HDGF_HUMAN - dbPTM
HDGF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDGF_HUMAN
UniProt AC P51858
Protein Name Hepatoma-derived growth factor
Gene Name HDGF
Organism Homo sapiens (Human).
Sequence Length 240
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Heparin-binding protein, with mitogenic activity for fibroblasts. Acts as a transcriptional repressor..
Protein Sequence MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL
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
11UbiquitinationSNRQKEYKCGDLVFA
CHHCCCCCCCCEEHH
32.6021890473
11SumoylationSNRQKEYKCGDLVFA
CHHCCCCCCCCEEHH
32.60-
11SumoylationSNRQKEYKCGDLVFA
CHHCCCCCCCCEEHH
32.60-
12S-palmitoylationNRQKEYKCGDLVFAK
HHCCCCCCCCEEHHH
5.1229575903
12GlutathionylationNRQKEYKCGDLVFAK
HHCCCCCCCCEEHHH
5.1222555962
19AcetylationCGDLVFAKMKGYPHW
CCCEEHHHCCCCCCC
29.6725953088
21UbiquitinationDLVFAKMKGYPHWPA
CEEHHHCCCCCCCCC
55.36-
23PhosphorylationVFAKMKGYPHWPARI
EHHHCCCCCCCCCCH
6.0925159151
27 (in isoform 3)Phosphorylation-14.5022496350
33SulfoxidationWPARIDEMPEAAVKS
CCCCHHHCCHHHHHH
3.0121406390
37AcetylationIDEMPEAAVKSTANK
HHHCCHHHHHHHCCC
13.9619608861
39UbiquitinationEMPEAAVKSTANKYQ
HCCHHHHHHHCCCEE
37.0421906983
39AcetylationEMPEAAVKSTANKYQ
HCCHHHHHHHCCCEE
37.0421339330
44AcetylationAVKSTANKYQVFFFG
HHHHHCCCEEEEEEE
34.3019608861
45PhosphorylationVKSTANKYQVFFFGT
HHHHCCCEEEEEEEC
15.09-
60AcetylationHETAFLGPKDLFPYE
CCCCCCCHHHCCCHH
29.1819608861
66PhosphorylationGPKDLFPYEESKEKF
CHHHCCCHHHHHHHH
25.6228152594
69PhosphorylationDLFPYEESKEKFGKP
HCCCHHHHHHHHCCC
33.8928152594
70UbiquitinationLFPYEESKEKFGKPN
CCCHHHHHHHHCCCC
69.10-
70AcetylationLFPYEESKEKFGKPN
CCCHHHHHHHHCCCC
69.1026051181
72AcetylationPYEESKEKFGKPNKR
CHHHHHHHHCCCCCC
64.2525953088
73UbiquitinationYEESKEKFGKPNKRK
HHHHHHHHCCCCCCC
18.6621890473
73UbiquitinationYEESKEKFGKPNKRK
HHHHHHHHCCCCCCC
18.6621890473
80SumoylationFGKPNKRKGFSEGLW
HCCCCCCCCCCCCCE
66.95-
80SumoylationFGKPNKRKGFSEGLW
HCCCCCCCCCCCCCE
66.9528112733
80AcetylationFGKPNKRKGFSEGLW
HCCCCCCCCCCCCCE
66.9527452117
80UbiquitinationFGKPNKRKGFSEGLW
HCCCCCCCCCCCCCE
66.9521890473
83PhosphorylationPNKRKGFSEGLWEIE
CCCCCCCCCCCEEEC
39.1530624053
94PhosphorylationWEIENNPTVKASGYQ
EEECCCCCCCCCCCC
36.4426074081
96UbiquitinationIENNPTVKASGYQSS
ECCCCCCCCCCCCCC
39.03-
96UbiquitinationIENNPTVKASGYQSS
ECCCCCCCCCCCCCC
39.0321890473
96SumoylationIENNPTVKASGYQSS
ECCCCCCCCCCCCCC
39.03-
98PhosphorylationNNPTVKASGYQSSQK
CCCCCCCCCCCCCCC
32.1126074081
99 (in isoform 3)Phosphorylation-29.3824719451
100PhosphorylationPTVKASGYQSSQKKS
CCCCCCCCCCCCCCC
11.6126074081
102PhosphorylationVKASGYQSSQKKSCV
CCCCCCCCCCCCCCC
26.6725849741
103PhosphorylationKASGYQSSQKKSCVE
CCCCCCCCCCCCCCC
30.4125849741
105UbiquitinationSGYQSSQKKSCVEEP
CCCCCCCCCCCCCCC
48.91-
105AcetylationSGYQSSQKKSCVEEP
CCCCCCCCCCCCCCC
48.9125953088
106AcetylationGYQSSQKKSCVEEPE
CCCCCCCCCCCCCCC
41.2630585617
106UbiquitinationGYQSSQKKSCVEEPE
CCCCCCCCCCCCCCC
41.26-
107PhosphorylationYQSSQKKSCVEEPEP
CCCCCCCCCCCCCCC
30.3623401153
108GlutathionylationQSSQKKSCVEEPEPE
CCCCCCCCCCCCCCC
6.4922555962
118 (in isoform 3)Phosphorylation-22.8724719451
119 (in isoform 3)Phosphorylation-21.4624719451
123 (in isoform 3)Phosphorylation-60.5424719451
125AcetylationAAEGDGDKKGNAEGS
HHCCCCCCCCCCCCC
69.0223236377
126UbiquitinationAEGDGDKKGNAEGSS
HCCCCCCCCCCCCCC
63.24-
132PhosphorylationKKGNAEGSSDEEGKL
CCCCCCCCCCCCCCE
26.5619664994
133PhosphorylationKGNAEGSSDEEGKLV
CCCCCCCCCCCCCEE
60.9519664994
146SuccinylationLVIDEPAKEKNEKGA
EECCCCCHHHCCCCH
78.8023954790
146AcetylationLVIDEPAKEKNEKGA
EECCCCCHHHCCCCH
78.8023236377
146UbiquitinationLVIDEPAKEKNEKGA
EECCCCCHHHCCCCH
78.80-
148 (in isoform 3)Phosphorylation-70.4724719451
149 (in isoform 3)Phosphorylation-58.2524719451
151AcetylationPAKEKNEKGALKRRA
CCHHHCCCCHHHHHH
59.9025953088
165PhosphorylationAGDLLEDSPKRPKEA
HHHHHCCCCCCCCCC
23.9719664994
167UbiquitinationDLLEDSPKRPKEAEN
HHHCCCCCCCCCCCC
82.41-
167AcetylationDLLEDSPKRPKEAEN
HHHCCCCCCCCCCCC
82.4126051181
180UbiquitinationENPEGEEKEAATLEV
CCCCCCHHHCCEEEE
48.64-
180AcetylationENPEGEEKEAATLEV
CCCCCCHHHCCEEEE
48.6425953088
181 (in isoform 3)Phosphorylation-46.9824719451
184PhosphorylationGEEKEAATLEVERPL
CCHHHCCEEEEECCC
30.4225159151
193SulfoxidationEVERPLPMEVEKNST
EEECCCCCCEECCCC
13.6821406390
197AcetylationPLPMEVEKNSTPSEP
CCCCCEECCCCCCCC
62.4623236377
197UbiquitinationPLPMEVEKNSTPSEP
CCCCCEECCCCCCCC
62.4621890473
199PhosphorylationPMEVEKNSTPSEPGS
CCCEECCCCCCCCCC
53.4130266825
200 (in isoform 3)Phosphorylation-39.9827251275
200PhosphorylationMEVEKNSTPSEPGSG
CCEECCCCCCCCCCC
39.9829255136
202PhosphorylationVEKNSTPSEPGSGRG
EECCCCCCCCCCCCC
57.4129255136
206PhosphorylationSTPSEPGSGRGPPQE
CCCCCCCCCCCCCHH
35.7130266825
208MethylationPSEPGSGRGPPQEEE
CCCCCCCCCCCHHHH
57.02115478363
215 (in isoform 3)Phosphorylation-70.7027251275
216 (in isoform 3)Phosphorylation-70.7127251275
218 (in isoform 3)Phosphorylation-74.1924719451
222 (in isoform 3)Phosphorylation-51.3827251275
225PhosphorylationEDEEEEATKEDAEAP
HHHHHHHHHHHHHCC
37.9423927012
226UbiquitinationDEEEEATKEDAEAPG
HHHHHHHHHHHHCCC
61.722190698
226AcetylationDEEEEATKEDAEAPG
HHHHHHHHHHHHCCC
61.7226051181
235MethylationDAEAPGIRDHESL--
HHHCCCCCCCCCC--
45.19115478355
239PhosphorylationPGIRDHESL------
CCCCCCCCC------
35.6425159151
241 (in isoform 3)Phosphorylation-27251275
255 (in isoform 3)Phosphorylation-24719451

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 HDGF_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
165SPhosphorylation

15302935

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 HDGF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XBP1_HUMANXBP1physical
20211142
ABCF1_HUMANABCF1physical
21907836
ATD3A_HUMANATAD3Aphysical
21907836
BMS1_HUMANBMS1physical
21907836
BRX1_HUMANBRIX1physical
21907836
INT13_HUMANASUNphysical
21907836
INT14_HUMANVWA9physical
21907836
CG026_HUMANC7orf26physical
21907836
CG050_HUMANC7orf50physical
21907836
CH033_HUMANC8orf33physical
21907836
CDK1_HUMANCDK1physical
21907836
CDC5L_HUMANCDC5Lphysical
21907836
DDX1_HUMANDDX1physical
21907836
DDX17_HUMANDDX17physical
21907836
DDX21_HUMANDDX21physical
21907836
DDX47_HUMANDDX47physical
21907836
DDX5_HUMANDDX5physical
21907836
DDX50_HUMANDDX50physical
21907836
DHX15_HUMANDHX15physical
21907836
DHX30_HUMANDHX30physical
21907836
DHX9_HUMANDHX9physical
21907836
DIM1_HUMANDIMT1physical
21907836
EBP2_HUMANEBNA1BP2physical
21907836
U5S1_HUMANEFTUD2physical
21907836
IF2A_HUMANEIF2S1physical
21907836
IF2G_HUMANEIF2S3physical
21907836
IF2P_HUMANEIF5Bphysical
21907836
EMD_HUMANEMDphysical
21907836
EXOSX_HUMANEXOSC10physical
21907836
EXOS2_HUMANEXOSC2physical
21907836
EXOS3_HUMANEXOSC3physical
21907836
EXOS6_HUMANEXOSC6physical
21907836
SYFB_HUMANFARSBphysical
21907836
FBRL_HUMANFBLphysical
21907836
GNL3_HUMANGNL3physical
21907836
GRWD1_HUMANGRWD1physical
21907836
GTPB1_HUMANGTPBP1physical
21907836
H1X_HUMANH1FXphysical
21907836
HDAC1_HUMANHDAC1physical
21907836
HDAC2_HUMANHDAC2physical
21907836
H14_HUMANHIST1H1Ephysical
21907836
H2B1K_HUMANHIST1H2BKphysical
21907836
H31_HUMANHIST1H3Aphysical
21907836
H4_HUMANHIST1H4Iphysical
21907836
ROA2_HUMANHNRNPA2B1physical
21907836
ROA3_HUMANHNRNPA3physical
21907836
HNRPU_HUMANHNRNPUphysical
21907836
INT10_HUMANINTS10physical
21907836
KIF2A_HUMANKIF2Aphysical
21907836
IMA1_HUMANKPNA2physical
21907836
LRC59_HUMANLRRC59physical
21907836
MRT4_HUMANMRTO4physical
21907836
MBB1A_HUMANMYBBP1Aphysical
21907836
NACAM_HUMANNACAphysical
21907836
NACA_HUMANNACAphysical
21907836
NUCL_HUMANNCLphysical
21907836
NOP2_HUMANNOP2physical
21907836
PARP1_HUMANPARP1physical
21907836
PGAM5_HUMANPGAM5physical
21907836
PDIP3_HUMANPOLDIP3physical
21907836
RPOM_HUMANPOLRMTphysical
21907836
PRKDC_HUMANPRKDCphysical
21907836
PSIP1_HUMANPSIP1physical
21907836
PWP2_HUMANPWP2physical
21907836
RBBP4_HUMANRBBP4physical
21907836
RBM39_HUMANRBM39physical
21907836
RCC2_HUMANRCC2physical
21907836
RFC1_HUMANRFC1physical
21907836
RFC4_HUMANRFC4physical
21907836
RFC5_HUMANRFC5physical
21907836
RFA1_HUMANRPA1physical
21907836
RL17_HUMANRPL17physical
21907836
RL19_HUMANRPL19physical
21907836
RL22_HUMANRPL22physical
21907836
RL32_HUMANRPL32physical
21907836
RL34_HUMANRPL34physical
21907836
RL35_HUMANRPL35physical
21907836
RL35A_HUMANRPL35Aphysical
21907836
RS11_HUMANRPS11physical
21907836
RS15A_HUMANRPS15Aphysical
21907836
RS23_HUMANRPS23physical
21907836
RRP1B_HUMANRRP1Bphysical
21907836
RL1D1_HUMANRSL1D1physical
21907836
SRSF1_HUMANSRSF1physical
21907836
SRSF2_HUMANSRSF2physical
21907836
SRSF3_HUMANSRSF3physical
21907836
SRSF5_HUMANSRSF5physical
21907836
SRSF7_HUMANSRSF7physical
21907836
MPCP_HUMANSLC25A3physical
21907836
ADT2_HUMANSLC25A5physical
21907836
SMC3_HUMANSMC3physical
21907836
SMD1_HUMANSNRPD1physical
21907836
SRPK1_HUMANSRPK1physical
21907836
SSRA_HUMANSSR1physical
21907836
SSRP1_HUMANSSRP1physical
21907836
STAU1_HUMANSTAU1physical
21907836
TCP4_HUMANSUB1physical
21907836
SP16H_HUMANSUPT16Hphysical
21907836
THOC4_HUMANALYREFphysical
21907836
LAP2A_HUMANTMPOphysical
21907836
LAP2B_HUMANTMPOphysical
21907836
TOP1_HUMANTOP1physical
21907836
TSR1_HUMANTSR1physical
21907836
U2AF1_HUMANU2AF1physical
21907836
WDR36_HUMANWDR36physical
21907836
WDR5_HUMANWDR5physical
21907836
XRCC5_HUMANXRCC5physical
21907836
XRCC6_HUMANXRCC6physical
21907836
ZCCHV_HUMANZC3HAV1physical
21907836
ACL6A_HUMANACTL6Aphysical
21907836
BAZ1B_HUMANBAZ1Bphysical
21907836
BUB3_HUMANBUB3physical
21907836
CBX3_HUMANCBX3physical
21907836
CKAP4_HUMANCKAP4physical
21907836
DEK_HUMANDEKphysical
21907836
DNJA1_HUMANDNAJA1physical
21907836
DRG1_HUMANDRG1physical
21907836
EF2_HUMANEEF2physical
21907836
E2AK2_HUMANEIF2AK2physical
21907836
IF2B_HUMANEIF2S2physical
21907836
H10_HUMANH1F0physical
21907836
H2AY_HUMANH2AFYphysical
21907836
H2AW_HUMANH2AFY2physical
21907836
H13_HUMANHIST1H1Dphysical
21907836
H12_HUMANHIST1H1Cphysical
21907836
H2B1D_HUMANHIST1H2BDphysical
21907836
H2B1C_HUMANHIST1H2BDphysical
21907836
HMGA2_HUMANHMGA2physical
21907836
HMGN1_HUMANHMGN1physical
21907836
HP1B3_HUMANHP1BP3physical
21907836
HCD2_HUMANHSD17B10physical
21907836
GRP75_HUMANHSPA9physical
21907836
LYAR_HUMANLYARphysical
21907836
MAGB2_HUMANMAGEB2physical
21907836
MAP4_HUMANMAP4physical
21907836
MK14_HUMANMAPK14physical
21907836
3MG_HUMANMPGphysical
21907836
RT22_HUMANMRPS22physical
21907836
RT27_HUMANMRPS27physical
21907836
NUDC_HUMANNUDCphysical
21907836
PHF6_HUMANPHF6physical
21907836
PLST_HUMANPLS3physical
21907836
RAN_HUMANRANphysical
21907836
RBMX_HUMANRBMXphysical
21907836
RCC1_HUMANRCC1physical
21907836
RCL1_HUMANRCL1physical
21907836
RFC3_HUMANRFC3physical
21907836
MRRP1_HUMANTRMT10Cphysical
21907836
RL10_HUMANRPL10physical
21907836
RPP38_HUMANRPP38physical
21907836
RUVB1_HUMANRUVBL1physical
21907836
SMCA5_HUMANSMARCA5physical
21907836
SRP68_HUMANSRP68physical
21907836
SRP72_HUMANSRP72physical
21907836
LA_HUMANSSBphysical
21907836
THOC3_HUMANTHOC3physical
21907836
U2AF2_HUMANU2AF2physical
21907836
RL40_HUMANUBA52physical
21907836
ZRAB2_HUMANZRANB2physical
21907836
K2C1_HUMANKRT1physical
21907836
K1C10_HUMANKRT10physical
21907836
K22E_HUMANKRT2physical
21907836
ANM5_HUMANPRMT5physical
21907836
TRY3_HUMANPRSS3physical
21907836
H2B2E_HUMANHIST2H2BEphysical
21907836
JUN_HUMANJUNphysical
21988832
ASB6_HUMANASB6physical
22863883
RUXF_HUMANSNRPFphysical
22863883

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 HDGF_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133; SER-165;THR-200; SER-206 AND SER-239, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-132; SER-133AND SER-165, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133; SER-165AND THR-200, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 ANDSER-165, AND MASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133; SER-165;THR-200 AND SER-202, AND MASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"SUMOylation of the hepatoma-derived growth factor negativelyinfluences its binding to chromatin.";
Thakar K., Niedenthal R., Okaz E., Franken S., Jakobs A., Gupta S.,Kelm S., Dietz F.;
FEBS J. 275:1411-1426(2008).
Cited for: SUMOYLATION AT LYS-80.

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