CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020196
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein U-like protein 1 
Protein Synonyms/Alias
 Adenovirus early region 1B-associated protein 5; E1B-55 kDa-associated protein 5; E1B-AP5 
Gene Name
 HNRNPUL1 
Gene Synonyms/Alias
 E1BAP5; HNRPUL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
117FYDTQVIKQENESGYsumoylation[1]
117FYDTQVIKQENESGYubiquitination[2, 3, 4]
146PEMKTEMKQGAPTSFubiquitination[4, 5]
162PPEASQLKPDRQQFQubiquitination[2, 3]
270INEEISVKHLPSTEPacetylation[6]
270INEEISVKHLPSTEPubiquitination[3, 4, 5, 7]
310GYGGTGKKSTNSRFEubiquitination[3]
350LSFTKNGKWMGIAFRubiquitination[3]
418GTVGPKSKAECEILMubiquitination[3]
440GKTTWAIKHAASNPSubiquitination[3, 4, 5]
461GTNAIMDKMRVMGLRubiquitination[3, 8]
517YGSAQRRKMRPFEGFubiquitination[3]
527PFEGFQRKAIVICPTubiquitination[3, 8]
539CPTDEDLKDRTIKRTubiquitination[3]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [6] 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]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] 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] 
Functional Description
 Acts as a basic transcriptional regulator. Represses basic transcription driven by several virus and cellular promoters. When associated with BRD7, activates transcription of glucocorticoid-responsive promoter in the absence of ligand- stimulation. Plays also a role in mRNA processing and transport. Binds avidly to poly(G) and poly(C) RNA homopolymers in vitro. 
Sequence Annotation
 DOMAIN 3 37 SAP.
 DOMAIN 191 388 B30.2/SPRY.
 REPEAT 612 614 1-1.
 REPEAT 620 622 1-2.
 REPEAT 639 641 1-3.
 REPEAT 645 647 1-4.
 REPEAT 656 658 1-5.
 REGION 1 103 Necessary for interaction with HRMT1L1.
 REGION 213 856 Necessary for interaction with TP53.
 REGION 456 594 Necessary for interaction with BRD7 and
 REGION 612 658 5 X 3 AA repeats of R-G-G.
 REGION 612 658 Necessary for transcription repression.
 MOD_RES 194 194 Phosphoserine.
 MOD_RES 512 512 Phosphoserine.
 MOD_RES 718 718 Phosphoserine.  
Keyword
 Activator; Alternative splicing; Complete proteome; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 856 AA 
Protein Sequence
MDVRRLKVNE LREELQRRGL DTRGLKAELA ERLQAALEAE EPDDERELDA DDEPGRPGHI 60
NEEVETEGGS ELEGTAQPPP PGLQPHAEPG GYSGPDGHYA MDNITRQNQF YDTQVIKQEN 120
ESGYERRPLE MEQQQAYRPE MKTEMKQGAP TSFLPPEASQ LKPDRQQFQS RKRPYEENRG 180
RGYFEHREDR RGRSPQPPAE EDEDDFDDTL VAIDTYNCDL HFKVARDRSS GYPLTIEGFA 240
YLWSGARASY GVRRGRVCFE MKINEEISVK HLPSTEPDPH VVRIGWSLDS CSTQLGEEPF 300
SYGYGGTGKK STNSRFENYG DKFAENDVIG CFADFECGND VELSFTKNGK WMGIAFRIQK 360
EALGGQALYP HVLVKNCAVE FNFGQRAEPY CSVLPGFTFI QHLPLSERIR GTVGPKSKAE 420
CEILMMVGLP AAGKTTWAIK HAASNPSKKY NILGTNAIMD KMRVMGLRRQ RNYAGRWDVL 480
IQQATQCLNR LIQIAARKKR NYILDQTNVY GSAQRRKMRP FEGFQRKAIV ICPTDEDLKD 540
RTIKRTDEEG KDVPDHAVLE MKANFTLPDV GDFLDEVLFI ELQREEADKL VRQYNEEGRK 600
AGPPPEKRFD NRGGGGFRGR GGGGGFQRYE NRGPPGGNRG GFQNRGGGSG GGGNYRGGFN 660
RSGGGGYSQN RWGNNNRDNN NSNNRGSYNR APQQQPPPQQ PPPPQPPPQQ PPPPPSYSPA 720
RNPPGASTYN KNSNIPGSSA NTSTPTVSSY SPPQPSYSQP PYNQGGYSQG YTAPPPPPPP 780
PPAYNYGSYG GYNPAPYTPP PPPTAQTYPQ PSYNQYQQYA QQWNQYYQNQ GQWPPYYGNY 840
DYGSYSGNTQ GGTSTQ 856 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0009615; P:response to virus; TAS:ProtInc.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR008985; ConA-like_lec_gl_sf.
 IPR027025; hnRNP_U_like_1.
 IPR027417; P-loop_NTPase.
 IPR003034; SAP_dom.
 IPR018355; SPla/RYanodine_receptor_subgr.
 IPR003877; SPRY_rcpt. 
Pfam
 PF02037; SAP
 PF00622; SPRY 
SMART
 SM00513; SAP
 SM00449; SPRY 
PROSITE
 PS50188; B302_SPRY
 PS50800; SAP 
PRINTS