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O60506 (HNRPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein Q

Short name=hnRNP Q
Alternative name(s):
Glycine- and tyrosine-rich RNA-binding protein
Short name=GRY-RBP
NS1-associated protein 1
Synaptotagmin-binding, cytoplasmic RNA-interacting protein
Gene names
Name:SYNCRIP
Synonyms:HNRPQ, NSAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.10 Ref.11 Ref.12 Ref.23 Ref.27

Subunit structure

Isoform 1 is a component of the APOB mRNA editosome complex and interacts with APOBEC1 and A1CF (APOBEC1 complementation factor). Part of a complex associated with the FOS mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR, HNRPD and SYNCRIP. Isoform 3 interacts with HNRPR. Interacts with POLR2A hyperphosphorylated C-terminal domain. Interacts with minute virus of mice (MVM) NS1 protein. Isoform 1, isoform 2 and isoform 3 interact with SMN. Isoform 3 interacts through its C-terminal domain with SYT7, SYT8 and SYT9 By similarity. The non-phosphorylated and phosphorylated forms are colocalized with PAIP1 in polysomes By similarity. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 By similarity. Identified in the spliceosome C complex. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with GTPBP1. Component of the GAIT complex; in humans the complex assembly seems to be a two-step process in which EPRS first associates with SYNCRIP to form a pre-GAIT complex which is deficient in GAIT element binding. Ref.1 Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.22 Ref.23 Ref.26

Subcellular location

Cytoplasm. Microsome By similarity. Endoplasmic reticulum By similarity. Nucleus By similarity. Note: The tyrosine phosphorylated form bound to RNA is found in microsomes By similarity. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.3 Ref.18 Ref.23

Isoform 1: Nucleusnucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.18 Ref.23

Isoform 2: Nucleusnucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.18 Ref.23

Isoform 3: Nucleusnucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.18 Ref.23

Tissue specificity

Ubiquitously expressed. Detected in heart, brain, pancreas, placenta, spleen, lung, liver, skeletal muscle, kidney, thymus, prostate, uterus, small intestine, colon, peripheral blood and testis. Ref.11

Domain

The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box) may be involved in RNA-binding and protein-protein interactions. It is methylated by PRMT1, and essential for nuclear localization.

Post-translational modification

Phosphorylated on tyrosine. The membrane-bound form found in microsomes is phosphorylated in vitro by insulin receptor tyrosine kinase (INSR). Phosphorylation is inhibited upon binding to RNA, whereas the cytoplasmic form is poorly phosphorylated By similarity. Ref.9

Sequence similarities

Contains 3 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAH15575.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 413.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA processing
mRNA splicing
Translation regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCRD-mediated mRNA stabilization

Inferred from mutant phenotype Ref.23. Source: UniProtKB

RNA processing

Traceable author statement Ref.1. Source: ProtInc

RNA splicing

Traceable author statement Ref.1. Source: ProtInc

cellular response to interferon-gamma

Inferred from direct assay Ref.16. Source: UniProtKB

mRNA splicing, via spliceosome

Inferred by curator Ref.15. Source: UniProtKB

negative regulation of translation

Inferred from direct assay Ref.27. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCRD-mediated mRNA stability complex

Inferred from direct assay Ref.23. Source: UniProtKB

GAIT complex

Inferred from direct assay Ref.16Ref.27. Source: UniProtKB

catalytic step 2 spliceosome

Inferred from direct assay Ref.15. Source: UniProtKB

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

histone pre-mRNA 3'end processing complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement Ref.1. Source: ProtInc

ribonucleoprotein complex

Inferred from direct assay Ref.16Ref.18. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

poly(A) binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60506-1)

Also known as: hnRNP Q3;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O60506-2)

Also known as: hnRNP Q2;

The sequence of this isoform differs from the canonical sequence as follows:
     302-336: Missing.
Note: May be due to a competing donor splice site.
Isoform 3 (identifier: O60506-3)

Also known as: hnRNP Q1;

The sequence of this isoform differs from the canonical sequence as follows:
     550-623: VRGARGGRGG...YQDTFGQQWK → QGKGVEAGPDLLQ
Note: May be due to a competing donor splice site and to an exon inclusion.
Isoform 4 (identifier: O60506-4)

The sequence of this isoform differs from the canonical sequence as follows:
     302-336: Missing.
     550-623: VRGARGGRGG...YQDTFGQQWK → QGKGVEAGPDLLQ
Note: May be due to a competing donor splice site and to an exon inclusion. No experimental confirmation available.
Isoform 5 (identifier: O60506-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: Missing.
     153-163: YSGQQPSVGTE → MEDHLQIPFIQ
     550-623: VRGARGGRGG...YQDTFGQQWK → QGKGVEAGPDLLQ
Note: May be due to a competing donor splice site and to an exon inclusion.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 623622Heterogeneous nuclear ribonucleoprotein Q
PRO_0000081867

Regions

Domain162 – 24180RRM 1
Domain243 – 32583RRM 2
Domain338 – 40871RRM 3
Repeat448 – 45031-1
Repeat451 – 45331-2
Repeat460 – 46452-1
Repeat469 – 47242-2
Repeat478 – 48031-3
Repeat485 – 48842-3
Repeat498 – 50031-4
Repeat526 – 52831-5
Repeat539 – 54131-6
Repeat554 – 55631-7
Repeat557 – 55931-8
Region400 – 561162Interaction with APOBEC1
Region448 – 5591128 X 3 AA repeats of R-G-G
Region460 – 488293 X 4 AA repeats of Y-Y-G-Y
Region518 – 54932Interaction with SMN
Motif564 – 57815Bipartite nuclear localization signal Potential
Compositional bias431 – 4344Poly-Tyr

Amino acid modifications

Modified residue21N-acetylalanine Ref.21
Modified residue2211N6-acetyllysine Ref.24
Modified residue3631N6-acetyllysine Ref.24
Modified residue3731Phosphotyrosine Ref.9
Modified residue4441Asymmetric dimethylarginine; by PRMT1; alternate Ref.28
Modified residue4441Omega-N-methylarginine; by PRMT1; alternate Ref.28
Modified residue4961Omega-N-methylarginine; by PRMT1 Ref.28
Modified residue5101Asymmetric dimethylarginine; by PRMT1 Ref.28
Modified residue5181Asymmetric dimethylarginine; by PRMT1; alternate Ref.28
Modified residue5181Omega-N-methylarginine; by PRMT1; alternate Ref.28
Modified residue5261Asymmetric dimethylarginine; by PRMT1; alternate Ref.28
Modified residue5261Omega-N-methylarginine; by PRMT1; alternate Ref.28
Modified residue5361Asymmetric dimethylarginine; by PRMT1; alternate Ref.28
Modified residue5361Omega-N-methylarginine; by PRMT1; alternate Ref.28
Modified residue5391Asymmetric dimethylarginine; by PRMT1; alternate Ref.28
Modified residue5391Omega-N-methylarginine; by PRMT1; alternate Ref.28
Modified residue5871Phosphoserine Ref.20
Cross-link123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.19

Natural variations

Alternative sequence1 – 152152Missing in isoform 5.
VSP_009581
Alternative sequence153 – 16311YSGQQPSVGTE → MEDHLQIPFIQ in isoform 5.
VSP_009582
Alternative sequence302 – 33635Missing in isoform 2 and isoform 4.
VSP_009583
Alternative sequence550 – 62374VRGAR…GQQWK → QGKGVEAGPDLLQ in isoform 3, isoform 4 and isoform 5.
VSP_009584

Experimental info

Sequence conflict2651K → Q in AAD38198. Ref.1
Sequence conflict2871G → S Ref.2
Sequence conflict2871G → S Ref.3
Sequence conflict2881F → S in AAH40844. Ref.7
Isoform 3:
Sequence conflict550 – 5512QG → V in AAK59705. Ref.5

Secondary structure

.............. 623
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (hnRNP Q3) [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 0669FA604E8FBBDF

FASTA62369,603
        10         20         30         40         50         60 
MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER 

        70         80         90        100        110        120 
AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD 

       130        140        150        160        170        180 
EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP 

       190        200        210        220        230        240 
LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV 

       250        260        270        280        290        300 
ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA 

       310        320        330        340        350        360 
QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKAFSQ 

       370        380        390        400        410        420 
FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR 

       430        440        450        460        470        480 
QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG 

       490        500        510        520        530        540 
YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG 

       550        560        570        580        590        600 
GAQQQRGRGV RGARGGRGGN VGGKRKADGY NQPDSKRRQT NNQNWGSQPI AQQPLQGGDH 

       610        620 
SGNYGYKSEN QEFYQDTFGQ QWK 

« Hide

Isoform 2 (hnRNP Q2) [UniParc].

Checksum: 907A3EFBF5502D3F
Show »

FASTA58865,682
Isoform 3 (hnRNP Q1) [UniParc].

Checksum: 32F5C37178197E45
Show »

FASTA56262,656
Isoform 4 [UniParc].

Checksum: C17388F6F991A127
Show »

FASTA52758,736
Isoform 5 [UniParc].

Checksum: 4F1AD0FE9570F7BD
Show »

FASTA41046,328

References

« Hide 'large scale' references
[1]"A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice."
Harris C.E., Boden R.A., Astell C.R.
J. Virol. 73:72-80(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH NS1.
Tissue: Cervix carcinoma.
[2]"Cloning of human and mouse GRY-RBP cDNA."
Du G., Pan M., Zhou Y., Chen J., Yao H., Yuan J., Qiang B.
Chin. Sci. Bull. 45:343-349(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"SMN interacts with a novel family of hnRNP and spliceosomal proteins."
Mourelatos Z., Abel L., Yong J., Kataoka N., Dreyfuss G.
EMBO J. 20:5443-5452(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION IN MRNA PROCESSING, SUBCELLULAR LOCATION, ASSOCIATION WITH THE SPLICEOSOME, INTERACTION WITH SMN AND HNRPR.
Tissue: Cervix carcinoma.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Liver.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/3; 4 AND 5).
Tissue: Eye, Lung and Urinary bladder.
[8]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 43-60 AND 370-381, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[9]"Signaling initiated by overexpression of the fibroblast growth factor receptor-1 investigated by mass spectrometry."
Hinsby A.M., Olsen J.V., Bennett K.L., Mann M.
Mol. Cell. Proteomics 2:29-36(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-373.
Tissue: Kidney.
[10]"A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex."
Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.
Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; PABPC1; PAIP1 AND CSDE1.
Tissue: Placenta.
[11]"Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome."
Lau P.P., Chang B.-H., Chan L.
Biochem. Biophys. Res. Commun. 282:977-983(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOB MRNA EDITING, INTERACTION WITH APOBEC1, TISSUE SPECIFICITY.
[12]"Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing."
Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A., Scott J., Davidson N.O.
J. Biol. Chem. 276:10272-10283(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOB MRNA EDITING, RNA-BINDING, INTERACTION WITH A1CF AND APOBEC1.
[13]"Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex."
Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M.
Nat. Genet. 20:46-50(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SPLICEOSOME.
[14]"Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing."
Carty S.M., Greenleaf A.L.
Mol. Cell. Proteomics 1:598-610(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POLR2A.
[15]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[16]"Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation."
Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.
Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE GAIT COMPLEX.
[17]"The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization."
Passos D.O., Quaresma A.J., Kobarg J.
Biochem. Biophys. Res. Commun. 346:517-525(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION BY PRMT1.
[18]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-123.
Tissue: Mammary cancer.
[20]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[22]"Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity."
Arif A., Jia J., Mukhopadhyay R., Willard B., Kinter M., Fox P.L.
Mol. Cell 35:164-180(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPRS.
[23]"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[24]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GTPBP1.
[27]"Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
Arif A., Chatterjee P., Moodt R.A., Fox P.L.
Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX.
[28]"A Y2H-seq approach defines the human protein methyltransferase interactome."
Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P., Meierhofer D., Benlasfer N., Valovka T., Timmermann B., Wanker E.E., Sauer S., Stelzl U.
Nat. Methods 10:339-342(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-444; ARG-496; ARG-510; ARG-518; ARG-526; ARG-536 AND ARG-539 BY PRMT1, IDENTIFICATION BY MASS SPECTROMETRY.
[29]"Solution structure of the RNA binding domain in heterogeneous nuclear ribonucleoprotein Q."
RIKEN structural genomics initiative (RSGI)
Submitted (SEP-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 334-423.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF155568 mRNA. Translation: AAD38198.1.
AF037448 mRNA. Translation: AAC12926.1.
AY034481 mRNA. Translation: AAK59703.1.
AY034482 mRNA. Translation: AAK59704.1.
AY034483 mRNA. Translation: AAK59705.1.
AK222776 mRNA. Translation: BAD96496.1.
AL136082 Genomic DNA. Translation: CAI20446.1.
AL136082 Genomic DNA. Translation: CAI20447.1.
CH471051 Genomic DNA. Translation: EAW48625.1.
CH471051 Genomic DNA. Translation: EAW48626.1.
CH471051 Genomic DNA. Translation: EAW48629.1.
CH471051 Genomic DNA. Translation: EAW48630.1.
BC015575 mRNA. Translation: AAH15575.1. Sequence problems.
BC032643 mRNA. Translation: AAH32643.1.
BC040844 mRNA. Translation: AAH40844.1.
RefSeqNP_001153145.1. NM_001159673.1.
NP_001153146.1. NM_001159674.1.
NP_001153147.1. NM_001159675.1.
NP_001153148.1. NM_001159676.1.
NP_001153149.1. NM_001159677.1.
NP_001240700.1. NM_001253771.1.
NP_006363.4. NM_006372.4.
XP_005248694.1. XM_005248637.1.
UniGeneHs.571177.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGUNMR-A334-423[»]
ProteinModelPortalO60506.
SMRO60506. Positions 96-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115755. 137 interactions.
DIPDIP-35540N.
IntActO60506. 36 interactions.
MINTMINT-2796763.

PTM databases

PhosphoSiteO60506.

Proteomic databases

PaxDbO60506.
PRIDEO60506.

Protocols and materials databases

DNASU10492.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355238; ENSP00000347380; ENSG00000135316. [O60506-3]
ENST00000369622; ENSP00000358635; ENSG00000135316. [O60506-1]
GeneID10492.
KEGGhsa:10492.
UCSCuc003pku.3. human. [O60506-1]
uc003pkv.3. human. [O60506-3]
uc003pkw.3. human. [O60506-4]
uc003pkx.3. human. [O60506-5]
uc003pkz.2. human. [O60506-2]

Organism-specific databases

CTD10492.
GeneCardsGC06M086317.
HGNCHGNC:16918. SYNCRIP.
HPACAB010895.
HPA041275.
neXtProtNX_O60506.
PharmGKBPA134985065.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258596.
HOVERGENHBG051917.
InParanoidO60506.
KOK13160.
OMAKSDNQEF.
OrthoDBEOG73JKW2.
PhylomeDBO60506.
TreeFamTF314932.

Gene expression databases

ArrayExpressO60506.
BgeeO60506.
CleanExHS_SYNCRIP.
GenevestigatorO60506.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR006535. HnRNP_R/Q_splicing_fac.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01648. hnRNP-R-Q. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYNCRIP. human.
EvolutionaryTraceO60506.
GeneWikiSYNCRIP.
GenomeRNAi10492.
NextBio39814.
PROO60506.

Entry information

Entry nameHNRPQ_HUMAN
AccessionPrimary (citable) accession number: O60506
Secondary accession number(s): E1P501 expand/collapse secondary AC list , E1P502, Q53H05, Q5TCG2, Q5TCG3, Q8IW78, Q8N599, Q96LC1, Q96LC2, Q9Y583
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM