ADDB_HUMAN - dbPTM
ADDB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADDB_HUMAN
UniProt AC P35612
Protein Name Beta-adducin
Gene Name ADD2
Organism Homo sapiens (Human).
Sequence Length 726
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 the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit..
Protein Sequence MSEETVPEAASPPPPQGQPYFDRFSEDDPEYMRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPTSSMNVSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFCLHSAIYAARPDVRCIIHLHTPATAAVSAMKWGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGVVALGDTVEEAFYKIFHLQAACEIQVSALSSAGGVENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES
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------MSEETVPEA
------CCCCCCCCC
44.11-
2Phosphorylation------MSEETVPEA
------CCCCCCCCC
44.1123025827
5Phosphorylation---MSEETVPEAASP
---CCCCCCCCCCCC
36.9922199227
11 (in isoform 3)Phosphorylation-45.01-
11 (in isoform 2)Phosphorylation-45.01-
11PhosphorylationETVPEAASPPPPQGQ
CCCCCCCCCCCCCCC
45.0128348404
14 (in isoform 9)Phosphorylation-36.9122210691
18 (in isoform 9)Phosphorylation-25.0322210691
20PhosphorylationPPPQGQPYFDRFSED
CCCCCCCCHHCCCCC
15.3828450419
25PhosphorylationQPYFDRFSEDDPEYM
CCCHHCCCCCCHHHH
40.8028450419
31PhosphorylationFSEDDPEYMRLRNRA
CCCCCHHHHHHHHHH
7.9124927040
36 (in isoform 9)Phosphorylation-42.4022210691
55PhosphorylationMEQKKRVTMILQSPS
HHHHHHEEEECCCHH
11.5221406692
60PhosphorylationRVTMILQSPSFREEL
HEEEECCCHHHHHHH
21.0429691806
62PhosphorylationTMILQSPSFREELEG
EEECCCHHHHHHHHH
42.0329691806
176PhosphorylationLISPKGVSCSEVTAS
EECCCCCCCCCCCHH
22.1625307156
178PhosphorylationSPKGVSCSEVTASSL
CCCCCCCCCCCHHHC
27.8223403867
184PhosphorylationCSEVTASSLIKVNIL
CCCCCHHHCEEEEEC
31.4824719451
344PhosphorylationHRPHEVGSVQWAGST
CCCCCCCCCEECCCC
19.13-
377PhosphorylationRMLDNLGYRTGYTYR
HHHHHHCCCCCCCCC
14.2543014423
392PhosphorylationHPFVQEKTKHKSEVE
CCCCCCCCCCCCCCC
37.3124719451
396PhosphorylationQEKTKHKSEVEIPAT
CCCCCCCCCCCCCEE
46.7421406692
403PhosphorylationSEVEIPATVTAFVFE
CCCCCCEEEEEEEEC
17.0321406692
405PhosphorylationVEIPATVTAFVFEED
CCCCEEEEEEEECCC
15.2621406692
436PhosphorylationEKTRWLNTPNTYLRV
HHHHHCCCCCCEEEE
18.7523025827
439PhosphorylationRWLNTPNTYLRVNVA
HHCCCCCCEEEEEHH
25.7429978859
440PhosphorylationWLNTPNTYLRVNVAD
HCCCCCCEEEEEHHH
10.1130804005
455PhosphorylationEVQRSMGSPRPKTTW
HHHHHCCCCCCCCCC
14.7527422710
464AcetylationRPKTTWMKADEVEKS
CCCCCCEEHHHCEEC
44.227676393
471PhosphorylationKADEVEKSSSGMPIR
EHHHCEECCCCCCEE
19.0723403867
472PhosphorylationADEVEKSSSGMPIRI
HHHCEECCCCCCEEE
41.8123403867
489PhosphorylationPNQFVPLYTDPQEVL
CCCEEECCCCHHHHH
11.7428796482
490PhosphorylationNQFVPLYTDPQEVLE
CCEEECCCCHHHHHH
49.2228796482
512PhosphorylationQNRQDVKSAGPQSQL
HHHHHHHHHCHHHHH
38.0031437679
522PhosphorylationPQSQLLASVIAEKSR
HHHHHHHHHHHHHCC
17.6423025827
528PhosphorylationASVIAEKSRSPSTES
HHHHHHHCCCCCHHH
29.5120363803
528 (in isoform 2)Phosphorylation-29.5124260401
530 (in isoform 2)Phosphorylation-30.2324719451
530PhosphorylationVIAEKSRSPSTESQL
HHHHHCCCCCHHHHH
30.2328787133
532 (in isoform 3)Phosphorylation-46.16-
532PhosphorylationAEKSRSPSTESQLMS
HHHCCCCCHHHHHHH
46.1619664994
533PhosphorylationEKSRSPSTESQLMSK
HHCCCCCHHHHHHHC
42.944076659
535PhosphorylationSRSPSTESQLMSKGD
CCCCCHHHHHHHCCC
28.8021082442
539PhosphorylationSTESQLMSKGDEDTK
CHHHHHHHCCCCCCC
41.9220363803
543 (in isoform 8)Phosphorylation-76.0124260401
544 (in isoform 9)Phosphorylation-64.8924260401
545PhosphorylationMSKGDEDTKDDSEET
HHCCCCCCCCCCCCC
34.0323286773
545 (in isoform 8)Phosphorylation-34.0324719451
546 (in isoform 9)Phosphorylation-72.3824719451
549PhosphorylationDEDTKDDSEETVPNP
CCCCCCCCCCCCCCH
47.6823286773
552PhosphorylationTKDDSEETVPNPFSQ
CCCCCCCCCCCHHHH
36.8924076635
561PhosphorylationPNPFSQLTDQELEEY
CCHHHHCCHHHHHHH
28.1815345747
561 (in isoform 3)Phosphorylation-28.18-
568PhosphorylationTDQELEEYKKEVERK
CHHHHHHHHHHHHHH
20.2726471730
576AcetylationKKEVERKKLELDGEK
HHHHHHHHCCCCCCC
54.1120167786
583AcetylationKLELDGEKETAPEEP
HCCCCCCCCCCCCCC
66.9320167786
585PhosphorylationELDGEKETAPEEPGS
CCCCCCCCCCCCCCC
59.5923927012
592PhosphorylationTAPEEPGSPAKSAPA
CCCCCCCCCCCCCCC
32.1923927012
595AcetylationEEPGSPAKSAPASPV
CCCCCCCCCCCCCCC
51.007367709
596PhosphorylationEPGSPAKSAPASPVQ
CCCCCCCCCCCCCCC
41.4122617229
600PhosphorylationPAKSAPASPVQSPAK
CCCCCCCCCCCCCCC
25.2522617229
604PhosphorylationAPASPVQSPAKEAET
CCCCCCCCCCCCCCC
27.3619413330
611PhosphorylationSPAKEAETKSPLVSP
CCCCCCCCCCCCCCC
43.8223898821
613PhosphorylationAKEAETKSPLVSPSK
CCCCCCCCCCCCCCC
30.7722617229
617PhosphorylationETKSPLVSPSKSLEE
CCCCCCCCCCCCCCC
31.0122617229
619PhosphorylationKSPLVSPSKSLEEGT
CCCCCCCCCCCCCCC
27.6322617229
621PhosphorylationPLVSPSKSLEEGTKK
CCCCCCCCCCCCCCC
45.4028787133
626PhosphorylationSKSLEEGTKKTETSK
CCCCCCCCCCCCCCC
32.4228450419
631PhosphorylationEGTKKTETSKAATTE
CCCCCCCCCCCCCCC
40.5362150401
632PhosphorylationGTKKTETSKAATTEP
CCCCCCCCCCCCCCC
17.6762150407
657O-linked_GlycosylationNGREEEQTAEEILSK
CCCCCHHHHHHHHHH
39.0430379171
663O-linked_GlycosylationQTAEEILSKGLSQMT
HHHHHHHHHHHHHHC
30.2730379171
667PhosphorylationEILSKGLSQMTTSAD
HHHHHHHHHHCCCCC
26.9522210691
671PhosphorylationKGLSQMTTSADTDVD
HHHHHHCCCCCCCCC
19.3022210691
672PhosphorylationGLSQMTTSADTDVDT
HHHHHCCCCCCCCCC
18.2527732954
675PhosphorylationQMTTSADTDVDTSKD
HHCCCCCCCCCCCCC
37.3230576142
679PhosphorylationSADTDVDTSKDKTES
CCCCCCCCCCCCCCC
37.2122210691
681AcetylationDTDVDTSKDKTESVT
CCCCCCCCCCCCCCC
66.397676407
683AcetylationDVDTSKDKTESVTSG
CCCCCCCCCCCCCCC
58.917676415
684PhosphorylationVDTSKDKTESVTSGP
CCCCCCCCCCCCCCC
43.5628450419
686PhosphorylationTSKDKTESVTSGPMS
CCCCCCCCCCCCCCC
35.6128450419
688PhosphorylationKDKTESVTSGPMSPE
CCCCCCCCCCCCCCC
36.9323927012
689PhosphorylationDKTESVTSGPMSPEG
CCCCCCCCCCCCCCC
38.4523927012
693PhosphorylationSVTSGPMSPEGSPSK
CCCCCCCCCCCCCCC
23.9623927012
697PhosphorylationGPMSPEGSPSKSPSK
CCCCCCCCCCCCCCC
25.0823927012
699PhosphorylationMSPEGSPSKSPSKKK
CCCCCCCCCCCCCCC
47.6823927012
701PhosphorylationPEGSPSKSPSKKKKK
CCCCCCCCCCCCCCC
38.4519664994
703PhosphorylationGSPSKSPSKKKKKFR
CCCCCCCCCCCCCCC
65.2923927012
711PhosphorylationKKKKKFRTPSFLKKS
CCCCCCCCHHHHHHH
26.8130266825
713PhosphorylationKKKFRTPSFLKKSKK
CCCCCCHHHHHHHHH
42.4719664994
718PhosphorylationTPSFLKKSKKKEKVE
CHHHHHHHHHHHHCC
48.3920835925
726PhosphorylationKKKEKVES-------
HHHHHCCC-------
48.819679146

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
55TPhosphorylationKinasePKA_GROUP-PhosphoELM
55TPhosphorylationKinasePKA-Uniprot
55TPhosphorylationKinasePKA-FAMILY-GPS
55TPhosphorylationKinasePRKACAP00517
GPS
489YPhosphorylationKinaseFYNP06241
PSP
592SPhosphorylationKinaseERK2P28482
PSP
596SPhosphorylationKinaseERK2P28482
PSP
600SPhosphorylationKinaseERK2P28482
PSP
604SPhosphorylationKinaseCDK5Q00535
PSP
613SPhosphorylationKinaseGSK3BP49841
PSP
617SPhosphorylationKinaseCDK5Q00535
PSP
693SPhosphorylationKinaseGSK3BP49841
PSP
701SPhosphorylationKinaseCDK5Q00535
PSP
703SPhosphorylationKinaseKPCAP17252
PhosphoELM
703SPhosphorylationKinasePRKCAP05696
GPS
703SPhosphorylationKinasePKC-Uniprot
713SPhosphorylationKinasePKCAP05696
PSP
713SPhosphorylationKinasePKC_GROUP-PhosphoELM
713SPhosphorylationKinasePKC-Uniprot
713SPhosphorylationKinasePKA-Uniprot
713SPhosphorylationKinaseCHEK1O14757
GPS
713SPhosphorylationKinasePKC-FAMILY-GPS
713SPhosphorylationKinasePRKCAP17252
GPS
713SPhosphorylationKinasePKA-FAMILY-GPS
713SPhosphorylationKinasePRKACAP00517
GPS
713SPhosphorylationKinasePKCAP04409
PSP
713SPhosphorylationKinasePRKCZQ05513
GPS
726SPhosphorylationKinasePKC-FAMILY-GPS
726SPhosphorylationKinasePKCAP04409
PSP
726SPhosphorylationKinasePKC_GROUP-PhosphoELM
726SPhosphorylationKinasePRKCAP17252
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADDB_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 ADDB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NUD12_HUMANNUDT12physical
28514442
ADDA_HUMANADD1physical
28514442
ADDG_HUMANADD3physical
28514442
ROCK1_HUMANROCK1physical
28514442
ROCK2_HUMANROCK2physical
28514442
A16A1_HUMANALDH16A1physical
28514442

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 ADDB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592; SER-596; SER-600;SER-604; SER-693; SER-697 AND SER-699, AND MASS 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 THR-55; SER-703 AND SER-713, AND PARTIAL PROTEINSEQUENCE.

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