2A5D_HUMAN - dbPTM
2A5D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2A5D_HUMAN
UniProt AC Q14738
Protein Name Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
Gene Name PPP2R5D
Organism Homo sapiens (Human).
Sequence Length 602
Subcellular Localization Cytoplasm. Nucleus. Nuclear in interphase, nuclear during mitosis.
Protein Description The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment..
Protein Sequence MPYKLKKEKEPPKVAKCTAKPSSSGKDGGGENTEEAQPQPQPQPQPQAQSQPPSSNKRPSNSTPPPTQLSKIKYSGGPQIVKKERRQSSSRFNLSKNRELQKLPALKDSPTQEREELFIQKLRQCCVLFDFVSDPLSDLKFKEVKRAGLNEMVEYITHSRDVVTEAIYPEAVTMFSVNLFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLALLDLFDSEDPRERDFLKTILHRIYGKFLGLRAYIRRQINHIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKMFLIRVLLPLHKVKSLSVYHPQLAYCVVQFLEKESSLTEPVIVGLLKFWPKTHSPKEVMFLNELEEILDVIEPSEFSKVMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAARVLPIMFPALYRNSKSHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQYKAEKQKGRFRMKEREEMWQKIEELARLNPQYPMFRAPPPLPPVYSMETETPTAEDIQLLKRTVETEAVQMLKDIKKEKVLLRRKSELPQDVYTIKALEAHKRAEEFLTASQEAL
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
18PhosphorylationPPKVAKCTAKPSSSG
CCCCCCCCCCCCCCC		36.69-
20AcetylationKVAKCTAKPSSSGKD
CCCCCCCCCCCCCCC		27.5526051181
26AcetylationAKPSSSGKDGGGENT
CCCCCCCCCCCCCCC		55.9726051181
54PhosphorylationQAQSQPPSSNKRPSN
CCCCCCCCCCCCCCC		53.91-
55PhosphorylationAQSQPPSSNKRPSNS
CCCCCCCCCCCCCCC		52.7428555341
60PhosphorylationPSSNKRPSNSTPPPT
CCCCCCCCCCCCCCC		47.6617110335
62PhosphorylationSNKRPSNSTPPPTQL
CCCCCCCCCCCCCHH		46.7825159151
63PhosphorylationNKRPSNSTPPPTQLS
CCCCCCCCCCCCHHH		44.0325159151
67PhosphorylationSNSTPPPTQLSKIKY
CCCCCCCCHHHCCEE		48.1729396449
70PhosphorylationTPPPTQLSKIKYSGG
CCCCCHHHCCEECCC		23.6329396449
71UbiquitinationPPPTQLSKIKYSGGP
CCCCHHHCCEECCCC		52.38-
73UbiquitinationPTQLSKIKYSGGPQI
CCHHHCCEECCCCHH		36.78-
73AcetylationPTQLSKIKYSGGPQI
CCHHHCCEECCCCHH		36.7825953088
74PhosphorylationTQLSKIKYSGGPQIV
CHHHCCEECCCCHHH		18.9328555341
75PhosphorylationQLSKIKYSGGPQIVK
HHHCCEECCCCHHHH		32.0725159151
82AcetylationSGGPQIVKKERRQSS
CCCCHHHHHHHHHCC		51.0125953088
82UbiquitinationSGGPQIVKKERRQSS
CCCCHHHHHHHHHCC		51.01-
88PhosphorylationVKKERRQSSSRFNLS
HHHHHHHCCCCCCCC		28.5923401153
89PhosphorylationKKERRQSSSRFNLSK
HHHHHHCCCCCCCCC		19.7322167270
90PhosphorylationKERRQSSSRFNLSKN
HHHHHCCCCCCCCCC		46.2523401153
95PhosphorylationSSSRFNLSKNRELQK
CCCCCCCCCCHHHHC		29.0522167270
96UbiquitinationSSRFNLSKNRELQKL
CCCCCCCCCHHHHCC		64.29-
102UbiquitinationSKNRELQKLPALKDS
CCCHHHHCCCCCCCC		69.89-
107UbiquitinationLQKLPALKDSPTQER
HHCCCCCCCCCCHHH		59.26-
109PhosphorylationKLPALKDSPTQEREE
CCCCCCCCCCHHHHH		28.4125159151
1212-HydroxyisobutyrylationREELFIQKLRQCCVL
HHHHHHHHHHHHHHH		40.60-
121UbiquitinationREELFIQKLRQCCVL
HHHHHHHHHHHHHHH		40.6021906983
121 (in isoform 1)Ubiquitination-40.6021890473
126 (in isoform 3)Ubiquitination-1.9521890473
140UbiquitinationSDPLSDLKFKEVKRA
CCCHHHCCHHHHHHH		60.42-
200 (in isoform 2)Ubiquitination-43.3921890473
232MalonylationDFQPNIAKKYIDQKF
CCCCCHHHHHCCHHH		42.1726320211
232UbiquitinationDFQPNIAKKYIDQKF
CCCCCHHHHHCCHHH		42.17-
232 (in isoform 1)Ubiquitination-42.1721890473
233UbiquitinationFQPNIAKKYIDQKFV
CCCCHHHHHCCHHHH		38.12-
268UbiquitinationILHRIYGKFLGLRAY
HHHHHHHHHHCHHHH		22.05-
332UbiquitinationRVLLPLHKVKSLSVY
HHHHHHHHCCCCCCC		60.07-
334UbiquitinationLLPLHKVKSLSVYHP
HHHHHHCCCCCCCCH		50.94-
335 (in isoform 2)Ubiquitination-28.94-
355 (in isoform 3)Phosphorylation-41.54-
367UbiquitinationPVIVGLLKFWPKTHS
CCHHHHHHHCCCCCC		50.8821890473
371UbiquitinationGLLKFWPKTHSPKEV
HHHHHCCCCCCHHHH		49.84-
402 (in isoform 3)Ubiquitination-20.7821890473
409UbiquitinationPLFRQLAKCVSSPHF
HHHHHHHHHHCCCCH		43.70-
412PhosphorylationRQLAKCVSSPHFQVA
HHHHHHHCCCCHHHH		47.8519366811
424PhosphorylationQVAERALYYWNNEYI
HHHHHHHHHCCCHHH		12.8817053785
425PhosphorylationVAERALYYWNNEYIM
HHHHHHHHCCCHHHH		11.5117053785
429 (in isoform 2)Phosphorylation-32.97-
430PhosphorylationLYYWNNEYIMSLISD
HHHCCCHHHHHHHCC		12.2117053785
442 (in isoform 3)Ubiquitination-6.8121890473
451PhosphorylationPIMFPALYRNSKSHW
HHHHHHHHHCCHHHH		15.17-
461PhosphorylationSKSHWNKTIHGLIYN
CHHHHHHHHHHHHHH		18.2620873877
467 (in isoform 3)Phosphorylation-10.22-
476 (in isoform 2)Ubiquitination-4.2921890473
477 (in isoform 3)Ubiquitination-23.6421890473
479UbiquitinationLFMEMNQKLFDDCTQ
HHHHHHHHHHHHHHH		46.23-
488PhosphorylationFDDCTQQYKAEKQKG
HHHHHHHHHHHHHHC		11.4421447384
489AcetylationDDCTQQYKAEKQKGR
HHHHHHHHHHHHHCC		45.8125953088
489MalonylationDDCTQQYKAEKQKGR
HHHHHHHHHHHHHCC		45.8132601280
489UbiquitinationDDCTQQYKAEKQKGR
HHHHHHHHHHHHHCC		45.81-
492 (in isoform 3)Phosphorylation-63.27-
500UbiquitinationQKGRFRMKEREEMWQ
HHCCCCHHHHHHHHH		49.73-
508 (in isoform 1)Ubiquitination-36.2521890473
508UbiquitinationEREEMWQKIEELARL
HHHHHHHHHHHHHHH		36.2521906983
516 (in isoform 2)Ubiquitination-18.9721890473
519PhosphorylationLARLNPQYPMFRAPP
HHHHCCCCCCCCCCC		9.64-
523MethylationNPQYPMFRAPPPLPP
CCCCCCCCCCCCCCC		39.6724396569
532PhosphorylationPPPLPPVYSMETETP
CCCCCCCCCCCCCCC		14.2021945579
533PhosphorylationPPLPPVYSMETETPT
CCCCCCCCCCCCCCC		15.4621945579
536PhosphorylationPPVYSMETETPTAED
CCCCCCCCCCCCHHH		36.2021945579
538PhosphorylationVYSMETETPTAEDIQ
CCCCCCCCCCHHHHH		33.1021945579
540PhosphorylationSMETETPTAEDIQLL
CCCCCCCCHHHHHHH		50.5321945579
541 (in isoform 2)Phosphorylation-17.42-
548UbiquitinationAEDIQLLKRTVETEA
HHHHHHHHHHHHHHH		55.4021906983
548 (in isoform 1)Ubiquitination-55.4021890473
551 (in isoform 2)Ubiquitination-11.2821890473
553PhosphorylationLLKRTVETEAVQMLK
HHHHHHHHHHHHHHH		25.5519060867
558SulfoxidationVETEAVQMLKDIKKE
HHHHHHHHHHHHHHH		3.9521406390
560UbiquitinationTEAVQMLKDIKKEKV
HHHHHHHHHHHHHHH		52.65-
566 (in isoform 2)Phosphorylation-47.24-
572UbiquitinationEKVLLRRKSELPQDV
HHHHHHCCCCCCCCC		41.68-
573PhosphorylationKVLLRRKSELPQDVY
HHHHHCCCCCCCCCH		42.4222167270
580PhosphorylationSELPQDVYTIKALEA
CCCCCCCHHHHHHHH		15.8423927012
581PhosphorylationELPQDVYTIKALEAH
CCCCCCHHHHHHHHH		18.8223927012
583 (in isoform 1)Ubiquitination-38.8421890473
583AcetylationPQDVYTIKALEAHKR
CCCCHHHHHHHHHHH		38.8426051181
583UbiquitinationPQDVYTIKALEAHKR
CCCCHHHHHHHHHHH		38.8421890473
589UbiquitinationIKALEAHKRAEEFLT
HHHHHHHHHHHHHHH		61.42-
589AcetylationIKALEAHKRAEEFLT
HHHHHHHHHHHHHHH		61.4226051181
596PhosphorylationKRAEEFLTASQEAL-
HHHHHHHHHHHHHC-		29.5923403867
598PhosphorylationAEEFLTASQEAL---
HHHHHHHHHHHC---		24.2617525332
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
60SPhosphorylationKinaseCHEK1O14757
GPS
60SPhosphorylationKinasePRKACAP17612
GPS
60SPhosphorylationKinasePKA-FAMILY-GPS
75SPhosphorylationKinasePRKACAP17612
GPS
75SPhosphorylationKinasePKA-FAMILY-GPS
88SPhosphorylationKinasePKA-FAMILY-GPS
573SPhosphorylationKinasePRKACAP17612
GPS
573SPhosphorylationKinasePKA-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2A5D_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 2A5D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAND2_HUMANHAND2physical
14636580
LIPA1_HUMANPPFIA1physical
16189514
HAND1_HUMANHAND1physical
14636580
PP2AA_HUMANPPP2CAphysical
8703017
2AAB_HUMANPPP2R1Bphysical
8703017
2AAA_HUMANPPP2R1Aphysical
22939629
2AAB_HUMANPPP2R1Bphysical
22939629
ARPC2_HUMANARPC2physical
22863883
NIF3L_HUMANNIF3L1physical
22863883
PRDX1_HUMANPRDX1physical
22863883
PRDX2_HUMANPRDX2physical
22863883
RAGP1_HUMANRANGAP1physical
22863883
RFA2_HUMANRPA2physical
22863883
SHLB1_HUMANSH3GLB1physical
22863883
TPD54_HUMANTPD52L2physical
22863883
USBP1_HUMANUSHBP1physical
25416956
FSD2_HUMANFSD2physical
25416956
RORG_HUMANRORCphysical
23555304
DAAF5_HUMANDNAAF5physical
26344197
SYLC_HUMANLARSphysical
26344197
PFD5_HUMANPFDN5physical
26344197
2AAA_HUMANPPP2R1Aphysical
26344197
2AAB_HUMANPPP2R1Bphysical
26344197
2ABA_HUMANPPP2R2Aphysical
26344197
2ABD_HUMANPPP2R2Dphysical
26344197
PTPRF_HUMANPTPRFphysical
26344197
RIR2_HUMANRRM2physical
26344197
XPO6_HUMANXPO6physical
26344197
PP2AA_HUMANPPP2CAphysical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
2AAB_HUMANPPP2R1Bphysical
26496610
LIPA1_HUMANPPFIA1physical
26496610
CCHCR_HUMANCCHCR1physical
26496610
CCD61_HUMANCCDC61physical
26496610
2AAA_HUMANPPP2R1Aphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616355Mental retardation, autosomal dominant 35 (MRD35)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 2A5D_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-573, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, 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 THR-553, AND MASSSPECTROMETRY.

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