UniProt Accession

 HNRPC_HUMAN; P07910; D3DS19; D3DS22; P22628; Q53EX2; Q59FD3; Q5FWE8; Q86SF8; Q86U45; Q96HK7; Q96HM4; Q96IY5; Q9BTS3 

Genbank Protein ID

 M29063; M16342; BX161480; BX247961; BX247992; AB209527; AK223517; CH471078; CH471078; CH471078; CH471078; CH471078; CH471078; CH471078; BC003394; BC007052; BC008364; BC008423; BC066932; BC089438; BC108658; BC103758 

Genbank Nucleotide ID

 AAA36576.1; AAA52680.1; CAD61934.1; CAD62300.1; CAD62326.1; BAD92764.1; BAD97237.1; EAW66392.1; EAW66393.1; EAW66394.1; EAW66395.1; EAW66396.1; EAW66399.1; EAW66400.1; AAH03394.1; AAH07052.1; AAH08364.1; AAH08423.1; AAH66932.1; AAH89438.1; AAI08659.1; AAI03759.1 

Protein Name

 Heterogeneous nuclear ribonucleoproteins C1/C2 

Protein Synonyms/Alias

 hnRNP C1/C2 

Gene Name

 HNRNPC 

Gene Synonyms/Alias

 HNRPC 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
8	MASNVTNKTDPRSMN	ubiquitination	[1, 2]
29	NLNTLVVKKSDVEAI	ubiquitination	[1, 2, 3, 4, 5]
30	LNTLVVKKSDVEAIF	ubiquitination	[2]
39	DVEAIFSKYGKIVGC	ubiquitination	[1, 2, 4, 5]
42	AIFSKYGKIVGCSVH	ubiquitination	[2, 5]
50	IVGCSVHKGFAFVQY	ubiquitination	[1, 2, 5]
89	INLAAEPKVNRGKAG	ubiquitination	[2, 4, 5]
176	GKSGFNSKSGQRGSS	ubiquitination	[5]
189	SSKSGKLKGDDLQAI	ubiquitination	[2]
198	DDLQAIKKELTQIKQ	ubiquitination	[2, 4]
204	KKELTQIKQKVDSLL	ubiquitination	[2, 5]
206	ELTQIKQKVDSLLEN	ubiquitination	[2, 4, 5]
216	SLLENLEKIEKEQSK	ubiquitination	[5]
219	ENLEKIEKEQSKQAV	ubiquitination	[2, 5]
223	KIEKEQSKQAVEMKN	ubiquitination	[2, 5]
229	SKQAVEMKNDKSEEE	ubiquitination	[2]
232	AVEMKNDKSEEEQSS	acetylation	[6]
232	AVEMKNDKSEEEQSS	sumoylation	[7]
232	AVEMKNDKSEEEQSS	ubiquitination	[2]
243	EQSSSSVKKDETNVK	acetylation	[6]
243	EQSSSSVKKDETNVK	ubiquitination	[5]
244	QSSSSVKKDETNVKM	acetylation	[6]
244	QSSSSVKKDETNVKM	ubiquitination	[5]
284	DDQLELIKDDEKEAE	ubiquitination	[5]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [7] 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] 

Functional Description

 Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. 

Sequence Annotation

 DOMAIN 16 87 RRM.
 MOTIF 155 161 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 109 109 Phosphothreonine.
 MOD_RES 113 113 Phosphoserine.
 MOD_RES 115 115 Phosphoserine.
 MOD_RES 162 162 Phosphoserine.
 MOD_RES 166 166 Phosphoserine.
 MOD_RES 233 233 Phosphoserine.
 MOD_RES 241 241 Phosphoserine.
 MOD_RES 253 253 Phosphoserine.
 MOD_RES 260 260 Phosphoserine.
 MOD_RES 299 299 Phosphoserine.
 MOD_RES 306 306 Phosphoserine.
 CROSSLNK 250 250 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 306 AA 

Protein Sequence

Gene Ontology

 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0045120; C:pronucleus; IEA:Compara.
 GO:0003729; F:mRNA binding; IEA:Compara.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; NAS:HGNC.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. 

Interpro

 IPR017347; hnRNP_C_Raly.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS