CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000654
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase Praja-2 
Protein Synonyms/Alias
 Praja2; RING finger protein 131 
Gene Name
 PJA2 
Gene Synonyms/Alias
 KIAA0438; RNF131 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46RHAYVSFKPCMTRHEacetylation[1]
268QDEMVSTKQQNNTSQubiquitination[2, 3, 4, 5, 6]
317PEQVVRPKVRKLISSubiquitination[6, 7]
320VVRPKVRKLISSSQVubiquitination[1, 3, 6, 7, 8, 9]
339GFNRHEAKQRSVQRWubiquitination[6, 8, 9]
667CVSIWLQKSGTCPVCubiquitination[6, 8, 9]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional 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. 
Sequence Annotation
 ZN_FING 634 675 RING-type; atypical.
 REGION 531 708 Interaction with PRKAR1A, PRKAR2A and
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 309 309 Phosphoserine.
 MOD_RES 323 323 Phosphoserine.
 MOD_RES 342 342 Phosphoserine; by PKA.
 MOD_RES 389 389 Phosphothreonine; by PKA.
 MOD_RES 432 432 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus; Ligase; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Synapse; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 708 AA 
Protein Sequence
MSQYTEKEPA AMDQESGKAV WPKPAGGYQT ITGRRYGRRH AYVSFKPCMT RHERSLGRAG 60
DDYEVLELDD VPKENSSGSS PLDQVDSSLP SEPIFEKSET EIPTCGSALN QTTESSQSFV 120
AVHHSEEGRD TLGSSTNLHN HSEGEYIPGA CSASSVQNGI ALVHTDSYDP DGKHGEDNDH 180
LQLSAEVVEG SRYQESLGNT VFELENREAE AYTGLSPPVP SFNCEVRDEF EELDSVPLVK 240
SSAGDTEFVH QNSQEIQRSS QDEMVSTKQQ NNTSQERQTE HSPEDAACGP GHICSEQNTN 300
DREKNHGSSP EQVVRPKVRK LISSSQVDQE TGFNRHEAKQ RSVQRWREAL EVEESGSDDL 360
LIKCEEYDGE HDCMFLDPPY SRVITQRETE NNQMTSESGA TAGRQEVDNT FWNGCGDYYQ 420
LYDKDEDSSE CSDGEWSASL PHRFSGTEKD QSSSDESWET LPGKDENEPE LQSDSSGPEE 480
ENQELSLQEG EQTSLEEGEI PWLQYNEVNE SSSDEGNEPA NEFAQPAFML DGNNNLEDDS 540
SVSEDLDVDW SLFDGFADGL GVAEAISYVD PQFLTYMALE ERLAQAMETA LAHLESLAVD 600
VEVANPPASK ESIDGLPETL VLEDHTAIGQ EQCCPICCSE YIKDDIATEL PCHHFFHKPC 660
VSIWLQKSGT CPVCRRHFPP AVIEASAAPS SEPDPDAPPS NDSIAEAP 708 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
 GO:0034236; F:protein kinase A catalytic subunit binding; IMP:UniProtKB.
 GO:0034237; F:protein kinase A regulatory subunit binding; IMP:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007616; P:long-term memory; ISS:UniProtKB.
 GO:0010738; P:regulation of protein kinase A signaling cascade; IMP:UniProtKB. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS