FKB15_MOUSE - dbPTM
FKB15_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKB15_MOUSE
UniProt AC Q6P9Q6
Protein Name FK506-binding protein 15
Gene Name Fkbp15
Organism Mus musculus (Mouse).
Sequence Length 1216
Subcellular Localization Cytoplasm . Cell projection, axon . Early endosome . Present in axons and neuronal growth cones.
Protein Description Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement (By similarity). May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase..
Protein Sequence MFGAGDEDDTDFLSPSGGAKLASLFGLDQATMGHGNEFFQYTAPKQPKKGQGTAAGNQTAPKPAPATTGTSSVLFATAVHAYRYINGQYAKQGKFGAAVLGNHTSREYRILLYISQQQPVTVATIHLNFELMVRPNNYSTFYDDQRQNWSIMFESEKAAVSFNKQVCVAKCNSISSLDAVLCQDLVAAEGPAVETGDSLEVAYTGWLLQNHVLGQVFDSTANKDKPLRLKLGSGKVVKGLEDGLLGMKKGGKRLIITPSACAAGSEGVIGWTQPTDSILVFEVEVRRVKFARDSGSDGHSVSSRDSAAPSPIPASDSLSADPVVTPLPLPLKPGEPGLRSKSNSLSEQLTVNSNPDTVKAKLISRMAKMGQPMLPILPPQLDSNDSETEDATVLRGAGQSLVTPSIQPSLQPAHPVLPQMASQAPQPSGSGLQTPSAALMQAVSLDSHSAVSGNAQNFQPYAGVQAYAYPQTPSVTSQLQPVRPLYPAPLSQAPHFQGSGDMMSFLMTEARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPLRPSLEQPGPATPGMPPAPPSGETQEAPEVLPEQVVGETTPLPLQALPTPENGAQTRKGEPAEAEVPSEIKDSSLPPQPAGIPAHRVLGPPTSIPPKPPGPVTMDSESEEMLAADQRTVQPNGLLGEEHVREVATDGLLQGNSRRLSLTPDPEKGEPPALDPESQGGEAQPPECKQAEDVSSSGPRETLLDTELASAAAGTSLRHNQDSQHCSLSGDEEDELFKGATLKVPRPTAQPEEEDEDEVSMKGRPPPTPLFGDDDDDDDDDIGWLG
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
1Acetylation-------MFGAGDED
-------CCCCCCCC		32.82-
10PhosphorylationGAGDEDDTDFLSPSG
CCCCCCCCCCCCCCH		40.7628576409
14PhosphorylationEDDTDFLSPSGGAKL
CCCCCCCCCCHHHHH		19.6025619855
16PhosphorylationDTDFLSPSGGAKLAS
CCCCCCCCHHHHHHH		46.6225619855
23PhosphorylationSGGAKLASLFGLDQA
CHHHHHHHHHCCCCC		34.37-
72PhosphorylationPATTGTSSVLFATAV
CCCCCCCHHHHHHHH		23.76-
91AcetylationYINGQYAKQGKFGAA
HHCCCCCCCCCCCEE		55.43-
235 (in isoform 2)Malonylation-45.6232601280
294PhosphorylationRVKFARDSGSDGHSV
EEEEECCCCCCCCCC		34.3425266776
296PhosphorylationKFARDSGSDGHSVSS
EEECCCCCCCCCCCC		44.3523684622
300PhosphorylationDSGSDGHSVSSRDSA
CCCCCCCCCCCCCCC		29.2625266776
302PhosphorylationGSDGHSVSSRDSAAP
CCCCCCCCCCCCCCC		23.7519060867
303PhosphorylationSDGHSVSSRDSAAPS
CCCCCCCCCCCCCCC		37.6422817900
306PhosphorylationHSVSSRDSAAPSPIP
CCCCCCCCCCCCCCC		25.8122942356
310PhosphorylationSRDSAAPSPIPASDS
CCCCCCCCCCCCCCC		30.6325521595
315PhosphorylationAPSPIPASDSLSADP
CCCCCCCCCCCCCCC		23.5221082442
317PhosphorylationSPIPASDSLSADPVV
CCCCCCCCCCCCCCC		23.0222942356
319PhosphorylationIPASDSLSADPVVTP
CCCCCCCCCCCCCCC		34.2822942356
325PhosphorylationLSADPVVTPLPLPLK
CCCCCCCCCCCCCCC		21.2422942356
340PhosphorylationPGEPGLRSKSNSLSE
CCCCCCCCCCCCCCC		45.5426824392
342PhosphorylationEPGLRSKSNSLSEQL
CCCCCCCCCCCCCCC		32.6627087446
344PhosphorylationGLRSKSNSLSEQLTV
CCCCCCCCCCCCCCC		40.1225521595
346PhosphorylationRSKSNSLSEQLTVNS
CCCCCCCCCCCCCCC		24.1027742792
350PhosphorylationNSLSEQLTVNSNPDT
CCCCCCCCCCCCHHH		19.8225619855
353PhosphorylationSEQLTVNSNPDTVKA
CCCCCCCCCHHHHHH		45.4625619855
357PhosphorylationTVNSNPDTVKAKLIS
CCCCCHHHHHHHHHH		25.7625619855
359UbiquitinationNSNPDTVKAKLISRM
CCCHHHHHHHHHHHH		41.7322790023
359 (in isoform 2)Ubiquitination-41.7322790023
383PhosphorylationILPPQLDSNDSETED
CCCCCCCCCCCCCCC		51.6422324799
386PhosphorylationPQLDSNDSETEDATV
CCCCCCCCCCCCCEE		51.1427087446
388PhosphorylationLDSNDSETEDATVLR
CCCCCCCCCCCEEEC		43.0222324799
392PhosphorylationDSETEDATVLRGAGQ
CCCCCCCEEECCCCC		32.1826643407
518DimethylationRQHNTEIRMAVNKVA
HHCCHHHHHHHHHHH		10.77-
617PhosphorylationMMEKRNNSLQTATEN
HHHHHCCCCCHHHHH		25.9622942356
620PhosphorylationKRNNSLQTATENTQA
HHCCCCCHHHHHHHH		40.6223984901
622PhosphorylationNNSLQTATENTQARI
CCCCCHHHHHHHHHH		32.9123984901
663AcetylationKMTAHQKKETELQLQ
HCCHHHHCCCHHHEE		64.4015609725
676AcetylationLQLTDNLKETDLLRG
EEECCCCHHHHHHHH		65.9015609735
721PhosphorylationRQLELKVTSLEEELT
HHHHEEEECHHHHHH		26.4629899451
722PhosphorylationQLELKVTSLEEELTD
HHHEEEECHHHHHHH		36.4522817900
735PhosphorylationTDLRAEKTSLEKNLS
HHHHHHHHHHHHHHH		30.0122942356
783PhosphorylationLLKKARVSTDQAAAE
HHHHHCCCHHHHHHH		22.2530635358
784PhosphorylationLKKARVSTDQAAAEQ
HHHHCCCHHHHHHHH		29.3130635358
868PhosphorylationQRLEKTKSQAPAGRA
HHHHHHHHHCCCCCC		36.4821454597
880PhosphorylationGRAAADPSEKVKKIM
CCCCCCHHHHHHHHH		51.0724759943
948PhosphorylationEKKPLRPSLEQPGPA
HHCCCCCCCCCCCCC		37.8025338131
1012PhosphorylationPAEAEVPSEIKDSSL
CCCCCCCCCCCCCCC		58.0721743459
1017PhosphorylationVPSEIKDSSLPPQPA
CCCCCCCCCCCCCCC		28.8622817900
1018PhosphorylationPSEIKDSSLPPQPAG
CCCCCCCCCCCCCCC		55.8425521595
1047PhosphorylationPKPPGPVTMDSESEE
CCCCCCCCCCCCCHH		20.5626239621
1050PhosphorylationPGPVTMDSESEEMLA
CCCCCCCCCCHHHHH		32.0026239621
1052PhosphorylationPVTMDSESEEMLAAD
CCCCCCCCHHHHHCC		42.6926239621
1087PhosphorylationDGLLQGNSRRLSLTP
CCCCCCCCCCCCCCC		26.1229514104
1091PhosphorylationQGNSRRLSLTPDPEK
CCCCCCCCCCCCCCC		28.5227087446
1093PhosphorylationNSRRLSLTPDPEKGE
CCCCCCCCCCCCCCC		23.4425521595
1108PhosphorylationPPALDPESQGGEAQP
CCCCCCHHCCCCCCC		39.2425619855
1125PhosphorylationCKQAEDVSSSGPRET
CCCCHHCCCCCCCHH		30.9825521595
1126PhosphorylationKQAEDVSSSGPRETL
CCCHHCCCCCCCHHH		38.8823684622
1127PhosphorylationQAEDVSSSGPRETLL
CCHHCCCCCCCHHHH		45.3625521595
1132PhosphorylationSSSGPRETLLDTELA
CCCCCCHHHHHHHHH		33.6223984901
1136PhosphorylationPRETLLDTELASAAA
CCHHHHHHHHHHHHH		32.6323984901
1140PhosphorylationLLDTELASAAAGTSL
HHHHHHHHHHHCCCC		30.9423984901
1145PhosphorylationLASAAAGTSLRHNQD
HHHHHHCCCCCCCCC		21.6223984901
1146PhosphorylationASAAAGTSLRHNQDS
HHHHHCCCCCCCCCC		23.6126824392
1153PhosphorylationSLRHNQDSQHCSLSG
CCCCCCCCCCCCCCC		16.4427742792
1157PhosphorylationNQDSQHCSLSGDEED
CCCCCCCCCCCCCCC		24.3625521595
1159PhosphorylationDSQHCSLSGDEEDEL
CCCCCCCCCCCCCHH		28.0927087446
1171PhosphorylationDELFKGATLKVPRPT
CHHHCCCEEECCCCC		35.4625777480
1190PhosphorylationEEDEDEVSMKGRPPP
CCCCCCCCCCCCCCC		16.8417203969
1198PhosphorylationMKGRPPPTPLFGDDD
CCCCCCCCCCCCCCC		38.1029514104
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 FKB15_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKB15_MOUSE !!
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 FKB15_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FKB15_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FKB15_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-340, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1091; THR-1093; SER-1157AND SER-1159, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1091; THR-1093; SER-1157AND SER-1159, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1190, AND MASSSPECTROMETRY.

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