rank	organism	gene	uniprot_id	taxon_id	category	priority	review_status	prior_project_triage	go_ids	evidence	references	rationale	uniprot_url	quickgo_url
1	mouse	Glyctk	Q8QZY2	10090	W-sugar	high	NO_REVIEW_FILE	no	GO:0006468	ISO;ISS	GO_REF:0000024;GO_REF:0000119	Glycerate kinase phosphorylates glycerate, not protein. Check the propagated protein-phosphorylation assertion.	https://www.uniprot.org/uniprotkb/Q8QZY2/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ8QZY2
2	mouse	Ilf3	Q9Z1X4	10090	S	high	NO_REVIEW_FILE	no	GO:0006468	IDA;ISO	GO_REF:0000119;PMID:21123651	RNA-binding protein activated by PKR-mediated phosphorylation; likely substrate-as-participant transfer.	https://www.uniprot.org/uniprotkb/Q9Z1X4/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9Z1X4
3	mouse	Klhl3	E0CZ16	10090	U	high	NO_REVIEW_FILE	no	GO:0006468	IGI;IMP	PMID:24821705;PMID:28743496	CUL3 ubiquitin-ligase substrate adaptor controls WNK1/WNK4 abundance. The cited mouse study measures the downstream WNK-SPAK/OSR1-NCC phosphorylation cascade.	https://www.uniprot.org/uniprotkb/E0CZ16/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AE0CZ16
4	mouse	Ppme1	Q8BVQ5	10090	R-enzyme	high	NO_REVIEW_FILE	no	GO:0006468	IMP	PMID:31213650	Protein phosphatase methylesterase demethylates/inhibits PP2A; the cited study explains increased IRF3 phosphorylation through reduced dephosphorylation.	https://www.uniprot.org/uniprotkb/Q8BVQ5/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ8BVQ5
5	mouse	Pkd1	O08852	10090	R-receptor	high	NO_REVIEW_FILE	no	GO:0018105	IMP	PMID:20181743	Polycystin-1 participates in receptor/channel signaling. The cited study measures flow-induced HDAC5 phosphorylation downstream of polycystins.	https://www.uniprot.org/uniprotkb/O08852/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AO08852
6	mouse	Cdc25b	P30306	10090	O	high	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	CDC25 phosphatase removes inhibitory phosphate from CDKs, thereby activating a kinase; distinguish dephosphorylation from regulation.	https://www.uniprot.org/uniprotkb/P30306/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP30306
7	mouse	Thy1	P01831	10090	R-ligand	high	NO_REVIEW_FILE	no	GO:0046777	ISO	GO_REF:0000096	GPI-anchored cell-surface protein; the rat reference reports FAK autophosphorylation triggered by Thy-1, not autophosphorylation of Thy-1.	https://www.uniprot.org/uniprotkb/P01831/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP01831
8	mouse	Prrt1	O35449	10090	R-adapter	high	NO_REVIEW_FILE	no	GO:0006468	IMP	PMID:31216424	AMPAR auxiliary protein changes basal GRIA1 phosphorylation and receptor trafficking; distinguish modulation from phosphate transfer.	https://www.uniprot.org/uniprotkb/O35449/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AO35449
9	mouse	Il15	P48346	10090	R-cytokine	high	NO_REVIEW_FILE	no	GO:0007260	ISO	GO_REF:0000119	Cytokine activates receptor-associated JAK/STAT signaling; JAK kinases execute STAT phosphorylation.	https://www.uniprot.org/uniprotkb/P48346/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP48346
10	rat	Epm2a	Q91XQ2	10116	O-carbohydrate	high	NO_REVIEW_FILE	no	GO:0046835	IEA;ISO	GO_REF:0000107;GO_REF:0000121	Laforin is a glycogen phosphatase that prevents glycogen hyperphosphorylation; carbohydrate phosphorylation is the opposite reaction.	https://www.uniprot.org/uniprotkb/Q91XQ2/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ91XQ2
11	DROME	Dref	Q94883	7227	S-tf	high	NO_REVIEW_FILE	yes	GO:0006468;GO:0046777	ISS	GO_REF:0000024	DNA replication-related transcription factor carries ISS transfers from CAMKK2. Check the donor/target functional mismatch.	https://www.uniprot.org/uniprotkb/Q94883/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ94883
12	DANRE	glyctk	Q08BL7	7955	W-sugar	high	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	Glycerate kinase phosphorylates glycerate, not protein. Check the propagated protein-phosphorylation assertion.	https://www.uniprot.org/uniprotkb/Q08BL7/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ08BL7
13	mouse	Adm2	Q7TNK8	10090	R-ligand	high	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	Peptide hormone signals through CALCRL-RAMP receptors; test regulation versus direct phosphorylation.	https://www.uniprot.org/uniprotkb/Q7TNK8/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ7TNK8
14	mouse	Calca	P70160	10090	R-ligand	high	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	Calcitonin/CGRP precursor produces receptor ligands; downstream phosphorylation does not establish catalysis by the ligand.	https://www.uniprot.org/uniprotkb/P70160/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP70160
15	mouse	Cops2	P61202	10090	C	medium	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	COP9 signalosome component; UniProt attributes associated phosphorylation to CK2/PKD. Check whether structural participation justifies the process term.	https://www.uniprot.org/uniprotkb/P61202/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP61202
16	mouse	Cops8	Q8VBV7	10090	C	medium	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	COP9 signalosome component; associated CK2/PKD perform phosphorylation. Complex membership alone is insufficient to resolve participation.	https://www.uniprot.org/uniprotkb/Q8VBV7/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ8VBV7
17	mouse	Erc1	Q99MI1	10090	R-adapter	medium	NO_REVIEW_FILE	no	GO:0007252	ISO	GO_REF:0000119	ELKS scaffold recruits I-kappaB to the IKK complex. Direct substrate recruitment could justify participation: retain as a discussion case.	https://www.uniprot.org/uniprotkb/Q99MI1/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ99MI1
18	mouse	Grm5	Q3UVX5	10090	R-receptor	high	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000096	Metabotropic glutamate GPCR activates downstream kinases; distinguish receptor signaling from direct phosphorylation.	https://www.uniprot.org/uniprotkb/Q3UVX5/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ3UVX5
19	mouse	Hcst	Q9QUJ0	10090	S-adapter	high	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	DAP10 transmembrane adaptor provides phosphotyrosine docking sites for signaling proteins; test substrate/adaptor versus catalyst attribution.	https://www.uniprot.org/uniprotkb/Q9QUJ0/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9QUJ0
20	mouse	Il21	Q9ES17	10090	R-cytokine	high	NO_REVIEW_FILE	no	GO:0007260	ISO	GO_REF:0000119	Cytokine triggers JAK/STAT signaling; investigate transfer of a STAT-phosphorylation readout to the ligand.	https://www.uniprot.org/uniprotkb/Q9ES17/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9ES17
21	mouse	Il24	Q925S4	10090	R-cytokine	high	NO_REVIEW_FILE	no	GO:0042501	ISO	GO_REF:0000096	Cytokine activates receptor signaling; test whether STAT serine phosphorylation was a downstream readout.	https://www.uniprot.org/uniprotkb/Q925S4/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ925S4
22	mouse	Ip6k3	Q8BWD2	10090	W-inositol	high	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	Inositol hexakisphosphate kinase makes inositol pyrophosphates. Its known substrate is a small molecule, not a protein.	https://www.uniprot.org/uniprotkb/Q8BWD2/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ8BWD2
23	mouse	Limd1	Q9QXD8	10090	S-adapter	high	NO_REVIEW_FILE	no	GO:0016310	ISO;ISS	GO_REF:0000024;GO_REF:0000119	LIM-domain scaffold/regulator; generic phosphorylation annotation is transferred from human LIMD1, whose project review identifies a substrate-related issue.	https://www.uniprot.org/uniprotkb/Q9QXD8/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9QXD8
24	mouse	Maml1	Q6T264	10090	R-adapter	medium	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	Transcriptional coactivator recruits CDK8 and enhances NOTCH phosphorylation. Assess direct complex participation versus regulation.	https://www.uniprot.org/uniprotkb/Q6T264/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ6T264
25	mouse	Pdgfb	P31240	10090	R-ligand	high	NO_REVIEW_FILE	no	GO:0006468;GO:0018108	ISO;ISS	GO_REF:0000024;GO_REF:0000119	PDGF ligand activates receptor tyrosine kinases; distinguish ligand action from receptor-catalyzed phosphorylation.	https://www.uniprot.org/uniprotkb/P31240/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP31240
26	mouse	Pick1	Q62083	10090	R-adapter	medium	NO_REVIEW_FILE	no	GO:0006468	ISO;ISS	GO_REF:0000024;GO_REF:0000096	PDZ adaptor binds PKC and organizes substrates/receptors. Direct scaffolding may warrant participation; read the assay before deciding.	https://www.uniprot.org/uniprotkb/Q62083/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ62083
27	mouse	Ppp3cb	P48453	10090	O	high	NO_REVIEW_FILE	no	GO:0006468	IMP	PMID:11978799	Calcineurin catalytic subunit is a protein phosphatase. Examine whether phosphorylation changes reflect indirect regulation of kinases.	https://www.uniprot.org/uniprotkb/P48453/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP48453
28	mouse	Ptpn6	P29351	10090	O	high	NO_REVIEW_FILE	no	GO:0018108	ISO	GO_REF:0000119	SHP-1 is a protein tyrosine phosphatase; a positive tyrosine-phosphorylation assertion requires scrutiny of the regulatory mechanism.	https://www.uniprot.org/uniprotkb/P29351/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP29351
29	mouse	Rara	P11416	10090	S-tf	high	NO_REVIEW_FILE	no	GO:0006468	ISO	GO_REF:0000119	Retinoic-acid nuclear receptor/transcription factor; inspect the donor evidence for phosphorylation of RARA rather than by RARA.	https://www.uniprot.org/uniprotkb/P11416/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP11416
30	mouse	Runx3	Q64131	10090	S-tf	high	NO_REVIEW_FILE	no	GO:0006468	ISO;ISS	GO_REF:0000024;GO_REF:0000119	DNA-binding transcription factor; investigate propagation of a substrate phosphorylation assay.	https://www.uniprot.org/uniprotkb/Q64131/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ64131
31	mouse	Sqstm1	Q64337	10090	R-adapter	medium	NO_REVIEW_FILE	no	GO:0006468	IMP	PMID:32385399	p62 scaffold binds ATF2; the cited paper identifies p38 as the ATF2 kinase. Check whether p62 contributes directly to the phosphorylation step.	https://www.uniprot.org/uniprotkb/Q64337/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ64337
32	mouse	Tollip	Q9QZ06	10090	R-adapter	high	NO_REVIEW_FILE	no	GO:0016310	ISO;ISS	GO_REF:0000024;GO_REF:0000119	Ubiquitin/autophagy adaptor regulates IRAK1 phosphorylation. Trace the human donor, whose old annotation cites a problematic PMID.	https://www.uniprot.org/uniprotkb/Q9QZ06/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9QZ06
33	mouse	Usp25	P57080	10090	U	high	NO_REVIEW_FILE	no	GO:0007252	IMP	PMID:23042150	Deubiquitinase regulates TRAF signaling and downstream I-kappaB phosphorylation; test whether a regulatory process is more appropriate.	https://www.uniprot.org/uniprotkb/P57080/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP57080
34	mouse	Ywhaz	P63101	10090	R-adapter	medium	NO_REVIEW_FILE	no	GO:0006468	ISO;ISS	GO_REF:0000024;GO_REF:0000119	14-3-3 adaptor binds phosphoserine/threonine clients and modulates signaling. Evaluate direct participation versus regulation.	https://www.uniprot.org/uniprotkb/P63101/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP63101
35	DANRE	tollip	Q7ZV43	7955	R-adapter	high	NO_REVIEW_FILE	no	GO:0016310	ISS	GO_REF:0000024	Ubiquitin/autophagy adaptor regulates IRAK1 phosphorylation. Trace the human donor, whose old annotation cites a problematic PMID.	https://www.uniprot.org/uniprotkb/Q7ZV43/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ7ZV43
36	DROME	Glyctk	Q9VQC4	7227	W-sugar	high	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	Glycerate kinase phosphorylates glycerate, not protein. Check the propagated protein-phosphorylation assertion.	https://www.uniprot.org/uniprotkb/Q9VQC4/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9VQC4
37	rat	Gas6	Q63772	10116	R-ligand	high	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	Ligand activates TAM receptor tyrosine kinases; the receptor, not GAS6, transfers phosphate.	https://www.uniprot.org/uniprotkb/Q63772/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ63772
38	rat	Glyctk	Q0VGK3	10116	W-sugar	high	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	Glycerate kinase phosphorylates glycerate, not protein. Check the propagated protein-phosphorylation assertion.	https://www.uniprot.org/uniprotkb/Q0VGK3/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ0VGK3
39	rat	Grm5	P31424	10116	R-receptor	high	NO_REVIEW_FILE	yes	GO:0006468	IDA	PMID:15758184	Metabotropic glutamate GPCR activates downstream kinases; distinguish receptor signaling from direct phosphorylation.	https://www.uniprot.org/uniprotkb/P31424/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP31424
40	rat	Ilf3	Q9JIL3	10116	S	high	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	RNA-binding protein activated by PKR-mediated phosphorylation; likely substrate-as-participant transfer.	https://www.uniprot.org/uniprotkb/Q9JIL3/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9JIL3
41	rat	Limd1	B5DEH0	10116	S-adapter	high	NO_REVIEW_FILE	no	GO:0016310	ISS	GO_REF:0000024	LIM-domain scaffold/regulator; generic phosphorylation annotation is transferred from human LIMD1, whose project review identifies a substrate-related issue.	https://www.uniprot.org/uniprotkb/B5DEH0/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AB5DEH0
42	rat	Pdgfb	Q05028	10116	R-ligand	high	NO_REVIEW_FILE	yes	GO:0006468;GO:0018108	ISS	GO_REF:0000024	PDGF ligand activates receptor tyrosine kinases; distinguish ligand action from receptor-catalyzed phosphorylation.	https://www.uniprot.org/uniprotkb/Q05028/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ05028
43	rat	Pick1	Q9EP80	10116	R-adapter	medium	NO_REVIEW_FILE	yes	GO:0006468	IDA	PMID:11237868	PDZ adaptor binds PKC and organizes substrates/receptors. Direct scaffolding may warrant participation; read the assay before deciding.	https://www.uniprot.org/uniprotkb/Q9EP80/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ9EP80
44	rat	Ppp3cb	P20651	10116	O	high	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	Calcineurin catalytic subunit is a protein phosphatase. Examine whether phosphorylation changes reflect indirect regulation of kinases.	https://www.uniprot.org/uniprotkb/P20651/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP20651
45	rat	Prrt1	Q6MG82	10116	R-adapter	high	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	AMPAR auxiliary protein changes basal GRIA1 phosphorylation and receptor trafficking; distinguish modulation from phosphate transfer.	https://www.uniprot.org/uniprotkb/Q6MG82/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AQ6MG82
46	rat	Thy1	P01830	10116	R-ligand	high	NO_REVIEW_FILE	yes	GO:0046777	IDA	PMID:19723805	GPI-anchored cell-surface protein; the rat reference reports FAK autophosphorylation triggered by Thy-1, not autophosphorylation of Thy-1.	https://www.uniprot.org/uniprotkb/P01830/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP01830
47	rat	Tollip	A2RUW1	10116	R-adapter	high	NO_REVIEW_FILE	no	GO:0016310	ISS	GO_REF:0000024	Ubiquitin/autophagy adaptor regulates IRAK1 phosphorylation. Trace the human donor, whose old annotation cites a problematic PMID.	https://www.uniprot.org/uniprotkb/A2RUW1/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AA2RUW1
48	rat	Ywhaz	P63102	10116	R-adapter	medium	NO_REVIEW_FILE	yes	GO:0006468	ISS	GO_REF:0000024	14-3-3 adaptor binds phosphoserine/threonine clients and modulates signaling. Evaluate direct participation versus regulation.	https://www.uniprot.org/uniprotkb/P63102/entry	https://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB%3AP63102