CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020126
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein fem-1 homolog A 
Protein Synonyms/Alias
 FEM1a; FEM1-alpha; Prostaglandin E receptor 4-associated protein 
Gene Name
 FEM1A 
Gene Synonyms/Alias
 EPRAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15YNAARDGKLQLLQKLubiquitination[1]
21GKLQLLQKLLSGRSRubiquitination[1, 2, 3, 4]
182QVNRRSAKGNTALHDubiquitination[1]
206LQLLLGCKARMERDGubiquitination[1]
311LGATYVDKKRDLLGAubiquitination[1]
312GATYVDKKRDLLGALubiquitination[1]
320RDLLGALKHWRRAMEubiquitination[1, 2, 4]
452VLQDRAAKGSLGTQIubiquitination[1]
470DLMGVLTKGVREVERubiquitination[1]
624AYELLDEKLLARGTMubiquitination[1, 5, 6, 7]
651ARALDKNKIPYKGFIubiquitination[3, 6]
655DKNKIPYKGFIPEDLubiquitination[3, 5]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] 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
Functional Description
 Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit (By similarity). May participate in antiinflammatory signaling via its interaction with PTGER4. 
Sequence Annotation
 REPEAT 2 31 ANK 1.
 REPEAT 40 70 ANK 2.
 REPEAT 82 111 ANK 3.
 REPEAT 115 145 ANK 4.
 REPEAT 149 178 ANK 5.
 REPEAT 182 211 ANK 6.
 REPEAT 214 243 ANK 7.
 REPEAT 298 332 TPR 1.
 REPEAT 390 423 TPR 2.
 REPEAT 534 576 ANK 8.
 REPEAT 580 609 ANK 9.  
Keyword
 ANK repeat; Complete proteome; Cytoplasm; Polymorphism; Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 669 AA 
Protein Sequence
MDLRTAVYNA ARDGKLQLLQ KLLSGRSREE LDELTGEVAG GGTPLLIAAR YGHLDVVEYL 60
VDRCGASVEA GGSVHFDGET IEGAPPLWAA SAAGHLDVVR SLLRRGASVN RTTRTNSTPL 120
RAACFDGHLE VVRYLVGEHQ ADLEVANRHG HTCLMISCYK GHREIARYLL EQGAQVNRRS 180
AKGNTALHDC AESGSLEILQ LLLGCKARME RDGYGMTPLL AASVTGHTNI VEYLIQEQPG 240
QEQVAGGEAQ PGLPQEDPST SQGCAQPQGA PCCSSSPEEP LNGESYESCC PTSREAAVEA 300
LELLGATYVD KKRDLLGALK HWRRAMELRH QGGEYLPKPE PPQLVLAYDY SREVNTTEEL 360
EALITDPDEM RMQALLIRER ILGPSHPDTS YYIRYRGAVY ADSGNFERCI RLWKYALDMQ 420
QSNLEPLSPM TASSFLSFAE LFSYVLQDRA AKGSLGTQIG FADLMGVLTK GVREVERALQ 480
LPREPGDSAQ FTKALAIILH LLYLLEKVEC TPSQEHLKHQ TVYRLLKCAP RGKNGFTPLH 540
MAVDKDTTNV GRYPVGRFPS LHVVKVLLDC GADPDSRDFD NNTPLHIAAQ NNCPAIMNAL 600
IEAGAHMDAT NAFKKTAYEL LDEKLLARGT MQPFNYVTLQ CLAARALDKN KIPYKGFIPE 660
DLEAFIELH 669 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
 GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
 GO:0051438; P:regulation of ubiquitin-protein ligase activity; ISS:UniProtKB. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR011990; TPR-like_helical. 
Pfam
 PF00023; Ank
 PF12796; Ank_2 
SMART
 SM00248; ANK 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS
 PR01415; ANKYRIN.