PROX1_MOUSE - dbPTM
PROX1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PROX1_MOUSE
UniProt AC P48437
Protein Name Prospero homeobox protein 1
Gene Name Prox1
Organism Mus musculus (Mouse).
Sequence Length 737
Subcellular Localization Nucleus . RORG promotes its nuclear localization.
Protein Description Transcription factor involved in developmental processes such as cell fate determination, gene transcriptional regulation and progenitor cell regulation in a number of organs. Plays a critical role in embryonic development and functions as a key regulatory protein in neurogenesis and the development of the heart, eye lens, liver, pancreas and the lymphatic system. Involved in the regulation of the circadian rhythm. Represses: transcription of the retinoid-related orphan receptor RORG, transcriptional activator activity of RORA and RORG and the expression of RORA/G-target genes including core clock components: ARNTL/BMAL1, NPAS2 and CRY1 and metabolic genes: AVPR1A and ELOVL3..
Protein Sequence MPDHDSTALLSRQTKRRRVDIGVKRTVGTASAFFAKARATFFSAMNPQGSEQDVEYSVVQHADGEKSNVLRKLLKRANSYEDAMMPFPGATIISQLLKNNMNKNGGTEPSFQASGLSSTGSEVHQEDICSNSSRDSPPECLSPFGRPTMSQFDVDRLCDEHLRAKRARVENIIRGMSHSPSVALRGNENEREMAPQSVSPRESYRENKRKQKLPQQQQQSFQQLVSARKEQKREERRQLKQQLEDMQKQLRQLQEKFYQVYDSTDSENDEDGDLSEDSMRSEILDARAQDSVGRSDNEMCELDPGQFIDRARALIREQEMAENKPKREGSNKERDHGPNSLQPEGKHLAETLKQELNTAMSQVVDTVVKVFSAKPSRQVPQVFPPLQIPQARFAVNGENHNFHTANQRLQCFGDVIIPNPLDTFGSVQMPSSTDQTEALPLVVRKNSSEQSASGPATGGHHQPLHQSPLSATAGFTTPSFRHPFPLPLMAYPFQSPLGAPSGSFSGKDRASPESLDLTRDTTSLRTKMSSHHLSHHPCSPAHPPSTAEGLSLSLIKSECGDLQDMSDISPYSGSAMQEGLSPNHLKKAKLMFFYTRYPSSNMLKTYFSDVKFNRCITSQLIKWFSNFREFYYIQMEKYARQAINDGVTSTEELSITRDCELYRALNMHYNKANDFEVPERFLEVAQITLREFFNAIIAGKDVDPSWKKAIYKVICKLDSEVPEIFKSPNCLQELLHE
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
11PhosphorylationHDSTALLSRQTKRRR
HHHHHHHCHHHHCCC
24.1623567750
79PhosphorylationKLLKRANSYEDAMMP
HHHHHCCCCCHHCCC
28.9926643407
80PhosphorylationLLKRANSYEDAMMPF
HHHHCCCCCHHCCCC
20.0326643407
142PhosphorylationDSPPECLSPFGRPTM
CCCHHHCCCCCCCCH
29.8225521595
176OxidationVENIIRGMSHSPSVA
HHHHHHCCCCCCCCC
2.0417242355
177PhosphorylationENIIRGMSHSPSVAL
HHHHHCCCCCCCCCC
24.5225521595
179PhosphorylationIIRGMSHSPSVALRG
HHHCCCCCCCCCCCC
16.1525521595
181PhosphorylationRGMSHSPSVALRGNE
HCCCCCCCCCCCCCC
24.0422324799
193OxidationGNENEREMAPQSVSP
CCCCCCCCCCCCCCH
9.1517242355
197PhosphorylationEREMAPQSVSPRESY
CCCCCCCCCCHHHHH
24.4125521595
199PhosphorylationEMAPQSVSPRESYRE
CCCCCCCCHHHHHHH
24.4025521595
212UbiquitinationRENKRKQKLPQQQQQ
HHHHHHHCCCHHHHH
66.2322790023
220PhosphorylationLPQQQQQSFQQLVSA
CCHHHHHHHHHHHHH
22.2325521595
226PhosphorylationQSFQQLVSARKEQKR
HHHHHHHHHHHHHHH
30.8329472430
232SumoylationVSARKEQKREERRQL
HHHHHHHHHHHHHHH
63.97-
258PhosphorylationRQLQEKFYQVYDSTD
HHHHHHHHHHHHCCC
14.2422324799
261PhosphorylationQEKFYQVYDSTDSEN
HHHHHHHHHCCCCCC
6.6622324799
263PhosphorylationKFYQVYDSTDSENDE
HHHHHHHCCCCCCCC
19.2122324799
264PhosphorylationFYQVYDSTDSENDED
HHHHHHCCCCCCCCC
40.4222324799
266PhosphorylationQVYDSTDSENDEDGD
HHHHCCCCCCCCCCC
38.0922324799
275PhosphorylationNDEDGDLSEDSMRSE
CCCCCCCCHHHHHHH
44.0622324799
291PhosphorylationLDARAQDSVGRSDNE
HHHHHHHCCCCCCCC
17.8721082442
295PhosphorylationAQDSVGRSDNEMCEL
HHHCCCCCCCCCCCC
38.5725521595
299OxidationVGRSDNEMCELDPGQ
CCCCCCCCCCCCHHH
2.4217242355
326SumoylationEMAENKPKREGSNKE
HHHHCCCCCCCCCCC
65.77-
353SumoylationKHLAETLKQELNTAM
HHHHHHHHHHHHHHH
49.50-
392MethylationPLQIPQARFAVNGEN
CCCCCCEEEEECCCC
18.1430988941
432PhosphorylationGSVQMPSSTDQTEAL
CCCCCCCCCCCCCCC
30.08-
453PhosphorylationNSSEQSASGPATGGH
CCCCCCCCCCCCCCC
51.0223567750
457PhosphorylationQSASGPATGGHHQPL
CCCCCCCCCCCCCCC
46.9921743459
467PhosphorylationHHQPLHQSPLSATAG
CCCCCCCCCCCCCCC
19.6321743459
470PhosphorylationPLHQSPLSATAGFTT
CCCCCCCCCCCCCCC
27.2721743459
472PhosphorylationHQSPLSATAGFTTPS
CCCCCCCCCCCCCCC
24.7623567750
491PhosphorylationFPLPLMAYPFQSPLG
CCCCEEEECCCCCCC
7.2123984901
495PhosphorylationLMAYPFQSPLGAPSG
EEEECCCCCCCCCCC
23.5926643407
511PhosphorylationFSGKDRASPESLDLT
CCCCCCCCHHHCCCC
30.0525521595
514PhosphorylationKDRASPESLDLTRDT
CCCCCHHHCCCCCCC
30.4825521595
518PhosphorylationSPESLDLTRDTTSLR
CHHHCCCCCCCHHHH
26.6025521595
521PhosphorylationSLDLTRDTTSLRTKM
HCCCCCCCHHHHHHH
18.2623984901
522PhosphorylationLDLTRDTTSLRTKMS
CCCCCCCHHHHHHHH
30.0123984901
523PhosphorylationDLTRDTTSLRTKMSS
CCCCCCHHHHHHHHH
20.2523984901
526PhosphorylationRDTTSLRTKMSSHHL
CCCHHHHHHHHHCCC
36.0720469934
529PhosphorylationTSLRTKMSSHHLSHH
HHHHHHHHHCCCCCC
28.2426643407
530PhosphorylationSLRTKMSSHHLSHHP
HHHHHHHHCCCCCCC
16.0726643407
534PhosphorylationKMSSHHLSHHPCSPA
HHHHCCCCCCCCCCC
18.5226643407
539PhosphorylationHLSHHPCSPAHPPST
CCCCCCCCCCCCCCC
29.5826643407
545PhosphorylationCSPAHPPSTAEGLSL
CCCCCCCCCHHHHCH
44.71-
556SumoylationGLSLSLIKSECGDLQ
HHCHHHHHHHCCCCC
45.56-
557PhosphorylationLSLSLIKSECGDLQD
HCHHHHHHHCCCCCC
31.00-
566PhosphorylationCGDLQDMSDISPYSG
CCCCCCHHHCCCCCC
39.8326643407
569PhosphorylationLQDMSDISPYSGSAM
CCCHHHCCCCCCCHH
23.8326643407
571PhosphorylationDMSDISPYSGSAMQE
CHHHCCCCCCCHHHC
20.9026643407
572PhosphorylationMSDISPYSGSAMQEG
HHHCCCCCCCHHHCC
29.6529472430
574PhosphorylationDISPYSGSAMQEGLS
HCCCCCCCHHHCCCC
18.0229472430
581PhosphorylationSAMQEGLSPNHLKKA
CHHHCCCCHHHHHHC
34.2229472430
611UbiquitinationKTYFSDVKFNRCITS
HHHHHCCCCHHHHHH
41.7422790023
648PhosphorylationQAINDGVTSTEELSI
HHHHCCCCCHHHHHC
35.1517203969
649PhosphorylationAINDGVTSTEELSIT
HHHCCCCCHHHHHCC
31.2617203969
650PhosphorylationINDGVTSTEELSITR
HHCCCCCHHHHHCCC
24.9017203969
700UbiquitinationFNAIIAGKDVDPSWK
HHHHHCCCCCCHHHH
45.6222790023
716UbiquitinationAIYKVICKLDSEVPE
HHHHHHHHHCCCCCH
44.1822790023

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 PROX1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PROX1_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 PROX1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NKX25_MOUSENkx2-5genetic
22647876

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PROX1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND MASSSPECTROMETRY.
"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-177; SER-179; SER-291;SER-511 AND SER-514, 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 THR-650, AND MASSSPECTROMETRY.

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