Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Survival motor neuron protein  

UniProtKB / Swiss-Prot ID :  SMN_HUMAN

Gene Name (Synonyms) : 
SMN1, SMN, SMNT
SMN2, SMNC  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus, gem. Note=Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems). 

Protein Function :  The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm and is required for pre-mRNA splicing in the nucleus. It may also play a role in the metabolism of snoRNPs. 

Protein Sequence MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETSGKPKTTP...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCEEEECCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
2A -> G (in SMA2 and SMA3). VAR_005615
30D -> N (in SMA2). VAR_034803
44D -> V (in SMA3). VAR_034804
95G -> R (in SMA3; reduces SMN binding toSm proteins).
111A -> G (in SMA2; reduces SMN binding toSm proteins).
116I -> F (in SMA1). VAR_034807
136Q -> E (in SMA1). VAR_034808
245P -> L (in SMA3). VAR_010051
262S -> G (in SMA3). VAR_034809
262S -> I (in SMA3). VAR_005616
272Y -> C (in SMA1). VAR_005617
274T -> I (in SMA2 and SMA3). VAR_005618
275G -> S (in SMA3). VAR_005619
279G -> C (in SMA2 and SMA3). VAR_007990
279G -> V (in SMA1). VAR_005620
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAMSSG
---CCCCCC
13.43UniProtKB
Link-
4Phosphoserine-MAMSSGGS
-CCCCCCCC
19.12HPRD
Link-
4Phosphoserine-MAMSSGGS
-CCCCCCCC
19.12PhosphoELM
Link-
4Phosphoserine-MAMSSGGS
-CCCCCCCC
19.12Phosphositeplus
Link-
4Phosphoserine-MAMSSGGS
-CCCCCCCC
19.12SysPTM
Link-
4Phosphoserine; by PKA.-MAMSSGGS
-CCCCCCCC
19.12UniProtKB
Link-
5PhosphoserineMAMSSGGSG
CCCCCCCCC
33.80HPRD
Link-
5PhosphoserineMAMSSGGSG
CCCCCCCCC
33.80PhosphoELM
Link-
5PhosphoserineMAMSSGGSG
CCCCCCCCC
33.80Phosphositeplus
Link-
5PhosphoserineMAMSSGGSG
CCCCCCCCC
33.80SysPTM
Link-
5Phosphoserine; by PKA.MAMSSGGSG
CCCCCCCCC
33.80UniProtKB
Link-
8PhosphoserineSSGGSGGGV
CCCCCCCCC
37.48HPRD
Link-
8PhosphoserineSSGGSGGGV
CCCCCCCCC
37.48PhosphoELM
Link-
8PhosphoserineSSGGSGGGV
CCCCCCCCC
37.48Phosphositeplus
Link-
8PhosphoserineSSGGSGGGV
CCCCCCCCC
37.48SysPTM
Link-
8Phosphoserine; by PKA.SSGGSGGGV
CCCCCCCCC
37.48UniProtKB
Link-
18PhosphoserineEQEDSVLFR
CCCCCEEEE
21.70HPRD
Link-
18PhosphoserineEQEDSVLFR
CCCCCEEEE
21.70Phosphositeplus
Link-
25PhosphothreonineFRRGTGQSD
EECCCCCCC
30.18HPRD
Link-
25PhosphothreonineFRRGTGQSD
EECCCCCCC
30.18HPRD
Link-
25PhosphothreonineFRRGTGQSD
EECCCCCCC
30.18PhosphoELM
Link-
25PhosphothreonineFRRGTGQSD
EECCCCCCC
30.18Phosphositeplus
Link-
25PhosphothreonineFRRGTGQSD
EECCCCCCC
30.18SysPTM
Link-
25Phosphothreonine.FRRGTGQSD
EECCCCCCC
30.18UniProtKB
Link-
28PhosphoserineGTGQSDDSD
CCCCCCCCC
44.74HPRD
Link-
28PhosphoserineGTGQSDDSD
CCCCCCCCC
44.74HPRD
Link-
28PhosphoserineGTGQSDDSD
CCCCCCCCC
44.74PhosphoELM
Link-
28PhosphoserineGTGQSDDSD
CCCCCCCCC
44.74Phosphositeplus
Link-
28PhosphoserineGTGQSDDSD
CCCCCCCCC
44.74SysPTM
Link-
28Phosphoserine.GTGQSDDSD
CCCCCCCCC
44.74UniProtKB
Link-
31PhosphoserineQSDDSDIWD
CCCCCCHHH
35.67HPRD
Link-
31PhosphoserineQSDDSDIWD
CCCCCCHHH
35.67HPRD
Link-
31PhosphoserineQSDDSDIWD
CCCCCCHHH
35.67PhosphoELM
Link-
31PhosphoserineQSDDSDIWD
CCCCCCHHH
35.67Phosphositeplus
Link-
31PhosphoserineQSDDSDIWD
CCCCCCHHH
35.67SysPTM
Link-
31Phosphoserine.QSDDSDIWD
CCCCCCHHH
35.67UniProtKB
Link-
37PhosphothreonineIWDDTALIK
HHHHHHHHH
22.38HPRD
Link-
37PhosphothreonineIWDDTALIK
HHHHHHHHH
22.38Phosphositeplus
Link-
41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TALIKAYDK
HHHHHHHHH
41.57Phosphositeplus
Link-
43PhosphotyrosineLIKAYDKAV
HHHHHHHHH
16.99Phosphositeplus
Link-
69PhosphothreonineKPKTTPKRK
CCCCCCCCC
32.70HPRD
Link-
69PhosphothreonineKPKTTPKRK
CCCCCCCCC
32.70PhosphoELM
Link-
85PhosphothreonineQKKNTAASL
HHHHHCCCC
32.26Phosphositeplus
Link-
85Phosphothreonine; by PKA.QKKNTAASL
HHHHHCCCC
32.26UniProtKB
Link-
109PhosphotyrosineDGCIYPATI
CCCEEHHHH
7.29Phosphositeplus
Link
127PhosphotyrosineCVVVYTGYG
EEEEEECCC
5.26Phosphositeplus
Link
130PhosphotyrosineVYTGYGNRE
EEECCCCHH
11.92Phosphositeplus
Link
187PhosphoserineIKPKSAPWN
CCCCCCCCC
48.36Phosphositeplus
Link-
187Phosphoserine; by PKA.IKPKSAPWN
CCCCCCCCC
48.36UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GDF9_HUMANphysical interactionMINT-64288MINT16169070
SNRPA_HUMANphysical interactionMINT-14308MINT9323129
FBRL_HUMANphysical interactionMINT-18107MINT8670859
FBRL_HUMANphysical interactionMINT-18106MINT11509230
FBRL_HUMANphysical interactionMINT-18105MINT11509230
BAT3_HUMANphysical interactionMINT-64291MINT16169070
RUXG_HUMANphysical interactionMINT-13668MINT9323129
HNRPU_HUMANphysical interactionMINT-18162MINT8670859
TIAR_HUMANphysical interactionMINT-50603MINT15304326
SMN_HUMANphysical interactionMINT-68482MINT16189514
SMN_HUMANphysical interactionMINT-19077MINT8670859
CSN6_HUMANphysical interactionMINT-64290MINT16169070
LENG8_HUMANphysical interactionMINT-67330MINT16189514
GEMI5_HUMANphysical interactionMINT-50340MINT11714716
GEMI5_HUMANphysical interactionMINT-50341MINT11714716
GEMI7_HUMANphysical interactionMINT-49999MINT12065586
GEMI7_HUMANphysical interactionMINT-50005MINT12065586
CA103_HUMANphysical interactionMINT-64292MINT16169070
DDX20_HUMANphysical interactionMINT-13634MINT10601333
SMN_HUMANphysical interactionEBI-760456
intact16189514
RIF1_HUMANphysical interactionEBI-729327
intact16169070
BAT3_HUMANphysical interactionEBI-730831
intact16169070
UN119_HUMANphysical interactionEBI-730834
intact16169070
CSN6_HUMANphysical interactionEBI-733331
intact16169070
GDF9_HUMANphysical interactionEBI-733334
intact16169070
LENG8_HUMANphysical interactionEBI-756709
intact16189514
CH032_HUMANphysical interactionEBI-760117
intact16189514
GEMI2_HUMANphysical interaction
physical interaction
EBI-443699
EBI-443665
intact11714716
11714716
GEMI5_HUMANphysical interaction
physical interaction
physical interaction
colocalization
physical interaction
physical interaction
physical interacti
EBI-443699
EBI-443694
EBI-443
intact11714716
11714716
11714716
11714716
11714716
11714716
11714716
GEMI4_HUMANphysical interactionEBI-443665
intact11714716
FBRL_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:02646HPRD11509230
8670859
BCL2_HUMANin vitro
yeast 2-hybrid
HPRD:02646HPRD9389483
P53_HUMANin vitro
in vivo
HPRD:02646HPRD11704667
RSMB_HUMANin vitro
in vivo
HPRD:02646HPRD11720283
9323129
P80C_HUMANin vitro
in vivo
HPRD:02646HPRD12361597
11641277
SMN_HUMANin vivo
yeast 2-hybrid
HPRD:02646HPRD8670859
16189514
CH032_HUMANyeast 2-hybridHPRD:02646HPRD16189514
CA103_HUMANyeast 2-hybridHPRD:02646HPRD16169070
UN119_HUMANyeast 2-hybridHPRD:02646HPRD16169070
CSN6_HUMANyeast 2-hybridHPRD:02646HPRD16169070
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Disease Reference
Kegg disease
OMIM disease
253300Spinal muscular atrophy 1 (SMA1)
253550Spinal muscular atrophy 2 (SMA2)
253400Spinal muscular atrophy 3 (SMA3)
271150Spinal muscular atrophy 4 (SMA4)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-5; SER-8; SER-28AND SER-31, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-25; SER-28 ANDSER-31, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31,AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-25; SER-28 AND SER-31, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-5; SER-8; THR-25;SER-28 AND SER-31, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-28 AND SER-31,AND MASS SPECTROMETRY.
"Identification of the phosphorylation sites in the survival motorneuron protein by protein kinase A.";
Wu C.Y., Curtis A., Choi Y.S., Maeda M., Xu M.J., Berg A., Joneja U.,Mason R.W., Lee K.H., Wang W.;
Biochim. Biophys. Acta 1814:1134-1139(2011).
Cited for: PHOSPHORYLATION AT SER-4; SER-5; SER-8; THR-85 AND SER-187 BY PKA.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures