LSMD1_HUMAN - dbPTM
LSMD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSMD1_HUMAN
UniProt AC Q9BRA0
Protein Name N-alpha-acetyltransferase 38, NatC auxiliary subunit
Gene Name NAA38
Organism Homo sapiens (Human).
Sequence Length 125
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues..
Protein Sequence MAGAGPTMLLREENGCCSRRQSSSSAGDSDGEREDSAAERARQQLEALLNKTMRIRMTDGRTLVGCFLCTDRDCNVILGSAQEFLKPSDSFSAGEPRVLGLAMVPGHHIVSIEVQRESLTGPPYL
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------MAGAGPTML
------CCCCCCCEE
19.2822814378
7Phosphorylation-MAGAGPTMLLREEN
-CCCCCCCEEEECCC
21.3822210691
18PhosphorylationREENGCCSRRQSSSS
ECCCCCCCCCCCCCC
34.2822777824
22PhosphorylationGCCSRRQSSSSAGDS
CCCCCCCCCCCCCCC
30.3129255136
23PhosphorylationCCSRRQSSSSAGDSD
CCCCCCCCCCCCCCC
21.7029255136
24PhosphorylationCSRRQSSSSAGDSDG
CCCCCCCCCCCCCCC
29.4729255136
25PhosphorylationSRRQSSSSAGDSDGE
CCCCCCCCCCCCCCC
37.9129255136
29PhosphorylationSSSSAGDSDGEREDS
CCCCCCCCCCCCCHH
46.7429255136
36PhosphorylationSDGEREDSAAERARQ
CCCCCCHHHHHHHHH
25.3224275569
51UbiquitinationQLEALLNKTMRIRMT
HHHHHHHHCCEEEEC
43.6021890473
51 (in isoform 1)Ubiquitination-43.6021890473
86UbiquitinationGSAQEFLKPSDSFSA
CCHHHHCCCCCCCCC
48.04-
88PhosphorylationAQEFLKPSDSFSAGE
HHHHCCCCCCCCCCC
44.2821406692
90PhosphorylationEFLKPSDSFSAGEPR
HHCCCCCCCCCCCCE
25.9921406692
92PhosphorylationLKPSDSFSAGEPRVL
CCCCCCCCCCCCEEE
39.0421712546
99UbiquitinationSAGEPRVLGLAMVPG
CCCCCEEEEEEEECC
4.99-
99 (in isoform 2)Ubiquitination-4.9921890473
134Ubiquitination----------------
----------------
-
134 (in isoform 2)Ubiquitination--
138Phosphorylation--------------------
--------------------
-
140Phosphorylation----------------------
----------------------
-

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 LSMD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSMD1_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 LSMD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PR20E_HUMANPRR20Aphysical
25416956
PR20C_HUMANPRR20Aphysical
25416956
PR20D_HUMANPRR20Aphysical
25416956
PR20B_HUMANPRR20Aphysical
25416956
PR20A_HUMANPRR20Aphysical
25416956
API5_HUMANAPI5physical
26344197
LSM7_HUMANLSM7physical
26344197
AFAD_HUMANMLLT4physical
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 LSMD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-22; SER-25 AND SER-29,AND MASS SPECTROMETRY.

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