PPWD1_HUMAN - dbPTM
PPWD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPWD1_HUMAN
UniProt AC Q96BP3
Protein Name Peptidylprolyl isomerase domain and WD repeat-containing protein 1 {ECO:0000305}
Gene Name PPWD1 {ECO:0000312|HGNC:HGNC:28954}
Organism Homo sapiens (Human).
Sequence Length 646
Subcellular Localization Nucleus . Associated with spliceosomal complexes.
Protein Description PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. [PubMed: 20676357 May be involved in pre-mRNA splicing]
Protein Sequence MAAESGSDFQQRRRRRRDPEEPEKTELSERELAVAVAVSQENDEENEERWVGPLPVEATLAKKRKVLEFERVYLDNLPSASMYERSYMHRDVITHVVCTKTDFIITASHDGHVKFWKKIEEGIEFVKHFRSHLGVIESIAVSSEGALFCSVGDDKAMKVFDVVNFDMINMLKLGYFPGQCEWIYCPGDAISSVAASEKSTGKIFIYDGRGDNQPLHIFDKLHTSPLTQIRLNPVYKAVVSSDKSGMIEYWTGPPHEYKFPKNVNWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFDESLSMFTELQQMRQQLPDMEFGRRMAVERELEKVDAVRLINIVFDETGHFVLYGTMLGIKVINVETNRCVRILGKQENIRVMQLALFQGIAKKHRAATTIEMKASENPVLQNIQADPTIVCTSFKKNRFYMFTKREPEDTKSADSDRDVFNEKPSKEEVMAATQAEGPKRVSDSAIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPKTDKPYEDVSIINITVK
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
2Acetylation------MAAESGSDF
------CCCCCCHHH		21.6722223895
5Phosphorylation---MAAESGSDFQQR
---CCCCCCHHHHHH		38.5825159151
7Phosphorylation-MAAESGSDFQQRRR
-CCCCCCHHHHHHHH		44.5225627689
39PhosphorylationLAVAVAVSQENDEEN
HHHEEEECCCCCCCC		23.2626699800
62AcetylationPVEATLAKKRKVLEF
CHHHHHHHHCCEEEE		57.1125953088
62UbiquitinationPVEATLAKKRKVLEF
CHHHHHHHHCCEEEE		57.11-
64UbiquitinationEATLAKKRKVLEFER
HHHHHHHCCEEEEEE		33.34-
65UbiquitinationATLAKKRKVLEFERV
HHHHHHCCEEEEEEE		61.11-
99PhosphorylationVITHVVCTKTDFIIT
HHEEEEEECCCEEEE		25.93-
122UbiquitinationFWKKIEEGIEFVKHF
HHHHHHHHHHHHHHH		16.37-
127UbiquitinationEEGIEFVKHFRSHLG
HHHHHHHHHHHHHCC		42.2021890473
127UbiquitinationEEGIEFVKHFRSHLG
HHHHHHHHHHHHHCC		42.2021890473
196UbiquitinationAISSVAASEKSTGKI
HHHHHHCCCCCCCCE		35.50-
220UbiquitinationQPLHIFDKLHTSPLT
CCEEEEECCCCCCCC		31.27-
238UbiquitinationLNPVYKAVVSSDKSG
CCHHHEEHHCCCCCC		3.62-
240PhosphorylationPVYKAVVSSDKSGMI
HHHEEHHCCCCCCCE		26.65-
243UbiquitinationKAVVSSDKSGMIEYW
EEHHCCCCCCCEEEE		51.35-
258UbiquitinationTGPPHEYKFPKNVNW
CCCCHHCCCCCCCCC		52.81-
261UbiquitinationPHEYKFPKNVNWEYK
CHHCCCCCCCCCEEC		76.34-
268UbiquitinationKNVNWEYKTDTDLYE
CCCCCEECCCCCHHH		28.54-
274PhosphorylationYKTDTDLYEFAKCKA
ECCCCCHHHHHCCCC		16.2928152594
278UbiquitinationTDLYEFAKCKAYPTS
CCHHHHHCCCCCCCC		41.40-
288UbiquitinationAYPTSVCFSPDGKKI
CCCCCEEECCCCCEE		12.76-
289PhosphorylationYPTSVCFSPDGKKIA
CCCCEEECCCCCEEE		19.5621815630
293AcetylationVCFSPDGKKIATIGS
EEECCCCCEEEEECC		48.6825953088
294UbiquitinationCFSPDGKKIATIGSD
EECCCCCEEEEECCC		43.00-
352UbiquitinationAVERELEKVDAVRLI
HHHHHHHHCCCEEEE		59.02-
394UbiquitinationRCVRILGKQENIRVM
CEEHHHCCHHCHHHH		51.50-
394AcetylationRCVRILGKQENIRVM
CEEHHHCCHHCHHHH		51.507974817
412UbiquitinationLFQGIAKKHRAATTI
HHHHHHHHHHCCEEE		29.33-
422UbiquitinationAATTIEMKASENPVL
CCEEEEEECCCCCHH		35.65-
444MethylationTIVCTSFKKNRFYMF
EEEEEECCCCEEEEE		49.2424469639
444AcetylationTIVCTSFKKNRFYMF
EEEEEECCCCEEEEE		49.2426051181
444UbiquitinationTIVCTSFKKNRFYMF
EEEEEECCCCEEEEE		49.24-
445MethylationIVCTSFKKNRFYMFT
EEEEECCCCEEEEEE		51.88115975609
453UbiquitinationNRFYMFTKREPEDTK
CEEEEEEECCCCCCC		43.42-
461PhosphorylationREPEDTKSADSDRDV
CCCCCCCCCCCCCHH		39.1320873877
464PhosphorylationEDTKSADSDRDVFNE
CCCCCCCCCCHHHCC		33.9725849741
475UbiquitinationVFNEKPSKEEVMAAT
HHCCCCCHHHHHHHH		67.43-
479SulfoxidationKPSKEEVMAATQAEG
CCCHHHHHHHHHCCC		2.0721406390
623PhosphorylationMEVVQRISNVKVNPK
HHHHHHHHCCCCCCC		37.4520068231
626AcetylationVQRISNVKVNPKTDK
HHHHHCCCCCCCCCC		40.3125953088
631PhosphorylationNVKVNPKTDKPYEDV
CCCCCCCCCCCCCCC		50.9828152594
635PhosphorylationNPKTDKPYEDVSIIN
CCCCCCCCCCCEEEE		30.4228152594
639PhosphorylationDKPYEDVSIINITVK
CCCCCCCEEEEEEEC		30.0328152594
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 PPWD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPWD1_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 PPWD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARBK1_HUMANADRBK1physical
26344197
PTBP3_HUMANPTBP3physical
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 PPWD1_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 ALA-2, AND MASS SPECTROMETRY.

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