SMD1_HUMAN - dbPTM
SMD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMD1_HUMAN
UniProt AC P62314
Protein Name Small nuclear ribonucleoprotein Sm D1
Gene Name SNRPD1
Organism Homo sapiens (Human).
Sequence Length 119
Subcellular Localization Cytoplasm, cytosol . Nucleus . SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.
Protein Description 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 a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA..
Protein Sequence MKLVRFLMKLSHETVTIELKNGTQVHGTITGVDVSMNTHLKAVKMTLKNREPVQLETLSIRGNNIRYFILPDSLPLDTLLVDVEPKVKSKKREAVAGRGRGRGRGRGRGRGRGRGGPRR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9UbiquitinationKLVRFLMKLSHETVT
HHHHHHHHHCCCEEE
49.32-
11PhosphorylationVRFLMKLSHETVTIE
HHHHHHHCCCEEEEE
17.4819664994
23PhosphorylationTIELKNGTQVHGTIT
EEEECCCCEEEEEEE
36.4920068231
28PhosphorylationNGTQVHGTITGVDVS
CCCEEEEEEEEEECC
10.6520068231
30PhosphorylationTQVHGTITGVDVSMN
CEEEEEEEEEECCCC
30.8720068231
35PhosphorylationTITGVDVSMNTHLKA
EEEEEECCCCHHHHE
11.2326074081
38PhosphorylationGVDVSMNTHLKAVKM
EEECCCCHHHHEEEE
21.6820068231
41AcetylationVSMNTHLKAVKMTLK
CCCCHHHHEEEEHHC
43.4625953088
44UbiquitinationNTHLKAVKMTLKNRE
CHHHHEEEEHHCCCC
30.9032142685
44AcetylationNTHLKAVKMTLKNRE
CHHHHEEEEHHCCCC
30.9025953088
442-HydroxyisobutyrylationNTHLKAVKMTLKNRE
CHHHHEEEEHHCCCC
30.90-
48UbiquitinationKAVKMTLKNREPVQL
HEEEEHHCCCCCEEE
44.8032015554
57MethylationREPVQLETLSIRGNN
CCCEEEEEEEECCCE
34.1010747894
57PhosphorylationREPVQLETLSIRGNN
CCCEEEEEEEECCCE
34.1030108239
59MethylationPVQLETLSIRGNNIR
CEEEEEEEECCCEEE
20.0510747894
59PhosphorylationPVQLETLSIRGNNIR
CEEEEEEEECCCEEE
20.0524719451
61MethylationQLETLSIRGNNIRYF
EEEEEEECCCEEEEE
38.11115917389
63MethylationETLSIRGNNIRYFIL
EEEEECCCEEEEEEC
30.7910747894
67PhosphorylationIRGNNIRYFILPDSL
ECCCEEEEEECCCCC
7.3818083107
69MethylationGNNIRYFILPDSLPL
CCEEEEEECCCCCCC
3.9610747894
71MethylationNIRYFILPDSLPLDT
EEEEEECCCCCCCCE
25.0710747894
73MethylationRYFILPDSLPLDTLL
EEEECCCCCCCCEEE
29.9110747894
73PhosphorylationRYFILPDSLPLDTLL
EEEECCCCCCCCEEE
29.9128464451
78PhosphorylationPDSLPLDTLLVDVEP
CCCCCCCEEEEECCH
29.6727732954
86SumoylationLLVDVEPKVKSKKRE
EEEECCHHHCCCCCH
49.1128112733
86UbiquitinationLLVDVEPKVKSKKRE
EEEECCHHHCCCCCH
49.1129967540
88UbiquitinationVDVEPKVKSKKREAV
EECCHHHCCCCCHHH
63.78-
98DimethylationKREAVAGRGRGRGRG
CCHHHCCCCCCCCCC
23.15-
98MethylationKREAVAGRGRGRGRG
CCHHHCCCCCCCCCC
23.1580700813
100DimethylationEAVAGRGRGRGRGRG
HHHCCCCCCCCCCCC
30.21-
100MethylationEAVAGRGRGRGRGRG
HHHCCCCCCCCCCCC
30.2180700819
102DimethylationVAGRGRGRGRGRGRG
HCCCCCCCCCCCCCC
30.21-
102MethylationVAGRGRGRGRGRGRG
HCCCCCCCCCCCCCC
30.2180700825
104MethylationGRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC
30.21134903
104DimethylationGRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC
30.21-
106DimethylationGRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC
30.21-
106MethylationGRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC
30.21134907
108DimethylationGRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC
30.21-
108MethylationGRGRGRGRGRGRGRG
CCCCCCCCCCCCCCC
30.21134911
110DimethylationGRGRGRGRGRGRGGP
CCCCCCCCCCCCCCC
30.21-
110MethylationGRGRGRGRGRGRGGP
CCCCCCCCCCCCCCC
30.21134915
112DimethylationGRGRGRGRGRGGPRR
CCCCCCCCCCCCCCC
30.21-
112MethylationGRGRGRGRGRGGPRR
CCCCCCCCCCCCCCC
30.212561025
114DimethylationGRGRGRGRGGPRR--
CCCCCCCCCCCCC--
45.60-
114MethylationGRGRGRGRGGPRR--
CCCCCCCCCCCCC--
45.602561023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SMD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMD1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SMD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM5_HUMANPRMT5physical
11713266
ICLN_HUMANCLNS1Aphysical
11713266
SMD2_HUMANSNRPD2physical
9417867
SMD2_HUMANSNRPD2physical
10025403
SMD2_HUMANSNRPD2physical
22939629
SMD3_HUMANSNRPD3physical
22939629
YBOX1_HUMANYBX1physical
22939629
U520_HUMANSNRNP200physical
22939629
U5S1_HUMANEFTUD2physical
22939629
U2AF2_HUMANU2AF2physical
22939629
TPR_HUMANTPRphysical
22939629
SNUT1_HUMANSART1physical
22939629
SPF27_HUMANBCAS2physical
22939629
TOP1_HUMANTOP1physical
22939629
UCHL3_HUMANUCHL3physical
22939629
TIF1B_HUMANTRIM28physical
22939629
SRP14_HUMANSRP14physical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
TEBP_HUMANPTGES3physical
22939629
U2AF1_HUMANU2AF1physical
22365833
LSM3_HUMANLSM3physical
22365833
ICLN_HUMANCLNS1Aphysical
22365833
IL7RA_HUMANIL7Rphysical
23151878
FERM2_HUMANFERMT2physical
22863883
ODPB_HUMANPDHBphysical
22863883
SCLY_HUMANSCLYphysical
22863883
MCFD2_HUMANMCFD2physical
26344197
PRP31_HUMANPRPF31physical
26344197
RCC2_HUMANRCC2physical
26344197
RUVB1_HUMANRUVBL1physical
26344197
SF3A1_HUMANSF3A1physical
26344197
SF3A3_HUMANSF3A3physical
26344197
SF3B3_HUMANSF3B3physical
26344197
RUXE_HUMANSNRPEphysical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMD1_HUMAN

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Related Literatures of Post-Translational Modification

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