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Protein

Small nuclear ribonucleoprotein Sm D2

Gene

SNRPD2

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.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. ncRNA metabolic process Source: Reactome
  4. RNA splicing Source: Reactome
  5. spliceosomal complex assembly Source: ProtInc
  6. spliceosomal snRNP assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

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
Synonyms:SNRPD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11159. SNRPD2.

Subcellular locationi

  1. Cytoplasmcytosol 1 Publication
  2. Nucleus 1 Publication

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

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. methylosome Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. pICln-Sm protein complex Source: UniProtKB
  7. small nuclear ribonucleoprotein complex Source: ProtInc
  8. SMN-Sm protein complex Source: UniProtKB
  9. spliceosomal complex Source: ProtInc
  10. U12-type spliceosomal complex Source: UniProtKB
  11. U1 snRNP Source: UniProtKB
  12. U4 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36000.

Polymorphism and mutation databases

BioMutaiSNRPD2.
DMDMi51338666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 118117Small nuclear ribonucleoprotein Sm D2PRO_0000122207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei12 – 121Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62316.
PaxDbiP62316.
PeptideAtlasiP62316.
PRIDEiP62316.

PTM databases

PhosphoSiteiP62316.

Expressioni

Gene expression databases

BgeeiP62316.
CleanExiHS_SNRPD1.
HS_SNRPD2.
ExpressionAtlasiP62316. baseline and differential.
GenevestigatoriP62316.

Organism-specific databases

HPAiHPA041437.

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP70Q8NHQ13EBI-297993,EBI-739624
CLNS1AP541058EBI-297993,EBI-724693
LSM2Q9Y3333EBI-297993,EBI-347416

Protein-protein interaction databases

BioGridi112517. 105 interactions.
DIPiDIP-31219N.
IntActiP62316. 35 interactions.
MINTiMINT-5002672.
STRINGi9606.ENSP00000342374.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 273Combined sources
Helixi28 – 3811Combined sources
Beta strandi41 – 466Combined sources
Beta strandi51 – 599Combined sources
Beta strandi65 – 739Combined sources
Beta strandi94 – 1018Combined sources
Helixi103 – 1053Combined sources
Beta strandi106 – 1116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B34X-ray2.50B1-118[»]
3CW1X-ray5.49C/P/Q/R1-118[»]
3PGWX-ray4.40V/Y1-118[»]
3S6NX-ray2.50B1-118[»]
4F7UX-ray1.90B/D1-118[»]
4PJOX-ray3.30D/R/d/r1-118[»]
4V98X-ray3.10AB/AJ/AR/AZ/Ah/Ap/Ax/BB/BJ/BR/BZ/Bh/Bp/Bx/CB/CJ/CR/CZ/Ch/Cp1-118[»]
4WZJX-ray3.60AC/AJ/AQ/BC/BJ/BQ/CC/CJ/CQ/DC/DJ/DQ1-118[»]
ProteinModelPortaliP62316.
SMRiP62316. Positions 12-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62316.

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP core protein family.Curated

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00390000017608.
HOGENOMiHOG000223545.
HOVERGENiHBG054415.
InParanoidiP62316.
KOiK11096.
OMAiCRNNHKL.
OrthoDBiEOG7HB5CJ.
PhylomeDBiP62316.
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.

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: P62316-1) [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
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
Isoform 2 (identifier: P62316-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: Missing.

Note: No experimental confirmation available.

Show »
Length:108
Mass (Da):12,399
Checksum:i3E92B3D47F961A7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381N → S in BU531743 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1010Missing in isoform 2. 1 PublicationVSP_045371

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15008 mRNA. Translation: AAC13776.1.
AK291912 mRNA. Translation: BAF84601.1.
AC007191 Genomic DNA. Translation: AAD22673.1.
CH471126 Genomic DNA. Translation: EAW57373.1.
CH471126 Genomic DNA. Translation: EAW57374.1.
BC000486 mRNA. Translation: AAH00486.1.
BC001930 mRNA. Translation: AAH01930.1.
BU531743 mRNA. No translation available.
CCDSiCCDS33053.1. [P62316-1]
CCDS54281.1. [P62316-2]
PIRiI38861.
RefSeqiNP_004588.1. NM_004597.5. [P62316-1]
NP_808210.2. NM_177542.2. [P62316-2]
XP_005259237.1. XM_005259180.1. [P62316-1]
UniGeneiHs.515472.

Genome annotation databases

EnsembliENST00000342669; ENSP00000342374; ENSG00000125743. [P62316-1]
ENST00000391932; ENSP00000375798; ENSG00000125743. [P62316-2]
ENST00000587367; ENSP00000465952; ENSG00000125743. [P62316-2]
ENST00000588301; ENSP00000465216; ENSG00000125743. [P62316-1]
ENST00000588599; ENSP00000466152; ENSG00000125743. [P62316-2]
GeneIDi6633.
KEGGihsa:6633.
UCSCiuc002pcv.3. human. [P62316-1]

Polymorphism and mutation databases

BioMutaiSNRPD2.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15008 mRNA. Translation: AAC13776.1.
AK291912 mRNA. Translation: BAF84601.1.
AC007191 Genomic DNA. Translation: AAD22673.1.
CH471126 Genomic DNA. Translation: EAW57373.1.
CH471126 Genomic DNA. Translation: EAW57374.1.
BC000486 mRNA. Translation: AAH00486.1.
BC001930 mRNA. Translation: AAH01930.1.
BU531743 mRNA. No translation available.
CCDSiCCDS33053.1. [P62316-1]
CCDS54281.1. [P62316-2]
PIRiI38861.
RefSeqiNP_004588.1. NM_004597.5. [P62316-1]
NP_808210.2. NM_177542.2. [P62316-2]
XP_005259237.1. XM_005259180.1. [P62316-1]
UniGeneiHs.515472.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B34X-ray2.50B1-118[»]
3CW1X-ray5.49C/P/Q/R1-118[»]
3PGWX-ray4.40V/Y1-118[»]
3S6NX-ray2.50B1-118[»]
4F7UX-ray1.90B/D1-118[»]
4PJOX-ray3.30D/R/d/r1-118[»]
4V98X-ray3.10AB/AJ/AR/AZ/Ah/Ap/Ax/BB/BJ/BR/BZ/Bh/Bp/Bx/CB/CJ/CR/CZ/Ch/Cp1-118[»]
4WZJX-ray3.60AC/AJ/AQ/BC/BJ/BQ/CC/CJ/CQ/DC/DJ/DQ1-118[»]
ProteinModelPortaliP62316.
SMRiP62316. Positions 12-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112517. 105 interactions.
DIPiDIP-31219N.
IntActiP62316. 35 interactions.
MINTiMINT-5002672.
STRINGi9606.ENSP00000342374.

PTM databases

PhosphoSiteiP62316.

Polymorphism and mutation databases

BioMutaiSNRPD2.
DMDMi51338666.

Proteomic databases

MaxQBiP62316.
PaxDbiP62316.
PeptideAtlasiP62316.
PRIDEiP62316.

Protocols and materials databases

DNASUi6633.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342669; ENSP00000342374; ENSG00000125743. [P62316-1]
ENST00000391932; ENSP00000375798; ENSG00000125743. [P62316-2]
ENST00000587367; ENSP00000465952; ENSG00000125743. [P62316-2]
ENST00000588301; ENSP00000465216; ENSG00000125743. [P62316-1]
ENST00000588599; ENSP00000466152; ENSG00000125743. [P62316-2]
GeneIDi6633.
KEGGihsa:6633.
UCSCiuc002pcv.3. human. [P62316-1]

Organism-specific databases

CTDi6633.
GeneCardsiGC19M046190.
HGNCiHGNC:11159. SNRPD2.
HPAiHPA041437.
MIMi601061. gene.
neXtProtiNX_P62316.
PharmGKBiPA36000.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00390000017608.
HOGENOMiHOG000223545.
HOVERGENiHBG054415.
InParanoidiP62316.
KOiK11096.
OMAiCRNNHKL.
OrthoDBiEOG7HB5CJ.
PhylomeDBiP62316.
TreeFamiTF319595.

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSNRPD2. human.
EvolutionaryTraceiP62316.
GenomeRNAii6633.
NextBioi25839.
PROiP62316.
SOURCEiSearch...

Gene expression databases

BgeeiP62316.
CleanExiHS_SNRPD1.
HS_SNRPD2.
ExpressionAtlasiP62316. baseline and differential.
GenevestigatoriP62316.

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

« 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), PROTEIN SEQUENCE OF 75-96 AND 103-118.
  2. "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 1).
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORMS 1 AND 2).
    Tissue: Lung.
  6. Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.
    Submitted (FEB-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-47; 72-79 AND 103-118, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma and Mammary carcinoma.
  7. "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.
  8. "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.
  9. "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.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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 (2.5 ANGSTROMS) OF 26-118 IN COMPLEX WITH SNRPD1.
  15. "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.
  16. "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.
  17. "Structural basis of assembly chaperone-mediated snRNP formation."
    Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K., Stark H., Schindelin H., Fischer U.
    Mol. Cell 49:692-703(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN 6S PICLN-SM COMPLEX, FUNCTION IN CORE U1 SNRNP BIOGENESIS.

Entry informationi

Entry nameiSMD2_HUMAN
AccessioniPrimary (citable) accession number: P62316
Secondary accession number(s): A8K797, J3KPM5, P43330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 124 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 19
    Human chromosome 19: 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.