HDGR2_MOUSE - dbPTM
HDGR2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDGR2_MOUSE
UniProt AC Q3UMU9
Protein Name Hepatoma-derived growth factor-related protein 2
Gene Name Hdgfl2
Organism Mus musculus (Mouse).
Sequence Length 669
Subcellular Localization Nucleus . Isoform 4 displays a punctate pattern and colocalizes with N-terminally processed HDFG.
Protein Description Involved in cellular growth control, through the regulation of cyclin D1 expression (By similarity). Associates with chromatin. Isoform 1 and isoform 3 bind to condensed chromatin in mitotic cells. Isoform 4 binds to non-condensed chromatin in the presence of HDGF..
Protein Sequence MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEGLWEIQNNPHASYSAPPPVSSSDSEAPEADLGCGSDVDKDKESRRVMTVTAVTTTATSDRMESDSDSDKSSDHSGLKRKTPVLKVSVSKRARRASSDLDQASVSPSEEDSESPSESEKTSDQDFTPEKKTAARPPRRGPLGGRKKKKVPSASDSDSKADSDGAKEEPVVTAQPSPSSSSSSSSSSSSDSDVSVKKPPRGRKPAEKPPPKPRGRRPKPERPPSTSSSDSDSDSGEVDRISEWKRRDEERRRELEARRRREQEEELRRLREQEREEKERRKERAERGGSSGEELEDEEPVKKRSRKARGRGTPSSSDSEPEGELGKEGKKLAKKSQLPGSESARKPGQKEKRGRPDEKPRARPVKVERTRKRSEGLSLERKGEKKKEPSVEERLQKLHSEIKFALKVDNPDVRKCLSALEELGTLQVTSQILQKNTDVVATLKKIRRYKANKDVMAKAAEVYTRLKSRVLGPKVEALQKVNKAGAEKERADNEKLEEQPGEQAPRELAEDEPSTDRSAPVNGEATSQKGENMEDRAQEDGQDSEDGPRGGSSEELHDSPRDNSDPAKPGNERQDHERTRLASESANDDNEDS
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
6Acetylation--MPHAFKPGDLVFA
--CCCCCCCCCEEEE		49.2022826441
39AcetylationAVKPPPNKYPIFFFG
CCCCCCCCCCEEEEE		59.1722826441
63UbiquitinationKDLFPYDKCKDKYGK
HHCCCHHHHHHCCCC		37.02-
114PhosphorylationEADLGCGSDVDKDKE
HHHCCCCCCCCCCCH		38.24-
127PhosphorylationKESRRVMTVTAVTTT
CHHCCEEEEEEEEEE		16.3125619855
129PhosphorylationSRRVMTVTAVTTTAT
HCCEEEEEEEEEECC		13.2725619855
132PhosphorylationVMTVTAVTTTATSDR
EEEEEEEEEECCCCC		18.9025619855
133PhosphorylationMTVTAVTTTATSDRM
EEEEEEEEECCCCCC		14.0825619855
134PhosphorylationTVTAVTTTATSDRME
EEEEEEEECCCCCCC		20.6925521595
136PhosphorylationTAVTTTATSDRMESD
EEEEEECCCCCCCCC		29.1225521595
137PhosphorylationAVTTTATSDRMESDS
EEEEECCCCCCCCCC		22.2825521595
146PhosphorylationRMESDSDSDKSSDHS
CCCCCCCCCCCCCCC		51.3825195567
149PhosphorylationSDSDSDKSSDHSGLK
CCCCCCCCCCCCCCC		46.0925195567
150PhosphorylationDSDSDKSSDHSGLKR
CCCCCCCCCCCCCCC		45.1225195567
153PhosphorylationSDKSSDHSGLKRKTP
CCCCCCCCCCCCCCC		51.3027841257
159PhosphorylationHSGLKRKTPVLKVSV
CCCCCCCCCEEEEEH		23.7426060331
165PhosphorylationKTPVLKVSVSKRARR
CCCEEEEEHHHHHHH		21.0624719451
167PhosphorylationPVLKVSVSKRARRAS
CEEEEEHHHHHHHHC		14.6629176673
174PhosphorylationSKRARRASSDLDQAS
HHHHHHHCCCCHHHC		23.6725619855
175PhosphorylationKRARRASSDLDQASV
HHHHHHCCCCHHHCC		41.0025619855
181PhosphorylationSSDLDQASVSPSEED
CCCCHHHCCCCCCCC		19.9325619855
183PhosphorylationDLDQASVSPSEEDSE
CCHHHCCCCCCCCCC		21.8825619855
185PhosphorylationDQASVSPSEEDSESP
HHHCCCCCCCCCCCC		46.2225619855
189PhosphorylationVSPSEEDSESPSESE
CCCCCCCCCCCCHHC		43.1625619855
191PhosphorylationPSEEDSESPSESEKT
CCCCCCCCCCHHCCC		37.3625619855
193PhosphorylationEEDSESPSESEKTSD
CCCCCCCCHHCCCCC		64.1325619855
195PhosphorylationDSESPSESEKTSDQD
CCCCCCHHCCCCCCC		49.0525619855
198PhosphorylationSPSESEKTSDQDFTP
CCCHHCCCCCCCCCC		33.2225521595
199PhosphorylationPSESEKTSDQDFTPE
CCHHCCCCCCCCCCC		44.3225521595
204PhosphorylationKTSDQDFTPEKKTAA
CCCCCCCCCCHHCCC		38.5427149854
228 (in isoform 2)Phosphorylation-32.8127841257
228 (in isoform 3)Phosphorylation-32.8128285833
229PhosphorylationRKKKKVPSASDSDSK
CCCCCCCCCCCCCCC		43.3125521595
230 (in isoform 2)Phosphorylation-15.9927818261
230 (in isoform 3)Phosphorylation-15.9928285833
231PhosphorylationKKKVPSASDSDSKAD
CCCCCCCCCCCCCCC		41.8225521595
232 (in isoform 2)Phosphorylation-57.0627818261
233PhosphorylationKVPSASDSDSKADSD
CCCCCCCCCCCCCCC		41.0925521595
235PhosphorylationPSASDSDSKADSDGA
CCCCCCCCCCCCCCC		33.4223737553
238 (in isoform 3)Phosphorylation-51.5025195567
239PhosphorylationDSDSKADSDGAKEEP
CCCCCCCCCCCCCCC		42.6923684622
240 (in isoform 3)Phosphorylation-62.7125195567
242 (in isoform 3)Phosphorylation-22.5230352176
253PhosphorylationPVVTAQPSPSSSSSS
CCEEECCCCCCCCCC		25.9025293948
255PhosphorylationVTAQPSPSSSSSSSS
EEECCCCCCCCCCCC		47.3825293948
256PhosphorylationTAQPSPSSSSSSSSS
EECCCCCCCCCCCCC		37.3125293948
257PhosphorylationAQPSPSSSSSSSSSS
ECCCCCCCCCCCCCC		38.2825293948
258PhosphorylationQPSPSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8725293948
259PhosphorylationPSPSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.8725293948
260PhosphorylationSPSSSSSSSSSSSSD
CCCCCCCCCCCCCCC		35.8725293948
261PhosphorylationPSSSSSSSSSSSSDS
CCCCCCCCCCCCCCC		35.8725293948
262PhosphorylationSSSSSSSSSSSSDSD
CCCCCCCCCCCCCCC		35.8725293948
263PhosphorylationSSSSSSSSSSSDSDV
CCCCCCCCCCCCCCC		35.8725293948
264PhosphorylationSSSSSSSSSSDSDVS
CCCCCCCCCCCCCCC		35.4925293948
265PhosphorylationSSSSSSSSSDSDVSV
CCCCCCCCCCCCCCC		39.8625293948
266PhosphorylationSSSSSSSSDSDVSVK
CCCCCCCCCCCCCCC		42.9826525534
268PhosphorylationSSSSSSDSDVSVKKP
CCCCCCCCCCCCCCC		41.6925293948
271PhosphorylationSSSDSDVSVKKPPRG
CCCCCCCCCCCCCCC		32.9625293948
307PhosphorylationPSTSSSDSDSDSGEV
CCCCCCCCCCCCCCC		40.75-
309PhosphorylationTSSSDSDSDSGEVDR
CCCCCCCCCCCCCCH		37.3130165576
311PhosphorylationSSDSDSDSGEVDRIS
CCCCCCCCCCCCHHH		40.5830165576
348UbiquitinationEELRRLREQEREEKE
HHHHHHHHHHHHHHH		62.4827667366
357UbiquitinationEREEKERRKERAERG
HHHHHHHHHHHHHHC		46.4027667366
366PhosphorylationERAERGGSSGEELED
HHHHHCCCCCCCCCC		37.6818388127
367PhosphorylationRAERGGSSGEELEDE
HHHHCCCCCCCCCCC		54.2018388127
389PhosphorylationRKARGRGTPSSSDSE
HHHCCCCCCCCCCCC		20.7327087446
391PhosphorylationARGRGTPSSSDSEPE
HCCCCCCCCCCCCCC		42.1627087446
392PhosphorylationRGRGTPSSSDSEPEG
CCCCCCCCCCCCCCC		39.0927087446
393PhosphorylationGRGTPSSSDSEPEGE
CCCCCCCCCCCCCCC		49.8727087446
395PhosphorylationGTPSSSDSEPEGELG
CCCCCCCCCCCCCCC		57.9327087446
412PhosphorylationGKKLAKKSQLPGSES
HHHHHHHHCCCCCHH		35.9228066266
417PhosphorylationKKSQLPGSESARKPG
HHHCCCCCHHHCCCC		26.8329895711
419PhosphorylationSQLPGSESARKPGQK
HCCCCCHHHCCCCCC		34.7625266776
450PhosphorylationVERTRKRSEGLSLER
EEHHHHHHCCCCCCC		38.7726824392
454PhosphorylationRKRSEGLSLERKGEK
HHHHCCCCCCCCCCC		38.7526824392
472UbiquitinationPSVEERLQKLHSEIK
CCHHHHHHHHHHHHH		53.1127667366
473UbiquitinationSVEERLQKLHSEIKF
CHHHHHHHHHHHHHH		53.4027667366
482UbiquitinationHSEIKFALKVDNPDV
HHHHHHHHCCCCHHH		6.6427667366
483UbiquitinationSEIKFALKVDNPDVR
HHHHHHHCCCCHHHH		44.0822790023
483 (in isoform 3)Ubiquitination-44.0822790023
492 (in isoform 3)Ubiquitination-2.25-
520UbiquitinationTDVVATLKKIRRYKA
CHHHHHHHHHHHHHC		41.6322790023
520 (in isoform 3)Ubiquitination-41.6322790023
529 (in isoform 3)Ubiquitination-57.47-
544PhosphorylationEVYTRLKSRVLGPKV
HHHHHHHHHCCCHHH		32.0121183079
550AcetylationKSRVLGPKVEALQKV
HHHCCCHHHHHHHHH		51.4123806337
550UbiquitinationKSRVLGPKVEALQKV
HHHCCCHHHHHHHHH		51.4122790023
550 (in isoform 3)Ubiquitination-51.4122790023
556UbiquitinationPKVEALQKVNKAGAE
HHHHHHHHHHHHHHH		48.9322790023
556 (in isoform 3)Ubiquitination-48.9322790023
559 (in isoform 3)Ubiquitination-51.70-
565 (in isoform 3)Ubiquitination-44.60-
567 (in isoform 4)Phosphorylation-25.6825159016
575 (in isoform 4)Phosphorylation-41.7526824392
576 (in isoform 4)Phosphorylation-52.1227742792
586 (in isoform 4)Phosphorylation-75.4426824392
590PhosphorylationELAEDEPSTDRSAPV
HHHCCCCCCCCCCCC		40.6721149613
591PhosphorylationLAEDEPSTDRSAPVN
HHCCCCCCCCCCCCC		46.2628066266
594PhosphorylationDEPSTDRSAPVNGEA
CCCCCCCCCCCCCCC		39.4719060867
602PhosphorylationAPVNGEATSQKGENM
CCCCCCCCCCCCCCH		27.6429899451
603PhosphorylationPVNGEATSQKGENME
CCCCCCCCCCCCCHH		36.6225521595
619 (in isoform 2)Phosphorylation-60.5725159016
620PhosphorylationAQEDGQDSEDGPRGG
HHHCCCCCCCCCCCC		29.6925521595
627 (in isoform 2)Phosphorylation-29.3126824392
628PhosphorylationEDGPRGGSSEELHDS
CCCCCCCCHHHHCCC		37.0825521595
628 (in isoform 2)Phosphorylation-37.0827742792
629PhosphorylationDGPRGGSSEELHDSP
CCCCCCCHHHHCCCC		38.0625521595
635PhosphorylationSSEELHDSPRDNSDP
CHHHHCCCCCCCCCC		15.8725521595
638 (in isoform 2)Phosphorylation-63.4726824392
640PhosphorylationHDSPRDNSDPAKPGN
CCCCCCCCCCCCCCC		49.6226824392
655PhosphorylationERQDHERTRLASESA
CCCHHHHHHHHHHHC		27.3530635358
659PhosphorylationHERTRLASESANDDN
HHHHHHHHHHCCCCC		36.3525521595
661PhosphorylationRTRLASESANDDNED
HHHHHHHHCCCCCCC		29.8525521595
669PhosphorylationANDDNEDS-------
CCCCCCCC-------		35.6227149854
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 HDGR2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HDGR2_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 HDGR2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HDGR2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HDGR2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, ANDMASS SPECTROMETRY.
"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-366 AND SER-367, 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-231; SER-233; SER-235;SER-366; SER-367; THR-389; SER-391; SER-392; SER-393; SER-395;SER-450; SER-635 AND SER-640, 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-620; SER-628; SER-635;SER-659 AND SER-661, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-367; THR-389;SER-391; SER-392; SER-393 AND SER-395, 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-366 AND SER-367, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, ANDMASS SPECTROMETRY.

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