UniProt Accession

 HNRH3_HUMAN; P31942; A8K682; B3KRE1; Q9BSX1; Q9NP53; Q9NP96; Q9NPA7; Q9NPI4; Q9UFU4; Q9Y4J5 

Genbank Protein ID

 L32610; AF132360; AF132360; AF132360; AF132360; AF132360; AF132360; AF132361; AF132362; AF132363; AF132364; AK091411; AK291547; AL117395; CH471083; CH471083; BC004511; BC039824 

Genbank Nucleotide ID

 AAD45179.1; AAF68843.1; AAF68844.1; AAF68845.1; AAF68846.1; AAF68847.1; AAF68848.1; AAF68849.1; AAF68850.1; AAF68851.1; AAF68852.1; BAG52353.1; BAF84236.1; CAB55897.1; EAW54281.1; EAW54282.1; AAH04511.2; AAH39824.1 

Protein Name

 Heterogeneous nuclear ribonucleoprotein H3 

Protein Synonyms/Alias

 hnRNP H3; Heterogeneous nuclear ribonucleoprotein 2H9; hnRNP 2H9 

Gene Name

 HNRNPH3 

Gene Synonyms/Alias

 HNRPH3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MDWVMKHNGPNDA	ubiquitination	[1, 2, 3, 4, 5]
67	AFVQFASKEIAENAL	ubiquitination	[2, 4, 6, 7, 8, 9]
76	IAENALGKHKERIGH	ubiquitination	[4, 6, 9]
78	ENALGKHKERIGHRY	ubiquitination	[4]
97	RSSRSEIKGFYDPPR	ubiquitination	[1, 4, 5, 9]

Reference

 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 

Functional Description

 Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction. 

Sequence Annotation

 DOMAIN 16 93 RRM 1.
 DOMAIN 195 270 RRM 2.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 121 121 Asymmetric dimethylarginine.
 MOD_RES 216 216 Phosphoserine.
 MOD_RES 287 287 Omega-N-methylarginine.
 MOD_RES 298 298 Phosphoserine.
 MOD_RES 314 314 Phosphothreonine.  

Keyword

 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Methylation; mRNA processing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 346 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IDA:HPA.
 GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; NAS:UniProtKB. 

Interpro

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

Pfam

  

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS