HAP28_HUMAN - dbPTM
HAP28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAP28_HUMAN
UniProt AC Q13442
Protein Name 28 kDa heat- and acid-stable phosphoprotein
Gene Name PDAP1
Organism Homo sapiens (Human).
Sequence Length 181
Subcellular Localization
Protein Description Enhances PDGFA-stimulated cell growth in fibroblasts, but inhibits the mitogenic effect of PDGFB..
Protein Sequence MPKGGRKGGHKGRARQYTSPEEIDAQLQAEKQKAREEEEQKEGGDGAAGDPKKEKKSLDSDESEDEEDDYQQKRKGVEGLIDIENPNRVAQTTKKVTQLDLDGPKELSRREREEIEKQKAKERYMKMHLAGKTEQAKADLARLAIIRKQREEAARKKEEERKAKDDATLSGKRMQSLSLNK
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
7Methylation-MPKGGRKGGHKGRA
-CCCCCCCCCCCCCC		72.95116252659
17PhosphorylationHKGRARQYTSPEEID
CCCCCCCCCCHHHHH		12.0221945579
18PhosphorylationKGRARQYTSPEEIDA
CCCCCCCCCHHHHHH		29.4825159151
19PhosphorylationGRARQYTSPEEIDAQ
CCCCCCCCHHHHHHH		25.9425159151
31UbiquitinationDAQLQAEKQKAREEE
HHHHHHHHHHHHHHH		61.1821906983
31AcetylationDAQLQAEKQKAREEE
HHHHHHHHHHHHHHH		61.1826051181
33UbiquitinationQLQAEKQKAREEEEQ
HHHHHHHHHHHHHHH		61.5522817900
52AcetylationDGAAGDPKKEKKSLD
CCCCCCCHHHHCCCC		77.6012429493
52SumoylationDGAAGDPKKEKKSLD
CCCCCCCHHHHCCCC		77.6028112733
53AcetylationGAAGDPKKEKKSLDS
CCCCCCHHHHCCCCC		78.9612649937
55AcetylationAGDPKKEKKSLDSDE
CCCCHHHHCCCCCCC		57.4512649949
57PhosphorylationDPKKEKKSLDSDESE
CCHHHHCCCCCCCCC		48.7726846344
60PhosphorylationKEKKSLDSDESEDEE
HHHCCCCCCCCCCCH		48.8722167270
63PhosphorylationKSLDSDESEDEEDDY
CCCCCCCCCCCHHHH		56.1722167270
70PhosphorylationSEDEEDDYQQKRKGV
CCCCHHHHHHHHHCC		25.7623927012
75UbiquitinationDDYQQKRKGVEGLID
HHHHHHHHCCCCCCC		74.4824816145
75AcetylationDDYQQKRKGVEGLID
HHHHHHHHCCCCCCC		74.4826051181
95UbiquitinationRVAQTTKKVTQLDLD
HHHHHCCCEEECCCC		48.7124816145
97PhosphorylationAQTTKKVTQLDLDGP
HHHCCCEEECCCCCH		32.0927251275
105AcetylationQLDLDGPKELSRRER
ECCCCCHHHHCHHHH		76.4623236377
105UbiquitinationQLDLDGPKELSRRER
ECCCCCHHHHCHHHH		76.4622817900
117UbiquitinationREREEIEKQKAKERY
HHHHHHHHHHHHHHH		63.86-
119UbiquitinationREEIEKQKAKERYMK
HHHHHHHHHHHHHHH		72.9224816145
126MethylationKAKERYMKMHLAGKT
HHHHHHHHHHHCCCH		17.7724129315
1262-HydroxyisobutyrylationKAKERYMKMHLAGKT
HHHHHHHHHHHCCCH		17.77-
126AcetylationKAKERYMKMHLAGKT
HHHHHHHHHHHCCCH		17.7725953088
126UbiquitinationKAKERYMKMHLAGKT
HHHHHHHHHHHCCCH		17.7729967540
132UbiquitinationMKMHLAGKTEQAKAD
HHHHHCCCHHHHHHH		43.1919608861
1322-HydroxyisobutyrylationMKMHLAGKTEQAKAD
HHHHHCCCHHHHHHH		43.19-
132AcetylationMKMHLAGKTEQAKAD
HHHHHCCCHHHHHHH		43.1919608861
133PhosphorylationKMHLAGKTEQAKADL
HHHHCCCHHHHHHHH		32.2026437602
137UbiquitinationAGKTEQAKADLARLA
CCCHHHHHHHHHHHH		41.9724816145
137AcetylationAGKTEQAKADLARLA
CCCHHHHHHHHHHHH		41.9726822725
164MethylationKEEERKAKDDATLSG
HHHHHHHHHHCCCCC		60.2172620173
164AcetylationKEEERKAKDDATLSG
HHHHHHHHHHCCCCC		60.21-
164UbiquitinationKEEERKAKDDATLSG
HHHHHHHHHHCCCCC		60.2124816145
168PhosphorylationRKAKDDATLSGKRMQ
HHHHHHCCCCCHHHH		28.5723312004
170PhosphorylationAKDDATLSGKRMQSL
HHHHCCCCCHHHHHH		37.6021815630
172UbiquitinationDDATLSGKRMQSLSL
HHCCCCCHHHHHHCC		41.1233845483
172AcetylationDDATLSGKRMQSLSL
HHCCCCCHHHHHHCC		41.1223954790
1722-HydroxyisobutyrylationDDATLSGKRMQSLSL
HHCCCCCHHHHHHCC		41.12-
174SulfoxidationATLSGKRMQSLSLNK
CCCCCHHHHHHCCCC		3.4621406390
176PhosphorylationLSGKRMQSLSLNK--
CCCHHHHHHCCCC--		15.5829255136
178PhosphorylationGKRMQSLSLNK----
CHHHHHHCCCC----		34.8329255136
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 HAP28_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAP28_HUMAN !!
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 HAP28_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDGFA_HUMANPDGFAphysical
8780057
PDGFB_HUMANPDGFBphysical
8780057
A4_HUMANAPPphysical
21832049
RBM8A_HUMANRBM8Aphysical
26344197
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 HAP28_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-132, 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-57; SER-60; SER-63 ANDSER-176, AND MASS SPECTROMETRY.
"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-57; SER-60 AND SER-63,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-57; SER-60 AND SER-63,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-19; SER-57; SER-60;SER-63 AND SER-176, AND MASS SPECTROMETRY.
"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-60 AND SER-63, AND MASSSPECTROMETRY.
"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-63, AND MASSSPECTROMETRY.
"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-60; SER-63 AND TYR-70,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-63, AND MASSSPECTROMETRY.
"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-60 AND SER-63, 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-60 AND SER-63, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, AND MASSSPECTROMETRY.

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