SMD1_YEAST - dbPTM
SMD1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMD1_YEAST
UniProt AC Q02260
Protein Name Small nuclear ribonucleoprotein Sm D1
Gene Name SMD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 146
Subcellular Localization Nucleus.
Protein Description Involved in pre-mRNA splicing. Binds snRNA U1, U2, U4 and U5 which contain a highly conserved structural motif called the Sm binding site. Also binds telomerase RNA and is required for its accumulation..
Protein Sequence MKLVNFLKKLRNEQVTIELKNGTTVWGTLQSVSPQMNAILTDVKLTLPQPRLNKLNSNGIAMASLYLTGGQQPTASDNIASLQYINIRGNTIRQIILPDSLNLDSLLVDQKQLNSLRRSGQIANDPSKKRRRDFGAPANKRPRRGL
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
57PhosphorylationPRLNKLNSNGIAMAS
HHHHCCCCCCEEEEE
47.0429136822
64PhosphorylationSNGIAMASLYLTGGQ
CCCEEEEEEEECCCC
12.4029136822
66PhosphorylationGIAMASLYLTGGQQP
CEEEEEEEECCCCCC
10.3429136822
68PhosphorylationAMASLYLTGGQQPTA
EEEEEEECCCCCCCC
26.2129136822
74PhosphorylationLTGGQQPTASDNIAS
ECCCCCCCCCCCEEE
34.1629136822
76PhosphorylationGGQQPTASDNIASLQ
CCCCCCCCCCEEECE
33.4029136822
81PhosphorylationTASDNIASLQYINIR
CCCCCEEECEEEECC
16.5329136822
84PhosphorylationDNIASLQYINIRGNT
CCEEECEEEECCCCE
10.9629136822
91PhosphorylationYINIRGNTIRQIILP
EEECCCCEEEEEECC
21.9929136822
119PhosphorylationQLNSLRRSGQIANDP
HHHHHHHHCCCCCCC
28.7230377154
128AcetylationQIANDPSKKRRRDFG
CCCCCCCHHHHHCCC
56.5425381059
140AcetylationDFGAPANKRPRRGL-
CCCCCCCCCCCCCC-
66.9225381059

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_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMD1_YEAST !!

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_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RU2A_YEASTLEA1physical
11805826
PRP21_YEASTPRP21physical
11805826
PRP31_YEASTPRP31physical
11805826
PRP39_YEASTPRP39physical
11805826
PRP6_YEASTPRP6physical
11805826
PRP9_YEASTPRP9physical
11805826
RSMB_YEASTSMB1physical
11805826
SMD3_YEASTSMD3physical
11805826
SN114_YEASTSNU114physical
11805826
SNU56_YEASTSNU56physical
11805826
XPOT_YEASTLOS1physical
9207794
SAC7_YEASTSAC7physical
9207794
SLU7_YEASTSLU7physical
9207794
QDR3_YEASTQDR3physical
9207794
ARO8_YEASTARO8physical
9207794
RAV1_YEASTRAV1physical
9207794
PXA2_YEASTPXA2physical
9207794
SEC39_YEASTSEC39physical
9207794
LHP1_YEASTLHP1genetic
10747032
LSM2_YEASTLSM2physical
16554755
SNU71_YEASTSNU71physical
16554755
PRP40_YEASTPRP40physical
16554755
SMD3_YEASTSMD3physical
16554755
SMD2_YEASTSMD2physical
16554755
RUXE_YEASTSME1physical
16554755
RU2A_YEASTLEA1physical
16554755
BRR1_YEASTBRR1physical
16554755
RUXF_YEASTSMX3physical
16554755
BRR2_YEASTBRR2physical
16429126
RU2A_YEASTLEA1physical
16429126
PRP21_YEASTPRP21physical
16429126
PRP31_YEASTPRP31physical
16429126
PRP39_YEASTPRP39physical
16429126
PRP6_YEASTPRP6physical
16429126
PRP8_YEASTPRP8physical
16429126
PRP9_YEASTPRP9physical
16429126
RSMB_YEASTSMB1physical
16429126
SMD3_YEASTSMD3physical
16429126
SN114_YEASTSNU114physical
16429126
SNU56_YEASTSNU56physical
16429126
LOT5_YEASTLOT5physical
18719252

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMD1_YEAST

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Related Literatures of Post-Translational Modification

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