PSPC1_HUMAN - dbPTM
PSPC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSPC1_HUMAN
UniProt AC Q8WXF1
Protein Name Paraspeckle component 1
Gene Name PSPC1
Organism Homo sapiens (Human).
Sequence Length 523
Subcellular Localization Nucleus, nucleolus. Nucleus matrix. Cytoplasm. Nucleus speckle. In punctate subnuclear structures often located adjacent to splicing speckles, called paraspeckles. Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar caps in an RNA-depend
Protein Description Regulates, cooperatively with NONO and SFPQ, androgen receptor-mediated gene transcription activity in Sertoli cell line (By similarity). Binds to poly(A), poly(G) and poly(U) RNA homopolymers. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer (By similarity). Together with NONO, required for the formation of nuclear paraspeckles. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway..
Protein Sequence MMLRGNLKQVRIEKNPARLRALESAVGESEPAAAAAMALALAGEPAPPAPAPPEDHPDEEMGFTIDIKSFLKPGEKTYTQRCRLFVGNLPTDITEEDFKRLFERYGEPSEVFINRDRGFGFIRLESRTLAEIAKAELDGTILKSRPLRIRFATHGAALTVKNLSPVVSNELLEQAFSQFGPVEKAVVVVDDRGRATGKGFVEFAAKPPARKALERCGDGAFLLTTTPRPVIVEPMEQFDDEDGLPEKLMQKTQQYHKEREQPPRFAQPGTFEFEYASRWKALDEMEKQQREQVDRNIREAKEKLEAEMEAARHEHQLMLMRQDLMRRQEELRRLEELRNQELQKRKQIQLRHEEEHRRREEEMIRHREQEELRRQQEGFKPNYMENREQEMRMGDMGPRGAINMGDAFSPAPAGNQGPPPMMGMNMNNRATIPGPPMGPGPAMGPEGAANMGTPMMPDNGAVHNDRFPQGPPSQMGSPMGSRTGSETPQAPMSGVGPVSGGPGGFGRGSQGGNFEGPNKRRRY
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-------MMLRGNLK
-------CCCCCCCE		5.2819413330
4Methylation----MMLRGNLKQVR
----CCCCCCCEEEE		17.66115368473
8AcetylationMMLRGNLKQVRIEKN
CCCCCCCEEEEECCC		51.2325953088
8UbiquitinationMMLRGNLKQVRIEKN
CCCCCCCEEEEECCC		51.2329967540
14AcetylationLKQVRIEKNPARLRA
CEEEEECCCHHHHHH		66.9025953088
14UbiquitinationLKQVRIEKNPARLRA
CEEEEECCCHHHHHH		66.9024816145
69PhosphorylationGFTIDIKSFLKPGEK
CEEEEHHHHCCCCCC		35.8224719451
72UbiquitinationIDIKSFLKPGEKTYT
EEHHHHCCCCCCCCC		49.3029967540
76UbiquitinationSFLKPGEKTYTQRCR
HHCCCCCCCCCCCEE		53.3929967540
76AcetylationSFLKPGEKTYTQRCR
HHCCCCCCCCCCCEE		53.3926051181
99AcetylationDITEEDFKRLFERYG
CCCHHHHHHHHHHHC		61.5925953088
99UbiquitinationDITEEDFKRLFERYG
CCCHHHHHHHHHHHC		61.5924816145
105PhosphorylationFKRLFERYGEPSEVF
HHHHHHHHCCCCEEE		20.7428152594
134UbiquitinationRTLAEIAKAELDGTI
CHHHHHHHHHCCCCE		48.3229967540
134AcetylationRTLAEIAKAELDGTI
CHHHHHHHHHCCCCE		48.3225953088
143AcetylationELDGTILKSRPLRIR
HCCCCEECCCCEEEE		40.3425953088
143UbiquitinationELDGTILKSRPLRIR
HCCCCEECCCCEEEE		40.3433845483
153PhosphorylationPLRIRFATHGAALTV
CEEEEEEECCCEEEE		20.3820068231
159PhosphorylationATHGAALTVKNLSPV
EECCCEEEECCCCHH		25.3820068231
164PhosphorylationALTVKNLSPVVSNEL
EEEECCCCHHCCHHH		25.6625159151
168PhosphorylationKNLSPVVSNELLEQA
CCCCHHCCHHHHHHH		25.4828464451
177PhosphorylationELLEQAFSQFGPVEK
HHHHHHHHHHCCCCE		27.8420068231
196PhosphorylationVDDRGRATGKGFVEF
ECCCCCEECCCHHHC		37.7620068231
198AcetylationDRGRATGKGFVEFAA
CCCCEECCCHHHCCC		44.8326051181
198 (in isoform 1)Ubiquitination-44.8321890473
198 (in isoform 2)Ubiquitination-44.8321890473
198UbiquitinationDRGRATGKGFVEFAA
CCCCEECCCHHHCCC		44.8322817900
206AcetylationGFVEFAAKPPARKAL
CHHHCCCCCCHHHHH		48.3719608861
206UbiquitinationGFVEFAAKPPARKAL
CHHHCCCCCCHHHHH		48.3732142685
206MalonylationGFVEFAAKPPARKAL
CHHHCCCCCCHHHHH		48.3726320211
247UbiquitinationDEDGLPEKLMQKTQQ
CCCCCCHHHHHHHHH		47.5224816145
251UbiquitinationLPEKLMQKTQQYHKE
CCHHHHHHHHHHHHH		34.0429967540
255PhosphorylationLMQKTQQYHKEREQP
HHHHHHHHHHHHCCC		12.68-
270PhosphorylationPRFAQPGTFEFEYAS
CCCCCCCEEEEEHHH		27.0328152594
275PhosphorylationPGTFEFEYASRWKAL
CCEEEEEHHHHHHHH		18.3928152594
277PhosphorylationTFEFEYASRWKALDE
EEEEEHHHHHHHHHH		37.4628152594
280UbiquitinationFEYASRWKALDEMEK
EEHHHHHHHHHHHHH		37.6529967540
303UbiquitinationNIREAKEKLEAEMEA
HHHHHHHHHHHHHHH		51.4224816145
308SulfoxidationKEKLEAEMEAARHEH
HHHHHHHHHHHHHHH		5.6821406390
338MethylationLRRLEELRNQELQKR
HHHHHHHHHHHHHHH		46.17115489515
373MethylationHREQEELRRQQEGFK
HHHHHHHHHHHCCCC		37.33115489507
380AcetylationRRQQEGFKPNYMENR
HHHHCCCCCCHHHHH		43.1223954790
380UbiquitinationRRQQEGFKPNYMENR
HHHHCCCCCCHHHHH		43.1224816145
409PhosphorylationINMGDAFSPAPAGNQ
CCCCCCCCCCCCCCC		23.1325159151
431PhosphorylationMNMNNRATIPGPPMG
CCCCCCCCCCCCCCC		25.1927251275
453PhosphorylationEGAANMGTPMMPDNG
CCCCCCCCCCCCCCC		9.3927251275
473PhosphorylationRFPQGPPSQMGSPMG
CCCCCCHHHCCCCCC		35.6123401153
477PhosphorylationGPPSQMGSPMGSRTG
CCHHHCCCCCCCCCC		13.3329255136
481PhosphorylationQMGSPMGSRTGSETP
HCCCCCCCCCCCCCC		22.0329255136
483PhosphorylationGSPMGSRTGSETPQA
CCCCCCCCCCCCCCC		46.9228450419
485PhosphorylationPMGSRTGSETPQAPM
CCCCCCCCCCCCCCC		37.3728450419
487PhosphorylationGSRTGSETPQAPMSG
CCCCCCCCCCCCCCC		23.5428450419
492SulfoxidationSETPQAPMSGVGPVS
CCCCCCCCCCCCCCC		6.4521406390
493PhosphorylationETPQAPMSGVGPVSG
CCCCCCCCCCCCCCC		29.3028450419
499PhosphorylationMSGVGPVSGGPGGFG
CCCCCCCCCCCCCCC		40.9627251275
507DimethylationGGPGGFGRGSQGGNF
CCCCCCCCCCCCCCC		39.05-
507MethylationGGPGGFGRGSQGGNF
CCCCCCCCCCCCCCC		39.0524129315
509PhosphorylationPGGFGRGSQGGNFEG
CCCCCCCCCCCCCCC		25.0417525332
519AcetylationGNFEGPNKRRRY---
CCCCCCCCCCCC---		50.8725953088
519UbiquitinationGNFEGPNKRRRY---
CCCCCCCCCCCC---		50.8724816145
519MethylationGNFEGPNKRRRY---
CCCCCCCCCCCC---		50.8724471223
520MethylationNFEGPNKRRRY----
CCCCCCCCCCC----		34.6418958521
520DimethylationNFEGPNKRRRY----
CCCCCCCCCCC----		34.64-
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
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSPC1_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 PSPC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRIF1_HUMANLRIF1physical
16169070
NONO_HUMANNONOphysical
16169070
RBP17_HUMANRANBP17physical
22939629
TENN_HUMANTNNphysical
22939629
KR131_HUMANKRTAP13-1physical
25416956
DNJB4_HUMANDNAJB4physical
26344197
IF4H_HUMANEIF4Hphysical
26344197
HIP1R_HUMANHIP1Rphysical
26344197
LZTL1_HUMANLZTFL1physical
26344197
PPP5_HUMANPPP5Cphysical
26344197
TATD1_HUMANTATDN1physical
26344197
WDR12_HUMANWDR12physical
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 PSPC1_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-473 AND SER-477, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206, AND MASS SPECTROMETRY.
Phosphorylation
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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-473 AND SER-477, AND MASS SPECTROMETRY.
"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-509, AND MASSSPECTROMETRY.

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