PQBP1_HUMAN - dbPTM
PQBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PQBP1_HUMAN
UniProt AC O60828
Protein Name Polyglutamine-binding protein 1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963}
Gene Name PQBP1 {ECO:0000303|PubMed:10332029, ECO:0000303|PubMed:11163963, ECO:0000312|HGNC:HGNC:9330}
Organism Homo sapiens (Human).
Sequence Length 265
Subcellular Localization Nucleus . Nucleus speckle . Cytoplasmic granule . Colocalizes with SRSF2 in nuclear speckles (By similarity). Colocalized with POU3F2 (PubMed:10332029). Colocalized with ATXN1 in nuclear inclusion bodies (PubMed:12062018). Localizes to cytoplasmic st
Protein Description Intrinsically disordered protein that acts as a scaffold, and which is involved in different processes, such as pre-mRNA splicing, transcription regulation, innate immunity and neuron development. [PubMed: 10198427]
Protein Sequence MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD
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
9PhosphorylationPLPVALQTRLAKRGI
CCCHHHHHHHHHCCH		28.6220068231
10MethylationLPVALQTRLAKRGIL
CCHHHHHHHHHCCHH		21.4954558275
18AcetylationLAKRGILKHLEPEPE
HHHCCHHHHCCCCCH		44.1926051181
18UbiquitinationLAKRGILKHLEPEPE
HHHCCHHHHCCCCCH		44.19-
33PhosphorylationEEIIAEDYDDDPVDY
HHCCCCCCCCCCCCH		16.8728796482
40PhosphorylationYDDDPVDYEATRLEG
CCCCCCCHHHHCCCC		14.0128796482
43PhosphorylationDPVDYEATRLEGLPP
CCCCHHHHCCCCCCC		24.6928796482
51 (in isoform 8)Phosphorylation-40.8930631047
77PhosphorylationTDLVSWLSPHDPNSV
CCHHHHCCCCCCCCH		17.5825159151
94PhosphorylationKSAKKLRSSNADAEE
HHHHHHHHCCCCHHH		38.0825159151
95PhosphorylationSAKKLRSSNADAEEK
HHHHHHHCCCCHHHH		29.6025159151
102AcetylationSNADAEEKLDRSHDK
CCCCHHHHHHHHCCC		47.3926051181
106PhosphorylationAEEKLDRSHDKSDRG
HHHHHHHHCCCCCCC		35.3929496963
110PhosphorylationLDRSHDKSDRGHDKS
HHHHCCCCCCCCCCC		38.3029496963
114 (in isoform 7)Phosphorylation-39.9720068231
116 (in isoform 7)Phosphorylation-48.8920068231
120 (in isoform 7)Phosphorylation-40.7720068231
120O-linked_GlycosylationGHDKSDRSHEKLDRG
CCCCCHHHHHHHHCC		40.7730379171
121 (in isoform 7)Phosphorylation-36.7820068231
138PhosphorylationSDRGHDKSDRDRERG
CCCCCCCCHHHHHCC		43.8927134283
146PhosphorylationDRDRERGYDKVDRER
HHHHHCCHHHHHHHH		20.8628796482
187PhosphorylationRREELAPYPKSKKAV
CHHHHCCCCCCHHCC		20.0621815630
191MethylationLAPYPKSKKAVSRKD
HCCCCCCHHCCCCCC		51.37116251901
195PhosphorylationPKSKKAVSRKDEELD
CCCHHCCCCCCCCCC		38.1728555341
197AcetylationSKKAVSRKDEELDPM
CHHCCCCCCCCCCCC		63.0826051181
207PhosphorylationELDPMDPSSYSDAPR
CCCCCCHHHCCCCCC		37.3328796482
208PhosphorylationLDPMDPSSYSDAPRG
CCCCCHHHCCCCCCC		33.7628796482
209PhosphorylationDPMDPSSYSDAPRGT
CCCCHHHCCCCCCCC		18.2028796482
210PhosphorylationPMDPSSYSDAPRGTW
CCCHHHCCCCCCCCC		29.2828796482
214MethylationSSYSDAPRGTWSTGL
HHCCCCCCCCCCCCC		57.82115488641
216PhosphorylationYSDAPRGTWSTGLPK
CCCCCCCCCCCCCCC		19.9527251275
218PhosphorylationDAPRGTWSTGLPKRN
CCCCCCCCCCCCCCC		16.6625159151
219PhosphorylationAPRGTWSTGLPKRNE
CCCCCCCCCCCCCCC		34.0129396449
229PhosphorylationPKRNEAKTGADTTAA
CCCCCCCCCCCCCCC		44.6529396449
233PhosphorylationEAKTGADTTAAGPLF
CCCCCCCCCCCCHHH		20.1429396449
234PhosphorylationAKTGADTTAAGPLFQ
CCCCCCCCCCCHHHH		18.3020068231
245PhosphorylationPLFQQRPYPSPGAVL
HHHHCCCCCCCCHHH		20.6622617229
247PhosphorylationFQQRPYPSPGAVLRA
HHCCCCCCCCHHHHH		30.0725159151
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 ligaseLNX1Q8TBB1
PMID:22889411
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PQBP1_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 PQBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TXN4A_HUMANTXNL4Aphysical
11054566
WBP11_HUMANWBP11physical
10593949
ERG28_HUMANC14orf1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
MED31_HUMANMED31physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
RPB1_HUMANPOLR2Aphysical
12062018
TLX3_HUMANTLX3physical
20211142
TXN4A_HUMANTXNL4Aphysical
10873650
PSPC_HUMANSFTPCphysical
19366705
RECO_HUMANRCVRNphysical
16713569
WBP11_HUMANWBP11physical
16713569
A4_HUMANAPPphysical
21832049
VDAC3_HUMANVDAC3physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
RBMS1_HUMANRBMS1physical
22939629
RM53_HUMANMRPL53physical
22939629
RS28_HUMANRPS28physical
22939629
SRPRB_HUMANSRPRBphysical
22939629
SLIRP_HUMANSLIRPphysical
22939629
RIDA_HUMANHRSP12physical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
SCO2_HUMANSCO2physical
22939629
RRBP1_HUMANRRBP1physical
22939629
RT28_HUMANMRPS28physical
22939629
SUGP1_HUMANSUGP1physical
22939629
AQR_HUMANAQRphysical
22365833
MEP50_HUMANWDR77physical
22365833
HNRH2_HUMANHNRNPH2physical
22365833
MARE1_HUMANMAPRE1physical
25416956
LZTS2_HUMANLZTS2physical
25416956
PP1R7_HUMANPPP1R7physical
27173435
PP1A_HUMANPPP1CAphysical
27173435
PP1B_HUMANPPP1CBphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
309500Renpenning syndrome 1 (RENS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PQBP1_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-247, AND MASSSPECTROMETRY.

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