PUM5_ARATH - dbPTM
PUM5_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUM5_ARATH
UniProt AC Q9LJX4
Protein Name Pumilio homolog 5
Gene Name APUM5
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 961
Subcellular Localization Cytoplasm .
Protein Description Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. Binds the APUM-binding elements (APBEs) in the 3'-UTR mRNA sequence of CLV1, PNH, WUS and FAS2..
Protein Sequence MTTTQSAMRMVEGDHIKNWQASSDSGIFGSLDMAVEDLGFLMKRNRLDSGDQTGKFPSRSESAPPSMEGSFAALRNLLKQQEGSSSEVLSRAIENYDSEEEIRSDPAYVAYYLSNINLNPRLPPPLISRENQHLLRHFGDNNQSPTTSWDNMGIRSSLHSSRTALSTHREEPEDEASSGEQQSYASLAGRRKSIADMIQEDFPLTLSSVFKRPHSAGNRPIAQDIHAISSDTSSEHARRLPESDINSVNLLRETDSLSSDAIASEDPFTTDLASQSFTNAQTERLNARQASHEDNNLSVFGASPPSSVASRMRRNQEDQQSQGRRMPPQYTPSSYQVQASSPQQMSYPRIGGTQDMMQSLPKIATGEVHSTFQSPHGLAPPPMYTSTAAYMTSLSPFYHQNFQSSGMFVPQYNYGGYPPASGIVPQYMSGYPSHEATVPMPYDISSTSSGYNNPRLLPGVSSSGQNIPSLVDPFQLQYFQQAQVDAYAPPFQSSTDSFGQKDQQAVGYMANHEPLNSPLSPGYGLQSPRHMGNYFAVPPGVRVMPQYPGSPLASPVMPSSPVGGMMSHFGRRSETRYHQQGPSRNTGIYPGGWQGNRGGASSIVDDLKRHSFLDELKSPNARKLELSDIAGRVVEFSVDQHGSRFIQQKLEHCSDEEKASVFSEVLPQASKLMTDVFGNYVIQKFIEHGTPAQREELVKQLAGQMVSLSLQMYGCRVIQKALEVIDVDQKTELIRELDGNVLKCVRDQNGNHVIQKCIESMPAGRIGFVIAAFRGQVATLSTHPYGCRVIQRILEHCSDDEETHCIIDEILESAFALAHDQYGNYVTQHVLERGKPDERRQIIEKLTGNVVQMSQHKYASNVVEKCLEHADSTEREFLIEEIMGKSEEDNHLLAMMKDQFANYVVQKVLEISKDQQREILVQRMKIHLQSLRKYTYGKHIVARFEQLFGEESEVSEEGTEG
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
49PhosphorylationMKRNRLDSGDQTGKF
HHHCCCCCCCCCCCC		49.1927288362
53PhosphorylationRLDSGDQTGKFPSRS
CCCCCCCCCCCCCCC		47.2627288362
60PhosphorylationTGKFPSRSESAPPSM
CCCCCCCCCCCCCCH		39.9923776212
62PhosphorylationKFPSRSESAPPSMEG
CCCCCCCCCCCCHHH		47.5230291188
66PhosphorylationRSESAPPSMEGSFAA
CCCCCCCCHHHHHHH		28.5423776212
70PhosphorylationAPPSMEGSFAALRNL
CCCCHHHHHHHHHHH		9.8223776212
96PhosphorylationLSRAIENYDSEEEIR
HHHHHHCCCCHHHHH		14.2025561503
98PhosphorylationRAIENYDSEEEIRSD
HHHHCCCCHHHHHCC		36.2323111157
163PhosphorylationSSLHSSRTALSTHRE
HHHHHHCCHHHHCCC		33.6230407730
166PhosphorylationHSSRTALSTHREEPE
HHHCCHHHHCCCCCC		21.5030407730
167PhosphorylationSSRTALSTHREEPED
HHCCHHHHCCCCCCC		26.2930407730
177PhosphorylationEEPEDEASSGEQQSY
CCCCCCCCCHHHHHH		36.5130407730
178PhosphorylationEPEDEASSGEQQSYA
CCCCCCCCHHHHHHH		54.0930407730
183PhosphorylationASSGEQQSYASLAGR
CCCHHHHHHHHHHCC		23.5130407730
184PhosphorylationSSGEQQSYASLAGRR
CCHHHHHHHHHHCCH		8.8930407730
193PhosphorylationSLAGRRKSIADMIQE
HHHCCHHHHHHHHHH		22.61-
203 (in isoform 2)Phosphorylation-36.4430589143
243PhosphorylationHARRLPESDINSVNL
HHHHCCHHHCCHHHH		41.6825561503
247PhosphorylationLPESDINSVNLLRET
CCHHHCCHHHHHHHC		16.8329654922
254PhosphorylationSVNLLRETDSLSSDA
HHHHHHHCCCCCCCC		25.1823776212
256PhosphorylationNLLRETDSLSSDAIA
HHHHHCCCCCCCCCC		37.2623776212
258PhosphorylationLRETDSLSSDAIASE
HHHCCCCCCCCCCCC		30.0823776212
259PhosphorylationRETDSLSSDAIASED
HHCCCCCCCCCCCCC		36.0323776212
264PhosphorylationLSSDAIASEDPFTTD
CCCCCCCCCCCCCHH		36.1023776212
269PhosphorylationIASEDPFTTDLASQS
CCCCCCCCHHHHHCC		25.4523776212
270PhosphorylationASEDPFTTDLASQSF
CCCCCCCHHHHHCCC		29.4223776212
274PhosphorylationPFTTDLASQSFTNAQ
CCCHHHHHCCCCHHH		33.3823776212
276PhosphorylationTTDLASQSFTNAQTE
CHHHHHCCCCHHHHH		31.3823776212
278PhosphorylationDLASQSFTNAQTERL
HHHHCCCCHHHHHHH		34.5923776212
282PhosphorylationQSFTNAQTERLNARQ
CCCCHHHHHHHHHHH		22.2123776212
303PhosphorylationNLSVFGASPPSSVAS
CCCCCCCCCCHHHHH		37.4127531888
306PhosphorylationVFGASPPSSVASRMR
CCCCCCCHHHHHHHH		40.6125561503
307PhosphorylationFGASPPSSVASRMRR
CCCCCCHHHHHHHHH		27.7225561503
421PhosphorylationYGGYPPASGIVPQYM
CCCCCCCCCCCCCHH		34.5228011693
517PhosphorylationANHEPLNSPLSPGYG
CCCCCCCCCCCCCCC		34.6027288362
520PhosphorylationEPLNSPLSPGYGLQS
CCCCCCCCCCCCCCC		21.4727545962
523PhosphorylationNSPLSPGYGLQSPRH
CCCCCCCCCCCCCCC		20.3227545962
527PhosphorylationSPGYGLQSPRHMGNY
CCCCCCCCCCCCCCC		29.0124601666
534PhosphorylationSPRHMGNYFAVPPGV
CCCCCCCCCCCCCCC		6.2819376835
547PhosphorylationGVRVMPQYPGSPLAS
CCEECCCCCCCCCCC		12.0427288362
550PhosphorylationVMPQYPGSPLASPVM
ECCCCCCCCCCCCCC		16.5530589143
554PhosphorylationYPGSPLASPVMPSSP
CCCCCCCCCCCCCCC		26.2227288362
559PhosphorylationLASPVMPSSPVGGMM
CCCCCCCCCCCCHHH		29.2227288362
560PhosphorylationASPVMPSSPVGGMMS
CCCCCCCCCCCHHHH		20.1030589143
567PhosphorylationSPVGGMMSHFGRRSE
CCCCHHHHHCCCCCC		13.5327288362
602PhosphorylationGNRGGASSIVDDLKR
CCCCCHHHHHHHHHH		26.5419880383
618PhosphorylationSFLDELKSPNARKLE
CCHHHHCCCCCCCCC		35.6924601666
663PhosphorylationEEKASVFSEVLPQAS
HHHHHHHHHHHHHHH		25.3324243849
952PhosphorylationEQLFGEESEVSEEGT
HHHHCCCCCCCCCCC		38.7127531888
955PhosphorylationFGEESEVSEEGTEG-
HCCCCCCCCCCCCC-		26.3627531888
959PhosphorylationSEVSEEGTEG-----
CCCCCCCCCC-----		40.5929654922
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 PUM5_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUM5_ARATH !!
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 PUM5_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PUM5_ARATH !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUM5_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-534, AND IDENTIFICATIONBY MASS SPECTROMETRY.

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