O75940 (SPF30_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Survival of motor neuron-related-splicing factor 30

Alternative name(s):
30 kDa splicing factor SMNrp
SMN-related protein
Survival motor neuron domain-containing protein 1

Gene names

Name:	SMNDC1
Synonyms:	SMNR, SPF30

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	238 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Necessary for spliceosome assembly. Overexpression causes apoptosis. Ref.6 Ref.7 Ref.8
Subunit structure	Associates with spliceosomes. Associates with U4/U5/U6 tri-snRNP and with U2 snRNP.
Subcellular location	Nucleus speckle. Nucleus › Cajal body. Note: Detected in nuclear speckles containing snRNP and in Cajal (coiled) bodies. Ref.6 Ref.8
Tissue specificity	Detected at intermediate levels in skeletal muscle, and at low levels in heart and pancreas. Ref.6
Sequence similarities	Belongs to the SMN family. Contains 1 Tudor domain.

Ontologies

Keywords
Biological process	Apoptosis mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	RNA splicing, via transesterification reactions Traceable author statement Ref.1. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis Traceable author statement. Source: ProtInc mRNA processing Traceable author statement. Source: ProtInc
Cellular component	Cajal body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: InterPro nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Traceable author statement. Source: ProtInc
Molecular function	RNA binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KPNB1	Q14974	2	EBI-1052641,EBI-286758

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 238	238	Survival of motor neuron-related-splicing factor 30		PRO_0000218908
Regions
	Domain	72 – 132	61	Tudor
	Motif	142 – 160	19	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	201	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	219	1	N6-acetyllysine Ref.13

Sequences

	Sequence		Length	Mass (Da)
	O75940 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 7F60852AD4D1F53A	FASTA	238	26,711
	10 20 30 40 50 60 MSEDLAKQLA SYKAQLQQVE AALSGNGENE DLLKLKKDLQ EVIELTKDLL STQPSETLAS 70 80 90 100 110 120 SDSFASTQPT HSWKVGDKCM AVWSEDGQCY EAEIEEIDEE NGTAAITFAG YGNAEVTPLL 130 140 150 160 170 180 NLKPVEEGRK AKEDSGNKPM SKKEMIAQQR EYKKKKALKK AQRIKELEQE REDQKVKWQQ 190 200 210 220 230 FNNRAYSKNK KGQVKRSIFA SPESVTGKVG VGTCGIADKP MTQYQDTSKY NVRHLMPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex." Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M. Nat. Genet. 20:46-50(1998) [PubMed: 9731529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
[2]	"Isolating and cloning HSP cDNA." Chen J.H., Luo W.Q., Zhou Y., Huang X.W., Yuan J.G., Qiang B.Q. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Characterization of a gene encoding survival motor neuron (SMN)-related protein, a constituent of the spliceosome complex." Talbot K., Miguel-Aliaga I., Mohaghegh P., Ponting C.P., Davies K.E. Hum. Mol. Genet. 7:2149-2156(1998) [PubMed: 9817934] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]	"SMNrp is an essential pre-mRNA splicing factor required for the formation of the mature spliceosome." Meister G., Hannus S., Ploettner O., Baars T., Hartmann E., Fakan S., Laggerbauer B., Fischer U. EMBO J. 20:2304-2314(2001) [PubMed: 11331595] [Abstract] Cited for: FUNCTION, INTERACTION WITH THE SPLICEOSOME; U2 SNRNP AND U4/U5/U6 TRI-SNRNP.
[8]	"SPF30 is an essential human splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome." Rappsilber J., Ajuh P., Lamond A.I., Mann M. J. Biol. Chem. 276:31142-31150(2001) [PubMed: 11331295] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE SPLICEOSOME; WITH U2 SNRNP AND WITH U4/U5/U6 TRI-SNRNP.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219, MASS SPECTROMETRY.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF083385 mRNA. Translation: AAC64086.1.
AF107463 mRNA. Translation: AAC84148.1.
AL360182 Genomic DNA. Translation: CAI15482.1.
CH471066 Genomic DNA. Translation: EAW49561.1.
CH471066 Genomic DNA. Translation: EAW49562.1.
CH471066 Genomic DNA. Translation: EAW49564.1.
BC011234 mRNA. Translation: AAH11234.1.

IPI

IPI00025176.

RefSeq

NP_005862.1. NM_005871.3.

UniGene

Hs.632093.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A4F	NMR	-	A	65-128	[»]
4A4H	NMR	-	A	65-128	[»]

ProteinModelPortal

O75940.

SMR

O75940. Positions 71-126.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75940. 2 interactions.

MINT

MINT-4527315.

STRING

O75940.

PTM databases

PhosphoSite

O75940.

Proteomic databases

PeptideAtlas

O75940.

PRIDE

O75940.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369592; ENSP00000358605; ENSG00000119953.
ENST00000369603; ENSP00000358616; ENSG00000119953.

GeneID

10285.

KEGG

hsa:10285.

UCSC

uc001kzb.1. human.

Organism-specific databases

CTD

10285.

GeneCards

GC10M112042.

H-InvDB

HIX0009196.

HGNC

HGNC:16900. SMNDC1.

MIM

603519. gene.

neXtProt

NX_O75940.

PharmGKB

PA134990780.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07775.

GeneTree

ENSGT00560000077236.

HOGENOM

HBG280247.

HOVERGEN

HBG057021.

InParanoid

O75940.

OMA

GQYYDAT.

OrthoDB

EOG4H464Q.

PhylomeDB

O75940.

Gene expression databases

ArrayExpress

O75940.

Bgee

O75940.

CleanEx

HS_SMNDC1.

Genevestigator

O75940.

GermOnline

ENSG00000119953. Homo sapiens.

Family and domain databases

InterPro

IPR010304. Survival_motor_neuron.
IPR002999. Tudor.
IPR018351. Tudor_subgr.
[Graphical view]

KO

K12839.

Pfam

PF06003. SMN. 1 hit.
[Graphical view]

SMART

SM00333. TUDOR. 1 hit.
[Graphical view]

PROSITE

PS50304. TUDOR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

38968.

SOURCE

Search...

Entry information

Entry name

SPF30_HUMAN

Accession

Primary (citable) accession number: O75940
Secondary accession number(s): D3DRB1, Q5T3K6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2003
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.