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Reviewed, UniProtKB/Swiss-Prot O60506 (HNRPQ_HUMAN)

Last modified February 9, 2010. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Heterogeneous nuclear ribonucleoprotein Q
      Short name=hnRNP Q
      Short name=hnRNP-Q
Alternative name(s):
    Synaptotagmin-binding, cytoplasmic RNA-interacting protein
    Glycine- and tyrosine-rich RNA-binding protein
    GRY-RBP
    NS1-associated protein 1
Gene names
Name: SYNCRIP
Synonyms: HNRPQ, NSAP1
OrganismHomo sapiens (Human) [Complete 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. Ref.3 Ref.10 Ref.11 Ref.12 Ref.21

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, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. 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. Ref.3 Ref.11 Ref.12 Ref.1 Ref.14

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.21 Ref.16

Isoform 1: Nucleusnucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.21 Ref.16

Isoform 2: Nucleusnucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.21 Ref.16

Isoform 3: Nucleusnucleoplasm By similarity. Note: Expressed predominantly in the nucleoplasm By similarity. Ref.3 Ref.21 Ref.16

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 may be involved in RNA-binding and protein-protein interactions.

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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.18

Sequence similarities

Contains 3 RRM (RNA recognition motif) domains.

Sequence caution

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

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA processing
mRNA splicing
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processCRD-mediated mRNA stabilization Ref.21

Inferred from mutant phenotype. Source: UniProtKB

RNA splicing Ref.1

Traceable author statement. Source: ProtInc

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentCRD-mediated mRNA stability complex Ref.21

Inferred from direct assay. 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

microsome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

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.
Note: Expressed predominantly in the nucleoplasm (By similarity). Ref.3 Ref.21 Ref.16
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: Expressed predominantly in the nucleoplasm (By similarity). Ref.3 Ref.21 Ref.16 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: Expressed predominantly in the nucleoplasm (By similarity). Ref.3 Ref.21 Ref.16 May be due to a competing donor splice site and to an exon inclusion.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflict550 – 5512QG → V in AAK59705. Ref.5
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
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.20
Modified residue2211N6-acetyllysine Ref.22
Modified residue3631N6-acetyllysine Ref.22
Modified residue3731Phosphotyrosine Ref.9
Modified residue5871Phosphoserine Ref.18
Cross-link123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17

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

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).

Checksum: 907A3EFBF5502D3F
Show »

FASTA58865,682
Isoform 3 (hnRNP Q1).

Checksum: 32F5C37178197E45
Show »

FASTA56262,656
Isoform 4.

Checksum: C17388F6F991A127
Show »

FASTA52758,736
Isoform 5.

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: 9847309] [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: 11574476] [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: 14574404] [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: 15489334] [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, 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: 12601080] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, 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: 11051545] [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: 11352648] [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: 11134005] [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: 9731529] [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: 12376575] [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: 11991638] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
[16]"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: 17289661] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"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: 17370265] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-123, MASS SPECTROMETRY.
[18]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, MASS SPECTROMETRY.
[19]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[21]"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: 19029303] [Abstract]
Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-363, MASS SPECTROMETRY.
[23]"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.
BC015575 mRNA. Translation: AAH15575.1. Sequence problems.
BC032643 mRNA. Translation: AAH32643.1.
BC040844 mRNA. Translation: AAH40844.1.
IPIIPI00018140.
IPI00402182.
IPI00402183.
IPI00402184.
IPI00402185.
RefSeqNP_001153145.1.
NP_001153146.1.
NP_001153147.1.
NP_001153148.1.
NP_001153149.1.
NP_006363.4.
UniGeneHs.571177

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DGUNMR-A334-423[»]
SMRO60506. Positions 162-408.
ModBaseSearch...

Protein-protein interaction databases

IntActO60506. 15 interactions.
STRINGO60506.

PTM databases

PhosphoSiteO60506.

Proteomic databases

PRIDEO60506.

Genome annotation databases

EnsemblENST00000369622; ENSP00000358635; ENSG00000135316; Homo sapiens. [Genome view]
GeneID10492.
KEGGhsa:10492.
UCSCuc003pkw.1. human.
uc003pkx.1. human.
uc003pkz.1. human.
uc003pla.1. human.

Organism-specific databases

CTD10492.
GeneCardsGC06M086377.
H-InvDBHIX0006046.
HGNCHGNC:16918. SYNCRIP.
HPACAB010895.
PharmGKBPA134985065.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19478.
HOVERGENO60506.
InParanoidO60506.
OMATHMYDEY.
OrthoDBEOG9TF351.
PhylomeDBO60506.

Gene expression databases

ArrayExpressO60506.
BgeeO60506.
CleanExHS_SYNCRIP.
GenevestigatorO60506.
GermOnlineENSG00000135316. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR006535. HnRNP_R/Q_splicing_fac.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 3 hits.
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 Resources

NextBio39814.

Entry information

Entry nameHNRPQ_HUMAN
AccessionPrimary (citable) accession number: O60506
Secondary accession number(s): Q53H05 expand/collapse secondary AC list , 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: February 9, 2010
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 6

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents