SP110_HUMAN - dbPTM
SP110_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP110_HUMAN
UniProt AC Q9HB58
Protein Name Sp110 nuclear body protein
Gene Name SP110
Organism Homo sapiens (Human).
Sequence Length 689
Subcellular Localization Nucleus . Found in the nuclear body.
Protein Description Transcription factor. May be a nuclear hormone receptor coactivator. Enhances transcription of genes with retinoic acid response elements (RARE)..
Protein Sequence MFTMTRAMEEALFQHFMHQKLGIAYAIHKPFPFFEGLLDNSIITKRMYMESLEACRNLIPVSRVVHNILTQLERTFNLSLLVTLFSQINLREYPNLVTIYRSFKRVGASYEWQSRDTPILLEAPTGLAEGSSLHTPLALPPPQPPQPSCSPCAPRVSEPGTSSQQSDEILSESPSPSDPVLPLPALIQEGRSTSVTNDKLTSKMNAEEDSEEMPSLLTSTVQVASDNLIPQIRDKEDPQEMPHSPLGSMPEIRDNSPEPNDPEEPQEVSSTPSDKKGKKRKRCIWSTPKRRHKKKSLPGGTASSRHGIQKKLKRVDQVPQKKDDSTCNSTVETRAQKARTECARKSRSEEIIDGTSEMNEGKRSQKTPSTPRRVTQGAASPGHGIQEKLQVVDKVTQRKDDSTWNSEVMMRVQKARTKCARKSRLKEKKKEKDICSSSKRRFQKNIHRRGKPKSDTVDFHCSKLPVTCGEAKGILYKKKMKHGSSVKCIRNEDGTWLTPNEFEVEGKGRNAKNWKRNIRCEGMTLGELLKRKNSDECEVCCQGGQLLCCGTCPRVFHEDCHIPPVEAKRMLWSCTFCRMKRSSGSQQCHHVSKTLERQMQPQDQLIRDYGEPFQEAMWLDLVKERLITEMYTVAWFVRDMRLMFRNHKTFYKASDFGQVGLDLEAEFEKDLKDVLGFHEANDGGFWTLP
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
5Phosphorylation---MFTMTRAMEEAL
---CCCHHHHHHHHH		16.5329759185
45 (in isoform 4)Phosphorylation-25.43-
45UbiquitinationLDNSIITKRMYMESL
CCCCCHHHHHHHHHH		25.4333845483
51UbiquitinationTKRMYMESLEACRNL
HHHHHHHHHHHHHHC		18.2533845483
98PhosphorylationREYPNLVTIYRSFKR
CCCCCHHHHHHHHCC		18.5620068231
117PhosphorylationYEWQSRDTPILLEAP
EEECCCCCCEEEECC		15.89-
148PhosphorylationPPQPPQPSCSPCAPR
CCCCCCCCCCCCCCC		23.2128348404
150PhosphorylationQPPQPSCSPCAPRVS
CCCCCCCCCCCCCCC		27.6126657352
157PhosphorylationSPCAPRVSEPGTSSQ
CCCCCCCCCCCCCCH		39.0829978859
159UbiquitinationCAPRVSEPGTSSQQS
CCCCCCCCCCCCHHH		43.8024816145
161PhosphorylationPRVSEPGTSSQQSDE
CCCCCCCCCCHHHHH		35.6029978859
162PhosphorylationRVSEPGTSSQQSDEI
CCCCCCCCCHHHHHH		31.8729978859
163UbiquitinationVSEPGTSSQQSDEIL
CCCCCCCCHHHHHHH		31.8824816145
163PhosphorylationVSEPGTSSQQSDEIL
CCCCCCCCHHHHHHH		31.8830108239
166PhosphorylationPGTSSQQSDEILSES
CCCCCHHHHHHHHCC		29.5828450419
171PhosphorylationQQSDEILSESPSPSD
HHHHHHHHCCCCCCC		41.5128450419
173PhosphorylationSDEILSESPSPSDPV
HHHHHHCCCCCCCCC		27.5730278072
175PhosphorylationEILSESPSPSDPVLP
HHHHCCCCCCCCCCC		46.4430278072
177PhosphorylationLSESPSPSDPVLPLP
HHCCCCCCCCCCCHH		59.9128450419
192PhosphorylationALIQEGRSTSVTNDK
HHHHCCCCCCCCCHH		35.5728450419
193PhosphorylationLIQEGRSTSVTNDKL
HHHCCCCCCCCCHHH		26.3428450419
194PhosphorylationIQEGRSTSVTNDKLT
HHCCCCCCCCCHHHH		28.3523401153
196PhosphorylationEGRSTSVTNDKLTSK
CCCCCCCCCHHHHHC		37.1527486199
199AcetylationSTSVTNDKLTSKMNA
CCCCCCHHHHHCCCC		56.5923749302
210PhosphorylationKMNAEEDSEEMPSLL
CCCCCCCCCCCHHHH		38.4428348404
225PhosphorylationTSTVQVASDNLIPQI
HHHHHHHHCCCCHHC		28.33-
244PhosphorylationDPQEMPHSPLGSMPE
CCCCCCCCCCCCCCC		18.8929255136
248PhosphorylationMPHSPLGSMPEIRDN
CCCCCCCCCCCCCCC		38.5623927012
256PhosphorylationMPEIRDNSPEPNDPE
CCCCCCCCCCCCCCC		34.6229255136
262PhosphorylationNSPEPNDPEEPQEVS
CCCCCCCCCCCCCCC		55.2633259812
269PhosphorylationPEEPQEVSSTPSDKK
CCCCCCCCCCCCCCC		27.9522167270
270PhosphorylationEEPQEVSSTPSDKKG
CCCCCCCCCCCCCCC		49.8922167270
271PhosphorylationEPQEVSSTPSDKKGK
CCCCCCCCCCCCCCC		21.2122167270
273PhosphorylationQEVSSTPSDKKGKKR
CCCCCCCCCCCCCCC		63.2522167270
286PhosphorylationKRKRCIWSTPKRRHK
CCCCCCCCCCCCCCC		18.2127251275
287PhosphorylationRKRCIWSTPKRRHKK
CCCCCCCCCCCCCCC		20.1723898821
296PhosphorylationKRRHKKKSLPGGTAS
CCCCCCCCCCCCCHH		48.9929496963
301PhosphorylationKKSLPGGTASSRHGI
CCCCCCCCHHHHHHH		29.3127251275
303PhosphorylationSLPGGTASSRHGIQK
CCCCCCHHHHHHHHH		27.9527251275
304PhosphorylationLPGGTASSRHGIQKK
CCCCCHHHHHHHHHH		26.3227251275
316UbiquitinationQKKLKRVDQVPQKKD
HHHHHCHHCCCCCCC		48.0324816145
322UbiquitinationVDQVPQKKDDSTCNS
HHCCCCCCCCCCCCH		62.6124816145
346PhosphorylationRTECARKSRSEEIID
HHHHHHHHCCCHHCC		35.1728985074
347MethylationTECARKSRSEEIIDG
HHHHHHHCCCHHCCC		51.6418600497
348PhosphorylationECARKSRSEEIIDGT
HHHHHHCCCHHCCCC		46.8225159151
355PhosphorylationSEEIIDGTSEMNEGK
CCHHCCCCCCCCCCC		20.1230108239
356PhosphorylationEEIIDGTSEMNEGKR
CHHCCCCCCCCCCCC		40.1430108239
362AcetylationTSEMNEGKRSQKTPS
CCCCCCCCCCCCCCC		42.5725953088
362UbiquitinationTSEMNEGKRSQKTPS
CCCCCCCCCCCCCCC		42.5724816145
366UbiquitinationNEGKRSQKTPSTPRR
CCCCCCCCCCCCCCC		64.7524816145
366AcetylationNEGKRSQKTPSTPRR
CCCCCCCCCCCCCCC		64.7525953088
367PhosphorylationEGKRSQKTPSTPRRV
CCCCCCCCCCCCCCC		18.1626074081
368UbiquitinationGKRSQKTPSTPRRVT
CCCCCCCCCCCCCCC		43.1524816145
369PhosphorylationKRSQKTPSTPRRVTQ
CCCCCCCCCCCCCCC		57.1626074081
370PhosphorylationRSQKTPSTPRRVTQG
CCCCCCCCCCCCCCC		23.2426074081
372UbiquitinationQKTPSTPRRVTQGAA
CCCCCCCCCCCCCCC		45.8724816145
375PhosphorylationPSTPRRVTQGAASPG
CCCCCCCCCCCCCCC		21.3425159151
380PhosphorylationRVTQGAASPGHGIQE
CCCCCCCCCCCCHHH		30.7729255136
394 (in isoform 6)Ubiquitination-35.26-
394UbiquitinationEKLQVVDKVTQRKDD
HHHHEEEHHHHCCCC		35.26-
394AcetylationEKLQVVDKVTQRKDD
HHHHEEEHHHHCCCC		35.2623749302
406PhosphorylationKDDSTWNSEVMMRVQ
CCCCCCCHHHHHHHH		24.1126714015
472UbiquitinationPVTCGEAKGILYKKK
CCCCCCCCCEEEEEE		42.0329967540
478UbiquitinationAKGILYKKKMKHGSS
CCCEEEEEECCCCCC		44.5429967540
487UbiquitinationMKHGSSVKCIRNEDG
CCCCCCCEEEECCCC		26.3729967540
493UbiquitinationVKCIRNEDGTWLTPN
CEEEECCCCCEECCC		64.4729967540
498PhosphorylationNEDGTWLTPNEFEVE
CCCCCEECCCEEEEC		18.6726714015
507UbiquitinationNEFEVEGKGRNAKNW
CEEEECCCCCCCCCH		40.9929967540
513UbiquitinationGKGRNAKNWKRNIRC
CCCCCCCCHHHHCCC		47.2829967540
534PhosphorylationELLKRKNSDECEVCC
HHHHHCCCCCCCEEE		37.5127251275
593UbiquitinationQQCHHVSKTLERQMQ
HHHHHHHHHHHHHCC		56.92-
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 SP110_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SP110_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 SP110_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NP1L2_HUMANNAP1L2physical
20211142
ZSC9_HUMANZSCAN9physical
20211142
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
235550Hepatic venoocclusive disease with immunodeficiency (VODI)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SP110_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-256, AND MASSSPECTROMETRY.

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