PJA2_HUMAN - dbPTM
PJA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PJA2_HUMAN
UniProt AC O43164
Protein Name E3 ubiquitin-protein ligase Praja-2
Gene Name PJA2
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Cytoplasm . Cell membrane . Endoplasmic reticulum membrane
Peripheral membrane protein . Golgi apparatus membrane
Peripheral membrane protein . Cell junction, synapse. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Loca
Protein Description Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes..
Protein Sequence MSQYTEKEPAAMDQESGKAVWPKPAGGYQTITGRRYGRRHAYVSFKPCMTRHERSLGRAGDDYEVLELDDVPKENSSGSSPLDQVDSSLPSEPIFEKSETEIPTCGSALNQTTESSQSFVAVHHSEEGRDTLGSSTNLHNHSEGEYIPGACSASSVQNGIALVHTDSYDPDGKHGEDNDHLQLSAEVVEGSRYQESLGNTVFELENREAEAYTGLSPPVPSFNCEVRDEFEELDSVPLVKSSAGDTEFVHQNSQEIQRSSQDEMVSTKQQNNTSQERQTEHSPEDAACGPGHICSEQNTNDREKNHGSSPEQVVRPKVRKLISSSQVDQETGFNRHEAKQRSVQRWREALEVEESGSDDLLIKCEEYDGEHDCMFLDPPYSRVITQRETENNQMTSESGATAGRQEVDNTFWNGCGDYYQLYDKDEDSSECSDGEWSASLPHRFSGTEKDQSSSDESWETLPGKDENEPELQSDSSGPEEENQELSLQEGEQTSLEEGEIPWLQYNEVNESSSDEGNEPANEFAQPAFMLDGNNNLEDDSSVSEDLDVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDGLPETLVLEDHTAIGQEQCCPICCSEYIKDDIATELPCHHFFHKPCVSIWLQKSGTCPVCRRHFPPAVIEASAAPSSEPDPDAPPSNDSIAEAP
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------MSQYTEKEP
------CCCCCCCCC
31.71-
2Phosphorylation------MSQYTEKEP
------CCCCCCCCC
31.7123186163
4Phosphorylation----MSQYTEKEPAA
----CCCCCCCCCCC
15.0120068231
5Phosphorylation---MSQYTEKEPAAM
---CCCCCCCCCCCC
32.7023186163
16PhosphorylationPAAMDQESGKAVWPK
CCCCCCCCCCEECCC
39.7028985074
18UbiquitinationAMDQESGKAVWPKPA
CCCCCCCCEECCCCC
49.3929967540
28PhosphorylationWPKPAGGYQTITGRR
CCCCCCCEEEECCCE
11.1028796482
30PhosphorylationKPAGGYQTITGRRYG
CCCCCEEEECCCEEC
16.42-
42PhosphorylationRYGRRHAYVSFKPCM
EECCCEEEEEECCCC
7.1828796482
44PhosphorylationGRRHAYVSFKPCMTR
CCCEEEEEECCCCCH
18.1830576142
46AcetylationRHAYVSFKPCMTRHE
CEEEEEECCCCCHHH
29.7823749302
46MethylationRHAYVSFKPCMTRHE
CEEEEEECCCCCHHH
29.7866725095
50PhosphorylationVSFKPCMTRHERSLG
EEECCCCCHHHHHHC
35.2726434776
63PhosphorylationLGRAGDDYEVLELDD
HCCCCCCEEEEEHHC
16.8128796482
76PhosphorylationDDVPKENSSGSSPLD
HCCCCCCCCCCCCHH
36.8522199227
77PhosphorylationDVPKENSSGSSPLDQ
CCCCCCCCCCCCHHH
55.0322199227
79PhosphorylationPKENSSGSSPLDQVD
CCCCCCCCCCHHHCC
30.6322199227
80PhosphorylationKENSSGSSPLDQVDS
CCCCCCCCCHHHCCC
32.7626657352
87PhosphorylationSPLDQVDSSLPSEPI
CCHHHCCCCCCCCCC
34.6122199227
88PhosphorylationPLDQVDSSLPSEPIF
CHHHCCCCCCCCCCC
39.5722199227
91PhosphorylationQVDSSLPSEPIFEKS
HCCCCCCCCCCCCCC
62.3926074081
134PhosphorylationEGRDTLGSSTNLHNH
CCCCCCCCCCCCCCC
36.7824275569
152PhosphorylationEYIPGACSASSVQNG
CCCCCCCCCCHHCCC
30.5628348404
154PhosphorylationIPGACSASSVQNGIA
CCCCCCCCHHCCCEE
18.1028348404
155PhosphorylationPGACSASSVQNGIAL
CCCCCCCHHCCCEEE
27.6928348404
165PhosphorylationNGIALVHTDSYDPDG
CCEEEEECCCCCCCC
21.1128348404
167PhosphorylationIALVHTDSYDPDGKH
EEEEECCCCCCCCCC
32.3728348404
168PhosphorylationALVHTDSYDPDGKHG
EEEECCCCCCCCCCC
34.0128348404
193PhosphorylationEVVEGSRYQESLGNT
EHHHCCHHHHHHCCE
20.5220873877
196PhosphorylationEGSRYQESLGNTVFE
HCCHHHHHHCCEEEE
26.5023663014
200PhosphorylationYQESLGNTVFELENR
HHHHHCCEEEEEECC
25.4420873877
212PhosphorylationENREAEAYTGLSPPV
ECCCHHHHCCCCCCC
7.8928796482
213PhosphorylationNREAEAYTGLSPPVP
CCCHHHHCCCCCCCC
38.4028796482
216PhosphorylationAEAYTGLSPPVPSFN
HHHHCCCCCCCCCCC
28.6225159151
221PhosphorylationGLSPPVPSFNCEVRD
CCCCCCCCCCEEECH
29.3528387310
235PhosphorylationDEFEELDSVPLVKSS
HHHHHHCCCCEEECC
37.9519664994
241PhosphorylationDSVPLVKSSAGDTEF
CCCCEEECCCCCCCC
20.2429691806
242PhosphorylationSVPLVKSSAGDTEFV
CCCEEECCCCCCCCC
30.4729691806
246PhosphorylationVKSSAGDTEFVHQNS
EECCCCCCCCCCCCH
30.3329691806
253PhosphorylationTEFVHQNSQEIQRSS
CCCCCCCHHHHHHHC
23.7123401153
259PhosphorylationNSQEIQRSSQDEMVS
CHHHHHHHCHHHHHH
18.9021406692
260PhosphorylationSQEIQRSSQDEMVST
HHHHHHHCHHHHHHH
43.7921406692
266PhosphorylationSSQDEMVSTKQQNNT
HCHHHHHHHHHHCCC
28.6921406692
267PhosphorylationSQDEMVSTKQQNNTS
CHHHHHHHHHHCCCH
22.8221406692
268 (in isoform 1)Ubiquitination-42.2421890473
268UbiquitinationQDEMVSTKQQNNTSQ
HHHHHHHHHHCCCHH
42.2427667366
268 (in isoform 2)Ubiquitination-42.2421890473
273PhosphorylationSTKQQNNTSQERQTE
HHHHHCCCHHHHHHC
39.0629759185
274PhosphorylationTKQQNNTSQERQTEH
HHHHCCCHHHHHHCC
31.9721406692
282PhosphorylationQERQTEHSPEDAACG
HHHHHCCCCCHHCCC
24.6125159151
304UbiquitinationQNTNDREKNHGSSPE
CCCCHHHHCCCCCHH
55.9529967540
308PhosphorylationDREKNHGSSPEQVVR
HHHHCCCCCHHHHHC
34.8630266825
309PhosphorylationREKNHGSSPEQVVRP
HHHCCCCCHHHHHCH
36.7325159151
317UbiquitinationPEQVVRPKVRKLISS
HHHHHCHHHHHHHCC
44.0723000965
320UbiquitinationVVRPKVRKLISSSQV
HHCHHHHHHHCCCCC
53.8323000965
320 (in isoform 1)Ubiquitination-53.8321890473
320 (in isoform 2)Ubiquitination-53.8321890473
323PhosphorylationPKVRKLISSSQVDQE
HHHHHHHCCCCCCHH
34.0830266825
324PhosphorylationKVRKLISSSQVDQET
HHHHHHCCCCCCHHH
20.1430266825
325PhosphorylationVRKLISSSQVDQETG
HHHHHCCCCCCHHHC
27.6819690332
339UbiquitinationGFNRHEAKQRSVQRW
CCCHHHHHHHHHHHH
43.1721890473
339 (in isoform 2)Ubiquitination-43.1721890473
339 (in isoform 1)Ubiquitination-43.1721890473
342PhosphorylationRHEAKQRSVQRWREA
HHHHHHHHHHHHHHH
21.8021423175
355PhosphorylationEALEVEESGSDDLLI
HHHHHHHHCCCCEEE
30.0520873877
357PhosphorylationLEVEESGSDDLLIKC
HHHHHHCCCCEEEEE
36.9120873877
367PhosphorylationLLIKCEEYDGEHDCM
EEEEEEEECCCCCEE
13.62-
380PhosphorylationCMFLDPPYSRVITQR
EEEECCCCCEEEEEH
17.9422817900
381PhosphorylationMFLDPPYSRVITQRE
EEECCCCCEEEEEHH
26.3322817900
385PhosphorylationPPYSRVITQRETENN
CCCCEEEEEHHCCCC
20.7922817900
389PhosphorylationRVITQRETENNQMTS
EEEEEHHCCCCCCCC
46.3220873877
395PhosphorylationETENNQMTSESGATA
HCCCCCCCCCCCCCC
21.4120873877
396PhosphorylationTENNQMTSESGATAG
CCCCCCCCCCCCCCC
25.1520873877
398PhosphorylationNNQMTSESGATAGRQ
CCCCCCCCCCCCCCH
33.2320873877
428PhosphorylationLYDKDEDSSECSDGE
EEECCCCCCCCCCCC
26.4525159151
429PhosphorylationYDKDEDSSECSDGEW
EECCCCCCCCCCCCE
55.7525159151
432PhosphorylationDEDSSECSDGEWSAS
CCCCCCCCCCCEECC
44.6025159151
437PhosphorylationECSDGEWSASLPHRF
CCCCCCEECCCCCCC
12.0427251275
452PhosphorylationSGTEKDQSSSDESWE
CCCCCCCCCCCCCCC
41.7820363803
453PhosphorylationGTEKDQSSSDESWET
CCCCCCCCCCCCCCC
35.8520363803
454PhosphorylationTEKDQSSSDESWETL
CCCCCCCCCCCCCCC
51.1220363803
457PhosphorylationDQSSSDESWETLPGK
CCCCCCCCCCCCCCC
34.8920363803
460PhosphorylationSSDESWETLPGKDEN
CCCCCCCCCCCCCCC
31.8125159151
486PhosphorylationEEENQELSLQEGEQT
HHHHHCCCCCCCCCC
27.5326074081
493PhosphorylationSLQEGEQTSLEEGEI
CCCCCCCCCCCCCCC
30.8626074081
494PhosphorylationLQEGEQTSLEEGEIP
CCCCCCCCCCCCCCC
33.2126074081
576PhosphorylationVDPQFLTYMALEERL
CCHHHHHHHHHHHHH
5.2022817900
596PhosphorylationTALAHLESLAVDVEV
HHHHHHHHHCCEEEE
28.1724275569
647 (in isoform 2)Ubiquitination-11.3021890473
658UbiquitinationPCHHFFHKPCVSIWL
CCCHHCCCCEEEEEE
34.6529967540
667UbiquitinationCVSIWLQKSGTCPVC
EEEEEEECCCCCCCC
49.0022817900
667 (in isoform 1)Ubiquitination-49.0021890473

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
342SPhosphorylationKinasePRKACAP17612
GPS
342SPhosphorylationKinasePKA-FAMILY-GPS
342SPhosphorylationKinasePKA-Uniprot
389TPhosphorylationKinasePRKACAP17612
GPS
389TPhosphorylationKinasePKA-FAMILY-GPS
389TPhosphorylationKinasePKA-Uniprot
-KUbiquitinationE3 ubiquitin ligasePJA2O43164
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PJA2_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 PJA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2D2_HUMANUBE2D2physical
12036302
KAP2_HUMANPRKAR2Aphysical
21423175
KAP0_HUMANPRKAR1Aphysical
21423175
UB2D3_HUMANUBE2D3physical
21423175
PJA2_HUMANPJA2physical
12036302
KSR1_HUMANKSR1physical
27195677
MFHA1_HUMANMFHAS1physical
28471450

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 PJA2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Control of PKA stability and signalling by the RING ligase praja2.";
Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R.,Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.;
Nat. Cell Biol. 13:412-422(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKAR1A; PRKAR2A ANDPRKAR2B, AND PHOSPHORYLATION AT SER-342 AND THR-389.
"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-323, 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 TYR-380; SER-381; THR-385;SER-428; SER-429 AND SER-432, AND MASS SPECTROMETRY.

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