ADDG_HUMAN - dbPTM
ADDG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADDG_HUMAN
UniProt AC Q9UEY8
Protein Name Gamma-adducin
Gene Name ADD3
Organism Homo sapiens (Human).
Sequence Length 706
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. Plays a role in actin filament capping. [PubMed: 23836506 Binds to calmodulin.]
Protein Sequence MSSDASQGVITTPPPPSMPHKERYFDRINENDPEYIRERNMSPDLRQDFNMMEQRKRVTQILQSPAFREDLECLIQEQMKKGHNPTGLLALQQIADYIMANSFSGFSSPPLSLGMVTPINDLPGADTSSYVKGEKLTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLLGDVAYYDYQGSLEEQEERIQLQKVLGPSCKVLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAGAGGVDNLHVLDFQKYKAFTYTVAASGGGGVNMGSHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLIREKPRHKSDVEIPATVTAFSFEDDTVPLSPLKYMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDSSKVSGGTPIKIEDPNQFVPLNTNPNEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMQFEDDDHGPPAPPNPFSHLTEGELEEYKRTIERKQQGLEDAEQELLSDDASSVSQIQSQTQSPQNVPEKLEENHELFSKSFISMEVPVMVVNGKDDMHDVEDELAKRVSRLSTSTTIENIEITIKSPEKIEEVLSPEGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA
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------MSSDASQGV
------CCCCCCCCC
36.6020068231
2Phosphorylation------MSSDASQGV
------CCCCCCCCC
36.6028464451
2 (in isoform 2)Acetylation-36.60-
3Phosphorylation-----MSSDASQGVI
-----CCCCCCCCCC
35.5826552605
6Phosphorylation--MSSDASQGVITTP
--CCCCCCCCCCCCC
32.2423401153
11PhosphorylationDASQGVITTPPPPSM
CCCCCCCCCCCCCCC
30.7323401153
11 (in isoform 2)Phosphorylation-30.73-
12PhosphorylationASQGVITTPPPPSMP
CCCCCCCCCCCCCCC
23.7523401153
12 (in isoform 2)Phosphorylation-23.75-
17PhosphorylationITTPPPPSMPHKERY
CCCCCCCCCCCHHHH
51.2023401153
21UbiquitinationPPPSMPHKERYFDRI
CCCCCCCHHHHHHHC
37.71-
24PhosphorylationSMPHKERYFDRINEN
CCCCHHHHHHHCCCC
15.7826074081
27MethylationHKERYFDRINENDPE
CHHHHHHHCCCCCHH
24.59-
35PhosphorylationINENDPEYIRERNMS
CCCCCHHHHHHCCCC
15.6355009
42PhosphorylationYIRERNMSPDLRQDF
HHHHCCCCHHHHHHH
20.8619664994
42 (in isoform 2)Phosphorylation-20.86-
59PhosphorylationMEQRKRVTQILQSPA
HHHHHHHHHHHHCHH
17.5846159761
64PhosphorylationRVTQILQSPAFREDL
HHHHHHHCHHHHHHH
18.1019664994
64 (in isoform 2)Phosphorylation-18.10-
86PhosphorylationMKKGHNPTGLLALQQ
HHCCCCHHHHHHHHH
45.8622210691
97PhosphorylationALQQIADYIMANSFS
HHHHHHHHHHHCCCC
5.4222210691
102PhosphorylationADYIMANSFSGFSSP
HHHHHHCCCCCCCCC
15.9722210691
104PhosphorylationYIMANSFSGFSSPPL
HHHHCCCCCCCCCCC
38.4622210691
107PhosphorylationANSFSGFSSPPLSLG
HCCCCCCCCCCCEEC
45.5222210691
108PhosphorylationNSFSGFSSPPLSLGM
CCCCCCCCCCCEECC
28.4222210691
112PhosphorylationGFSSPPLSLGMVTPI
CCCCCCCEECCCCCC
28.7522210691
117PhosphorylationPLSLGMVTPINDLPG
CCEECCCCCCCCCCC
15.0122210691
140AcetylationGEKLTRCKLASLYRL
CCCCHHHHHHHHHHH
43.7425953088
159O-linked_GlycosylationGWAHLANTYISVRIS
HHHHHHCCEEEEEEC
19.3430379171
162O-linked_GlycosylationHLANTYISVRISKEQ
HHHCCEEEEEECCCC
8.5730379171
166PhosphorylationTYISVRISKEQDHII
CEEEEEECCCCCEEE
21.4122210691
180PhosphorylationIIIPRGLSFSEATAS
EEEECCCCCCHHHHH
29.5620068231
180 (in isoform 2)Phosphorylation-29.56-
182PhosphorylationIPRGLSFSEATASNL
EECCCCCCHHHHHCC
23.9728348404
185PhosphorylationGLSFSEATASNLVKV
CCCCCHHHHHCCEEE
26.9420068231
187PhosphorylationSFSEATASNLVKVNI
CCCHHHHHCCEEEEE
26.7520068231
187 (in isoform 2)Phosphorylation-26.75-
203PhosphorylationGEVVDQGSTNLKIDH
EEEECCCCCCEEECC
14.4322210691
204PhosphorylationEVVDQGSTNLKIDHT
EEECCCCCCEEECCC
51.9322210691
280UbiquitinationEERIQLQKVLGPSCK
HHHHHHHHHHCCCCE
48.28-
340MethylationLHVLDFQKYKAFTYT
EEEECHHHEEEEEEE
49.03-
351PhosphorylationFTYTVAASGGGGVNM
EEEEEEECCCCCCCC
28.3827080861
358SulfoxidationSGGGGVNMGSHQKWK
CCCCCCCCCCCCCEE
5.6030846556
360PhosphorylationGGGVNMGSHQKWKVG
CCCCCCCCCCCEEEC
16.3946159743
375SulfoxidationEIEFEGLMRTLDNLG
EEEHHHHHHHHHHHC
4.5330846556
383PhosphorylationRTLDNLGYRTGYAYR
HHHHHHCCCCCCCCC
14.2520068231
383 (in isoform 2)Phosphorylation-14.25-
389PhosphorylationGYRTGYAYRHPLIRE
CCCCCCCCCCCCCCC
10.8522817900
390MethylationYRTGYAYRHPLIREK
CCCCCCCCCCCCCCC
19.44-
402PhosphorylationREKPRHKSDVEIPAT
CCCCCCCCCCCCCCE
40.5430266825
402 (in isoform 2)Phosphorylation-40.54-
409PhosphorylationSDVEIPATVTAFSFE
CCCCCCCEEEEEECC
17.0330266825
411PhosphorylationVEIPATVTAFSFEDD
CCCCCEEEEEECCCC
20.0322115753
414PhosphorylationPATVTAFSFEDDTVP
CCEEEEEECCCCCCC
25.8421712546
419PhosphorylationAFSFEDDTVPLSPLK
EEECCCCCCCCCHHH
36.0221712546
423PhosphorylationEDDTVPLSPLKYMAQ
CCCCCCCCHHHHHHH
23.3225159151
423 (in isoform 2)Phosphorylation-23.32-
426UbiquitinationTVPLSPLKYMAQRQQ
CCCCCHHHHHHHHHH
36.04-
427PhosphorylationVPLSPLKYMAQRQQR
CCCCHHHHHHHHHHH
12.8326074081
436AcetylationAQRQQREKTRWLNSP
HHHHHHHHHHHCCCC
45.657427887
442PhosphorylationEKTRWLNSPNTYMKV
HHHHHCCCCCCEEEE
19.8425159151
442 (in isoform 2)Phosphorylation-19.84-
445PhosphorylationRWLNSPNTYMKVNVP
HHCCCCCCEEEEECC
28.5122115753
446PhosphorylationWLNSPNTYMKVNVPE
HCCCCCCEEEEECCH
11.1122617229
448UbiquitinationNSPNTYMKVNVPEES
CCCCCEEEEECCHHH
21.9021890473
448UbiquitinationNSPNTYMKVNVPEES
CCCCCEEEEECCHHH
21.9021890473
448 (in isoform 1)Ubiquitination-21.9021890473
448 (in isoform 2)Ubiquitination-21.9021890473
455PhosphorylationKVNVPEESRNGETSP
EEECCHHHCCCCCCC
29.4125159151
460PhosphorylationEESRNGETSPRTKIT
HHHCCCCCCCCCEEE
45.4925159151
461PhosphorylationESRNGETSPRTKITW
HHCCCCCCCCCEEEE
14.2128355574
461 (in isoform 2)Phosphorylation-14.21-
464O-linked_GlycosylationNGETSPRTKITWMKA
CCCCCCCCEEEEEEE
30.1330379171
464PhosphorylationNGETSPRTKITWMKA
CCCCCCCCEEEEEEE
30.1330576142
467PhosphorylationTSPRTKITWMKAEDS
CCCCCEEEEEEECCC
22.5146159755
474PhosphorylationTWMKAEDSSKVSGGT
EEEEECCCCCCCCCC
24.4628857561
478PhosphorylationAEDSSKVSGGTPIKI
ECCCCCCCCCCCCCC
34.9323401153
478 (in isoform 2)Phosphorylation-34.93-
481PhosphorylationSSKVSGGTPIKIEDP
CCCCCCCCCCCCCCC
25.9325159151
484SumoylationVSGGTPIKIEDPNQF
CCCCCCCCCCCCCCC
41.0428112733
504UbiquitinationNPNEVLEKRNKIREQ
CHHHHHHHHHHHHHH
58.05-
514PhosphorylationKIREQNRYDLKTAGP
HHHHHHCCCCCCCCC
32.9328796482
565PhosphorylationTEGELEEYKRTIERK
CHHHHHHHHHHHHHH
9.0846159773
585PhosphorylationDAEQELLSDDASSVS
HHHHHHHCCCHHHHH
46.1728464451
589PhosphorylationELLSDDASSVSQIQS
HHHCCCHHHHHHHHH
37.9626657352
590PhosphorylationLLSDDASSVSQIQSQ
HHCCCHHHHHHHHHH
27.7530576142
592PhosphorylationSDDASSVSQIQSQTQ
CCCHHHHHHHHHHCC
24.4226074081
596PhosphorylationSSVSQIQSQTQSPQN
HHHHHHHHHCCCCCC
36.5029496963
598PhosphorylationVSQIQSQTQSPQNVP
HHHHHHHCCCCCCCC
35.9428464451
600PhosphorylationQIQSQTQSPQNVPEK
HHHHHCCCCCCCCHH
31.6626657352
616PhosphorylationEENHELFSKSFISME
HHHHHHHHHHCEECC
39.7624719451
618PhosphorylationNHELFSKSFISMEVP
HHHHHHHHCEECCCC
26.9822199227
618 (in isoform 2)Phosphorylation-26.98-
621PhosphorylationLFSKSFISMEVPVMV
HHHHHCEECCCCEEE
13.5929802988
641 (in isoform 2)Phosphorylation-36.80-
645 (in isoform 2)Phosphorylation-26.49-
647PhosphorylationDELAKRVSRLSTSTT
HHHHHHHHHHCCCCE
31.3822617229
647 (in isoform 2)Phosphorylation-31.38-
649 (in isoform 2)Phosphorylation-5.22-
650PhosphorylationAKRVSRLSTSTTIEN
HHHHHHHCCCCEEEE
21.1425159151
651PhosphorylationKRVSRLSTSTTIENI
HHHHHHCCCCEEEEE
34.3825159151
651 (in isoform 2)Phosphorylation-34.38-
652PhosphorylationRVSRLSTSTTIENIE
HHHHHCCCCEEEEEE
21.8524706070
653PhosphorylationVSRLSTSTTIENIEI
HHHHCCCCEEEEEEE
31.7028122231
654PhosphorylationSRLSTSTTIENIEIT
HHHCCCCEEEEEEEE
26.5128348404
659 (in isoform 2)Phosphorylation-45.74-
661PhosphorylationTIENIEITIKSPEKI
EEEEEEEEECCHHHH
15.0122199227
661 (in isoform 2)Phosphorylation-15.01-
664PhosphorylationNIEITIKSPEKIEEV
EEEEEECCHHHHHHH
34.1523927012
673PhosphorylationEKIEEVLSPEGSPSK
HHHHHHHCCCCCCCC
26.5319664994
677PhosphorylationEVLSPEGSPSKSPSK
HHHCCCCCCCCCCCH
25.0819664994
679PhosphorylationLSPEGSPSKSPSKKK
HCCCCCCCCCCCHHC
47.6829255136
681PhosphorylationPEGSPSKSPSKKKKK
CCCCCCCCCCHHCCC
38.4519664994
683PhosphorylationGSPSKSPSKKKKKFR
CCCCCCCCHHCCCCC
65.2929255136
691PhosphorylationKKKKKFRTPSFLKKN
HHCCCCCCHHHHHHC
26.8130266825
693PhosphorylationKKKFRTPSFLKKNKK
CCCCCCHHHHHHCCH
42.4719664994

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
423SPhosphorylationKinaseCDK2P24941
PSP
693SPhosphorylationKinaseCHEK1O14757
GPS
693SPhosphorylationKinasePKC-FAMILY-GPS
693SPhosphorylationKinasePKC_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADDG_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 ADDG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ADDG_HUMAN !!

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 ADDG_HUMAN

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Related Literatures of Post-Translational Modification
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-402; SER-423; SER-673;SER-677 AND SER-681, AND MASS 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-42; SER-423; SER-442;SER-673; SER-677; SER-681 AND SER-693, 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-42 AND SER-681, AND MASSSPECTROMETRY.
"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-681, 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-673; SER-677 ANDSER-693, AND MASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-12, AND MASSSPECTROMETRY.

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