PJA1_HUMAN - dbPTM
PJA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PJA1_HUMAN
UniProt AC Q8NG27
Protein Name E3 ubiquitin-protein ligase Praja-1
Gene Name PJA1
Organism Homo sapiens (Human).
Sequence Length 643
Subcellular Localization
Protein Description Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting..
Protein Sequence MGQESSKPVWPNPTGGYQSNTGRRYGRRHAYVSFRPPTSQRERIASQRKTNSEVPMHRSAPSQTTKRSRSPFSTTRRSWDDSESSGTNLNIDNEDYSRYPPREYRASGSRRGMAYGHIDSYGADDSEEEGAGPVERPPVRGKTGKFKDDKLYDPEKGARSLAGPPPHFSSFSRDVREERDKLDPVPAARCSASRADFLPQSSVASQSSSEGKLATKGDSSERERREQNLPARPSRAPVSICGGGENTSKSAEEPVVRPKIRNLASPNCVKPKIFFDTDDDDDMPHSTSRWRDTANDNEGHSDGLARRGRGESSSGYPEPKYPEDKREARSDQVKPEKVPRRRRTMADPDFWTHSDDYYKYCDEDSDSDKEWIAALRRKYRSREQTLSSSGESWETLPGKEEREPPQAKVSASTGTSPGPGASASAGAGAGASAGSNGSNYLEEVREPSLQEEQASLEEGEIPWLQYHENDSSSEGDNDSGHELMQPGVFMLDGNNNLEDDSSVSEDLEVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDALPEILVTEDHGAVGQEMCCPICCSEYVKGEVATELPCHHYFHKPCVSIWLQKSGTCPVCRCMFPPPL
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
11UbiquitinationESSKPVWPNPTGGYQ
CCCCCCCCCCCCCCC
36.8422053931
50PhosphorylationRIASQRKTNSEVPMH
HHHHHCCCCCCCCCC
46.2822210691
52PhosphorylationASQRKTNSEVPMHRS
HHHCCCCCCCCCCCC
45.2422210691
59PhosphorylationSEVPMHRSAPSQTTK
CCCCCCCCCCCCCCC
29.8322199227
62PhosphorylationPMHRSAPSQTTKRSR
CCCCCCCCCCCCCCC
39.6224425749
64PhosphorylationHRSAPSQTTKRSRSP
CCCCCCCCCCCCCCC
38.3322199227
65PhosphorylationRSAPSQTTKRSRSPF
CCCCCCCCCCCCCCC
19.4722210691
66 (in isoform 2)Ubiquitination-52.3321890473
66UbiquitinationSAPSQTTKRSRSPFS
CCCCCCCCCCCCCCC
52.3322053931
68PhosphorylationPSQTTKRSRSPFSTT
CCCCCCCCCCCCCCC
38.3730266825
70 (in isoform 2)Phosphorylation-31.38-
70PhosphorylationQTTKRSRSPFSTTRR
CCCCCCCCCCCCCCC
31.3823911959
71PhosphorylationTTKRSRSPFSTTRRS
CCCCCCCCCCCCCCC
26.5432142685
73PhosphorylationKRSRSPFSTTRRSWD
CCCCCCCCCCCCCCC
32.0523927012
74PhosphorylationRSRSPFSTTRRSWDD
CCCCCCCCCCCCCCC
25.3823186163
75PhosphorylationSRSPFSTTRRSWDDS
CCCCCCCCCCCCCCC
23.9223186163
78PhosphorylationPFSTTRRSWDDSESS
CCCCCCCCCCCCCCC
31.4028348404
87PhosphorylationDDSESSGTNLNIDNE
CCCCCCCCCCCCCCC
38.18-
115PhosphorylationGSRRGMAYGHIDSYG
CCCCCCCCCCCCCCC
10.5929978859
120PhosphorylationMAYGHIDSYGADDSE
CCCCCCCCCCCCCCC
25.5129978859
121PhosphorylationAYGHIDSYGADDSEE
CCCCCCCCCCCCCCC
16.7630576142
126PhosphorylationDSYGADDSEEEGAGP
CCCCCCCCCCCCCCC
47.6723401153
149UbiquitinationKTGKFKDDKLYDPEK
CCCCCCCCCCCCHHH
43.3720972266
169PhosphorylationAGPPPHFSSFSRDVR
CCCCCCHHHCCHHHH
27.6924719451
179PhosphorylationSRDVREERDKLDPVP
CHHHHHHHHCCCCCC
41.4333259812
194UbiquitinationAARCSASRADFLPQS
CHHHCCCCCCCCCCC
37.5832015554
210PhosphorylationVASQSSSEGKLATKG
CCCCCCCCCCCCCCC
63.4032142685
211UbiquitinationASQSSSEGKLATKGD
CCCCCCCCCCCCCCC
32.0232015554
212AcetylationSQSSSEGKLATKGDS
CCCCCCCCCCCCCCH
30.7825953088
222PhosphorylationTKGDSSERERREQNL
CCCCHHHHHHHHHCC
44.6732142685
249UbiquitinationGGGENTSKSAEEPVV
CCCCCCCCCCCCCCC
52.2032015554
250PhosphorylationGGENTSKSAEEPVVR
CCCCCCCCCCCCCCC
40.4528348404
265O-linked_GlycosylationPKIRNLASPNCVKPK
HHHHHCCCCCCCCCE
21.5830379171
265PhosphorylationPKIRNLASPNCVKPK
HHHHHCCCCCCCCCE
21.5823401153
277PhosphorylationKPKIFFDTDDDDDMP
CCEEECCCCCCCCCC
35.8529255136
282UbiquitinationFDTDDDDDMPHSTSR
CCCCCCCCCCCCCCC
60.5520972266
286PhosphorylationDDDDMPHSTSRWRDT
CCCCCCCCCCCCCCC
23.3923403867
287PhosphorylationDDDMPHSTSRWRDTA
CCCCCCCCCCCCCCC
21.1923403867
288PhosphorylationDDMPHSTSRWRDTAN
CCCCCCCCCCCCCCC
32.6223403867
301PhosphorylationANDNEGHSDGLARRG
CCCCCCCCCCCHHCC
44.2029449344
312PhosphorylationARRGRGESSSGYPEP
HHCCCCCCCCCCCCC
32.4025394399
313PhosphorylationRRGRGESSSGYPEPK
HCCCCCCCCCCCCCC
24.3923312004
314PhosphorylationRGRGESSSGYPEPKY
CCCCCCCCCCCCCCC
52.1823312004
316PhosphorylationRGESSSGYPEPKYPE
CCCCCCCCCCCCCCH
13.33-
337UbiquitinationSDQVKPEKVPRRRRT
HCCCCHHHCCCCCCC
67.1020972266
344UbiquitinationKVPRRRRTMADPDFW
HCCCCCCCCCCCCCC
18.2032015554
344PhosphorylationKVPRRRRTMADPDFW
HCCCCCCCCCCCCCC
18.2027251275
354PhosphorylationDPDFWTHSDDYYKYC
CCCCCCCCCCHHHHC
25.46-
360PhosphorylationHSDDYYKYCDEDSDS
CCCCHHHHCCCCCCC
6.7622617229
365PhosphorylationYKYCDEDSDSDKEWI
HHHCCCCCCCCHHHH
36.6522617229
367PhosphorylationYCDEDSDSDKEWIAA
HCCCCCCCCHHHHHH
55.3122617229
381PhosphorylationALRRKYRSREQTLSS
HHHHHHHCHHHHHCC
36.7624719451
385PhosphorylationKYRSREQTLSSSGES
HHHCHHHHHCCCCCC
24.6925850435
387PhosphorylationRSREQTLSSSGESWE
HCHHHHHCCCCCCCC
26.3325850435
388PhosphorylationSREQTLSSSGESWET
CHHHHHCCCCCCCCC
45.5420363803
389PhosphorylationREQTLSSSGESWETL
HHHHHCCCCCCCCCC
43.1125850435
392PhosphorylationTLSSSGESWETLPGK
HHCCCCCCCCCCCCC
33.4620363803
399UbiquitinationSWETLPGKEEREPPQ
CCCCCCCCCCCCCCC
55.2332015554
440 (in isoform 2)Ubiquitination-19.7221890473
440UbiquitinationAGSNGSNYLEEVREP
CCCCCCCHHHHHCCC
19.7221890473
440PhosphorylationAGSNGSNYLEEVREP
CCCCCCCHHHHHCCC
19.72-
448PhosphorylationLEEVREPSLQEEQAS
HHHHCCCCHHHHHHH
37.62-
537PhosphorylationVDPQFLTYMALEERL
CCHHHHHHHHHHHHH
5.2022817900
557PhosphorylationTALAHLESLAVDVEV
HHHHHHHHHCCEEEE
28.1724275569
573UbiquitinationNPPASKESIDALPEI
CCCCCHHHHHCCCCE
29.5121890473
573UbiquitinationNPPASKESIDALPEI
CCCCCHHHHHCCCCE
29.5121890473
628UbiquitinationCVSIWLQKSGTCPVC
CEEEECCCCCCCCCC
49.0022817900
628 (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

Oops, there are no upstream regulatory protein records of PJA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PJA1_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 PJA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGD1_HUMANMAGED1physical
11959851
SPTB2_HUMANSPTBN1physical
16247473
UB2D2_HUMANUBE2D2physical
12036302
EZH2_HUMANEZH2physical
21513699
SUZ12_HUMANSUZ12physical
21513699
EED_HUMANEEDphysical
21513699
PJA1_HUMANPJA1physical
21513699
UBP20_HUMANUSP20physical
22626734
UBP51_HUMANUSP51physical
22626734
UBP5_HUMANUSP5physical
22626734
ATX3_HUMANATXN3physical
22626734
UBP7_HUMANUSP7physical
22626734
STABP_HUMANSTAMBPphysical
22626734
OTUB1_HUMANOTUB1physical
22626734
JOS1_HUMANJOSD1physical
22626734
UCHL3_HUMANUCHL3physical
22626734
UBP8_HUMANUSP8physical
22626734
UCHL5_HUMANUCHL5physical
22626734
OTUB2_HUMANOTUB2physical
22626734
ATX3L_HUMANATXN3Lphysical
22626734
UBP28_HUMANUSP28physical
22626734
ESPL1_HUMANESPL1physical
22626734
STAM1_HUMANSTAMphysical
22626734
UB2D3_HUMANUBE2D3physical
22626734
UB2L3_HUMANUBE2L3physical
21513699
PJA1_HUMANPJA1physical
12036302
MAGD4_HUMANMAGED4Bphysical
28514442
SMC5_HUMANSMC5physical
28514442
SMC6_HUMANSMC6physical
28514442
NSE4A_HUMANNSMCE4Aphysical
28514442
NSE3_HUMANNDNL2physical
28514442
CHRC1_HUMANCHRAC1physical
28514442
UBP7_HUMANUSP7physical
28514442
FAF2_HUMANFAF2physical
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 PJA1_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 THR-277, AND MASSSPECTROMETRY.

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