LSM5_HUMAN - dbPTM
LSM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSM5_HUMAN
UniProt AC Q9Y4Y9
Protein Name U6 snRNA-associated Sm-like protein LSm5
Gene Name LSM5
Organism Homo sapiens (Human).
Sequence Length 91
Subcellular Localization Nucleus.
Protein Description Plays a role in U6 snRNP assembly and function. Binds to the 3' end of U6 snRNA, thereby facilitating formation of the spliceosomal U4/U6 duplex formation in vitro..
Protein Sequence MAANATTNPSQLLPLELVDKCIGSRIHIVMKSDKEIVGTLLGFDDFVNMVLEDVTEFEITPEGRRITKLDQILLNGNNITMLVPGGEGPEV
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
2Acetylation------MAANATTNP
------CCCCCCCCH
14.9322223895
6Phosphorylation--MAANATTNPSQLL
--CCCCCCCCHHHCC
27.2419664995
20UbiquitinationLPLELVDKCIGSRIH
CCHHHHHHHHCCCEE
21.9221890473
67PhosphorylationTPEGRRITKLDQILL
CCCCCCCCCHHEEEE
24.6027461979
68AcetylationPEGRRITKLDQILLN
CCCCCCCCHHEEEEC
47.9323236377
68UbiquitinationPEGRRITKLDQILLN
CCCCCCCCHHEEEEC
47.93-
80PhosphorylationLLNGNNITMLVPGGE
EECCCCEEEEEECCC
13.4327461979

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 LSM5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSM5_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 LSM5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUXE_HUMANSNRPEphysical
15231747
LSM6_HUMANLSM6physical
22939629
LSM7_HUMANLSM7physical
22939629
RMI2_HUMANRMI2physical
22939629
SPTB1_HUMANSPTBphysical
22939629
PP1RA_HUMANPPP1R10physical
22939629
UBE3A_HUMANUBE3Aphysical
22939629
MI4GD_HUMANMIF4GDphysical
22939629
TF2B_HUMANGTF2Bphysical
22939629
RUXF_HUMANSNRPFphysical
22365833
LSM6_HUMANLSM6physical
22365833
LSM7_HUMANLSM7physical
22365833
LSM7_HUMANLSM7physical
15231747
RUXF_HUMANSNRPFphysical
15231747
LSM3_HUMANLSM3physical
15231747
LSM6_HUMANLSM6physical
15231747
LSM7_HUMANLSM7physical
25416956
LSM2_HUMANLSM2physical
26344197
LSM3_HUMANLSM3physical
26344197
LSM4_HUMANLSM4physical
26344197
LSM6_HUMANLSM6physical
26344197
LSM7_HUMANLSM7physical
26344197
LSMD1_HUMANNAA38physical
26344197
PATL1_HUMANPATL1physical
28514442
POLH_HUMANPOLHphysical
28514442
ZN511_HUMANZNF511physical
28514442
AKA7A_HUMANAKAP7physical
28514442
AKA7G_HUMANAKAP7physical
28514442
LSM1_HUMANLSM1physical
28514442
STPAP_HUMANTUT1physical
28514442
ZGPAT_HUMANZGPATphysical
28514442
PRPF3_HUMANPRPF3physical
28514442
LSM4_HUMANLSM4physical
28514442
SNR27_HUMANSNRNP27physical
28514442
LSM7_HUMANLSM7physical
28514442
LSM2_HUMANLSM2physical
28514442
MEPCE_HUMANMEPCEphysical
28514442
HPLN3_HUMANHAPLN3physical
28514442
LSM8_HUMANLSM8physical
28514442
LSM3_HUMANLSM3physical
28514442
TMCO6_HUMANTMCO6physical
28514442
SART3_HUMANSART3physical
28514442
S100B_HUMANS100Bphysical
28514442
PRP4_HUMANPRPF4physical
28514442
RBM42_HUMANRBM42physical
28514442
RDH13_HUMANRDH13physical
28514442
PRP31_HUMANPRPF31physical
28514442
SNUT1_HUMANSART1physical
28514442
SMD2_HUMANSNRPD2physical
28514442
RUXF_HUMANSNRPFphysical
28514442
NH2L1_HUMANNHP2L1physical
28514442
DDX23_HUMANDDX23physical
28514442

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 LSM5_HUMAN

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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, AND MASS SPECTROMETRY.

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