CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018199
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heterogeneous nuclear ribonucleoprotein U 
Protein Synonyms/Alias
 hnRNP U; Scaffold attachment factor A; SAF-A 
Gene Name
 Hnrnpu 
Gene Synonyms/Alias
 Hnrpu 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
328PVRHLYTKDIDIHEVacetylation[1]
771RGNNRGYKNQSQGYNubiquitination[2]
789QGQFWGQKPWSQHYHacetylation[3, 4, 5, 6]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] 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]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] 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]
 [5] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Binds to pre-mRNA. Has high affinity for scaffold-attached region (SAR) DNA. Binds to double- and single- stranded DNA and RNA (By similarity). 
Sequence Annotation
 DOMAIN 8 42 SAP.
 DOMAIN 244 440 B30.2/SPRY.
 NP_BIND 480 487 ATP (Potential).
 REGION 690 715 RNA-binding RGG-box (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 4 4 Phosphoserine (By similarity).
 MOD_RES 58 58 Phosphoserine.
 MOD_RES 241 241 N6-acetyllysine (By similarity).
 MOD_RES 247 247 Phosphoserine.
 MOD_RES 328 328 N6-acetyllysine (By similarity).
 MOD_RES 492 492 N6-acetyllysine (By similarity).
 MOD_RES 500 500 N6-acetyllysine (By similarity).
 MOD_RES 527 527 N6-acetyllysine (By similarity).
 MOD_RES 541 541 N6-acetyllysine (By similarity).
 MOD_RES 611 611 N6-acetyllysine (By similarity).
 MOD_RES 709 709 Omega-N-methylated arginine (By
 MOD_RES 715 715 Dimethylated arginine; alternate (By
 MOD_RES 715 715 Omega-N-methylated arginine; alternate
 MOD_RES 789 789 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 800 AA 
Protein Sequence
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KADLMDRLQA ALDNEAGGRP AMEPGNGSLD 60
LGGDAAGRSG AGLEQEAAAG AEDDEEEEGI AALDGDQMEL GEENGAAGAA DAGAMEEEEA 120
ASEDENGDDQ GFQEGEDELG DEEEGAGDEN GHGEQQSQPP AAAAQQQPSQ QRGAGKEAAG 180
KSSGPTSLFA VTVAPPGARQ GQQQAGGDGK TEQKGGDKKR GVKRPREDHG RGYFEYIEEN 240
KYSRAKSPQP PVEEEDEHFD DTVVCLDTYN CDLHFKISRD RLSASSLTME SFAFLWAGGR 300
ASYGVSKGKV CFEMKVTEKI PVRHLYTKDI DIHEVRIGWS LTTSGMLLGE EEFSYGYSLK 360
GIKTCNCETE DYGEKFDEND VITCFANFET DEVELSYAKN GQDLGVAFKI SKEVLADRPL 420
FPHVLCHNCA VEFNFGQKEK PYFPIPEDCT FIQNVPLEDR VRGPKGPEEK KDCEVVMMIG 480
LPGAGKTTWV TKHAAENPGK YNILGTNTIM DKMMVAGFKK QMADTGKLNT LLQRAPQCLG 540
KFIEIAARKK RNFILDQTNV SAAAQRRKMC LFAGFQRKAV VVCPKDEDYK QRTQKKAEVE 600
GKDLPEHAVL KMKGNFTLPE VAECFDEITY VELQKEEAQK LLEQYKEESK KALPPEKKQN 660
TGSKKSNKNK SGKNQFNRGG GHRGRGGFNM RGGNFRGGAP GNRGGYNRRG NMPQRGGGGG 720
SGGIGYPYPR GPVFPGRGGY SNRGNYNRGG MPNRGNYNQN FRGRGNNRGY KNQSQGYNQW 780
QQGQFWGQKP WSQHYHQGYY 800 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IEA:Compara.
 GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
 GO:0070937; C:CRD-mediated mRNA stability complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0070934; P:CRD-mediated mRNA stabilization; IEA:Compara.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR008985; ConA-like_lec_gl_sf.
 IPR026745; hnRNP_U.
 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