ADDA_HUMAN - dbPTM
ADDA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADDA_HUMAN
UniProt AC P35611
Protein Name Alpha-adducin
Gene Name ADD1
Organism Homo sapiens (Human).
Sequence Length 737
Subcellular Localization Cytoplasm, cytoskeleton. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin..
Protein Sequence MNGDSRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTTNVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLNPEKYKAKSRSPGSPVGEGTGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALREKSKKYSDVEVPASVTGYSFASDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS
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
1Acetylation-------MNGDSRAA
-------CCCCCCCE
13.1119413330
5Phosphorylation---MNGDSRAAVVTS
---CCCCCCCEEECC
25.8026074081
11PhosphorylationDSRAAVVTSPPPTTA
CCCCEEECCCCCCCC
28.9929255136
12PhosphorylationSRAAVVTSPPPTTAP
CCCEEECCCCCCCCC
24.6529255136
16PhosphorylationVVTSPPPTTAPHKER
EECCCCCCCCCCHHH
41.1730278072
17PhosphorylationVTSPPPTTAPHKERY
ECCCCCCCCCCHHHH
43.9230278072
21UbiquitinationPPTTAPHKERYFDRV
CCCCCCCHHHHHCCC
42.71-
21UbiquitinationPPTTAPHKERYFDRV
CCCCCCCHHHHHCCC
42.7132015554
21 (in isoform 3)Ubiquitination-42.71-
24PhosphorylationTAPHKERYFDRVDEN
CCCCHHHHHCCCCCC
15.7826074081
27MethylationHKERYFDRVDENNPE
CHHHHHCCCCCCCHH
28.08-
35PhosphorylationVDENNPEYLRERNMA
CCCCCHHHHHHHCCC
16.5929978859
55UbiquitinationDFNMMEQKKRVSMIL
HHHHHHHHHHHHHHH
29.28-
55UbiquitinationDFNMMEQKKRVSMIL
HHHHHHHHHHHHHHH
29.2821906983
55 (in isoform 1)Ubiquitination-29.2821906983
55 (in isoform 2)Ubiquitination-29.2821906983
55 (in isoform 3)Ubiquitination-29.2821906983
55UbiquitinationDFNMMEQKKRVSMIL
HHHHHHHHHHHHHHH
29.2821906983
56UbiquitinationFNMMEQKKRVSMILQ
HHHHHHHHHHHHHHH
58.7024816145
59PhosphorylationMEQKKRVSMILQSPA
HHHHHHHHHHHHCHH
12.2525159151
64PhosphorylationRVSMILQSPAFCEEL
HHHHHHHCHHHHHHH
18.1029496963
73PhosphorylationAFCEELESMIQEQFK
HHHHHHHHHHHHHHH
33.5328270605
80UbiquitinationSMIQEQFKKGKNPTG
HHHHHHHHCCCCHHH
61.3832015554
133PhosphorylationPVNDLRGSDSIAYDK
CHHHCCCCCCCCCCC
23.0421815630
135PhosphorylationNDLRGSDSIAYDKGE
HHCCCCCCCCCCCCC
15.7128857561
138PhosphorylationRGSDSIAYDKGEKLL
CCCCCCCCCCCCHHH
19.2722985185
140AcetylationSDSIAYDKGEKLLRC
CCCCCCCCCCHHHHH
57.18-
140UbiquitinationSDSIAYDKGEKLLRC
CCCCCCCCCCHHHHH
57.18-
140AcetylationSDSIAYDKGEKLLRC
CCCCCCCCCCHHHHH
57.1823749302
140UbiquitinationSDSIAYDKGEKLLRC
CCCCCCCCCCHHHHH
57.1821906983
140 (in isoform 1)Ubiquitination-57.1821906983
140 (in isoform 2)Ubiquitination-57.1821906983
140 (in isoform 3)Ubiquitination-57.1821906983
140UbiquitinationSDSIAYDKGEKLLRC
CCCCCCCCCCHHHHH
57.1821906983
143UbiquitinationIAYDKGEKLLRCKLA
CCCCCCCHHHHHHHH
62.58-
143AcetylationIAYDKGEKLLRCKLA
CCCCCCCHHHHHHHH
62.5825953088
143UbiquitinationIAYDKGEKLLRCKLA
CCCCCCCHHHHHHHH
62.5824816145
143 (in isoform 3)Ubiquitination-62.58-
148UbiquitinationGEKLLRCKLAAFYRL
CCHHHHHHHHHHHHH
34.42-
148UbiquitinationGEKLLRCKLAAFYRL
CCHHHHHHHHHHHHH
34.42-
148 (in isoform 3)Ubiquitination-34.42-
166PhosphorylationFGWSQLIYNHITTRV
HCHHHHHHHHHHHCC
14.8524719451
170PhosphorylationQLIYNHITTRVNSEQ
HHHHHHHHHCCCCCC
10.8624719451
171PhosphorylationLIYNHITTRVNSEQE
HHHHHHHHCCCCCCC
31.8324719451
283UbiquitinationILVDEEEKVLIQKNL
EECCHHHHHHEECCC
45.6923000965
288UbiquitinationEEKVLIQKNLGPKSK
HHHHHEECCCCCCCE
47.34-
288UbiquitinationEEKVLIQKNLGPKSK
HHHHHEECCCCCCCE
47.3423000965
288 (in isoform 3)Ubiquitination-47.34-
293UbiquitinationIQKNLGPKSKVLILR
EECCCCCCCEEEEEE
62.2023000965
331PhosphorylationACEIQVRTLASAGGP
EEEEEHHHHHHCCCC
28.0218669648
334PhosphorylationIQVRTLASAGGPDNL
EEHHHHHHCCCCCCE
30.4718669648
348UbiquitinationLVLLNPEKYKAKSRS
EEEECHHHHCCCCCC
53.99-
348UbiquitinationLVLLNPEKYKAKSRS
EEEECHHHHCCCCCC
53.992190698
348 (in isoform 1)Ubiquitination-53.9921906983
348 (in isoform 2)Ubiquitination-53.9921906983
348 (in isoform 3)Ubiquitination-53.9921906983
348UbiquitinationLVLLNPEKYKAKSRS
EEEECHHHHCCCCCC
53.9921906983
350UbiquitinationLLNPEKYKAKSRSPG
EECHHHHCCCCCCCC
61.48-
350 (in isoform 3)Ubiquitination-61.48-
353PhosphorylationPEKYKAKSRSPGSPV
HHHHCCCCCCCCCCC
42.7320201521
355PhosphorylationKYKAKSRSPGSPVGE
HHCCCCCCCCCCCCC
40.4823927012
358PhosphorylationAKSRSPGSPVGEGTG
CCCCCCCCCCCCCCC
21.5719664994
364PhosphorylationGSPVGEGTGSPPKWQ
CCCCCCCCCCCCCCC
30.1323927012
366PhosphorylationPVGEGTGSPPKWQIG
CCCCCCCCCCCCCCC
37.5619664994
393PhosphorylationNLGYRTGYPYRYPAL
HCCCCCCCCCCCHHH
9.1174103147
395PhosphorylationGYRTGYPYRYPALRE
CCCCCCCCCCHHHHH
17.8174103145
404PhosphorylationYPALREKSKKYSDVE
CHHHHHHCCCCCCCC
29.6323312004
406UbiquitinationALREKSKKYSDVEVP
HHHHHCCCCCCCCCC
58.0129967540
407PhosphorylationLREKSKKYSDVEVPA
HHHHCCCCCCCCCCE
17.5323927012
408PhosphorylationREKSKKYSDVEVPAS
HHHCCCCCCCCCCEE
44.0225159151
415PhosphorylationSDVEVPASVTGYSFA
CCCCCCEEECCEEEC
17.7223927012
417PhosphorylationVEVPASVTGYSFASD
CCCCEEECCEEECCC
28.1022167270
419PhosphorylationVPASVTGYSFASDGD
CCEEECCEEECCCCC
7.4023927012
420PhosphorylationPASVTGYSFASDGDS
CEEECCEEECCCCCC
18.7122167270
423PhosphorylationVTGYSFASDGDSGTC
ECCEEECCCCCCCCC
39.8730266825
427PhosphorylationSFASDGDSGTCSPLR
EECCCCCCCCCCCCH
41.3423401153
429PhosphorylationASDGDSGTCSPLRHS
CCCCCCCCCCCCHHH
17.4822167270
431PhosphorylationDGDSGTCSPLRHSFQ
CCCCCCCCCCHHHHH
27.1422167270
436PhosphorylationTCSPLRHSFQKQQRE
CCCCCHHHHHHHHHH
23.9622167270
439UbiquitinationPLRHSFQKQQREKTR
CCHHHHHHHHHHHHH
46.5229967540
445PhosphorylationQKQQREKTRWLNSGR
HHHHHHHHHHHHCCC
23.4810209029
450PhosphorylationEKTRWLNSGRGDEAS
HHHHHHHCCCCHHHC
27.9123403867
457PhosphorylationSGRGDEASEEGQNGS
CCCCHHHCCCCCCCC
33.8523927012
464PhosphorylationSEEGQNGSSPKSKTK
CCCCCCCCCCCCCCC
51.5229255136
464 (in isoform 3)Phosphorylation-51.5219664995
464 (in isoform 5)Phosphorylation-51.5219664995
464 (in isoform 6)Phosphorylation-51.5219664995
465PhosphorylationEEGQNGSSPKSKTKW
CCCCCCCCCCCCCCC
37.4329255136
465 (in isoform 3)Phosphorylation-37.4319664995
465 (in isoform 5)Phosphorylation-37.4319664995
465 (in isoform 6)Phosphorylation-37.4319664995
468PhosphorylationQNGSSPKSKTKWTKE
CCCCCCCCCCCCCCC
49.2826074081
470PhosphorylationGSSPKSKTKWTKEDG
CCCCCCCCCCCCCCC
38.6226074081
473PhosphorylationPKSKTKWTKEDGHRT
CCCCCCCCCCCCCCC
26.5526074081
480PhosphorylationTKEDGHRTSTSAVPN
CCCCCCCCCCCCCCC
30.5923401153
481PhosphorylationKEDGHRTSTSAVPNL
CCCCCCCCCCCCCCE
21.9625159151
482PhosphorylationEDGHRTSTSAVPNLF
CCCCCCCCCCCCCEE
21.7925159151
483PhosphorylationDGHRTSTSAVPNLFV
CCCCCCCCCCCCEEE
27.3425159151
489 (in isoform 3)Phosphorylation-7.2727251275
489 (in isoform 6)Phosphorylation-7.2727251275
490 (in isoform 3)Phosphorylation-6.2527251275
490 (in isoform 6)Phosphorylation-6.2527251275
494PhosphorylationNLFVPLNTNPKEVQE
CEEECCCCCHHHHHH
61.6620068231
497UbiquitinationVPLNTNPKEVQEMRN
ECCCCCHHHHHHHHH
73.0024816145
511 (in isoform 3)Phosphorylation-4.9010209029
511 (in isoform 6)Phosphorylation-4.9010209029
514PhosphorylationREQNLQDIKTAGPQS
HHHHHHHHHHHCCHH
2.4932142685
515UbiquitinationEQNLQDIKTAGPQSQ
HHHHHHHHHHCCHHH
40.3824816145
516PhosphorylationQNLQDIKTAGPQSQV
HHHHHHHHHCCHHHE
36.8627251275
521PhosphorylationIKTAGPQSQVLCGVV
HHHHCCHHHEEEEEE
25.9527251275
528UbiquitinationSQVLCGVVMDRSLVQ
HHEEEEEEECCHHHC
1.6824816145
529SulfoxidationQVLCGVVMDRSLVQG
HEEEEEEECCHHHCC
3.0921406390
531MethylationLCGVVMDRSLVQGEL
EEEEEECCHHHCCCE
17.50-
532PhosphorylationCGVVMDRSLVQGELV
EEEEECCHHHCCCEE
28.7329255136
540O-linked_GlycosylationLVQGELVTASKAIIE
HHCCCEEECCHHHHH
37.5323301498
540PhosphorylationLVQGELVTASKAIIE
HHCCCEEECCHHHHH
37.5323025827
542O-linked_GlycosylationQGELVTASKAIIEKE
CCCEEECCHHHHHHH
17.1623301498
542PhosphorylationQGELVTASKAIIEKE
CCCEEECCHHHHHHH
17.1623025827
543AcetylationGELVTASKAIIEKEY
CCEEECCHHHHHHHH
40.9325953088
543UbiquitinationGELVTASKAIIEKEY
CCEEECCHHHHHHHH
40.9332015554
546UbiquitinationVTASKAIIEKEYQPH
EECCHHHHHHHHCCC
8.0624816145
550PhosphorylationKAIIEKEYQPHVIVS
HHHHHHHHCCCEEEE
38.1125884760
557O-linked_GlycosylationYQPHVIVSTTGPNPF
HCCCEEEECCCCCCC
14.7723301498
557 (in isoform 4)Phosphorylation-14.7724076635
558O-linked_GlycosylationQPHVIVSTTGPNPFT
CCCEEEECCCCCCCC
25.5223301498
559O-linked_GlycosylationPHVIVSTTGPNPFTT
CCEEEECCCCCCCCC
43.0423301498
559PhosphorylationPHVIVSTTGPNPFTT
CCEEEECCCCCCCCC
43.0446159737
565O-linked_GlycosylationTTGPNPFTTLTDREL
CCCCCCCCCCCHHHH
23.3523301498
568O-linked_GlycosylationPNPFTTLTDRELEEY
CCCCCCCCHHHHHHH
30.8023301498
574UbiquitinationLTDRELEEYRREVER
CCHHHHHHHHHHHHH
57.8932015554
575PhosphorylationTDRELEEYRREVERK
CHHHHHHHHHHHHHH
12.9524927040
584UbiquitinationREVERKQKGSEENLD
HHHHHHHCCCHHHHH
68.3924816145
586PhosphorylationVERKQKGSEENLDEA
HHHHHCCCHHHHHHH
49.0929255136
600PhosphorylationAREQKEKSPPDQPAV
HHHHHHHCCCCCCCC
42.6425159151
600 (in isoform 2)Phosphorylation-42.6430177828
613PhosphorylationAVPHPPPSTPIKLEE
CCCCCCCCCCCCCCC
53.2230266825
613 (in isoform 2)Phosphorylation-53.2222210691
614PhosphorylationVPHPPPSTPIKLEED
CCCCCCCCCCCCCCC
34.5030266825
614 (in isoform 2)Phosphorylation-34.5026657352
615UbiquitinationPHPPPSTPIKLEEDL
CCCCCCCCCCCCCCC
26.5024816145
627PhosphorylationEDLVPEPTTGDDSDA
CCCCCCCCCCCCCCC
41.5727080861
628PhosphorylationDLVPEPTTGDDSDAA
CCCCCCCCCCCCCCC
49.7027080861
628 (in isoform 2)Phosphorylation-49.70-
631PhosphorylationPEPTTGDDSDAATFK
CCCCCCCCCCCCCCC
50.1632142685
631 (in isoform 4)Phosphorylation-50.1630177828
631 (in isoform 6)Phosphorylation-50.1630177828
632PhosphorylationEPTTGDDSDAATFKP
CCCCCCCCCCCCCCC
33.6121406692
636PhosphorylationGDDSDAATFKPTLPD
CCCCCCCCCCCCCCC
33.6327080861
640PhosphorylationDAATFKPTLPDLSPD
CCCCCCCCCCCCCCC
52.0621406692
644 (in isoform 4)Phosphorylation-8.2722210691
644 (in isoform 6)Phosphorylation-8.2722210691
645PhosphorylationKPTLPDLSPDEPSEA
CCCCCCCCCCCHHHH
37.3728192239
645 (in isoform 4)Phosphorylation-37.3726657352
645 (in isoform 6)Phosphorylation-37.3726657352
646UbiquitinationPTLPDLSPDEPSEAL
CCCCCCCCCCHHHHC
58.2324816145
650PhosphorylationDLSPDEPSEALGFPM
CCCCCCHHHHCCCCC
33.1926074081
659 (in isoform 4)Phosphorylation-52.77-
659 (in isoform 6)Phosphorylation-52.77-
662PhosphorylationFPMLEKEEEAHRPPS
CCCCCCHHHHCCCCC
72.1132142685
669PhosphorylationEEAHRPPSPTEAPTE
HHHCCCCCCCCCCCC
47.3228355574
671PhosphorylationAHRPPSPTEAPTEAS
HCCCCCCCCCCCCCC
49.4769004617
675PhosphorylationPSPTEAPTEASPEPA
CCCCCCCCCCCCCCC
51.7526074081
678PhosphorylationTEAPTEASPEPAPDP
CCCCCCCCCCCCCCC
24.4630576142
695PhosphorylationVAEEAAPSAVEEGAA
CCHHHCCCHHHHCCC
39.9730576142
707PhosphorylationGAAADPGSDGSPGKS
CCCCCCCCCCCCCCC
44.1628355574
710PhosphorylationADPGSDGSPGKSPSK
CCCCCCCCCCCCCCH
35.1517081983
714PhosphorylationSDGSPGKSPSKKKKK
CCCCCCCCCCHHHCC
40.0820068230
716PhosphorylationGSPGKSPSKKKKKFR
CCCCCCCCHHHCCCC
65.2917081983
724PhosphorylationKKKKKFRTPSFLKKS
HHHCCCCCHHHHHHH
26.8130266825
726PhosphorylationKKKFRTPSFLKKSKK
HCCCCCHHHHHHHHC
42.4719664994
731PhosphorylationTPSFLKKSKKKSDS-
CHHHHHHHHCCCCC-
48.3920835919
734UbiquitinationFLKKSKKKSDS----
HHHHHHCCCCC----
64.3324816145
735PhosphorylationLKKSKKKSDS-----
HHHHHCCCCC-----
52.5550563741
737PhosphorylationKSKKKSDS-------
HHHCCCCC-------
49.5750563749
765Ubiquitination-----------------------------------
-----------------------------------
24816145
796Ubiquitination------------------------------------------------------------------
------------------------------------------------------------------
24816145

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
5SPhosphorylationKinasePRKCZQ05513
GPS
5SPhosphorylationKinasePRKCAP17252
GPS
12SPhosphorylationKinaseCDK1P06493
PSP
59SPhosphorylationKinasePKA_GROUP-PhosphoELM
59SPhosphorylationKinasePKA-FAMILY-GPS
59SPhosphorylationKinasePRKACAP00517
GPS
59SPhosphorylationKinasePKA-Uniprot
355SPhosphorylationKinaseERK2P28482
PSP
355SPhosphorylationKinaseCDK1P06493
PSP
358SPhosphorylationKinaseERK2P28482
PSP
408SPhosphorylationKinasePKA_GROUP-PhosphoELM
408SPhosphorylationKinasePKA-Uniprot
408SPhosphorylationKinasePRKACAP00517
GPS
408SPhosphorylationKinasePKA-FAMILY-GPS
436SPhosphorylationKinasePKA-Uniprot
436SPhosphorylationKinasePRKACAP00517
GPS
436SPhosphorylationKinasePKA_GROUP-PhosphoELM
436SPhosphorylationKinasePKA-FAMILY-GPS
445TPhosphorylationKinaseROCK-SUBFAMILY-GPS
445TPhosphorylationKinaseROCK2O75116
Uniprot
445TPhosphorylationKinaseROCK1Q13464
PSP
445TPhosphorylationKinaseROCK_GROUP-PhosphoELM
480TPhosphorylationKinaseROCK1Q13464
PSP
480TPhosphorylationKinaseROCK_GROUP-PhosphoELM
480TPhosphorylationKinaseROCK2O75116
Uniprot
480TPhosphorylationKinaseROCK-SUBFAMILY-GPS
481SPhosphorylationKinasePRKACAP00517
GPS
481SPhosphorylationKinasePKA_GROUP-PhosphoELM
481SPhosphorylationKinasePKA-FAMILY-GPS
481SPhosphorylationKinasePKA-Uniprot
669SPhosphorylationKinaseERK2P28482
PSP
707SPhosphorylationKinaseERK2P28482
PSP
716SPhosphorylationKinasePKC-Uniprot
716SPhosphorylationKinasePRKCAP17252
GPS
716SPhosphorylationKinasePKCAP05696
PSP
716SPhosphorylationKinasePKCAP04409
PSP
724TPhosphorylationKinaseCDK5Q00535
PSP
726SPhosphorylationKinasePKCAP04409
PSP
726SPhosphorylationKinasePKACAP17612
PSP
726SPhosphorylationKinasePKCAP05696
PSP
726SPhosphorylationKinasePKC-FAMILY-GPS
726SPhosphorylationKinasePKA-Uniprot
726SPhosphorylationKinasePKC-Uniprot
726SPhosphorylationKinasePRKCDQ05655
GPS
726SPhosphorylationKinasePRKCZQ05513
GPS
726SPhosphorylationKinasePRKACAP00517
GPS
726SPhosphorylationKinasePRKCAP17252
GPS
726SPhosphorylationKinaseCHEK1O14757
GPS
726SPhosphorylationKinasePKA-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADDA_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 ADDA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPTB1_HUMANSPTBphysical
8663089
SMCA4_HUMANSMARCA4physical
17074803
SMRC1_HUMANSMARCC1physical
17074803
SMCA2_HUMANSMARCA2physical
17074803
SIN3A_HUMANSIN3Aphysical
17074803
HDAC1_HUMANHDAC1physical
17074803
HM20A_HUMANHMG20Aphysical
25416956
ADDG_HUMANADD3physical
26496610
DYST_HUMANDSTphysical
26496610
PGBM_HUMANHSPG2physical
26496610
SPTN1_HUMANSPTAN1physical
26496610
SPTB2_HUMANSPTBN1physical
26496610
SVIL_HUMANSVILphysical
26496610
TMOD1_HUMANTMOD1physical
26496610
TPM2_HUMANTPM2physical
26496610
TPM3_HUMANTPM3physical
26496610
TPM4_HUMANTPM4physical
26496610
UBIA1_HUMANUBIAD1physical
26496610
NUP54_HUMANNUP54physical
26496610
INF2_HUMANINF2physical
26496610

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 ADDA_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 MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-355; SER-358; SER-464; SER-465 AND SER-726, 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 SER-358 AND SER-465, ANDMASS 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-355; SER-358; SER-464; SER-465 AND SER-726, 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-12; THR-331; SER-334;SER-358; SER-431; SER-436 AND SER-465, 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-12 AND SER-358, 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-353; SER-355; SER-358AND SER-465, AND MASS SPECTROMETRY.
"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-707; SER-710 ANDSER-716, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex.";
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.;
J. Proteome Res. 4:306-315(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-358, ANDMASS SPECTROMETRY.
"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-358 AND SER-465, ANDMASS SPECTROMETRY.
"Adducin regulation. Definition of the calmodulin-binding domain andsites of phosphorylation by protein kinases A and C.";
Matsuoka Y., Hughes C.A., Bennett V.;
J. Biol. Chem. 271:25157-25166(1996).
Cited for: PHOSPHORYLATION AT SER-59; SER-408; SER-436; SER-481; SER-716 ANDSER-726, AND PARTIAL PROTEIN SEQUENCE.
"Phosphorylation of adducin by Rho-kinase plays a crucial role in cellmotility.";
Fukata Y., Oshiro N., Kinoshita N., Kawano Y., Matsuoka Y.,Bennett V., Matsuura Y., Kaibuchi K.;
J. Cell Biol. 145:347-361(1999).
Cited for: PHOSPHORYLATION AT THR-445 AND THR-480, AND MUTAGENESIS OF THR-445 ANDTHR-480.

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