SNPC3_HUMAN - dbPTM
SNPC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNPC3_HUMAN
UniProt AC Q92966
Protein Name snRNA-activating protein complex subunit 3
Gene Name SNAPC3
Organism Homo sapiens (Human).
Sequence Length 411
Subcellular Localization Nucleus.
Protein Description Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box..
Protein Sequence MAEGSRGGPTCSGVGGRQDPVSGSGGCNFPEYELPELNTRAFHVGAFGELWRGRLRGAGDLSLREPPASALPGSQAADSDREDAAVARDLDCSLEAAAELRAVCGLDKLKCLEDGEDPEVIPENTDLVTLGVRKRFLEHREETITIDRACRQETFVYEMESHAIGKKPENSADMIEEGELILSVNILYPVIFHKHKEHKPYQTMLVLGSQKLTQLRDSIRCVSDLQIGGEFSNTPDQAPEHISKDLYKSAFFYFEGTFYNDKRYPECRDLSRTIIEWSESHDRGYGKFQTARMEDFTFNDLCIKLGFPYLYCHQGDCEHVIVITDIRLVHHDDCLDRTLYPLLIKKHWLWTRKCFVCKMYTARWVTNNDSFAPEDPCFFCDVCFRMLHYDSEGNKLGEFLAYPYVDPGTFN
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
6Methylation--MAEGSRGGPTCSG
--CCCCCCCCCCCCC
66.01115917337
62PhosphorylationLRGAGDLSLREPPAS
CCCCCCCCCCCCCCC
30.0724719451
74PhosphorylationPASALPGSQAADSDR
CCCCCCCCCCCCCCH
18.0817525332
93PhosphorylationVARDLDCSLEAAAEL
HHHHHHCHHHHHHHH
28.9830576142
108UbiquitinationRAVCGLDKLKCLEDG
HHHHCCCHHCCCCCC
55.6922817900
110UbiquitinationVCGLDKLKCLEDGED
HHCCCHHCCCCCCCC
42.3821963094
161PhosphorylationTFVYEMESHAIGKKP
CEEEEEHHHHCCCCC
19.5325849741
244UbiquitinationQAPEHISKDLYKSAF
CCCHHHCHHHHHHHH
51.6722505724
287UbiquitinationSHDRGYGKFQTARME
HCCCCCCCCCCCEEC
26.3022817900
287AcetylationSHDRGYGKFQTARME
HCCCCCCCCCCCEEC
26.3026051181
338PhosphorylationHDDCLDRTLYPLLIK
CHHHCHHCHHHHHHH
30.25-
345UbiquitinationTLYPLLIKKHWLWTR
CHHHHHHHHHHHHCC
38.2621890473
345AcetylationTLYPLLIKKHWLWTR
CHHHHHHHHHHHHCC
38.2626051181
346UbiquitinationLYPLLIKKHWLWTRK
HHHHHHHHHHHHCCC
32.78-
395UbiquitinationHYDSEGNKLGEFLAY
EECCCCCCCCEECCC
69.5922817900

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 SNPC3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNPC3_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 SNPC3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
11094070
SNPC1_HUMANSNAPC1physical
9003788
DHB14_HUMANHSD17B14physical
25416956
CE57L_HUMANCEP57L1physical
25416956

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 SNPC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.

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