UniProt Accession

 RBM39_HUMAN; Q14498; A2RRD3; A5D8W2; B0BLV3; E1P5S0; E1P5S1; Q14499 

Genbank Protein ID

 L10910; L10911; AK299678; AL357374; AL357374; CH471077; CH471077; CH471077; CH471077; BC131543; BC141835; BC158172 

Genbank Nucleotide ID

 AAA16346.1; AAA16347.1; BAG61586.1; CAC11118.1; CAC11119.1; EAW76159.1; EAW76161.1; EAW76162.1; EAW76163.1; AAI31544.1; AAI41836.1; AAI58173.1 

Protein Name

 RNA-binding protein 39 

Protein Synonyms/Alias

 Hepatocellular carcinoma protein 1; RNA-binding motif protein 39; RNA-binding region-containing protein 2; Splicing factor HCC1 

Gene Name

 RBM39 

Gene Synonyms/Alias

 HCC1; RNPC2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
119	IGLPHSIKLSRRRSR	ubiquitination	[1, 2, 3, 4, 5]
178	EFFSTVGKVRDVRMI	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
232	VQASQAEKNRAAAMA	ubiquitination	[2, 3, 4, 8]
244	AMANNLQKGSAGPMR	ubiquitination	[2, 4, 8, 9]
322	ELAGRPMKVGHVTER	ubiquitination	[4]
477	AQGNVYVKCPSIAAA	ubiquitination	[4]

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] 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]
 [3] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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] 

Functional Description

 Transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha and ESR2/ER-beta, and JUN/AP-1 (By similarity). May be involved in pre-mRNA splicing process. 

Sequence Annotation

 DOMAIN 153 230 RRM 1.
 DOMAIN 250 328 RRM 2.
 DOMAIN 445 508 RRM 3.
 REGION 291 406 Interaction with JUN (By similarity).
 REGION 291 355 Activating domain (By similarity).
 REGION 355 406 Interaction with ESR1 and ESR2 (By
 REGION 406 530 Interaction with NCOA6 (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 95 95 Phosphotyrosine.
 MOD_RES 97 97 Phosphoserine.
 MOD_RES 100 100 Phosphoserine.
 MOD_RES 136 136 Phosphoserine.
 MOD_RES 146 146 Phosphothreonine.
 MOD_RES 334 334 Phosphoserine.
 MOD_RES 337 337 Phosphoserine.
 MOD_RES 341 341 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Activator; Alternative splicing; Complete proteome; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 530 AA 

Protein Sequence

Gene Ontology

 GO:0005813; C:centrosome; IDA:HPA.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:ProtInc.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006396; P:RNA processing; TAS:ProtInc.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR006509; CC1_SF.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS