916
Last modified:July 5, 2004 - v1
Checksum:i59A6E78E860AA3E0
GO
Isoform 2 (identifier: P62318-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     107-126: VAARGRGRGMGRGNIFQKRR → GYLSSLEWVLVHIC

Note: No experimental confirmation available.
Show »
Length:120
Mass (Da):13,292
Checksum:iFAEF4075E9ED6E9D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei107 – 12620VAARG…FQKRR → GYLSSLEWVLVHIC in isoform 2. 1 PublicationVSP_056478Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15009 mRNA. Translation: AAA57034.1.
CR456583 mRNA. Translation: CAG30469.1.
AK296173 mRNA. Translation: BAG58909.1.
AB451249 mRNA. Translation: BAG70063.1.
AB451373 mRNA. Translation: BAG70187.1.
AP000356 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59670.1.
BC000457 mRNA. Translation: AAH00457.1.
BC003150 mRNA. Translation: AAH03150.1.
CCDSiCCDS13828.1. [P62318-1]
RefSeqiNP_001265585.1. NM_001278656.1. [P62318-1]
NP_004166.1. NM_004175.4. [P62318-1]
UniGeneiHs.356549.

Genome annotation databases

EnsembliENST00000215829; ENSP00000215829; ENSG00000100028. [P62318-1]
ENST00000402849; ENSP00000385266; ENSG00000100028. [P62318-2]
ENST00000404603; ENSP00000456090; ENSG00000100028. [P62318-1]
GeneIDi6634.
KEGGihsa:6634.
UCSCiuc003aam.1. human. [P62318-1]
uc011aju.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15009 mRNA. Translation: AAA57034.1.
CR456583 mRNA. Translation: CAG30469.1.
AK296173 mRNA. Translation: BAG58909.1.
AB451249 mRNA. Translation: BAG70063.1.
AB451373 mRNA. Translation: BAG70187.1.
AP000356 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW59670.1.
BC000457 mRNA. Translation: AAH00457.1.
BC003150 mRNA. Translation: AAH03150.1.
CCDSiCCDS13828.1. [P62318-1]
RefSeqiNP_001265585.1. NM_001278656.1. [P62318-1]
NP_004166.1. NM_004175.4. [P62318-1]
UniGeneiHs.356549.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3BX-ray2.00A/C/E/G/I/K1-75[»]
3CW1X-ray5.49D/S/T/U1-126[»]
3PGWX-ray4.40W/Z1-126[»]
3VRIX-ray1.60C54-63[»]
4PJOX-ray3.30A/O/a/o1-126[»]
4WZJX-ray3.60AD/AK/AR/BD/BK/BR/CD/CK/CR/DD/DK/DR1-126[»]
ProteinModelPortaliP62318.
SMRiP62318. Positions 1-84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112518. 95 interactions.
DIPiDIP-31216N.
IntActiP62318. 39 interactions.
MINTiMINT-5002679.
STRINGi9606.ENSP00000215829.

PTM databases

PhosphoSiteiP62318.

Polymorphism and mutation databases

DMDMi51338667.

Proteomic databases

MaxQBiP62318.
PaxDbiP62318.
PeptideAtlasiP62318.
PRIDEiP62318.

Protocols and materials databases

DNASUi6634.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215829; ENSP00000215829; ENSG00000100028. [P62318-1]
ENST00000402849; ENSP00000385266; ENSG00000100028. [P62318-2]
ENST00000404603; ENSP00000456090; ENSG00000100028. [P62318-1]
GeneIDi6634.
KEGGihsa:6634.
UCSCiuc003aam.1. human. [P62318-1]
uc011aju.2. human.

Organism-specific databases

CTDi6634.
GeneCardsiGC22P024951.
HGNCiHGNC:11160. SNRPD3.
HPAiHPA001170.
MIMi601062. gene.
neXtProtiNX_P62318.
PharmGKBiPA36001.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00610000086153.
HOGENOMiHOG000182712.
HOVERGENiHBG105305.
InParanoidiP62318.
KOiK11088.
OMAiIMRANAR.
OrthoDBiEOG7VTDQF.
PhylomeDBiP62318.
TreeFamiTF354302.

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSNRPD3. human.
EvolutionaryTraceiP62318.
GeneWikiiSNRPD3.
GenomeRNAii6634.
NextBioi25845.
PROiP62318.
SOURCEiSearch...

Gene expression databases

BgeeiP62318.
CleanExiHS_SNRPD3.
ExpressionAtlasiP62318. baseline and differential.
GenevisibleiP62318. HS.

Family and domain databases

InterProiIPR027141. LSm4/Sm_D1/D3.
IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PANTHERiPTHR23338. PTHR23338. 1 hit.
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction."
    Lehmeier T., Raker V., Hermann H., Luehrmann R.
    Proc. Natl. Acad. Sci. U.S.A. 91:12317-12321(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORM 2).
    Tissue: Thalamus.
  4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Lung.
  8. "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln."
    Meister G., Eggert C., Buehler D., Brahms H., Kambach C., Fischer U.
    Curr. Biol. 11:1990-1994(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION.
  9. "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein."
    Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.
    EMBO J. 20:5470-5479(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE U7 SNRNP COMPLEX.
  10. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  11. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
    Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
    RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins."
    Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I., Matera A.G.
    J. Cell Biol. 178:733-740(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION, INTERACTION WITH PRMT5 AND PRMT7.
  13. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
    Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
    Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX, SUBCELLULAR LOCATION.
  14. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs."
    Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., Raker V.A., Luehrmann R., Li J., Nagai K.
    Cell 96:375-387(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4-75 IN COMPLEX WITH SNRPB.
  17. "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
    Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
    Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP.
  18. "Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis."
    Leung A.K., Nagai K., Li J.
    Nature 473:536-539(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP.

Entry informationi

Entry nameiSMD3_HUMAN
AccessioniPrimary (citable) accession number: P62318
Secondary accession number(s): B4DJP7, B5BU13, P43331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 123 of the entry and version 1 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

Miscellaneous

In the autoimmune disease systemic lupus erythematosus, antinuclear antibodies are developed with Sm specificity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.