ANXA6_HUMAN - dbPTM
ANXA6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANXA6_HUMAN
UniProt AC P08133
Protein Name Annexin A6
Gene Name ANXA6
Organism Homo sapiens (Human).
Sequence Length 673
Subcellular Localization Cytoplasm. Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description May associate with CD21. May regulate the release of Ca(2+) from intracellular stores..
Protein Sequence MAKPAQGAKYRGSIHDFPGFDPNQDAEALYTAMKGFGSDKEAILDIITSRSNRQRQEVCQSYKSLYGKDLIADLKYELTGKFERLIVGLMRPPAYCDAKEIKDAISGIGTDEKCLIEILASRTNEQMHQLVAAYKDAYERDLEADIIGDTSGHFQKMLVVLLQGTREEDDVVSEDLVQQDVQDLYEAGELKWGTDEAQFIYILGNRSKQHLRLVFDEYLKTTGKPIEASIRGELSGDFEKLMLAVVKCIRSTPEYFAERLFKAMKGLGTRDNTLIRIMVSRSELDMLDIREIFRTKYEKSLYSMIKNDTSGEYKKTLLKLSGGDDDAAGQFFPEAAQVAYQMWELSAVARVELKGTVRPANDFNPDADAKALRKAMKGLGTDEDTIIDIITHRSNVQRQQIRQTFKSHFGRDLMTDLKSEISGDLARLILGLMMPPAHYDAKQLKKAMEGAGTDEKALIEILATRTNAEIRAINEAYKEDYHKSLEDALSSDTSGHFRRILISLATGHREEGGENLDQAREDAQVAAEILEIADTPSGDKTSLETRFMTILCTRSYPHLRRVFQEFIKMTNYDVEHTIKKEMSGDVRDAFVAIVQSVKNKPLFFADKLYKSMKGAGTDEKTLTRIMVSRSEIDLLNIRREFIEKYDKSLHQAIEGDTSGDFLKALLALCGGED
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------MAKPAQGAK
------CCCCCCCCC
26.9225944712
3Acetylation-----MAKPAQGAKY
-----CCCCCCCCCC
39.3223749302
92-HydroxyisobutyrylationAKPAQGAKYRGSIHD
CCCCCCCCCCCCCCC
42.16-
9AcetylationAKPAQGAKYRGSIHD
CCCCCCCCCCCCCCC
42.1623749302
9UbiquitinationAKPAQGAKYRGSIHD
CCCCCCCCCCCCCCC
42.16-
10PhosphorylationKPAQGAKYRGSIHDF
CCCCCCCCCCCCCCC
21.4826657352
11MethylationPAQGAKYRGSIHDFP
CCCCCCCCCCCCCCC
31.51-
13PhosphorylationQGAKYRGSIHDFPGF
CCCCCCCCCCCCCCC
14.0428258704
30PhosphorylationNQDAEALYTAMKGFG
CCCHHHHHHHHHCCC
10.2521082442
31AcetylationQDAEALYTAMKGFGS
CCHHHHHHHHHCCCC
22.5619608861
31PhosphorylationQDAEALYTAMKGFGS
CCHHHHHHHHHCCCC
22.5628796482
31UbiquitinationQDAEALYTAMKGFGS
CCHHHHHHHHHCCCC
22.5619608861
33SulfoxidationAEALYTAMKGFGSDK
HHHHHHHHHCCCCCH
3.1730846556
34UbiquitinationEALYTAMKGFGSDKE
HHHHHHHHCCCCCHH
48.93-
36AcetylationLYTAMKGFGSDKEAI
HHHHHHCCCCCHHHH
7.6519608861
36UbiquitinationLYTAMKGFGSDKEAI
HHHHHHCCCCCHHHH
7.6519608861
38PhosphorylationTAMKGFGSDKEAILD
HHHHCCCCCHHHHHH
43.1630108239
40AcetylationMKGFGSDKEAILDII
HHCCCCCHHHHHHHH
51.2323954790
40UbiquitinationMKGFGSDKEAILDII
HHCCCCCHHHHHHHH
51.23-
43AcetylationFGSDKEAILDIITSR
CCCCHHHHHHHHHCC
3.5819608861
48PhosphorylationEAILDIITSRSNRQR
HHHHHHHHCCCHHHH
20.5820068231
49AcetylationAILDIITSRSNRQRQ
HHHHHHHCCCHHHHH
24.2519608861
49PhosphorylationAILDIITSRSNRQRQ
HHHHHHHCCCHHHHH
24.2520068231
49UbiquitinationAILDIITSRSNRQRQ
HHHHHHHCCCHHHHH
24.2519608861
51PhosphorylationLDIITSRSNRQRQEV
HHHHHCCCHHHHHHH
35.8124043423
61PhosphorylationQRQEVCQSYKSLYGK
HHHHHHHHHHHHHCC
29.4224275569
63AcetylationQEVCQSYKSLYGKDL
HHHHHHHHHHHCCHH
38.9519608861
63MalonylationQEVCQSYKSLYGKDL
HHHHHHHHHHHCCHH
38.9526320211
63UbiquitinationQEVCQSYKSLYGKDL
HHHHHHHHHHHCCHH
38.9519608861
64PhosphorylationEVCQSYKSLYGKDLI
HHHHHHHHHHCCHHH
20.7028258704
66PhosphorylationCQSYKSLYGKDLIAD
HHHHHHHHCCHHHHH
29.2628258704
68UbiquitinationSYKSLYGKDLIADLK
HHHHHHCCHHHHHHH
35.4921890473
68AcetylationSYKSLYGKDLIADLK
HHHHHHCCHHHHHHH
35.4919608861
68UbiquitinationSYKSLYGKDLIADLK
HHHHHHCCHHHHHHH
35.4921890473
752-HydroxyisobutyrylationKDLIADLKYELTGKF
CHHHHHHHHHHCCCC
36.91-
75AcetylationKDLIADLKYELTGKF
CHHHHHHHHHHCCCC
36.9119608861
75UbiquitinationKDLIADLKYELTGKF
CHHHHHHHHHHCCCC
36.9119608861
76PhosphorylationDLIADLKYELTGKFE
HHHHHHHHHHCCCCH
24.3820560785
81UbiquitinationLKYELTGKFERLIVG
HHHHHCCCCHHHHHH
38.5221890473
812-HydroxyisobutyrylationLKYELTGKFERLIVG
HHHHHCCCCHHHHHH
38.52-
81AcetylationLKYELTGKFERLIVG
HHHHHCCCCHHHHHH
38.5219608861
81UbiquitinationLKYELTGKFERLIVG
HHHHHCCCCHHHHHH
38.5221890473
90SulfoxidationERLIVGLMRPPAYCD
HHHHHHHCCCCCCCC
5.0730846556
95PhosphorylationGLMRPPAYCDAKEIK
HHCCCCCCCCHHHHH
9.1730108239
99AcetylationPPAYCDAKEIKDAIS
CCCCCCHHHHHHHHC
46.8823749302
99MalonylationPPAYCDAKEIKDAIS
CCCCCCHHHHHHHHC
46.8826320211
99UbiquitinationPPAYCDAKEIKDAIS
CCCCCCHHHHHHHHC
46.88-
1022-HydroxyisobutyrylationYCDAKEIKDAISGIG
CCCHHHHHHHHCCCC
42.05-
102AcetylationYCDAKEIKDAISGIG
CCCHHHHHHHHCCCC
42.0523749302
102UbiquitinationYCDAKEIKDAISGIG
CCCHHHHHHHHCCCC
42.0521906983
106PhosphorylationKEIKDAISGIGTDEK
HHHHHHHCCCCCCHH
26.5320873877
110PhosphorylationDAISGIGTDEKCLIE
HHHCCCCCCHHHHHH
38.7826437602
1132-HydroxyisobutyrylationSGIGTDEKCLIEILA
CCCCCCHHHHHHHHH
36.83-
113AcetylationSGIGTDEKCLIEILA
CCCCCCHHHHHHHHH
36.8326822725
113UbiquitinationSGIGTDEKCLIEILA
CCCCCCHHHHHHHHH
36.8321906983
114S-nitrosocysteineGIGTDEKCLIEILAS
CCCCCHHHHHHHHHH
4.32-
114S-nitrosylationGIGTDEKCLIEILAS
CCCCCHHHHHHHHHH
4.3219483679
114S-palmitoylationGIGTDEKCLIEILAS
CCCCCHHHHHHHHHH
4.3229575903
121PhosphorylationCLIEILASRTNEQMH
HHHHHHHHCCHHHHH
35.8721712546
127SulfoxidationASRTNEQMHQLVAAY
HHCCHHHHHHHHHHH
1.4530846556
135UbiquitinationHQLVAAYKDAYERDL
HHHHHHHHHHHHHHH
31.0221890473
1352-HydroxyisobutyrylationHQLVAAYKDAYERDL
HHHHHHHHHHHHHHH
31.02-
135AcetylationHQLVAAYKDAYERDL
HHHHHHHHHHHHHHH
31.0226822725
135UbiquitinationHQLVAAYKDAYERDL
HHHHHHHHHHHHHHH
31.0221906983
150PhosphorylationEADIIGDTSGHFQKM
HCCCCCCCCHHHHHH
31.2530108239
151PhosphorylationADIIGDTSGHFQKML
CCCCCCCCHHHHHHH
34.7030108239
173PhosphorylationREEDDVVSEDLVQQD
CCCCCCCCHHHHHHH
25.8220873877
185PhosphorylationQQDVQDLYEAGELKW
HHHHHHHHHHCCCCC
16.4250565703
201PhosphorylationTDEAQFIYILGNRSK
CCHHHEEEEECCCCH
7.4421082442
218NitrationLRLVFDEYLKTTGKP
HHHHHHHHHHHHCCC
18.49-
220AcetylationLVFDEYLKTTGKPIE
HHHHHHHHHHCCCCC
43.0426051181
220UbiquitinationLVFDEYLKTTGKPIE
HHHHHHHHHHCCCCC
43.04-
221O-linked_GlycosylationVFDEYLKTTGKPIEA
HHHHHHHHHCCCCCH
37.8830379171
221PhosphorylationVFDEYLKTTGKPIEA
HHHHHHHHHCCCCCH
37.8820068231
222O-linked_GlycosylationFDEYLKTTGKPIEAS
HHHHHHHHCCCCCHH
41.4430379171
222PhosphorylationFDEYLKTTGKPIEAS
HHHHHHHHCCCCCHH
41.4420068231
224AcetylationEYLKTTGKPIEASIR
HHHHHHCCCCCHHHC
40.5026051181
224UbiquitinationEYLKTTGKPIEASIR
HHHHHHCCCCCHHHC
40.50-
229PhosphorylationTGKPIEASIRGELSG
HCCCCCHHHCCCCCC
10.4620068231
235PhosphorylationASIRGELSGDFEKLM
HHHCCCCCCCHHHHH
31.8226657352
240UbiquitinationELSGDFEKLMLAVVK
CCCCCHHHHHHHHHH
38.91-
247UbiquitinationKLMLAVVKCIRSTPE
HHHHHHHHHHHCCHH
19.83-
251PhosphorylationAVVKCIRSTPEYFAE
HHHHHHHCCHHHHHH
28.5320068231
252PhosphorylationVVKCIRSTPEYFAER
HHHHHHCCHHHHHHH
15.4222210691
255PhosphorylationCIRSTPEYFAERLFK
HHHCCHHHHHHHHHH
14.8622210691
259MethylationTPEYFAERLFKAMKG
CHHHHHHHHHHHHCC
41.83-
265AcetylationERLFKAMKGLGTRDN
HHHHHHHCCCCCCCC
56.7125953088
265MalonylationERLFKAMKGLGTRDN
HHHHHHHCCCCCCCC
56.7126320211
267AcetylationLFKAMKGLGTRDNTL
HHHHHCCCCCCCCHH
5.4419608861
269PhosphorylationKAMKGLGTRDNTLIR
HHHCCCCCCCCHHEE
39.6317494752
273PhosphorylationGLGTRDNTLIRIMVS
CCCCCCCHHEEEEEE
28.0554887405
274AcetylationLGTRDNTLIRIMVSR
CCCCCCHHEEEEEEH
2.8819608861
282PhosphorylationIRIMVSRSELDMLDI
EEEEEEHHHHCCCCH
34.7063735769
286SulfoxidationVSRSELDMLDIREIF
EEHHHHCCCCHHHHH
5.9121406390
297PhosphorylationREIFRTKYEKSLYSM
HHHHHHHHHHHHHHH
28.1629759185
299AcetylationIFRTKYEKSLYSMIK
HHHHHHHHHHHHHHH
42.5423236377
299MalonylationIFRTKYEKSLYSMIK
HHHHHHHHHHHHHHH
42.5426320211
299UbiquitinationIFRTKYEKSLYSMIK
HHHHHHHHHHHHHHH
42.5419608861
300PhosphorylationFRTKYEKSLYSMIKN
HHHHHHHHHHHHHHC
22.1728258704
302PhosphorylationTKYEKSLYSMIKNDT
HHHHHHHHHHHHCCC
11.8621082442
303PhosphorylationKYEKSLYSMIKNDTS
HHHHHHHHHHHCCCC
21.2328258704
306AcetylationKSLYSMIKNDTSGEY
HHHHHHHHCCCCCHH
39.8819608861
306MalonylationKSLYSMIKNDTSGEY
HHHHHHHHCCCCCHH
39.8826320211
306UbiquitinationKSLYSMIKNDTSGEY
HHHHHHHHCCCCCHH
39.8819608861
310PhosphorylationSMIKNDTSGEYKKTL
HHHHCCCCCHHHHEE
32.2726437602
313PhosphorylationKNDTSGEYKKTLLKL
HCCCCCHHHHEEEHH
22.7011079915
314AcetylationNDTSGEYKKTLLKLS
CCCCCHHHHEEEHHC
34.6725953088
338AcetylationFFPEAAQVAYQMWEL
HCHHHHHHHHHHHHH
4.6119608861
338UbiquitinationFFPEAAQVAYQMWEL
HCHHHHHHHHHHHHH
4.6119608861
340PhosphorylationPEAAQVAYQMWELSA
HHHHHHHHHHHHHHC
10.47119653
342SulfoxidationAAQVAYQMWELSAVA
HHHHHHHHHHHHCEE
1.6330846556
354AcetylationAVARVELKGTVRPAN
CEEEEEECCEECCCH
38.7425953088
354MalonylationAVARVELKGTVRPAN
CEEEEEECCEECCCH
38.7426320211
356PhosphorylationARVELKGTVRPANDF
EEEEECCEECCCHHC
16.2621406692
370AcetylationFNPDADAKALRKAMK
CCCCHHHHHHHHHHH
48.8019608861
370MalonylationFNPDADAKALRKAMK
CCCCHHHHHHHHHHH
48.8026320211
370UbiquitinationFNPDADAKALRKAMK
CCCCHHHHHHHHHHH
48.8019608861
377UbiquitinationKALRKAMKGLGTDED
HHHHHHHHCCCCCHH
56.7121890473
377AcetylationKALRKAMKGLGTDED
HHHHHHHHCCCCCHH
56.7125953088
377UbiquitinationKALRKAMKGLGTDED
HHHHHHHHCCCCCHH
56.7121890473
381PhosphorylationKAMKGLGTDEDTIID
HHHHCCCCCHHHHHH
41.0628450419
385PhosphorylationGLGTDEDTIIDIITH
CCCCCHHHHHHHHHC
20.1325338102
386AcetylationLGTDEDTIIDIITHR
CCCCHHHHHHHHHCC
4.0519608861
386UbiquitinationLGTDEDTIIDIITHR
CCCCHHHHHHHHHCC
4.0519608861
391PhosphorylationDTIIDIITHRSNVQR
HHHHHHHHCCHHHHH
16.1518767875
406AcetylationQQIRQTFKSHFGRDL
HHHHHHHHHHHCHHH
46.5425953088
406MalonylationQQIRQTFKSHFGRDL
HHHHHHHHHHHCHHH
46.5426320211
406UbiquitinationQQIRQTFKSHFGRDL
HHHHHHHHHHHCHHH
46.54-
410AcetylationQTFKSHFGRDLMTDL
HHHHHHHCHHHHHHH
19.4419608861
418AcetylationRDLMTDLKSEISGDL
HHHHHHHHHHHCHHH
49.1819608861
418UbiquitinationRDLMTDLKSEISGDL
HHHHHHHHHHHCHHH
49.1821906983
419PhosphorylationDLMTDLKSEISGDLA
HHHHHHHHHHCHHHH
47.6723911959
422PhosphorylationTDLKSEISGDLARLI
HHHHHHHCHHHHHHH
23.3973401921
433SulfoxidationARLILGLMMPPAHYD
HHHHHHHHCCCCCCC
3.4430846556
434SulfoxidationRLILGLMMPPAHYDA
HHHHHHHCCCCCCCH
4.2930846556
442AcetylationPPAHYDAKQLKKAME
CCCCCCHHHHHHHHC
53.9523954790
442MalonylationPPAHYDAKQLKKAME
CCCCCCHHHHHHHHC
53.9526320211
445AcetylationHYDAKQLKKAMEGAG
CCCHHHHHHHHCCCC
35.6723749302
446UbiquitinationYDAKQLKKAMEGAGT
CCHHHHHHHHCCCCC
62.65-
448SulfoxidationAKQLKKAMEGAGTDE
HHHHHHHHCCCCCCH
7.2030846556
451AcetylationLKKAMEGAGTDEKAL
HHHHHCCCCCCHHHH
12.3819608861
456AcetylationEGAGTDEKALIEILA
CCCCCCHHHHHHHHH
51.8325953088
456UbiquitinationEGAGTDEKALIEILA
CCCCCCHHHHHHHHH
51.83-
464PhosphorylationALIEILATRTNAEIR
HHHHHHHHCCHHHHH
34.2821406692
478AcetylationRAINEAYKEDYHKSL
HHHHHHHHHHHHHHH
51.6723749302
478UbiquitinationRAINEAYKEDYHKSL
HHHHHHHHHHHHHHH
51.67-
483AcetylationAYKEDYHKSLEDALS
HHHHHHHHHHHHHHH
50.9719608861
483UbiquitinationAYKEDYHKSLEDALS
HHHHHHHHHHHHHHH
50.9719608861
484PhosphorylationYKEDYHKSLEDALSS
HHHHHHHHHHHHHHC
24.5523312004
490PhosphorylationKSLEDALSSDTSGHF
HHHHHHHHCCCCHHH
28.0830108239
491PhosphorylationSLEDALSSDTSGHFR
HHHHHHHCCCCHHHH
45.8430108239
493PhosphorylationEDALSSDTSGHFRRI
HHHHHCCCCHHHHHH
38.2630108239
494PhosphorylationDALSSDTSGHFRRIL
HHHHCCCCHHHHHHH
34.9530108239
503PhosphorylationHFRRILISLATGHRE
HHHHHHHHHHHCCCH
14.4323312004
506PhosphorylationRILISLATGHREEGG
HHHHHHHHCCCHHCC
38.5223312004
535PhosphorylationEILEIADTPSGDKTS
HHHHHCCCCCCCCCC
15.4426657352
537PhosphorylationLEIADTPSGDKTSLE
HHHCCCCCCCCCCHH
62.8126471730
540AcetylationADTPSGDKTSLETRF
CCCCCCCCCCHHHHH
43.4726051181
540UbiquitinationADTPSGDKTSLETRF
CCCCCCCCCCHHHHH
43.4721890473
548SulfoxidationTSLETRFMTILCTRS
CCHHHHHHHHHHCCC
1.7321406390
549PhosphorylationSLETRFMTILCTRSY
CHHHHHHHHHHCCCC
14.2126074081
568AcetylationRVFQEFIKMTNYDVE
HHHHHHHHHHCCCHH
45.0226051181
568UbiquitinationRVFQEFIKMTNYDVE
HHHHHHHHHHCCCHH
45.0221906983
569SulfoxidationVFQEFIKMTNYDVEH
HHHHHHHHHCCCHHH
2.2230846556
570PhosphorylationFQEFIKMTNYDVEHT
HHHHHHHHCCCHHHH
26.1428270605
572PhosphorylationEFIKMTNYDVEHTIK
HHHHHHCCCHHHHHH
16.5246164741
575AcetylationKMTNYDVEHTIKKEM
HHHCCCHHHHHHHHH
32.2019608861
5792-HydroxyisobutyrylationYDVEHTIKKEMSGDV
CCHHHHHHHHHCCCH
43.78-
579AcetylationYDVEHTIKKEMSGDV
CCHHHHHHHHHCCCH
43.7825953088
579MalonylationYDVEHTIKKEMSGDV
CCHHHHHHHHHCCCH
43.7826320211
579UbiquitinationYDVEHTIKKEMSGDV
CCHHHHHHHHHCCCH
43.78-
580AcetylationDVEHTIKKEMSGDVR
CHHHHHHHHHCCCHH
55.5919809363
583PhosphorylationHTIKKEMSGDVRDAF
HHHHHHHCCCHHHHH
32.6910398665
588AcetylationEMSGDVRDAFVAIVQ
HHCCCHHHHHHHHHH
44.1819608861
588UbiquitinationEMSGDVRDAFVAIVQ
HHCCCHHHHHHHHHH
44.1819608861
596PhosphorylationAFVAIVQSVKNKPLF
HHHHHHHHHCCCCCC
24.9463774529
6002-HydroxyisobutyrylationIVQSVKNKPLFFADK
HHHHHCCCCCCCHHH
37.06-
600AcetylationIVQSVKNKPLFFADK
HHHHHCCCCCCCHHH
37.0626051181
600UbiquitinationIVQSVKNKPLFFADK
HHHHHCCCCCCCHHH
37.06-
6072-HydroxyisobutyrylationKPLFFADKLYKSMKG
CCCCCHHHHHHHCCC
50.73-
607AcetylationKPLFFADKLYKSMKG
CCCCCHHHHHHHCCC
50.7319608861
607UbiquitinationKPLFFADKLYKSMKG
CCCCCHHHHHHHCCC
50.7319608861
609PhosphorylationLFFADKLYKSMKGAG
CCCHHHHHHHCCCCC
13.5225147952
610AcetylationFFADKLYKSMKGAGT
CCHHHHHHHCCCCCC
55.2827178108
611PhosphorylationFADKLYKSMKGAGTD
CHHHHHHHCCCCCCC
16.5122468782
613AcetylationDKLYKSMKGAGTDEK
HHHHHHCCCCCCCHH
53.3425953088
6202-HydroxyisobutyrylationKGAGTDEKTLTRIMV
CCCCCCHHHHHHHHH
52.20-
620AcetylationKGAGTDEKTLTRIMV
CCCCCCHHHHHHHHH
52.2019608861
620MalonylationKGAGTDEKTLTRIMV
CCCCCCHHHHHHHHH
52.2026320211
620UbiquitinationKGAGTDEKTLTRIMV
CCCCCCHHHHHHHHH
52.2019608861
628PhosphorylationTLTRIMVSRSEIDLL
HHHHHHHCHHHHCHH
16.8330108239
630PhosphorylationTRIMVSRSEIDLLNI
HHHHHCHHHHCHHHH
31.2563774319
644AcetylationIRREFIEKYDKSLHQ
HHHHHHHHHCHHHHH
54.6726051181
644UbiquitinationIRREFIEKYDKSLHQ
HHHHHHHHHCHHHHH
54.67-
645PhosphorylationRREFIEKYDKSLHQA
HHHHHHHHCHHHHHH
18.8024275569
647AcetylationEFIEKYDKSLHQAIE
HHHHHHCHHHHHHHC
52.4025953088
647MalonylationEFIEKYDKSLHQAIE
HHHHHHCHHHHHHHC
52.4026320211
647UbiquitinationEFIEKYDKSLHQAIE
HHHHHHCHHHHHHHC
52.40-
648PhosphorylationFIEKYDKSLHQAIEG
HHHHHCHHHHHHHCC
28.3426437602
657PhosphorylationHQAIEGDTSGDFLKA
HHHHCCCCCHHHHHH
45.5369003001
658PhosphorylationQAIEGDTSGDFLKAL
HHHCCCCCHHHHHHH
40.9028857561
663UbiquitinationDTSGDFLKALLALCG
CCCHHHHHHHHHHCC
36.66-

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANXA6_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 ANXA6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC73_HUMANCDC73physical
16169070
RASA1_RATRasa1physical
8798684
S10A1_HUMANS100A1physical
9883272
S100B_HUMANS100Bphysical
9883272
PURA2_HUMANADSSphysical
22863883
HPRT_HUMANHPRT1physical
22863883
IDHC_HUMANIDH1physical
22863883
NAMPT_HUMANNAMPTphysical
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 ANXA6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Structure and properties of calphobindin II, an anticoagulant proteinfrom human placenta.";
Yoshizaki H., Mizoguchi T., Arai K., Shiratsuchi M., Shidara Y.,Maki M.;
J. Biochem. 107:43-50(1990).
Cited for: PROTEIN SEQUENCE OF 2-673.
"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-63; LYS-68; LYS-75; LYS-81;LYS-299; LYS-306; LYS-370; LYS-418; LYS-483; LYS-607 AND LYS-620, ANDMASS 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 TYR-30, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND MASSSPECTROMETRY.

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