PGBD1_HUMAN - dbPTM
PGBD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGBD1_HUMAN
UniProt AC Q96JS3
Protein Name PiggyBac transposable element-derived protein 1
Gene Name PGBD1
Organism Homo sapiens (Human).
Sequence Length 809
Subcellular Localization
Protein Description
Protein Sequence MYEALPGPAPENEDGLVKVKEEDPTWEQVCNSQEGSSHTQEICRLRFRHFCYQEAHGPQEALAQLRELCHQWLRPEMHTKEQIMELLVLEQFLTILPKELQPCVKTYPLESGEEAVTVLENLETGSGDTGQQASVYIQGQDMHPMVAEYQGVSLECQSLQLLPGITTLKCEPPQRPQGNPQEVSGPVPHGSAHLQEKNPRDKAVVPVFNPVRSQTLVKTEEETAQAVAAEKWSHLSLTRRNLCGNSAQETVMSLSPMTEEIVTKDRLFKAKQETSEEMEQSGEASGKPNRECAPQIPCSTPIATERTVAHLNTLKDRHPGDLWARMHISSLEYAAGDITRKGRKKDKARVSELLQGLSFSGDSDVEKDNEPEIQPAQKKLKVSCFPEKSWTKRDIKPNFPSWSALDSGLLNLKSEKLNPVELFELFFDDETFNLIVNETNNYASQKNVSLEVTVQEMRCVFGVLLLSGFMRHPRREMYWEVSDTDQNLVRDAIRRDRFELIFSNLHFADNGHLDQKDKFTKLRPLIKQMNKNFLLYAPLEEYYCFDKSMCECFDSDQFLNGKPIRIGYKIWCGTTTQGYLVWFEPYQEESTMKVDEDPDLGLGGNLVMNFADVLLERGQYPYHLCFDSFFTSVKLLSALKKKGVRATGTIRENRTEKCPLMNVEHMKKMKRGYFDFRIEENNEIILCRWYGDGIISLCSNAVGIEPVNEVSCCDADNEEIPQISQPSIVKVYDECKEGVAKMDQIISKYRVRIRSKKWYSILVSYMIDVAMNNAWQLHRACNPGASLDPLDFRRFVAHFYLEHNAHLSD
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
2Phosphorylation------MYEALPGPA
------CCCCCCCCC		15.2027642862
32PhosphorylationTWEQVCNSQEGSSHT
CHHHHHCCCCCCCHH		25.20-
218SumoylationVRSQTLVKTEEETAQ
CCCCCCCCCHHHHHH		54.0228112733
219PhosphorylationRSQTLVKTEEETAQA
CCCCCCCCHHHHHHH		40.9428270605
223PhosphorylationLVKTEEETAQAVAAE
CCCCHHHHHHHHHHH		27.6128270605
231UbiquitinationAQAVAAEKWSHLSLT
HHHHHHHHCHHHHCC		49.6329967540
236PhosphorylationAEKWSHLSLTRRNLC
HHHCHHHHCCCCCCC		23.4424719451
246PhosphorylationRRNLCGNSAQETVMS
CCCCCCCHHHHHHHH		19.3328270605
250PhosphorylationCGNSAQETVMSLSPM
CCCHHHHHHHHCCCC		14.9328270605
253PhosphorylationSAQETVMSLSPMTEE
HHHHHHHHCCCCCHH		22.7428270605
255PhosphorylationQETVMSLSPMTEEIV
HHHHHHCCCCCHHHH		12.8128270605
258PhosphorylationVMSLSPMTEEIVTKD
HHHCCCCCHHHHCHH		33.5728270605
263PhosphorylationPMTEEIVTKDRLFKA
CCCHHHHCHHHHHHH		32.6528270605
299PhosphorylationCAPQIPCSTPIATER
CCCCCCCCCCCCCHH		31.6825627689
300PhosphorylationAPQIPCSTPIATERT
CCCCCCCCCCCCHHH		25.9821815630
304PhosphorylationPCSTPIATERTVAHL
CCCCCCCCHHHHHHH		27.07-
313PhosphorylationRTVAHLNTLKDRHPG
HHHHHHHCCCCCCCC		41.3620068231
351PhosphorylationKKDKARVSELLQGLS
CCCHHHHHHHHHHCC		19.5718669648
358PhosphorylationSELLQGLSFSGDSDV
HHHHHHCCCCCCCCC		24.9620068231
360PhosphorylationLLQGLSFSGDSDVEK
HHHHCCCCCCCCCCC		38.0122617229
363PhosphorylationGLSFSGDSDVEKDNE
HCCCCCCCCCCCCCC		47.2722617229
520PhosphorylationLDQKDKFTKLRPLIK
CCCHHHHHHHHHHHH		34.60-
637PhosphorylationFTSVKLLSALKKKGV
HHHHHHHHHHHHCCC		41.83-
649PhosphorylationKGVRATGTIRENRTE
CCCCCCCCCCCCCCC		16.71-
736AcetylationVKVYDECKEGVAKMD
HHHHHHHHHHHHHHH		56.2924888445
736UbiquitinationVKVYDECKEGVAKMD
HHHHHHHHHHHHHHH		56.29-
741AcetylationECKEGVAKMDQIISK
HHHHHHHHHHHHHHH		40.3724888451
747PhosphorylationAKMDQIISKYRVRIR
HHHHHHHHHHHHEEC		25.8424719451
748AcetylationKMDQIISKYRVRIRS
HHHHHHHHHHHEECC		27.0224888457
800PhosphorylationRRFVAHFYLEHNAHL
HHHHHHHHHHCCCCC		11.00-
808PhosphorylationLEHNAHLSD------
HHCCCCCCC------		31.2627251275
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 PGBD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGBD1_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 PGBD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PGBD1_HUMANPGBD1physical
25416956
ZSC22_HUMANZSCAN22physical
25416956
PGBD2_HUMANPGBD2physical
28514442
ZN174_HUMANZNF174physical
28514442
ZSC18_HUMANZSCAN18physical
28514442
ZN446_HUMANZNF446physical
28514442
ZN213_HUMANZNF213physical
28514442
ZNF24_HUMANZNF24physical
28514442
ZKSC3_HUMANZKSCAN3physical
28514442
SCND1_HUMANSCAND1physical
28514442
MYCB2_HUMANMYCBP2physical
28514442
ZKSC1_HUMANZKSCAN1physical
28514442
ZKSC8_HUMANZKSCAN8physical
28514442
ZSC25_HUMANZSCAN25physical
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 PGBD1_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-351 AND SER-360, ANDMASS SPECTROMETRY.

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