CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009400
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein K 
Protein Synonyms/Alias
 hnRNP K; Transformation up-regulated nuclear protein; TUNP 
Gene Name
 HNRNPK 
Gene Synonyms/Alias
 HNRPK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21ETNGEFGKRPAEDMEacetylation[1]
34MEEEQAFKRSRNTDEacetylation[1, 2, 3]
34MEEEQAFKRSRNTDEubiquitination[3, 4, 5, 6, 7, 8, 9, 10]
52LRILLQSKNAGAVIGubiquitination[3, 4, 5, 7, 8, 9, 10]
60NAGAVIGKGGKNIKAacetylation[11, 12]
60NAGAVIGKGGKNIKAubiquitination[3, 5, 8, 10]
63AVIGKGGKNIKALRTacetylation[11]
63AVIGKGGKNIKALRTubiquitination[9]
66GKGGKNIKALRTDYNacetylation[11]
66GKGGKNIKALRTDYNubiquitination[7, 9]
102ETIGEILKKIIPTLEubiquitination[5]
103TIGEILKKIIPTLEEubiquitination[8]
139CLNYQHYKGSDFDCEmethylation[13]
139CLNYQHYKGSDFDCEubiquitination[4]
163AGGIIGVKGAKIKELubiquitination[3, 4, 5, 6, 7, 8, 9, 10]
166IIGVKGAKIKELRENubiquitination[9]
168GVKGAKIKELRENTQubiquitination[9]
179ENTQTTIKLFQECCPacetylation[3]
179ENTQTTIKLFQECCPubiquitination[3, 5, 7, 8, 9]
198RVVLIGGKPDRVVECubiquitination[3, 4, 5, 7, 8, 9]
207DRVVECIKIILDLISubiquitination[5]
219LISESPIKGRAQPYDubiquitination[3, 4, 5, 6, 7, 8, 9, 10, 14, 15]
396TTQVTIPKDLAGSIIubiquitination[3, 5, 7]
405LAGSIIGKGGQRIKQacetylation[1]
405LAGSIIGKGGQRIKQubiquitination[3, 4, 5, 6, 7, 8, 9, 10, 14]
422HESGASIKIDEPLEGacetylation[1]
422HESGASIKIDEPLEGsumoylation[16]
422HESGASIKIDEPLEGubiquitination[3, 4, 5, 6, 7, 10]
456YLLQNSVKQYSGKFFubiquitination[3, 4, 5, 6, 7, 9, 10]
461SVKQYSGKFF*****acetylation[1, 2]
461SVKQYSGKFF*****ubiquitination[4, 8, 9]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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]
 [9] 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]
 [10] 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]
 [11] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [12] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [13] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077]
 [14] 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]
 [15] 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]
 [16] DNA damage-induced heterogeneous nuclear ribonucleoprotein K sumoylation regulates p53 transcriptional activation.
 Pelisch F, Pozzi B, Risso G, Muñoz MJ, Srebrow A.
 J Biol Chem. 2012 Aug 31;287(36):30789-99. [PMID: 22825850] 
Functional Description
 One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single- stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. 
Sequence Annotation
 DOMAIN 42 104 KH 1.
 REPEAT 54 76 1-1.
 REPEAT 59 62 3-1.
 DOMAIN 144 209 KH 2.
 REPEAT 245 250 2-1.
 REPEAT 257 260 3-2.
 REPEAT 267 270 3-3.
 REPEAT 295 298 3-4.
 REPEAT 324 329 2-2.
 DOMAIN 387 451 KH 3.
 REPEAT 399 421 1-2.
 REPEAT 404 407 3-5.
 REGION 1 276 Necessary for interaction with DDX1.
 REGION 35 197 Interaction with ASFV p30.
 REGION 54 421 2 X 22 AA approximate repeats.
 REGION 59 407 5 X 4 AA repeats of G-X-G-G.
 REGION 209 337 Interaction with ZIK1 (By similarity).
 REGION 236 273 RNA-binding RGG-box.
 REGION 245 329 2 X 6 AA approximate repeats.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 116 116 Phosphoserine.
 MOD_RES 214 214 Phosphoserine.
 MOD_RES 216 216 Phosphoserine.
 MOD_RES 284 284 Phosphoserine.
 MOD_RES 379 379 Phosphoserine.
 MOD_RES 380 380 Phosphotyrosine.
 CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Cell junction; Cell projection; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Glycoprotein; Host-virus interaction; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding; Spliceosome; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 463 AA 
Protein Sequence
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK 60
GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT 120
SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL 180
FQECCPHSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT 240
MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG 300
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID TWSPSEWQMA 360
YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS 420
IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYSG KFF 463 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0042995; C:cell projection; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IMP:BHF-UCL.
 GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IMP:BHF-UCL.
 GO:0003697; F:single-stranded DNA binding; TAS:BHF-UCL.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0045716; P:positive regulation of low-density lipoprotein particle receptor biosynthetic process; IMP:BHF-UCL.
 GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:BHF-UCL.
 GO:0072369; P:regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0010988; P:regulation of low-density lipoprotein particle clearance; IMP:BHF-UCL.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1.
 IPR012987; ROK_N. 
Pfam
 PF00013; KH_1
 PF08067; ROKNT 
SMART
 SM00322; KH 
PROSITE
 PS50084; KH_TYPE_1 
PRINTS