CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021324
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pinin 
Protein Synonyms/Alias
 140 kDa nuclear and cell adhesion-related phosphoprotein; Desmosome-associated protein; Domain-rich serine protein; DRS protein; DRSP; Melanoma metastasis clone A protein; Nuclear protein SDK3; SR-like protein 
Gene Name
 PNN 
Gene Synonyms/Alias
 DRS; MEMA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
16QEQLEKAKESLKNVDubiquitination[1]
137QDQNMDEKGKQRNRRubiquitination[1, 2, 3, 4]
157MGTLQKFKQESTVATubiquitination[1]
238KYIRTKTKPHLFYIPacetylation[4, 5]
262LIEESQRKMNALFEGubiquitination[1]
304VVRNEEQKAEQEEGKsumoylation[6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634] 
Functional Description
 Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma. 
Sequence Annotation
 REGION 2 284 Necessary for interaction with RNPS1.
 REGION 2 167 Necessary for mediating alternative 5'
 REGION 2 98 Necessary for interactions with KRT8,
 REGION 606 717 Necessary for interaction with PPIG.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 58 58 Phosphoserine.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 96 96 Phosphoserine.
 MOD_RES 100 100 Phosphoserine.
 MOD_RES 114 114 Phosphoserine.
 MOD_RES 115 115 Phosphoserine.
 MOD_RES 124 124 Phosphothreonine.
 MOD_RES 238 238 N6-acetyllysine.
 MOD_RES 347 347 Phosphoserine.
 MOD_RES 375 375 Phosphoserine.
 MOD_RES 381 381 Phosphoserine.
 MOD_RES 441 441 Phosphoserine (By similarity).
 MOD_RES 443 443 Phosphoserine.
 MOD_RES 450 450 Phosphoserine.
 MOD_RES 552 552 Phosphoserine.
 MOD_RES 658 658 Phosphoserine.
 MOD_RES 671 671 Phosphoserine (By similarity).
 MOD_RES 692 692 Phosphoserine.
 MOD_RES 695 695 Phosphoserine.  
Keyword
 Acetylation; Activator; Alternative splicing; Cell junction; Coiled coil; Complete proteome; Direct protein sequencing; DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Spliceosome; Transcription; Transcription regulation; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 717 AA 
Protein Sequence
MAVAVRTLQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL 60
LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS 120
KERTRRDLIQ DQNMDEKGKQ RNRRIFGLLM GTLQKFKQES TVATERQKRR QEIEQKLEVQ 180
AEEERKQVEN ERRELFEERR AKQTELRLLE QKVELAQLQE EWNEHNAKII KYIRTKTKPH 240
LFYIPGRMCP ATQKLIEESQ RKMNALFEGR RIEFAEQINK MEARPRRQSM KEKEHQVVRN 300
EEQKAEQEEG KVAQREEELE ETGNQHNDVE IEEAGEEEEK EIAIVHSDAE KEQEEEEQKQ 360
EMEVKMEEET EVRESEKQQD SQPEEVMDVL EMVENVKHVI ADQEVMETNR VESVEPSENE 420
ASKELEPEME FEIEPDKECK SLSPGKENVS ALDMEKESEE KEEKESEPQP EPVAQPQPQS 480
QPQLQLQSQS QPVLQSQPPS QPEDLSLAVL QPTPQVTQEQ GHLLPERKDF PVESVKLTEV 540
PVEPVLTVHP ESKSKTKTRS RSRGRARNKT SKSRSRSSSS SSSSSSSTSS SSGSSSSSGS 600
SSSRSSSSSS SSTSGSSSRD SSSSTSSSSE SRSRSRGRGH NRDRKHRRSV DRKRRDTSGL 660
ERSHKSSKGG SSRDTKGSKD KNSRSDRKRS ISESSRSGKR SSRSERDRKS DRKDKRR 717 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005911; C:cell-cell junction; TAS:ProtInc.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
 GO:0005882; C:intermediate filament; TAS:ProtInc.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:ProtInc.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0005198; F:structural molecule activity; NAS:ProtInc.
 GO:0007155; P:cell adhesion; TAS:ProtInc.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR006786; Pinin_SDK_MemA.
 IPR006787; Pinin_SDK_N. 
Pfam
 PF04696; Pinin_SDK_memA
 PF04697; Pinin_SDK_N 
SMART
  
PROSITE
  
PRINTS