CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016024
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
317VVRPKVRKVISSSQVubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 (By similarity). 
Sequence Annotation
 ZN_FING 633 674 RING-type; atypical.
 REGION 530 707 Interaction with PRKAR1A, PRKAR2A and
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 306 306 Phosphoserine (By similarity).
 MOD_RES 320 320 Phosphoserine (By similarity).
 MOD_RES 339 339 Phosphoserine; by PKA (By similarity).
 MOD_RES 385 385 Phosphothreonine; by PKA (By similarity).
 MOD_RES 430 430 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus; Ligase; Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 707 AA 
Protein Sequence
MSQYTEKEPS VMDQESSKAA WPKPAGGYQT ITGRRYGRRH AYVSFKPCMT RHERSLGRAG 60
DDYEVLELDD VPKENTSGSS SLDQVHPALP NEPTVEKSET EISTCGPALN QSTESSPSIA 120
TVCHSEEVRE TLESNTNLHN RTETEHTPAV CNVSSVQNGI MLVHTDSYDP DSKHDENGSL 180
QLGAEAVEGG RHQKGLGRAV FELENGEAEI YADLSPSVPS LNGEISEAFE ELDSAPLEKS 240
STADAELVHQ NGQEFQRSSE DGVVRKRRQD DTDQGRQTEN STEDADCAPG HVEQNTSDRA 300
NHHGSSPEQV VRPKVRKVIS SSQVDQEIGF NRHEAKQRSV QRWREALEVE ECSSDDPIIK 360
CDDYDGDHDC MFLTPTYSRV TQRETERNRV TSENGATASG RQESRDNAFW NACGEYYQLF 420
DKDEDSSECS DGEWSASLPH RFSGTEKDQS SSDDSWETLP GKDENDPELQ SDSSGPEEEN 480
QELSLQEGEQ TSLEEGEIPW LQYNEVNESS SDEGNEPANE FAQPEAFMLD GNNNLEDDSS 540
VSEDLDVDWS LFDGFADGLG VAEAISYVDP QFLTYMALEE RLAQAMETAL AHLESLAVDV 600
EVANPPASKE SIDGLPETLV LEDHTAIGQE QCCPICCSEY IKDDIATELP CHHFFHKPCV 660
SIWLQKSGTC PVCRRHFPPA VIDASAAASS DPDPDASPAN DNAEEAP 707 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
 GO:0034237; F:protein kinase A regulatory subunit binding; ISS:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 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; ISS: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