PYR1_HUMAN - dbPTM
PYR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PYR1_HUMAN
UniProt AC P27708
Protein Name CAD protein
Gene Name CAD {ECO:0000312|HGNC:HGNC:1424}
Organism Homo sapiens (Human).
Sequence Length 2225
Subcellular Localization Cytoplasm . Nucleus . Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth.
Protein Description This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)..
Protein Sequence MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
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
2Acetylation------MAALVLEDG
------CCEEEECCC
22.3222223895
10PhosphorylationALVLEDGSVLRGQPF
EEEECCCCEECCCCC
30.2420068231
37UbiquitinationQTGMVGYPEALTDPS
ECCCCCCHHHHCCCC
17.9221890473
127UbiquitinationDTRELTKKLREQGSL
CHHHHHHHHHHHCCH
47.76-
133PhosphorylationKKLREQGSLLGKLVQ
HHHHHHCCHHHHHHH
21.8123532336
137UbiquitinationEQGSLLGKLVQNGTE
HHCCHHHHHHHCCCC
45.5121906983
165UbiquitinationLVPEVSIKTPRVFNT
CCCCEEECCCCCCCC
44.9921906983
166PhosphorylationVPEVSIKTPRVFNTG
CCCEEECCCCCCCCC
18.0423312004
172PhosphorylationKTPRVFNTGGAPRIL
CCCCCCCCCCCCCEE
26.0620068231
177MethylationFNTGGAPRILALDCG
CCCCCCCCEEEEECC
35.70-
183GlutathionylationPRILALDCGLKYNQI
CCEEEEECCCCHHHH
7.7622555962
186AcetylationLALDCGLKYNQIRCL
EEEECCCCHHHHHHH
27.6925953088
186MethylationLALDCGLKYNQIRCL
EEEECCCCHHHHHHH
27.69-
186UbiquitinationLALDCGLKYNQIRCL
EEEECCCCHHHHHHH
27.69-
267PhosphorylationLAIGAKTYKMRYGNR
HHHCCEEEECCCCCC
11.33-
285PhosphorylationQPCLLVGSGRCFLTS
CCEEEECCCCEEECC
18.6528857561
375PhosphorylationQTVRERLTERLCPPG
HHHHHHHHHCCCCCC
25.8618767875
379GlutathionylationERLTERLCPPGIPTP
HHHHHCCCCCCCCCC
4.8422555962
424UbiquitinationSQAIKALKEENIQTL
HHHHHHHHHCCCCEE
68.7721906983
456PhosphorylationKVYFLPITPHYVTQV
EEEEEECCHHHHHHH
11.3215890648
475PhosphorylationRPDGVLLTFGGQTAL
CCCCEEEEECCEEHH
18.97-
484GlutathionylationGGQTALNCGVELTKA
CCEEHHCCCCEEHHH
7.2222555962
490UbiquitinationNCGVELTKAGVLARY
CCCCEEHHHHHHHHH
56.63-
504PhosphorylationYGVRVLGTPVETIEL
HCEEECCCCEEEEEC
21.7220068231
585PhosphorylationVAPAFAHTSQVLVDK
HHHHHCCCCHHEECC
19.88-
586PhosphorylationAPAFAHTSQVLVDKS
HHHHCCCCHHEECCC
14.39-
592UbiquitinationTSQVLVDKSLKGWKE
CCHHEECCCCCCCEE
50.6521890473
598UbiquitinationDKSLKGWKEIEYEVV
CCCCCCCEEEEEEEH
58.4421890473
602PhosphorylationKGWKEIEYEVVRDAY
CCCEEEEEEEHHHHC
21.4920068231
690PhosphorylationVNARLSRSSALASKA
EECEECCHHHHHHHC
19.3122798277
696SuccinylationRSSALASKATGYPLA
CHHHHHHHCCCCCHH
44.3423954790
696UbiquitinationRSSALASKATGYPLA
CHHHHHHHCCCCCHH
44.3421890473
698PhosphorylationSALASKATGYPLAYV
HHHHHHCCCCCHHHH
40.7728152594
700PhosphorylationLASKATGYPLAYVAA
HHHHCCCCCHHHHHH
7.2428152594
723O-linked_GlycosylationPELRNSVTGGTAAFE
HHHHCCCCCCCCCCC
29.7023301498
726O-linked_GlycosylationRNSVTGGTAAFEPSV
HCCCCCCCCCCCCCC
19.0223301498
732PhosphorylationGTAAFEPSVDYCVVK
CCCCCCCCCCEEEEE
22.0328152594
735PhosphorylationAFEPSVDYCVVKIPR
CCCCCCCEEEEEECC
5.7428152594
736GlutathionylationFEPSVDYCVVKIPRW
CCCCCCEEEEEECCC
2.1622555962
739UbiquitinationSVDYCVVKIPRWDLS
CCCEEEEEECCCCHH
26.96-
7472-HydroxyisobutyrylationIPRWDLSKFLRVSTK
ECCCCHHHHHHHHHH
56.57-
747AcetylationIPRWDLSKFLRVSTK
ECCCCHHHHHHHHHH
56.5719608861
747UbiquitinationIPRWDLSKFLRVSTK
ECCCCHHHHHHHHHH
56.5721890473
754AcetylationKFLRVSTKIGSCMKS
HHHHHHHHHHHHHHH
37.2525953088
754UbiquitinationKFLRVSTKIGSCMKS
HHHHHHHHHHHHHHH
37.25-
760AcetylationTKIGSCMKSVGEVMG
HHHHHHHHHHHHHHC
46.4425953088
760UbiquitinationTKIGSCMKSVGEVMG
HHHHHHHHHHHHHHC
46.44-
761PhosphorylationKIGSCMKSVGEVMGI
HHHHHHHHHHHHHCC
14.42-
766SulfoxidationMKSVGEVMGIGRSFE
HHHHHHHHCCCCCHH
2.5521406390
7782-HydroxyisobutyrylationSFEEAFQKALRMVDE
CHHHHHHHHHHHHHH
42.82-
778AcetylationSFEEAFQKALRMVDE
CHHHHHHHHHHHHHH
42.8226822725
778UbiquitinationSFEEAFQKALRMVDE
CHHHHHHHHHHHHHH
42.8221890473
795UbiquitinationVGFDHTVKPVSDMEL
CCCCCCCCCCCCCCC
40.64-
808UbiquitinationELETPTDKRIFVVAA
CCCCCCCCCHHHHHH
50.28-
867UbiquitinationPDLLQQAKCLGFSDK
HHHHHHHHHHCCCHH
26.17-
874UbiquitinationKCLGFSDKQIALAVL
HHHCCCHHHHHHHHH
42.26-
883PhosphorylationIALAVLSTELAVRKL
HHHHHHCHHHHHHHH
30.75-
889UbiquitinationSTELAVRKLRQELGI
CHHHHHHHHHHHHCC
41.23-
897GlutathionylationLRQELGICPAVKQID
HHHHHCCCCHHHCCC
1.3522555962
969PhosphorylationLRKMGYKTIMVNYNP
HHHCCCEEEEECCCC
13.0621406692
974PhosphorylationYKTIMVNYNPETVST
CEEEEECCCCCCCCC
22.2321406692
978PhosphorylationMVNYNPETVSTDYDM
EECCCCCCCCCCHHH
22.4821406692
980PhosphorylationNYNPETVSTDYDMCD
CCCCCCCCCCHHHCC
23.9921406692
981PhosphorylationYNPETVSTDYDMCDR
CCCCCCCCCHHHCCC
33.9521406692
983PhosphorylationPETVSTDYDMCDRLY
CCCCCCCHHHCCCEE
12.9821406692
1037PhosphorylationQQCRVLGTSPEAIDS
HHHHHHCCCHHHHHH
36.6330266825
1038PhosphorylationQCRVLGTSPEAIDSA
HHHHHCCCHHHHHHH
20.9530266825
1044PhosphorylationTSPEAIDSAENRFKF
CCHHHHHHHHHHHHH
31.2223403867
1057PhosphorylationKFSRLLDTIGISQPQ
HHHHHHHHHCCCCHH
22.5221406692
1061PhosphorylationLLDTIGISQPQWREL
HHHHHCCCCHHHHHH
30.5121406692
1069PhosphorylationQPQWRELSDLESARQ
CHHHHHHHHHHHHHH
35.0820068231
1073PhosphorylationRELSDLESARQFCQT
HHHHHHHHHHHHHHH
35.7320068231
1080O-linked_GlycosylationSARQFCQTVGYPCVV
HHHHHHHHHCCCEEE
19.6523301498
1112PhosphorylationGDLERFLSSAAAVSK
CCHHHHHHHHHHHCC
18.4120068231
1113PhosphorylationDLERFLSSAAAVSKE
CHHHHHHHHHHHCCC
24.8723312004
1118PhosphorylationLSSAAAVSKEHPVVI
HHHHHHHCCCCCCHH
27.8320068231
1119UbiquitinationSSAAAVSKEHPVVIS
HHHHHHCCCCCCHHH
54.1421890473
1127AcetylationEHPVVISKFIQEAKE
CCCCHHHHHHHHHHC
35.0525953088
1127UbiquitinationEHPVVISKFIQEAKE
CCCCHHHHHHHHHHC
35.0521906983
1177UbiquitinationPPQDITAKTLERIKA
CCCCCCHHHHHHHHH
45.02-
1206UbiquitinationFNLQLIAKDDQLKVI
CCEEEEECCCCEEEE
55.64-
1211AcetylationIAKDDQLKVIECNVR
EECCCCEEEEEEEEE
35.2225953088
1211UbiquitinationIAKDDQLKVIECNVR
EECCCCEEEEEEEEE
35.22-
1220PhosphorylationIECNVRVSRSFPFVS
EEEEEEECCCCCCCC
16.1921406692
1222PhosphorylationCNVRVSRSFPFVSKT
EEEEECCCCCCCCCC
29.7521406692
1227PhosphorylationSRSFPFVSKTLGVDL
CCCCCCCCCCCCCCH
21.9422210691
1228UbiquitinationRSFPFVSKTLGVDLV
CCCCCCCCCCCCCHH
42.3321890473
1262UbiquitinationGSGVVGVKVPQFSFS
CCCEEEEECCCCCHH
42.1221890473
1267PhosphorylationGVKVPQFSFSRLAGA
EEECCCCCHHHHCCC
19.6428857561
1301MethylationSRCEAYLKAMLSTGF
HHHHHHHHHHHHCCC
21.05-
1303SulfoxidationCEAYLKAMLSTGFKI
HHHHHHHHHHCCCCC
2.6521406390
1309AcetylationAMLSTGFKIPKKNIL
HHHHCCCCCCCCCEE
60.4925953088
1309UbiquitinationAMLSTGFKIPKKNIL
HHHHCCCCCCCCCEE
60.4921890473
1313MalonylationTGFKIPKKNILLTIG
CCCCCCCCCEEEEEC
43.8126320211
1313UbiquitinationTGFKIPKKNILLTIG
CCCCCCCCCEEEEEC
43.81-
1318PhosphorylationPKKNILLTIGSYKNK
CCCCEEEEECCCCCH
21.6130108239
1321PhosphorylationNILLTIGSYKNKSEL
CEEEEECCCCCHHHH
29.1430108239
1322PhosphorylationILLTIGSYKNKSELL
EEEEECCCCCHHHHH
17.2322817900
1323MalonylationLLTIGSYKNKSELLP
EEEECCCCCHHHHHH
60.6426320211
1323UbiquitinationLLTIGSYKNKSELLP
EEEECCCCCHHHHHH
60.64-
1325MalonylationTIGSYKNKSELLPTV
EECCCCCHHHHHHHH
40.9526320211
1325UbiquitinationTIGSYKNKSELLPTV
EECCCCCHHHHHHHH
40.9521906983
1337PhosphorylationPTVRLLESLGYSLYA
HHHHHHHHHCCHHHH
27.3621601212
1343PhosphorylationESLGYSLYASLGTAD
HHHCCHHHHCCCCCC
6.5521601212
1379PhosphorylationGECPPQRSILEQLAE
CCCCCCHHHHHHHHH
26.6928555341
1387UbiquitinationILEQLAEKNFELVIN
HHHHHHHCCCEEEEE
62.42-
1406DephosphorylationGAGGRRLSSFVTKGY
CCCCCCHHHHHCCCH
21.664092695
1406PhosphorylationGAGGRRLSSFVTKGY
CCCCCCHHHHHCCCH
21.6629255136
1407PhosphorylationAGGRRLSSFVTKGYR
CCCCCHHHHHCCCHH
28.4723401153
1410PhosphorylationRRLSSFVTKGYRTRR
CCHHHHHCCCHHHCC
19.4223927012
1411AcetylationRLSSFVTKGYRTRRL
CHHHHHCCCHHHCCC
48.9519608861
1411UbiquitinationRLSSFVTKGYRTRRL
CHHHHHCCCHHHCCC
48.9521890473
1413PhosphorylationSSFVTKGYRTRRLAA
HHHHCCCHHHCCCCC
15.4622210691
1423PhosphorylationRRLAADFSVPLIIDI
CCCCCCCCCCEEEEE
24.3122817900
1431UbiquitinationVPLIIDIKCTKLFVE
CCEEEEECCCHHHHH
31.9121906983
1434UbiquitinationIIDIKCTKLFVEALG
EEEECCCHHHHHHHH
49.77-
1450SumoylationIGPAPPLKVHVDCMT
CCCCCCEEEEEEECC
35.75-
1450UbiquitinationIGPAPPLKVHVDCMT
CCCCCCEEEEEEECC
35.75-
1457PhosphorylationKVHVDCMTSQKLVRL
EEEEEECCCCHHHCC
34.0520873877
1458PhosphorylationVHVDCMTSQKLVRLP
EEEEECCCCHHHCCC
9.8320873877
1460UbiquitinationVDCMTSQKLVRLPGL
EEECCCCHHHCCCCE
49.03-
1521UbiquitinationPALALAQKLAEAGAR
HHHHHHHHHHHHHCC
44.02-
1556N6-carboxylysineAGSAAGLKLYLNETF
HHHHHHHHHHHCCCC
33.88-
1556CarboxylationAGSAAGLKLYLNETF
HHHHHHHHHHHCCCC
33.8824332717
1564PhosphorylationLYLNETFSELRLDSV
HHHCCCCHHHCHHHH
43.0424719451
1613S-palmitoylationTQRSVHICHVARKEE
HHCCHHHHEECCHHH
0.9621044946
1618UbiquitinationHICHVARKEEILLIK
HHHEECCHHHEEHHH
50.3821906983
1625UbiquitinationKEEILLIKAAKARGL
HHHEEHHHHHHHCCC
42.1121906983
1636S-palmitoylationARGLPVTCEVAPHHL
HCCCCEEEEECCCEE
3.9421044946
1646PhosphorylationAPHHLFLSHDDLERL
CCCEEECCHHHHHHH
19.96-
1657UbiquitinationLERLGPGKGEVRPEL
HHHHCCCCCCCCCCC
55.8421890473
1698PhosphorylationTLEEKCGSRPPPGFP
CHHHHHCCCCCCCCC
51.5924719451
1724PhosphorylationAVSEGRLSLDDLLQR
HHHCCCCCHHHHHHH
28.5221712546
1778UbiquitinationWTPFEGQKVKGTVRR
CCCCCCCCCCCEEEE
57.69-
1794PhosphorylationVLRGEVAYIDGQVLV
EECCEEEEEECEEEC
12.53-
1805PhosphorylationQVLVPPGYGQDVRKW
EEECCCCCCCCHHHC
19.86-
1823PhosphorylationAVPQLPPSAPATSEM
CCCCCCCCCCCCCCC
44.9730266825
1827PhosphorylationLPPSAPATSEMTTTP
CCCCCCCCCCCCCCC
24.9423401153
1828PhosphorylationPPSAPATSEMTTTPE
CCCCCCCCCCCCCCC
27.7230266825
1831PhosphorylationAPATSEMTTTPERPR
CCCCCCCCCCCCCCC
24.3823401153
1832PhosphorylationPATSEMTTTPERPRR
CCCCCCCCCCCCCCC
38.7630266825
1833PhosphorylationATSEMTTTPERPRRG
CCCCCCCCCCCCCCC
17.6230266825
1839MethylationTTPERPRRGIPGLPD
CCCCCCCCCCCCCCC
50.50-
1856PhosphorylationFHLPPRIHRASDPGL
CCCCCCCCCCCCCCC
22.12-
1859DephosphorylationPPRIHRASDPGLPAE
CCCCCCCCCCCCCCC
44.274092695
1859PhosphorylationPPRIHRASDPGLPAE
CCCCCCCCCCCCCCC
44.2719664994
1869UbiquitinationGLPAEEPKEKSSRKV
CCCCCCCCCHHCCCC
79.60-
1871UbiquitinationPAEEPKEKSSRKVAE
CCCCCCCHHCCCCCC
60.91-
1872PhosphorylationAEEPKEKSSRKVAEP
CCCCCCHHCCCCCCH
36.1426074081
1873PhosphorylationEEPKEKSSRKVAEPE
CCCCCHHCCCCCCHH
47.3826074081
1875UbiquitinationPKEKSSRKVAEPELM
CCCHHCCCCCCHHHC
47.98-
1884PhosphorylationAEPELMGTPDGTCYP
CCHHHCCCCCCCCCC
12.3030266825
1888PhosphorylationLMGTPDGTCYPPPPV
HCCCCCCCCCCCCCC
19.0830266825
1889GlutathionylationMGTPDGTCYPPPPVP
CCCCCCCCCCCCCCC
6.1622555962
1890PhosphorylationGTPDGTCYPPPPVPR
CCCCCCCCCCCCCCC
20.7230266825
1900PhosphorylationPPVPRQASPQNLGTP
CCCCCCCCCCCCCCC
20.7625159151
1906PhosphorylationASPQNLGTPGLLHPQ
CCCCCCCCCCCCCCC
19.8325159151
1914PhosphorylationPGLLHPQTSPLLHSL
CCCCCCCCHHHHHHH
36.4422199227
1915PhosphorylationGLLHPQTSPLLHSLV
CCCCCCCHHHHHHHH
14.3322199227
1920PhosphorylationQTSPLLHSLVGQHIL
CCHHHHHHHHHHHHH
25.3920068231
1928PhosphorylationLVGQHILSVQQFTKD
HHHHHHHHHEEECHH
19.7828464451
1933PhosphorylationILSVQQFTKDQMSHL
HHHHEEECHHHHHHH
29.4022199227
1938PhosphorylationQFTKDQMSHLFNVAH
EECHHHHHHHHHHHH
16.057766613
1953AcetylationTLRMMVQKERSLDIL
HHHHHHHHHHHHHHH
43.6225953088
1953UbiquitinationTLRMMVQKERSLDIL
HHHHHHHHHHHHHHH
43.62-
1956PhosphorylationMMVQKERSLDILKGK
HHHHHHHHHHHHCCC
31.3328060719
1961UbiquitinationERSLDILKGKVMASM
HHHHHHHCCCHHHHE
57.9521906983
1963UbiquitinationSLDILKGKVMASMFY
HHHHHCCCHHHHEEE
27.53-
1967PhosphorylationLKGKVMASMFYEVST
HCCCHHHHEEEECCC
7.4229759185
1970PhosphorylationKVMASMFYEVSTRTS
CHHHHEEEECCCCCC
13.5424043423
1973PhosphorylationASMFYEVSTRTSSSF
HHEEEECCCCCCHHH
10.5529759185
1974PhosphorylationSMFYEVSTRTSSSFA
HEEEECCCCCCHHHH
43.0424043423
1976PhosphorylationFYEVSTRTSSSFAAA
EEECCCCCCHHHHHH
32.8023186163
1977PhosphorylationYEVSTRTSSSFAAAM
EECCCCCCHHHHHHH
22.2423186163
1978PhosphorylationEVSTRTSSSFAAAMA
ECCCCCCHHHHHHHH
28.9423186163
2036AcetylationGAVELAAKHCRRPVI
CHHHHHHHHCCCCEE
37.3225953088
2036UbiquitinationGAVELAAKHCRRPVI
CHHHHHHHHCCCCEE
37.32-
2062PhosphorylationQALLDIFTIREELGT
HHHHHHHHHHHHHCC
21.3224719451
2069PhosphorylationTIREELGTVNGMTIT
HHHHHHCCCCCEEEE
24.3524114839
2074PhosphorylationLGTVNGMTITMVGDL
HCCCCCEEEEEECCC
18.0724114839
2076PhosphorylationTVNGMTITMVGDLKH
CCCCEEEEEECCCCC
9.1724114839
2082AcetylationITMVGDLKHGRTVHS
EEEECCCCCCCCHHH
49.0725953088
2086PhosphorylationGDLKHGRTVHSLACL
CCCCCCCCHHHHHHH
27.4527461979
2089PhosphorylationKHGRTVHSLACLLTQ
CCCCCHHHHHHHHHC
17.2127461979
2095PhosphorylationHSLACLLTQYRVSLR
HHHHHHHHCCCCEEE
15.5927461979
2097PhosphorylationLACLLTQYRVSLRYV
HHHHHHCCCCEEEEC
14.0327461979
2103PhosphorylationQYRVSLRYVAPPSLR
CCCCEEEECCCHHHC
13.27-
2124PhosphorylationAFVASRGTKQEEFES
HHHHCCCCCHHHHHH
28.5722210691
2125UbiquitinationFVASRGTKQEEFESI
HHHCCCCCHHHHHHH
59.542190698
2143PhosphorylationLPDTDVLYMTRIQKE
CCCCCEEEEEEECHH
9.0422210691
2145PhosphorylationDTDVLYMTRIQKERF
CCCEEEEEEECHHHH
15.8622210691
2154PhosphorylationIQKERFGSTQEYEAC
ECHHHHCCCHHHHHH
24.97-
2155PhosphorylationQKERFGSTQEYEACF
CHHHHCCCHHHHHHH
26.29-
2158PhosphorylationRFGSTQEYEACFGQF
HHCCCHHHHHHHHHH
10.06-
2178UbiquitinationIMTRAKKKMVVMHPM
HHHHHCCCEEEEECC
35.90-
2203PhosphorylationDSDPRAAYFRQAENG
CCCCCHHHHHHHHCC
9.79-
2212PhosphorylationRQAENGMYIRMALLA
HHHHCCHHHHHHHHH
6.1824144214
2220PhosphorylationIRMALLATVLGRF--
HHHHHHHHHHCCC--
19.0821406692

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
456TPhosphorylationKinaseMK01P28482
PhosphoELM
456TPhosphorylationKinaseMAPK3P27361
GPS
1406SPhosphorylationKinasePRKACAP17612
GPS
1406SPhosphorylationKinasePKA-FAMILY-GPS
1406SPhosphorylationKinasePKA-Uniprot
1406SPhosphorylationKinasePKA_GROUP-PhosphoELM
1859SPhosphorylationKinasePRKACAP17612
GPS
1859SPhosphorylationKinaseP70S6KP23443
PSP
1859SPhosphorylationKinasePKA-Uniprot
1873SPhosphorylationKinasePKC-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1406SPhosphorylation

17485345
1859SPhosphorylation

17081983

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 PYR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUVB2_HUMANRUVBL2physical
22939629
TBB4B_HUMANTUBB4Bphysical
22939629
TBA4A_HUMANTUBA4Aphysical
22939629
RUVB1_HUMANRUVBL1physical
22939629
XPO1_HUMANXPO1physical
22939629
TBB2A_HUMANTUBB2Aphysical
22939629
SMRC2_HUMANSMARCC2physical
22939629
RS3_HUMANRPS3physical
22939629
SMCA4_HUMANSMARCA4physical
22939629
SYVC_HUMANVARSphysical
22939629
ACTZ_HUMANACTR1Aphysical
26344197
TCPG_HUMANCCT3physical
26344197
TCPD_HUMANCCT4physical
26344197
TCPZ_HUMANCCT6Aphysical
26344197
TCPQ_HUMANCCT8physical
26344197
CLH1_HUMANCLTCphysical
26344197
COPB_HUMANCOPB1physical
26344197
DDX3X_HUMANDDX3Xphysical
26344197
DNJA1_HUMANDNAJA1physical
26344197
DNJA4_HUMANDNAJA4physical
26344197
EF1A1_HUMANEEF1A1physical
26344197
EI2BA_HUMANEIF2B1physical
26344197
IF2A_HUMANEIF2S1physical
26344197
SYEP_HUMANEPRSphysical
26344197
GFPT1_HUMANGFPT1physical
26344197
HSP7C_HUMANHSPA8physical
26344197
SYIC_HUMANIARSphysical
26344197
IDH3A_HUMANIDH3Aphysical
26344197
IPO4_HUMANIPO4physical
26344197
MCM7_HUMANMCM7physical
26344197
PRS6A_HUMANPSMC3physical
26344197
PRS6B_HUMANPSMC4physical
26344197
PRS8_HUMANPSMC5physical
26344197
PRS10_HUMANPSMC6physical
26344197
PSD12_HUMANPSMD12physical
26344197
PSMD2_HUMANPSMD2physical
26344197
PSMD4_HUMANPSMD4physical
26344197
RUVB1_HUMANRUVBL1physical
26344197
RUVB2_HUMANRUVBL2physical
26344197
MPCP_HUMANSLC25A3physical
26344197
UBR5_HUMANUBR5physical
26344197
QCR2_HUMANUQCRC2physical
26344197
YMEL1_HUMANYME1L1physical
26344197
FAS_HUMANFASNphysical
28775317

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
DB00128L-Aspartic Acid
DB00130L-Glutamine
Regulatory Network of PYR1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-747 AND LYS-1411, AND MASSSPECTROMETRY.
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-1038 AND SER-1859, ANDMASS 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 THR-1037 AND SER-1859, ANDMASS 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-1859 AND THR-1884, ANDMASS 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-1038; SER-1859 ANDTHR-1884, AND MASS 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-1423, AND MASSSPECTROMETRY.
"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-1859, AND MASSSPECTROMETRY.
"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-1823 AND SER-1859, ANDMASS SPECTROMETRY.

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