SNPC1_HUMAN - dbPTM
SNPC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNPC1_HUMAN
UniProt AC Q16533
Protein Name snRNA-activating protein complex subunit 1
Gene Name SNAPC1
Organism Homo sapiens (Human).
Sequence Length 368
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 MGTPPGLQTDCEALLSRFQETDSVRFEDFTELWRNMKFGTIFCGRMRNLEKNMFTKEALALAWRYFLPPYTFQIRVGALYLLYGLYNTQLCQPKQKIRVALKDWDEVLKFQQDLVNAQHFDAAYIFRKLRLDRAFHFTAMPKLLSYRMKKKIHRAEVTEEFKDPSDRVMKLITSDVLEEMLNVHDHYQNMKHVISVDKSKPDKALSLIKDDFFDNIKNIVLEHQQWHKDRKNPSLKSKTNDGEEKMEGNSQETERCERAESLAKIKSKAFSVVIQASKSRRHRQVKLDSSDSDSASGQGQVKATRKKEKKERLKPAGRKMSLRNKGNVQNIHKEDKPLSLSMPVITEEEENESLSGTEFTASKKRRKH
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
80PhosphorylationQIRVGALYLLYGLYN
HHHHHHHHHHHHHHH		8.30-
83PhosphorylationVGALYLLYGLYNTQL
HHHHHHHHHHHHCCC		11.50-
86PhosphorylationLYLLYGLYNTQLCQP
HHHHHHHHHCCCCCC		16.29-
88PhosphorylationLLYGLYNTQLCQPKQ
HHHHHHHCCCCCCCH		14.90-
102UbiquitinationQKIRVALKDWDEVLK
HHHHHHHCCHHHHHH		47.22-
142UbiquitinationFHFTAMPKLLSYRMK
HHHCHHHHHHHHHHH		49.3121890473
162UbiquitinationAEVTEEFKDPSDRVM
HHHCHHHCCHHHHHH		72.51-
173PhosphorylationDRVMKLITSDVLEEM
HHHHHHHHHHHHHHH		29.34-
174PhosphorylationRVMKLITSDVLEEML
HHHHHHHHHHHHHHH		20.80-
187PhosphorylationMLNVHDHYQNMKHVI
HHCCCHHHHHCCEEE		13.98-
191UbiquitinationHDHYQNMKHVISVDK
CHHHHHCCEEEECCC		42.12-
195PhosphorylationQNMKHVISVDKSKPD
HHCCEEEECCCCCCC		24.1524719451
198UbiquitinationKHVISVDKSKPDKAL
CEEEECCCCCCCHHH		59.22-
203UbiquitinationVDKSKPDKALSLIKD
CCCCCCCHHHHHHCH		60.81-
206PhosphorylationSKPDKALSLIKDDFF
CCCCHHHHHHCHHHH		32.6724719451
209UbiquitinationDKALSLIKDDFFDNI
CHHHHHHCHHHHHHH		57.44-
217UbiquitinationDDFFDNIKNIVLEHQ
HHHHHHHHHHHHHHH		47.04-
228UbiquitinationLEHQQWHKDRKNPSL
HHHHHHHHCCCCCCC		57.16-
264UbiquitinationERAESLAKIKSKAFS
HHHHHHHHHHHHHHH		56.83-
264AcetylationERAESLAKIKSKAFS
HHHHHHHHHHHHHHH		56.8321339330
286UbiquitinationSRRHRQVKLDSSDSD
CCCCCEEECCCCCCC		37.93-
289PhosphorylationHRQVKLDSSDSDSAS
CCEEECCCCCCCCCC		46.6229255136
290PhosphorylationRQVKLDSSDSDSASG
CEEECCCCCCCCCCC		40.5829255136
292PhosphorylationVKLDSSDSDSASGQG
EECCCCCCCCCCCCC		35.1029255136
294PhosphorylationLDSSDSDSASGQGQV
CCCCCCCCCCCCCCH		28.4325262027
296PhosphorylationSSDSDSASGQGQVKA
CCCCCCCCCCCCHHC		35.2829255136
302UbiquitinationASGQGQVKATRKKEK
CCCCCCHHCCCHHHH		35.83-
321PhosphorylationKPAGRKMSLRNKGNV
CCCCHHHHHHCCCCC		27.49-
325UbiquitinationRKMSLRNKGNVQNIH
HHHHHHCCCCCCCCC		45.49-
346PhosphorylationSLSMPVITEEEENES
EEECCCCCHHHHHCC		37.2628348404
353PhosphorylationTEEEENESLSGTEFT
CHHHHHCCCCCCCCC		39.1430576142
355PhosphorylationEEENESLSGTEFTAS
HHHHCCCCCCCCCCC		53.6130576142
357PhosphorylationENESLSGTEFTASKK
HHCCCCCCCCCCCHH		25.2629523821
360PhosphorylationSLSGTEFTASKKRRK
CCCCCCCCCCHHHCC		24.6429523821
362PhosphorylationSGTEFTASKKRRKH-
CCCCCCCCHHHCCC-		35.3328102081
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 SNPC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNPC1_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 SNPC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
11094070
SNPC3_HUMANSNAPC3physical
9003788
SNPC4_HUMANSNAPC4physical
11056176
SNPC5_HUMANSNAPC5physical
11056176
SNPC3_HUMANSNAPC3physical
11056176
NR2E3_HUMANNR2E3physical
20211142
TRI29_HUMANTRIM29physical
20211142
RHXF2_HUMANRHOXF2physical
20211142
SNPC5_HUMANSNAPC5physical
26186194
SNPC4_HUMANSNAPC4physical
26186194
SNPC2_HUMANSNAPC2physical
26186194
SNPC3_HUMANSNAPC3physical
26186194
ZG16B_HUMANZG16Bphysical
26186194
CYTS_HUMANCST4physical
26186194
SNPC3_HUMANSNAPC3physical
28514442
SNPC4_HUMANSNAPC4physical
28514442
SNPC2_HUMANSNAPC2physical
28514442
SNPC5_HUMANSNAPC5physical
28514442
ZG16B_HUMANZG16Bphysical
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 SNPC1_HUMAN

loading...

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-289; SER-290 ANDSER-292, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory