UniProt Accession

 HNRPQ_HUMAN; O60506; E1P501; E1P502; Q53H05; Q5TCG2; Q5TCG3; Q8IW78; Q8N599; Q96LC1; Q96LC2; Q9Y583 

Genbank Protein ID

 AF155568; AF037448; AY034481; AY034482; AY034483; AK222776; AL136082; AL136082; CH471051; CH471051; CH471051; CH471051; BC015575; BC032643; BC040844 

Genbank Nucleotide ID

 AAD38198.1; AAC12926.1; AAK59703.1; AAK59704.1; AAK59705.1; BAD96496.1; CAI20446.1; CAI20447.1; EAW48625.1; EAW48626.1; EAW48629.1; EAW48630.1; AAH15575.1; AAH32643.1; AAH40844.1 

Protein Name

 Heterogeneous nuclear ribonucleoprotein Q 

Protein Synonyms/Alias

 hnRNP Q; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protein 1; Synaptotagmin-binding, cytoplasmic RNA-interacting protein 

Gene Name

 SYNCRIP 

Gene Synonyms/Alias

 HNRPQ; NSAP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
81	LAVLQQFKDSDLSHV	ubiquitination	[1]
111	QREKQGTKVADSSKG	ubiquitination	[1]
117	TKVADSSKGPDEAKI	ubiquitination	[1]
123	SKGPDEAKIKALLER	ubiquitination	[2]
168	GTEIFVGKIPRDLFE	ubiquitination	[1]
213	AFVTFCTKEAAQEAV	methylation	[3]
221	EAAQEAVKLYNNHEI	acetylation	[4, 5]
221	EAAQEAVKLYNNHEI	ubiquitination	[1, 5, 6, 7, 8, 9]
312	RLMSGKVKVWGNVGT	ubiquitination	[1]
336	PDPEVMAKVKVLFVR	ubiquitination	[1, 10]
356	VTEEILEKAFSQFGK	ubiquitination	[1, 8, 9]
363	KAFSQFGKLERVKKL	acetylation	[4]
363	KAFSQFGKLERVKKL	ubiquitination	[1, 5, 6, 7, 8, 9, 10, 11]
371	LERVKKLKDYAFIHF	ubiquitination	[7, 8]
386	DERDGAVKAMEEMNG	ubiquitination	[1]
394	AMEEMNGKDLEGENI	ubiquitination	[9]
407	NIEIVFAKPPDQKRK	ubiquitination	[1, 9]

Reference

 [1] 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]
 [2] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [3] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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

 Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD- mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma- induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. 

Sequence Annotation

 DOMAIN 162 241 RRM 1.
 DOMAIN 243 325 RRM 2.
 DOMAIN 338 408 RRM 3.
 REPEAT 448 450 1-1.
 REPEAT 451 453 1-2.
 REPEAT 460 464 2-1.
 REPEAT 469 472 2-2.
 REPEAT 478 480 1-3.
 REPEAT 485 488 2-3.
 REPEAT 498 500 1-4.
 REPEAT 526 528 1-5.
 REPEAT 539 541 1-6.
 REPEAT 554 556 1-7.
 REPEAT 557 559 1-8.
 REGION 400 561 Interaction with APOBEC1.
 REGION 448 559 8 X 3 AA repeats of R-G-G.
 REGION 460 488 3 X 4 AA repeats of Y-Y-G-Y.
 REGION 518 549 Interaction with SMN.
 MOTIF 564 578 Bipartite nuclear localization signal
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 221 221 N6-acetyllysine.
 MOD_RES 363 363 N6-acetyllysine.
 MOD_RES 373 373 Phosphotyrosine.
 MOD_RES 444 444 Asymmetric dimethylarginine; by PRMT1;
 MOD_RES 444 444 Omega-N-methylarginine; by PRMT1;
 MOD_RES 496 496 Omega-N-methylarginine; by PRMT1.
 MOD_RES 510 510 Asymmetric dimethylarginine; by PRMT1.
 MOD_RES 518 518 Asymmetric dimethylarginine; by PRMT1;
 MOD_RES 518 518 Omega-N-methylarginine; by PRMT1;
 MOD_RES 536 536 Asymmetric dimethylarginine; by PRMT1;
 MOD_RES 536 536 Omega-N-methylarginine; by PRMT1;
 MOD_RES 539 539 Asymmetric dimethylarginine; by PRMT1;
 MOD_RES 539 539 Omega-N-methylarginine; by PRMT1;
 MOD_RES 587 587 Phosphoserine.
 CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Host-virus interaction; Isopeptide bond; Methylation; Microsome; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome; Translation regulation; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 623 AA 

Protein Sequence

Gene Ontology

 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008143; F:poly(A) RNA binding; IEA:Compara.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
 GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR006535; HnRNP_R/Q_splicing_fac.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

 PF00076; RRM_1 

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS