UniProt Accession

 HNRPU_HUMAN; Q00839; O75507; Q8N174; Q96HY9; Q9BQ09 

Genbank Protein ID

 X65488; AF068846; BX323046; BC003367; BC003621; BC007950; BC024767; BC034925 

Genbank Nucleotide ID

 CAA46472.1; AAC19382.1; CAI11058.1; AAH03367.1; AAH03621.1; AAH07950.2; AAH24767.1; AAH34925.1 

Protein Name

 Heterogeneous nuclear ribonucleoprotein U 

Protein Synonyms/Alias

 hnRNP U; Scaffold attachment factor A; SAF-A; p120; pp120 

Gene Name

 HNRNPU 

Gene Synonyms/Alias

 HNRPU; SAFA; U21.1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
9	SSSPVNVKKLKVSEL	acetylation	[1]
9	SSSPVNVKKLKVSEL	ubiquitination	[2, 3]
10	SSPVNVKKLKVSELK	ubiquitination	[3]
17	KLKVSELKEELKKRR	acetylation	[1]
21	SELKEELKKRRLSDK	acetylation	[1]
28	KKRRLSDKGLKAELM	acetylation	[1]
181	QQQRGAAKEAAGKSS	ubiquitination	[4]
186	AAKEAAGKSSGPTSL	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
215	QQAGGKKKAEGGGGG	acetylation	[9]
215	QQAGGKKKAEGGGGG	ubiquitination	[4, 7]
234	APAAGDGKTEQKGGD	acetylation	[1, 10, 11, 12]
234	APAAGDGKTEQKGGD	ubiquitination	[7]
265	FEYIEENKYSRAKSP	acetylation	[1, 10, 12]
265	FEYIEENKYSRAKSP	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 13]
331	RASYGVSKGKVCFEM	ubiquitination	[4]
333	SYGVSKGKVCFEMKV	acetylation	[9]
333	SYGVSKGKVCFEMKV	ubiquitination	[1, 2, 3, 4, 6, 14]
339	GKVCFEMKVTEKIPV	ubiquitination	[1, 14]
343	FEMKVTEKIPVRHLY	acetylation	[1]
343	FEMKVTEKIPVRHLY	ubiquitination	[1, 3, 6]
352	PVRHLYTKDIDIHEV	acetylation	[1, 10, 11, 12, 15]
352	PVRHLYTKDIDIHEV	ubiquitination	[1, 3, 4, 5, 6, 7, 8, 14]
387	GYSLKGIKTCNCETE	ubiquitination	[1, 6]
433	QDLGVAFKISKEVLA	ubiquitination	[1, 3]
436	GVAFKISKEVLAGRP	ubiquitination	[1, 2, 3]
464	FNFGQKEKPYFPIPE	acetylation	[10]
464	FNFGQKEKPYFPIPE	ubiquitination	[2, 3, 4, 5, 6, 7, 8, 14]
510	IGLPGAGKTTWVTKH	ubiquitination	[3, 4]
516	GKTTWVTKHAAENPG	acetylation	[1, 10]
516	GKTTWVTKHAAENPG	ubiquitination	[1, 3, 4, 5, 6, 7, 8]
524	HAAENPGKYNILGTN	acetylation	[10]
524	HAAENPGKYNILGTN	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 13, 14, 16, 17]
536	GTNTIMDKMMVAGFK	ubiquitination	[1, 3, 5, 6, 7, 8]
543	KMMVAGFKKQMADTG	ubiquitination	[2, 5, 7, 8]
544	MMVAGFKKQMADTGK	ubiquitination	[3, 4]
551	KQMADTGKLNTLLQR	acetylation	[1, 10, 11, 12]
551	KQMADTGKLNTLLQR	ubiquitination	[1, 3, 4, 5, 6, 8]
565	RAPQCLGKFIEIAAR	acetylation	[10, 11]
565	RAPQCLGKFIEIAAR	ubiquitination	[2, 3, 4, 5, 6, 8, 13]
592	SAAAQRRKMCLFAGF	ubiquitination	[2, 6]
602	LFAGFQRKAVVVCPK	ubiquitination	[1, 3]
609	KAVVVCPKDEDYKQR	acetylation	[1, 10]
609	KAVVVCPKDEDYKQR	ubiquitination	[1]
614	CPKDEDYKQRTQKKA	acetylation	[1]
614	CPKDEDYKQRTQKKA	ubiquitination	[2, 4]
626	KKAEVEGKDLPEHAV	acetylation	[1, 10, 11, 12]
626	KKAEVEGKDLPEHAV	ubiquitination	[1, 3, 4, 5, 8]
635	LPEHAVLKMKGNFTL	acetylation	[1, 10, 11]
635	LPEHAVLKMKGNFTL	ubiquitination	[1, 2, 3, 4, 5, 8]
664	LQKEEAQKLLEQYKE	acetylation	[12]
664	LQKEEAQKLLEQYKE	ubiquitination	[4, 5, 6, 7, 8]
670	QKLLEQYKEESKKAL	acetylation	[1, 10, 11]
670	QKLLEQYKEESKKAL	ubiquitination	[3]
674	EQYKEESKKALPPEK	acetylation	[1, 10]
674	EQYKEESKKALPPEK	ubiquitination	[3]
675	QYKEESKKALPPEKK	ubiquitination	[3]
814	QGQFWGQKPWSQHYH	acetylation	[1, 9, 10, 11, 12, 15]
814	QGQFWGQKPWSQHYH	ubiquitination	[5, 7, 8]

Reference

 [1] 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]
 [2] 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]
 [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] 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]
 [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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] 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]
 [14] 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]
 [15] 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]
 [16] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [17] 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] 

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. 

Sequence Annotation

 DOMAIN 8 42 SAP.
 DOMAIN 267 464 B30.2/SPRY.
 NP_BIND 504 511 ATP (Potential).
 REGION 714 739 RNA-binding RGG-box.
 MOD_RES 2 2 N-acetylserine; partial.
 MOD_RES 4 4 Phosphoserine.
 MOD_RES 59 59 Phosphoserine.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 265 265 N6-acetyllysine.
 MOD_RES 271 271 Phosphoserine.
 MOD_RES 352 352 N6-acetyllysine.
 MOD_RES 516 516 N6-acetyllysine.
 MOD_RES 524 524 N6-acetyllysine.
 MOD_RES 551 551 N6-acetyllysine.
 MOD_RES 565 565 N6-acetyllysine.
 MOD_RES 635 635 N6-acetyllysine.
 MOD_RES 739 739 Dimethylated arginine; in A2780 ovarian
 MOD_RES 739 739 Omega-N-methylated arginine.
 MOD_RES 814 814 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Methylation; mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 825 AA 

Protein Sequence

Gene Ontology

 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
 GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. 

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