dbPTM

PJA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PJA1_MOUSE
UniProt AC	O55176
Protein Name	E3 ubiquitin-protein ligase Praja-1
Gene Name	Pja1
Organism	Mus musculus (Mouse).
Sequence Length	578
Subcellular Localization
Protein Description	Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome. May be involved in protein sorting..
Protein Sequence	MSHQERIASQRRTTAEVPMHRSTANQSKRSRSPFASTRRRWDDSESSGASLAVESEDYSRYPPREYRASGSRRGLAYGHIDTVVARDSEEEGAGPVDRLPVRGKAGKFKDDPEKGARSSRFTSVNHDAKEECGKVESPPAARCSARRAELSKQNGSSASQISSAEGRAAAKGNNSLERERQNLPARPSRAPVSICGGGENTPKSAEEPVVRPKVRNVATPNCMKPKVFFDTDDDDDVPHSTSRWRDAADAEEAHAEGLARRGRGEAASSSEPRYAEDQDARSEQAKADKVPRRRRTMADPDFWAYTDDYYRYYEEDSDSDKEWMAALRRKYRSREQPQSSSGESWELLPGKEELERQQAGAGSLASAGSNGSGYPEEVQDPSLQEEEQASLEEGEIPWLRYNENESSSEGDNESTHELIQPGMFMLDGNNNLEDDSSVSEDLEVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDALPEILVTEDHGAVGQEMCCPICCSEYVKGEVATELPCHHYFHKPCVSIWLQKSGTCPVCRCMFPPPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	RIASQRRTTAEVPMH HHHHHCCCCCCCCCC	32.33	28576409
14	Phosphorylation	IASQRRTTAEVPMHR HHHHCCCCCCCCCCH	21.00	28576409
23	Phosphorylation	EVPMHRSTANQSKRS CCCCCHHHCCCCHHC	29.59	28576409
30	Phosphorylation	TANQSKRSRSPFAST HCCCCHHCCCCCCCC	40.63	23684622
32	Phosphorylation	NQSKRSRSPFASTRR CCCHHCCCCCCCCCC	26.14	26824392
36	Phosphorylation	RSRSPFASTRRRWDD HCCCCCCCCCCCCCC	23.87	28833060
37	Phosphorylation	SRSPFASTRRRWDDS CCCCCCCCCCCCCCC	25.43	28833060
77	Phosphorylation	GSRRGLAYGHIDTVV CCCCCCCCCCCEEEE	17.80	29514104
82	Phosphorylation	LAYGHIDTVVARDSE CCCCCCEEEEECCCC	19.10	26824392
88	Phosphorylation	DTVVARDSEEEGAGP EEEEECCCCCCCCCC	41.16	26824392
123	Phosphorylation	ARSSRFTSVNHDAKE CCCCCCCCCCCHHHH	20.43	27841257
137	Phosphorylation	EECGKVESPPAARCS HHHCCCCCCHHHHHH	38.89	25521595
156	Phosphorylation	ELSKQNGSSASQISS HHHHHCCCCHHHHHH	30.22	23984901
157	Phosphorylation	LSKQNGSSASQISSA HHHHCCCCHHHHHHH	33.08	23984901
159	Phosphorylation	KQNGSSASQISSAEG HHCCCCHHHHHHHHH	29.96	23984901
163	Phosphorylation	SSASQISSAEGRAAA CCHHHHHHHHHHHHH	31.78	29899451
175	Phosphorylation	AAAKGNNSLERERQN HHHCCCCHHHHHHHC	35.29	26824392
201	Phosphorylation	ICGGGENTPKSAEEP ECCCCCCCCCCCCCC	28.00	26643407
203	Ubiquitination	GGGENTPKSAEEPVV CCCCCCCCCCCCCCC	61.33	-
204	Phosphorylation	GGENTPKSAEEPVVR CCCCCCCCCCCCCCC	41.96	26824392
219	Phosphorylation	PKVRNVATPNCMKPK CCCCCCCCCCCCCCC	15.68	29514104
231	Phosphorylation	KPKVFFDTDDDDDVP CCCEEECCCCCCCCC	35.85	27087446
240	Phosphorylation	DDDDVPHSTSRWRDA CCCCCCCCHHHCCHH	23.23	25619855
241	Phosphorylation	DDDVPHSTSRWRDAA CCCCCCCHHHCCHHH	21.19	25619855
242	Phosphorylation	DDVPHSTSRWRDAAD CCCCCCHHHCCHHHH	32.62	25619855
282	Phosphorylation	AEDQDARSEQAKADK CCCHHHHHHHHHHHC	35.46	29899451
296	Phosphorylation	KVPRRRRTMADPDFW CCCCHHHCCCCCCHH	18.20	-
305	Phosphorylation	ADPDFWAYTDDYYRY CCCCHHHCCCCHHHH	10.99	21183079
306	Phosphorylation	DPDFWAYTDDYYRYY CCCHHHCCCCHHHHC	18.04	21183079
312	Phosphorylation	YTDDYYRYYEEDSDS CCCCHHHHCCCCCCC	10.10	22324799
313	Phosphorylation	TDDYYRYYEEDSDSD CCCHHHHCCCCCCCC	12.12	29899451
317	Phosphorylation	YRYYEEDSDSDKEWM HHHCCCCCCCCHHHH	42.15	25521595
319	Phosphorylation	YYEEDSDSDKEWMAA HCCCCCCCCHHHHHH	55.31	25521595
339	Phosphorylation	RSREQPQSSSGESWE HCCCCCCCCCCCCCE	32.90	29899451
340	Phosphorylation	SREQPQSSSGESWEL CCCCCCCCCCCCCEE	36.80	29899451
341	Phosphorylation	REQPQSSSGESWELL CCCCCCCCCCCCEEC	52.40	25521595
344	Phosphorylation	PQSSSGESWELLPGK CCCCCCCCCEECCCH	29.40	21183079
351	Ubiquitination	SWELLPGKEELERQQ CCEECCCHHHHHHHH	46.18	22790023
390	Phosphorylation	LQEEEQASLEEGEIP CCHHHHHHHHCCCCC	35.69	25338131
563	Ubiquitination	CVSIWLQKSGTCPVC CEEEECCCCCCCCCC	49.00	-

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_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PJA1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
UBC_HUMAN	UBC	physical	10500182

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PJA1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231, AND MASSSPECTROMETRY.	19367708 [Abstract]