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PDB 
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Phospho-sites

Showing 21 results

Swiss-Prot Position Modification Source Evidence Singly phosphorylated
19 PhosphoT PRIDE yes
115 PhosphoT UP, PRIDE Similarity yes
117 PhosphoS UP, PRIDE Combined yes
134 PhosphoS UP, PRIDE Similarity yes
185 PhosphoT UP Combined
201 PhosphoS UP, PRIDE Combined yes
206 PhosphoS UP, PRIDE Combined yes
213 PhosphoS UP Similarity
353 PhosphoY UP, PRIDE Similarity yes
357 PhosphoT PRIDE yes
369 PhosphoS UP Similarity
378 PhosphoS UP Combined
408 PhosphoS PRIDE yes
467 PhosphoT UP Experimental
477 PhosphoS UP Similarity
485 PhosphoS UP, PRIDE Similarity yes
505 PhosphoS UP, PRIDE Combined yes
507 PhosphoT UP, PRIDE Similarity yes
541 PhosphoS UP Similarity
553 PhosphoT PRIDE
556 PhosphoT PRIDE

3D structure is not available

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Phosphorylated amino acids are colored red on the inner ring.

The first amino acid of the protein sequence is colored darker on each ring.

Phospho peptides

Showing 14 results

Sequence Modified position (Swiss-Prot) Peptide start Peptide end Modified position (Peptide) Number of projects
19 9 23 11 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD006482 4 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
115 108 130 8 12
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD004252 2 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD001060 1 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell -
PXD000612 3 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD001546 1 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004415 3 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD003531 6 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell
PXD004940 1 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD001333 1 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD006482 4 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 5 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD004452 6 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD000680 3 Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination Homo sapiens (Human) COMPLETE 2014-04-15 HeLa cell,HEK-293 cell -
117 108 130 10 14
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD001060 2 Fe-IMAC column based phospho enrichment Homo sapiens (Human) PARTIAL 2015-08-19 Epithelial cell
PXD004252 1 Modulating the selectivity of affinity absorbents to multi-phosphopeptides by a novel competitive substitution strategy Homo sapiens (Human) PARTIAL 2016-08-03 cell culture -
PXD004940 2 Performance of the Orbitrap Fusion Lumos Tribrid in single-shot analyses of human samples Homo sapiens (Human) PARTIAL 2017-03-09 HeLa cell -
PXD003531 108 Proteomics of Primary cells derived from Ovarian Cancer Homo sapiens (Human) PARTIAL 2017-04-03 primary cell -
PXD001333 4 Anion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC Homo sapiens (Human) PARTIAL 2015-04-23 HeLa cell -
PXD006482 16 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
PXD005366 102 Robust, sensitive and automated phosphopeptide enrichment optimized for low sample amounts applied to primary hippocampal neurons Homo sapiens (Human),Rattus norvegicus (Rat) PARTIAL 2016-12-14 cell culture -
PXD001550 19 Human CRC cell line baseline phosphoproteomics Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
PXD004452 89 HeLa proteome of 12,250 protein-coding genes Homo sapiens (Human) PARTIAL 2017-06-12 liver,colon -
PXD002394 23 Proteomic and phosphoproteomic analysis of cisplatin resistance in patient derived serous ovarian cancer Homo sapiens (Human) PARTIAL 2017-05-02 cell suspension culture -
PXD001374 5 Label-free quantitative phosphoproteomics with novel pairwise abundance normalization reveals synergistic RAS and CIP2A signaling Homo sapiens (Human) PARTIAL 2015-08-24 HeLa cell -
PXD000612 82 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture -
PXD004415 20 Quantitative phosphoproteome analysis of cisplatin-induced apoptosis in Jurkat T cells Homo sapiens (Human) COMPLETE 2017-05-11 T lymphocyte -
PXD001546 10 Reproducibility of label-free single-shot phosphoproteomics applied to CRC cell lines Homo sapiens (Human) PARTIAL 2015-04-15 cell culture -
134 131 146 4 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
201 201 209 1 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 3 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
206 201 209 6 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
353 350 360 4 3
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 23 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
PXD001565 4 Evaluation of phospho-tyrosine antibodies for label-free phosphoproteomics Homo sapiens (Human) PARTIAL 2015-12-09 colon,brain -
PXD003198 12 Characterisation of pancreatic ductal adenocarcinoma subtypes by global phosphotyrosine profiling Homo sapiens (Human) PARTIAL 2016-06-09 pancreatic cell line -
357 350 360 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney
408 407 414 2 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 5 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
485 465 491 21 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 1 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
505 504 515 2 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 5 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
PXD006482 1 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
507 504 515 4 2
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD002286 1 Phospo-proteomic profiling of Castration Resistant Prostate Cancer Homo sapiens (Human) PARTIAL 2016-08-19 -
PXD006482 4 Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer Homo sapiens (Human) COMPLETE 2017-09-01 kidney -
553 546 562 8 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture
556 546 562 11 1
ProteomeXchange accession Peptide frequency Project Title Species Submission Type Publication Date Tissues USI
PXD000612 2 Ultra-deep human phosphoproteome reveals different regulatory nature of Tyr and Ser/Thr-based signaling Homo sapiens (Human) PARTIAL 2014-08-06 cell culture

Structures

Showing 5 results

PDB id Chain Method Resolution Stoichiometry Interfacing Molecule/Chain Complex Formation Significance Score (CSS) P-sites View Structure
5EPC A X-ray 1.850000023841858 Monomer [SO4]A:602 0.017926332 19, 115, 117, 134, 185, 201, 206, 213, 353, 357, 369, 378, 408, 467, 477, 485, 505, 541, 553, 556
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
19 19 THR C 0.79 116.6536636352539 0.0
115 115 THR C 1 2.8436810970306396 0.0
117 117 SER C 1 8.606541633605957 0.0
134 134 SER C 1 69.7120361328125 0.0
185 185 THR E 1 18.972362518310547 0.0
201 201 SER H 0.9 91.15269470214844 0.0
206 206 SER H 1 89.13216400146484 0.0
213 213 SER C 1 39.61088562011719 0.0
353 353 TYR E 1 50.00179672241211 0.0
357 357 THR C 0.91 66.94500732421875 12.885741233825684
369 369 SER C 0.47 69.50870513916016 0.0
378 378 SER C 1 28.97351837158203 0.0
408 408 SER C 1 48.56134796142578 0.0
467 467 THR E 0.91 29.557565689086914 0.0
477 477 SER E 0.83 70.10039520263672 0.0
485 485 SER E 0.68 18.643821716308594 0.0
505 505 SER C 0.91 43.084049224853516 7.796597003936768
541 541 SER H 0.91 43.27496337890625 0.0
553 553 THR H 0.9 31.400348663330078 0.0
556 556 THR C 0.79 114.10668182373047 0.0
5F9C A X-ray 2.5 2 [SO4]A:604 0.029801676 19, 115, 117, 134, 185, 201, 206, 213, 353, 357, 369, 378, 408, 467, 477, 485, 505, 541, 553, 556
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
19 19 THR C 0.79 119.80965423583984 0.0
115 115 THR C 1 5.63362455368042 0.0
117 117 SER C 1 16.449256896972656 0.0
134 134 SER C 1 69.29998779296875 0.0
185 185 THR E 1 18.099050521850586 0.0
201 201 SER H 0.9 87.55741882324219 0.0
206 206 SER H 1 82.11800384521484 0.0
213 213 SER C 1 48.144020080566406 0.0
353 353 TYR E 1 51.579647064208984 0.0
357 357 THR C 0.91 45.071868896484375 0.0
369 369 SER C 0.47 64.34344482421875 0.0
378 378 SER C 1 30.749629974365234 0.0
408 408 SER C 1 51.416847229003906 0.0
467 467 THR E 0.91 33.35346603393555 0.0
477 477 SER E 0.83 73.72077941894531 0.0
485 485 SER E 0.68 19.554716110229492 0.0
505 505 SER C 0.91 87.5908203125 0.0
541 541 SER H 0.91 67.00252532958984 0.0
553 553 THR H 0.9 22.70051383972168 0.0
556 556 THR C 0.79 113.24671173095703 0.0
5TR2 A X-ray 2.5 2 [SO4]A:602 0.03628998 19, 115, 134, 185, 201, 206, 213, 353, 357, 369, 378, 408, 467, 477, 485, 505, 507, 541, 553, 556
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
19 19 THR C 0.79 109.7823715209961 0.0
115 115 THR C 1 7.689825057983398 0.0
134 134 SER C 1 65.81295776367188 0.0
185 185 THR E 1 25.176830291748047 0.0
201 201 SER H 0.9 90.71664428710938 0.0
206 206 SER H 1 80.20490264892578 0.0
213 213 SER C 1 33.308563232421875 0.0
353 353 TYR E 1 59.905277252197266 0.0
357 357 THR C 0.91 49.930538177490234 3.3416028022766113
369 369 SER C 0.47 64.3853759765625 0.0
378 378 SER C 1 36.16191101074219 0.0
408 408 SER C 1 41.5496826171875 0.0
467 467 THR E 0.91 32.10492706298828 0.0
477 477 SER E 0.83 77.51371765136719 0.0
485 485 SER E 0.68 14.030083656311035 0.0
505 505 SER C 0.91 24.701143264770508 8.323629379272461
507 507 THR C 1 133.5570526123047 4.9270920753479
541 541 SER H 0.91 71.42933654785156 0.0
553 553 THR H 0.9 27.03417205810547 0.0
556 556 THR C 0.79 117.44623565673828 0.0
5JN5 A X-ray 1.75 2 [SO4]A:602 0.029735176 19, 115, 134, 185, 201, 206, 213, 353, 357, 369, 378, 408, 467, 477, 485, 505, 541, 553, 556
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
19 19 THR C 0.79 119.30244445800781 0.0
115 115 THR C 1 2.326770544052124 0.0
134 134 SER C 1 69.8072280883789 0.0
185 185 THR E 1 20.155811309814453 0.0
201 201 SER H 0.9 92.1595230102539 0.0
206 206 SER H 1 87.73416900634766 0.0
213 213 SER C 1 41.67333984375 0.0
353 353 TYR E 1 50.95214080810547 0.0
357 357 THR C 0.91 66.42941284179688 0.0
369 369 SER C 0.47 70.52567291259766 0.0
378 378 SER C 1 24.649770736694336 0.0
408 408 SER C 1 52.2456169128418 0.0
467 467 THR E 0.91 33.107234954833984 0.0
477 477 SER E 0.83 67.8636703491211 0.0
485 485 SER E 0.68 16.361495971679688 0.0
505 505 SER C 0.91 43.28200912475586 0.0
541 541 SER H 0.91 36.71324920654297 0.0
553 553 THR H 0.9 28.62360954284668 0.0
556 556 THR C 0.79 113.70879364013672 0.0
5HSH A X-ray 2.6500000953674316 2 [SO4]A:604 0.033401035 19, 115, 134, 185, 201, 206, 213, 353, 357, 369, 378, 408, 467, 477, 485, 505, 541, 553, 556
Swiss-Prot position PDB position Residue Secondary Structure Conserved Scale Accessible surface area Buried surface area
19 19 THR C 0.79 94.02732849121094 19.749801635742188
115 115 THR E 1 40.96479034423828 0.0
134 134 SER C 1 67.36592864990234 0.0
185 185 THR E 1 16.593740463256836 0.0
201 201 SER H 0.9 85.28897094726562 0.0
206 206 SER H 1 85.47142028808594 0.0
213 213 SER C 1 47.53361511230469 0.0
353 353 TYR E 1 65.3166275024414 0.0
357 357 THR C 0.91 32.99967575073242 0.0
369 369 SER C 0.47 69.58967590332031 0.0
378 378 SER C 1 18.21285057067871 0.0
408 408 SER C 1 53.35599136352539 0.0
467 467 THR E 0.91 45.101051330566406 0.0
477 477 SER E 0.83 76.89998626708984 0.0
485 485 SER E 0.68 19.30040168762207 0.0
505 505 SER C 0.91 75.42121124267578 0.0
541 541 SER H 0.91 71.249755859375 0.0
553 553 THR H 0.9 22.077312469482422 0.0
556 556 THR C 0.79 119.30675506591797 0.0

Mutations

Showing 17 results

Swiss-Prot Position Amino acid (Wild type) Amino acid (Variant) Variant Type Disease
19 T A Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
38 N Y Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
41 Q R Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
62 D H Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
68 K M Polymorphism
88 I V Polymorphism
115 T A Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
121 G R Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
221 R C Polymorphism
263 D Y Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
291 G R Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
330 G R Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
377 E K Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
388 E K Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]
420 Y H Polymorphism
501 V I Polymorphism
516 L P Disease Congenital disorder of glycosylation 1T (CDG1T) [MIM:614921]