SP30L_HUMAN - dbPTM
SP30L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP30L_HUMAN
UniProt AC Q9HAJ7
Protein Name Histone deacetylase complex subunit SAP30L
Gene Name SAP30L
Organism Homo sapiens (Human).
Sequence Length 183
Subcellular Localization Isoform 1: Nucleus, nucleolus .
Isoform 2: Nucleus, nucleolus .
Isoform 3: Nucleus, nucleolus .
Protein Description Isoform 1: Functions as transcription repressor, probably via its interaction with histone deacetylase complexes. [PubMed: 16820529]
Protein Sequence MNGFSTEEDSREGPPAAPAAAAPGYGQSCCLIEDGERCVRPAGNASFSKRVQKSISQKKLKLDIDKSVRHLYICDFHKNFIQSVRNKRKRKTSDDGGDSPEHDTDIPEVDLFQLQVNTLRRYKRHYKLQTRPGFNKAQLAETVSRHFRNIPVNEKETLAYFIYMVKSNKSRLDQKSEGGKQLE
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
1Acetylation-------MNGFSTEE
-------CCCCCCHH
11.3222814378
5Phosphorylation---MNGFSTEEDSRE
---CCCCCCHHHCCC
35.9925159151
46PhosphorylationVRPAGNASFSKRVQK
EEECCCCCHHHHHHH
33.7724719451
54PhosphorylationFSKRVQKSISQKKLK
HHHHHHHHHCCCCCC
15.4730631047
56PhosphorylationKRVQKSISQKKLKLD
HHHHHHHCCCCCCCC
42.9330631047
67PhosphorylationLKLDIDKSVRHLYIC
CCCCCCHHHCEEEEC
22.1924260401
78MethylationLYICDFHKNFIQSVR
EEECHHHHHHHHHHH
54.25-
92PhosphorylationRNKRKRKTSDDGGDS
HHHCCCCCCCCCCCC
41.2330266825
93PhosphorylationNKRKRKTSDDGGDSP
HHCCCCCCCCCCCCC
36.4230266825
99PhosphorylationTSDDGGDSPEHDTDI
CCCCCCCCCCCCCCC
35.1530266825
104PhosphorylationGDSPEHDTDIPEVDL
CCCCCCCCCCCCCCE
37.4230266825
118PhosphorylationLFQLQVNTLRRYKRH
EEHHHHHHHHHHHHH
23.8420068231
130PhosphorylationKRHYKLQTRPGFNKA
HHHHCCCCCCCCCHH
49.6324719451
144PhosphorylationAQLAETVSRHFRNIP
HHHHHHHHHHHHCCC
27.7024719451
157PhosphorylationIPVNEKETLAYFIYM
CCCCCHHHHHHHHHH
27.9629759185
163PhosphorylationETLAYFIYMVKSNKS
HHHHHHHHHHHCCCH
5.9729759185
167PhosphorylationYFIYMVKSNKSRLDQ
HHHHHHHCCCHHHHH
37.7729759185
170PhosphorylationYMVKSNKSRLDQKSE
HHHHCCCHHHHHCCC
42.1824719451
176PhosphorylationKSRLDQKSEGGKQLE
CHHHHHCCCCCCCCC
35.5224719451

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 SP30L_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SP30L_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 SP30L_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3A_HUMANSIN3Aphysical
16820529
SP30L_HUMANSAP30Lphysical
16820529
HDAC1_HUMANHDAC1physical
16820529
HDAC2_HUMANHDAC2physical
16820529
HDAC3_HUMANHDAC3physical
16820529
SIN3A_HUMANSIN3Aphysical
18070604

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 SP30L_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 THR-92 AND SER-99, AND MASSSPECTROMETRY.
"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-104, AND MASSSPECTROMETRY.

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