CPLM-008514

Genbank Nucleotide ID

Heterogeneous nuclear ribonucleoprotein F

Protein Synonyms/Alias

hnRNP F; Nucleolin-like protein mcs94-1; Heterogeneous nuclear ribonucleoprotein F, N-terminally processed

Homo sapiens (Human)

Position	Peptide	Type	References
14	GGEGFVVKLRGLPWS	ubiquitination	[1, 2, 3, 4]
68	LGSEDDVKMALKKDR	ubiquitination	[5]
87	HRYIEVFKSHRTEMD	acetylation	[4, 6, 7]
87	HRYIEVFKSHRTEMD	ubiquitination	[1, 2, 3, 4, 5, 8, 9, 10]
98	TEMDWVLKHSGPNSA	acetylation	[4, 7, 11]
98	TEMDWVLKHSGPNSA	ubiquitination	[1, 2, 3, 4, 5, 8, 9, 10]
167	ASQELAEKALGKHKE	ubiquitination	[1, 2, 3, 4, 5, 8, 9, 10]
185	HRYIEVFKSSQEEVR	ubiquitination	[1, 2, 3, 4, 5, 8, 9, 12]
200	SYSDPPLKFMSVQRP	ubiquitination	[1, 2, 10]
224	RRYIGIVKQAGLERM	acetylation	[6]
224	RRYIGIVKQAGLERM	ubiquitination	[1, 2, 3, 4, 5, 8, 9, 10, 12, 13, 14]
299	HMRGLPYKATENDIY	ubiquitination	[1, 2, 4, 5, 8, 9, 10]

[1] 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]
[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] 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]
[5] 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]
[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] 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]
[8] 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]
[9] 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]
[10] 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]
[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] 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]
[13] 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]
[14] 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 heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state.

DOMAIN 13 85 RRM 1.
DOMAIN 111 188 RRM 2.
DOMAIN 289 366 RRM 3.
REGION 81 86 Interaction with RNA.
REGION 179 184 Interaction with RNA.
REGION 355 360 Interaction with RNA.
MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
MOD_RES 2 2 N-acetylmethionine; in Heterogeneous
MOD_RES 104 104 Phosphoserine.
MOD_RES 161 161 Phosphoserine.
MOD_RES 187 187 Phosphoserine.
MOD_RES 224 224 N6-acetyllysine.
CROSSLNK 72 72 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0000166; F:nucleotide binding; IEA:InterPro.
GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.

IPR012677; Nucleotide-bd_a/b_plait.
IPR000504; RRM_dom.
IPR012996; Znf_CHHC.

PF00076; RRM_1
PF08080; zf-RNPHF