Full text data of SYNCRIP
SYNCRIP
(HNRPQ, NSAP1)
[Confidence: low (only semi-automatic identification from reviews)]
Heterogeneous nuclear ribonucleoprotein Q; hnRNP Q (Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protein 1; Synaptotagmin-binding, cytoplasmic RNA-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Heterogeneous nuclear ribonucleoprotein Q; hnRNP Q (Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protein 1; Synaptotagmin-binding, cytoplasmic RNA-interacting protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O60506
ID HNRPQ_HUMAN Reviewed; 623 AA.
AC O60506; E1P501; E1P502; Q53H05; Q5TCG2; Q5TCG3; Q8IW78; Q8N599;
read moreAC Q96LC1; Q96LC2; Q9Y583;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein Q;
DE Short=hnRNP Q;
DE AltName: Full=Glycine- and tyrosine-rich RNA-binding protein;
DE Short=GRY-RBP;
DE AltName: Full=NS1-associated protein 1;
DE AltName: Full=Synaptotagmin-binding, cytoplasmic RNA-interacting protein;
GN Name=SYNCRIP; Synonyms=HNRPQ, NSAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH NS1.
RC TISSUE=Cervix carcinoma;
RX PubMed=9847309;
RA Harris C.E., Boden R.A., Astell C.R.;
RT "A novel heterogeneous nuclear ribonucleoprotein-like protein
RT interacts with NS1 of the minute virus of mice.";
RL J. Virol. 73:72-80(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Du G., Pan M., Zhou Y., Chen J., Yao H., Yuan J., Qiang B.;
RT "Cloning of human and mouse GRY-RBP cDNA.";
RL Chin. Sci. Bull. 45:343-349(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION IN MRNA
RP PROCESSING, SUBCELLULAR LOCATION, ASSOCIATION WITH THE SPLICEOSOME,
RP AND INTERACTION WITH SMN AND HNRPR.
RC TISSUE=Cervix carcinoma;
RX PubMed=11574476; DOI=10.1093/emboj/20.19.5443;
RA Mourelatos Z., Abel L., Yong J., Kataoka N., Dreyfuss G.;
RT "SMN interacts with a novel family of hnRNP and spliceosomal
RT proteins.";
RL EMBO J. 20:5443-5452(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/3; 4 AND 5).
RC TISSUE=Eye, Lung, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 43-60 AND 370-381, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION AT
RP TYR-373.
RC TISSUE=Kidney;
RX PubMed=12601080; DOI=10.1074/mcp.M200075-MCP200;
RA Hinsby A.M., Olsen J.V., Bennett K.L., Mann M.;
RT "Signaling initiated by overexpression of the fibroblast growth factor
RT receptor-1 investigated by mass spectrometry.";
RL Mol. Cell. Proteomics 2:29-36(2003).
RN [10]
RP FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION
RP IN A COMPLEX WITH HNRPD; PABPC1; PAIP1 AND CSDE1.
RC TISSUE=Placenta;
RX PubMed=11051545; DOI=10.1016/S0092-8674(00)00102-1;
RA Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
RA Shyu A.-B.;
RT "A mechanism for translationally coupled mRNA turnover: interaction
RT between the poly(A) tail and a c-fos RNA coding determinant via a
RT protein complex.";
RL Cell 103:29-40(2000).
RN [11]
RP FUNCTION IN APOB MRNA EDITING, INTERACTION WITH APOBEC1, AND TISSUE
RP SPECIFICITY.
RX PubMed=11352648; DOI=10.1006/bbrc.2001.4679;
RA Lau P.P., Chang B.-H., Chan L.;
RT "Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
RT component of apobec-1 editosome.";
RL Biochem. Biophys. Res. Commun. 282:977-983(2001).
RN [12]
RP FUNCTION IN APOB MRNA EDITING, RNA-BINDING, AND INTERACTION WITH A1CF
RP AND APOBEC1.
RX PubMed=11134005; DOI=10.1074/jbc.M006435200;
RA Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S.,
RA Jarmuz A., Scott J., Davidson N.O.;
RT "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein
RT that interacts with both apobec-1 and apobec-1 complementation factor
RT to modulate C to U editing.";
RL J. Biol. Chem. 276:10272-10283(2001).
RN [13]
RP IDENTIFICATION IN SPLICEOSOME.
RX PubMed=9731529; DOI=10.1038/1700;
RA Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P.,
RA Sleeman J., Lamond A.I., Mann M.;
RT "Mass spectrometry and EST-database searching allows characterization
RT of the multi-protein spliceosome complex.";
RL Nat. Genet. 20:46-50(1998).
RN [14]
RP INTERACTION WITH POLR2A.
RX PubMed=12376575; DOI=10.1074/mcp.M200029-MCP200;
RA Carty S.M., Greenleaf A.L.;
RT "Hyperphosphorylated C-terminal repeat domain-associating proteins in
RT the nuclear proteome link transcription to DNA/chromatin modification
RT and RNA processing.";
RL Mol. Cell. Proteomics 1:598-610(2002).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [16]
RP IDENTIFICATION IN THE GAIT COMPLEX.
RX PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
RA Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
RA Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
RT "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
RT specific silencing of translation.";
RL Cell 119:195-208(2004).
RN [17]
RP METHYLATION BY PRMT1.
RX PubMed=16765914; DOI=10.1016/j.bbrc.2006.05.152;
RA Passos D.O., Quaresma A.J., Kobarg J.;
RT "The methylation of the C-terminal region of hnRNPQ (NSAP1) is
RT important for its nuclear localization.";
RL Biochem. Biophys. Res. Commun. 346:517-525(2006).
RN [18]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [19]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP INTERACTION WITH EPRS.
RX PubMed=19647514; DOI=10.1016/j.molcel.2009.05.028;
RA Arif A., Jia J., Mukhopadhyay R., Willard B., Kinter M., Fox P.L.;
RT "Two-site phosphorylation of EPRS coordinates multimodal regulation of
RT noncanonical translational control activity.";
RL Mol. Cell 35:164-180(2009).
RN [23]
RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX,
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-363, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP INTERACTION WITH GTPBP1.
RX PubMed=21515746; DOI=10.1096/fj.10-178715;
RA Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
RA Chung S.J., Senju S., Nishimura Y., Kim K.T.;
RT "Modulation of exosome-mediated mRNA turnover by interaction of GTP-
RT binding protein 1 (GTPBP1) with its target mRNAs.";
RL FASEB J. 25:2757-2769(2011).
RN [27]
RP FUNCTION, AND RECONSTITUTION OF THE GAIT COMPLEX.
RX PubMed=23071094; DOI=10.1128/MCB.01168-12;
RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT "Heterotrimeric GAIT complex drives transcript-selective translation
RT inhibition in murine macrophages.";
RL Mol. Cell. Biol. 32:5046-5055(2012).
RN [28]
RP METHYLATION AT ARG-444; ARG-496; ARG-510; ARG-518; ARG-526; ARG-536
RP AND ARG-539 BY PRMT1, AND MASS SPECTROMETRY.
RX PubMed=23455924; DOI=10.1038/nmeth.2397;
RA Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P.,
RA Meierhofer D., Benlasfer N., Valovka T., Timmermann B., Wanker E.E.,
RA Sauer S., Stelzl U.;
RT "A Y2H-seq approach defines the human protein methyltransferase
RT interactome.";
RL Nat. Methods 10:339-342(2013).
RN [29]
RP STRUCTURE BY NMR OF 334-423.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain in heterogeneous nuclear
RT ribonucleoprotein Q.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Heterogenous nuclear ribonucleoprotein (hnRNP)
CC implicated in mRNA processing mechanisms. Component of the CRD-
CC mediated complex that promotes MYC mRNA stability. Isoform 1,
CC isoform 2 and isoform 3 are associated in vitro with pre-mRNA,
CC splicing intermediates and mature mRNA protein complexes. Isoform
CC 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the
CC APOB mRNA editosome complex and may modulate the
CC postranscriptional C to U RNA-editing of the APOB mRNA through
CC either by binding to A1CF (APOBEC1 complementation factor), to
CC APOBEC1 or to RNA itself. May be involved in translationally
CC coupled mRNA turnover. Implicated with other RNA-binding proteins
CC in the cytoplasmic deadenylation/translational and decay interplay
CC of the FOS mRNA mediated by the major coding-region determinant of
CC instability (mCRD) domain. Interacts in vitro preferentially with
CC poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in
CC cytoplasmic vesicle-based mRNA transport through interaction with
CC synaptotagmins. Component of the GAIT (gamma interferon-activated
CC inhibitor of translation) complex which mediates interferon-gamma-
CC induced transcript-selective translation inhibition in
CC inflammation processes. Upon interferon-gamma activation assembles
CC into the GAIT complex which binds to stem loop-containing GAIT
CC elements in the 3'-UTR of diverse inflammatory mRNAs (such as
CC ceruplasmin) and suppresses their translation; seems not to be
CC essential for GAIT complex function.
CC -!- SUBUNIT: Isoform 1 is a component of the APOB mRNA editosome
CC complex and interacts with APOBEC1 and A1CF (APOBEC1
CC complementation factor). Part of a complex associated with the FOS
CC mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR, HNRPD and
CC SYNCRIP. Isoform 3 interacts with HNRPR. Interacts with POLR2A
CC hyperphosphorylated C-terminal domain. Interacts with minute virus
CC of mice (MVM) NS1 protein. Isoform 1, isoform 2 and isoform 3
CC interact with SMN. Isoform 3 interacts through its C-terminal
CC domain with SYT7, SYT8 and SYT9 (By similarity). The non-
CC phosphorylated and phosphorylated forms are colocalized with PAIP1
CC in polysomes (By similarity). Identified in a histone pre-mRNA
CC complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP
CC and YBX1 (By similarity). Identified in the spliceosome C complex.
CC Component of the coding region determinant (CRD)-mediated complex,
CC composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in
CC a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU,
CC IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Identified in a mRNP granule complex, at least composed of
CC ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with
CC GTPBP1. Component of the GAIT complex; in humans the complex
CC assembly seems to be a two-step process in which EPRS first
CC associates with SYNCRIP to form a pre-GAIT complex which is
CC deficient in GAIT element binding.
CC -!- INTERACTION:
CC Q5JVS0:HABP4; NbExp=2; IntAct=EBI-1024357, EBI-523625;
CC Q14103-4:HNRNPD; NbExp=3; IntAct=EBI-1024357, EBI-432545;
CC Q99873:PRMT1; NbExp=2; IntAct=EBI-1024357, EBI-78738;
CC Q9NR22:PRMT8; NbExp=3; IntAct=EBI-1024357, EBI-745545;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Microsome (By similarity).
CC Endoplasmic reticulum (By similarity). Nucleus (By similarity).
CC Note=The tyrosine phosphorylated form bound to RNA is found in
CC microsomes (By similarity). Localized in cytoplasmic mRNP granules
CC containing untranslated mRNAs.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleoplasm (By
CC similarity). Note=Expressed predominantly in the nucleoplasm (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleoplasm (By
CC similarity). Note=Expressed predominantly in the nucleoplasm (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleoplasm (By
CC similarity). Note=Expressed predominantly in the nucleoplasm (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=hnRNP Q3;
CC IsoId=O60506-1; Sequence=Displayed;
CC Name=2; Synonyms=hnRNP Q2;
CC IsoId=O60506-2; Sequence=VSP_009583;
CC Note=May be due to a competing donor splice site;
CC Name=3; Synonyms=hnRNP Q1;
CC IsoId=O60506-3; Sequence=VSP_009584;
CC Note=May be due to a competing donor splice site and to an exon
CC inclusion. Ref.5 (AAK59705) sequence is in conflict in
CC positions: 550:QG->V;
CC Name=4;
CC IsoId=O60506-4; Sequence=VSP_009583, VSP_009584;
CC Note=May be due to a competing donor splice site and to an exon
CC inclusion. No experimental confirmation available;
CC Name=5;
CC IsoId=O60506-5; Sequence=VSP_009581, VSP_009582, VSP_009584;
CC Note=May be due to a competing donor splice site and to an exon
CC inclusion;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Detected in heart,
CC brain, pancreas, placenta, spleen, lung, liver, skeletal muscle,
CC kidney, thymus, prostate, uterus, small intestine, colon,
CC peripheral blood and testis.
CC -!- DOMAIN: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-
CC box) may be involved in RNA-binding and protein-protein
CC interactions. It is methylated by PRMT1, and essential for nuclear
CC localization.
CC -!- PTM: Phosphorylated on tyrosine. The membrane-bound form found in
CC microsomes is phosphorylated in vitro by insulin receptor tyrosine
CC kinase (INSR). Phosphorylation is inhibited upon binding to RNA,
CC whereas the cytoplasmic form is poorly phosphorylated (By
CC similarity).
CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15575.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 413;
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DR EMBL; AF155568; AAD38198.1; -; mRNA.
DR EMBL; AF037448; AAC12926.1; -; mRNA.
DR EMBL; AY034481; AAK59703.1; -; mRNA.
DR EMBL; AY034482; AAK59704.1; -; mRNA.
DR EMBL; AY034483; AAK59705.1; -; mRNA.
DR EMBL; AK222776; BAD96496.1; -; mRNA.
DR EMBL; AL136082; CAI20446.1; -; Genomic_DNA.
DR EMBL; AL136082; CAI20447.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48625.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48626.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48629.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48630.1; -; Genomic_DNA.
DR EMBL; BC015575; AAH15575.1; ALT_SEQ; mRNA.
DR EMBL; BC032643; AAH32643.1; -; mRNA.
DR EMBL; BC040844; AAH40844.1; -; mRNA.
DR RefSeq; NP_001153145.1; NM_001159673.1.
DR RefSeq; NP_001153146.1; NM_001159674.1.
DR RefSeq; NP_001153147.1; NM_001159675.1.
DR RefSeq; NP_001153148.1; NM_001159676.1.
DR RefSeq; NP_001153149.1; NM_001159677.1.
DR RefSeq; NP_001240700.1; NM_001253771.1.
DR RefSeq; NP_006363.4; NM_006372.4.
DR RefSeq; XP_005248694.1; XM_005248637.1.
DR RefSeq; XP_005248695.1; XM_005248638.1.
DR RefSeq; XP_005248696.1; XM_005248639.1.
DR UniGene; Hs.571177; -.
DR PDB; 2DGU; NMR; -; A=334-423.
DR PDBsum; 2DGU; -.
DR ProteinModelPortal; O60506; -.
DR SMR; O60506; 96-423.
DR DIP; DIP-35540N; -.
DR IntAct; O60506; 36.
DR MINT; MINT-2796763; -.
DR PhosphoSite; O60506; -.
DR PaxDb; O60506; -.
DR PRIDE; O60506; -.
DR DNASU; 10492; -.
DR Ensembl; ENST00000355238; ENSP00000347380; ENSG00000135316.
DR Ensembl; ENST00000369622; ENSP00000358635; ENSG00000135316.
DR GeneID; 10492; -.
DR KEGG; hsa:10492; -.
DR UCSC; uc003pku.3; human.
DR CTD; 10492; -.
DR GeneCards; GC06M086317; -.
DR HGNC; HGNC:16918; SYNCRIP.
DR HPA; CAB010895; -.
DR neXtProt; NX_O60506; -.
DR PharmGKB; PA134985065; -.
DR eggNOG; NOG258596; -.
DR HOVERGEN; HBG051917; -.
DR InParanoid; O60506; -.
DR KO; K13160; -.
DR OMA; KSDNQEF; -.
DR OrthoDB; EOG73JKW2; -.
DR PhylomeDB; O60506; -.
DR ChiTaRS; SYNCRIP; human.
DR EvolutionaryTrace; O60506; -.
DR GeneWiki; SYNCRIP; -.
DR GenomeRNAi; 10492; -.
DR NextBio; 39814; -.
DR PRO; PR:O60506; -.
DR ArrayExpress; O60506; -.
DR Bgee; O60506; -.
DR CleanEx; HS_SYNCRIP; -.
DR Genevestigator; O60506; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008143; F:poly(A) RNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW Host-virus interaction; Isopeptide bond; Methylation; Microsome;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Translation regulation; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 623 Heterogeneous nuclear ribonucleoprotein
FT Q.
FT /FTId=PRO_0000081867.
FT DOMAIN 162 241 RRM 1.
FT DOMAIN 243 325 RRM 2.
FT DOMAIN 338 408 RRM 3.
FT REPEAT 448 450 1-1.
FT REPEAT 451 453 1-2.
FT REPEAT 460 464 2-1.
FT REPEAT 469 472 2-2.
FT REPEAT 478 480 1-3.
FT REPEAT 485 488 2-3.
FT REPEAT 498 500 1-4.
FT REPEAT 526 528 1-5.
FT REPEAT 539 541 1-6.
FT REPEAT 554 556 1-7.
FT REPEAT 557 559 1-8.
FT REGION 400 561 Interaction with APOBEC1.
FT REGION 448 559 8 X 3 AA repeats of R-G-G.
FT REGION 460 488 3 X 4 AA repeats of Y-Y-G-Y.
FT REGION 518 549 Interaction with SMN.
FT MOTIF 564 578 Bipartite nuclear localization signal
FT (Potential).
FT COMPBIAS 431 434 Poly-Tyr.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 363 363 N6-acetyllysine.
FT MOD_RES 373 373 Phosphotyrosine.
FT MOD_RES 444 444 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 444 444 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 496 496 Omega-N-methylarginine; by PRMT1.
FT MOD_RES 510 510 Asymmetric dimethylarginine; by PRMT1.
FT MOD_RES 518 518 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 518 518 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 536 536 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 536 536 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 539 539 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 539 539 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 587 587 Phosphoserine.
FT CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 152 Missing (in isoform 5).
FT /FTId=VSP_009581.
FT VAR_SEQ 153 163 YSGQQPSVGTE -> MEDHLQIPFIQ (in isoform
FT 5).
FT /FTId=VSP_009582.
FT VAR_SEQ 302 336 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_009583.
FT VAR_SEQ 550 623 VRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPI
FT AQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK -> QGKG
FT VEAGPDLLQ (in isoform 3, isoform 4 and
FT isoform 5).
FT /FTId=VSP_009584.
FT CONFLICT 265 265 K -> Q (in Ref. 1; AAD38198).
FT CONFLICT 287 287 G -> S (in Ref. 2 and 3).
FT CONFLICT 288 288 F -> S (in Ref. 7; AAH40844).
FT STRAND 340 343
FT HELIX 351 361
FT STRAND 364 369
FT STRAND 374 380
FT HELIX 381 391
FT STRAND 394 396
FT STRAND 399 405
SQ SEQUENCE 623 AA; 69603 MW; 0669FA604E8FBBDF CRC64;
MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER
AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD
EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP
LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV
ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA
QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKAFSQ
FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR
QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG
YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG
GAQQQRGRGV RGARGGRGGN VGGKRKADGY NQPDSKRRQT NNQNWGSQPI AQQPLQGGDH
SGNYGYKSEN QEFYQDTFGQ QWK
//
ID HNRPQ_HUMAN Reviewed; 623 AA.
AC O60506; E1P501; E1P502; Q53H05; Q5TCG2; Q5TCG3; Q8IW78; Q8N599;
read moreAC Q96LC1; Q96LC2; Q9Y583;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein Q;
DE Short=hnRNP Q;
DE AltName: Full=Glycine- and tyrosine-rich RNA-binding protein;
DE Short=GRY-RBP;
DE AltName: Full=NS1-associated protein 1;
DE AltName: Full=Synaptotagmin-binding, cytoplasmic RNA-interacting protein;
GN Name=SYNCRIP; Synonyms=HNRPQ, NSAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH NS1.
RC TISSUE=Cervix carcinoma;
RX PubMed=9847309;
RA Harris C.E., Boden R.A., Astell C.R.;
RT "A novel heterogeneous nuclear ribonucleoprotein-like protein
RT interacts with NS1 of the minute virus of mice.";
RL J. Virol. 73:72-80(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Du G., Pan M., Zhou Y., Chen J., Yao H., Yuan J., Qiang B.;
RT "Cloning of human and mouse GRY-RBP cDNA.";
RL Chin. Sci. Bull. 45:343-349(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION IN MRNA
RP PROCESSING, SUBCELLULAR LOCATION, ASSOCIATION WITH THE SPLICEOSOME,
RP AND INTERACTION WITH SMN AND HNRPR.
RC TISSUE=Cervix carcinoma;
RX PubMed=11574476; DOI=10.1093/emboj/20.19.5443;
RA Mourelatos Z., Abel L., Yong J., Kataoka N., Dreyfuss G.;
RT "SMN interacts with a novel family of hnRNP and spliceosomal
RT proteins.";
RL EMBO J. 20:5443-5452(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/3; 4 AND 5).
RC TISSUE=Eye, Lung, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 43-60 AND 370-381, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND PHOSPHORYLATION AT
RP TYR-373.
RC TISSUE=Kidney;
RX PubMed=12601080; DOI=10.1074/mcp.M200075-MCP200;
RA Hinsby A.M., Olsen J.V., Bennett K.L., Mann M.;
RT "Signaling initiated by overexpression of the fibroblast growth factor
RT receptor-1 investigated by mass spectrometry.";
RL Mol. Cell. Proteomics 2:29-36(2003).
RN [10]
RP FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION
RP IN A COMPLEX WITH HNRPD; PABPC1; PAIP1 AND CSDE1.
RC TISSUE=Placenta;
RX PubMed=11051545; DOI=10.1016/S0092-8674(00)00102-1;
RA Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
RA Shyu A.-B.;
RT "A mechanism for translationally coupled mRNA turnover: interaction
RT between the poly(A) tail and a c-fos RNA coding determinant via a
RT protein complex.";
RL Cell 103:29-40(2000).
RN [11]
RP FUNCTION IN APOB MRNA EDITING, INTERACTION WITH APOBEC1, AND TISSUE
RP SPECIFICITY.
RX PubMed=11352648; DOI=10.1006/bbrc.2001.4679;
RA Lau P.P., Chang B.-H., Chan L.;
RT "Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
RT component of apobec-1 editosome.";
RL Biochem. Biophys. Res. Commun. 282:977-983(2001).
RN [12]
RP FUNCTION IN APOB MRNA EDITING, RNA-BINDING, AND INTERACTION WITH A1CF
RP AND APOBEC1.
RX PubMed=11134005; DOI=10.1074/jbc.M006435200;
RA Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S.,
RA Jarmuz A., Scott J., Davidson N.O.;
RT "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein
RT that interacts with both apobec-1 and apobec-1 complementation factor
RT to modulate C to U editing.";
RL J. Biol. Chem. 276:10272-10283(2001).
RN [13]
RP IDENTIFICATION IN SPLICEOSOME.
RX PubMed=9731529; DOI=10.1038/1700;
RA Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P.,
RA Sleeman J., Lamond A.I., Mann M.;
RT "Mass spectrometry and EST-database searching allows characterization
RT of the multi-protein spliceosome complex.";
RL Nat. Genet. 20:46-50(1998).
RN [14]
RP INTERACTION WITH POLR2A.
RX PubMed=12376575; DOI=10.1074/mcp.M200029-MCP200;
RA Carty S.M., Greenleaf A.L.;
RT "Hyperphosphorylated C-terminal repeat domain-associating proteins in
RT the nuclear proteome link transcription to DNA/chromatin modification
RT and RNA processing.";
RL Mol. Cell. Proteomics 1:598-610(2002).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [16]
RP IDENTIFICATION IN THE GAIT COMPLEX.
RX PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
RA Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
RA Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
RT "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
RT specific silencing of translation.";
RL Cell 119:195-208(2004).
RN [17]
RP METHYLATION BY PRMT1.
RX PubMed=16765914; DOI=10.1016/j.bbrc.2006.05.152;
RA Passos D.O., Quaresma A.J., Kobarg J.;
RT "The methylation of the C-terminal region of hnRNPQ (NSAP1) is
RT important for its nuclear localization.";
RL Biochem. Biophys. Res. Commun. 346:517-525(2006).
RN [18]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [19]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP INTERACTION WITH EPRS.
RX PubMed=19647514; DOI=10.1016/j.molcel.2009.05.028;
RA Arif A., Jia J., Mukhopadhyay R., Willard B., Kinter M., Fox P.L.;
RT "Two-site phosphorylation of EPRS coordinates multimodal regulation of
RT noncanonical translational control activity.";
RL Mol. Cell 35:164-180(2009).
RN [23]
RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX,
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-363, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP INTERACTION WITH GTPBP1.
RX PubMed=21515746; DOI=10.1096/fj.10-178715;
RA Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
RA Chung S.J., Senju S., Nishimura Y., Kim K.T.;
RT "Modulation of exosome-mediated mRNA turnover by interaction of GTP-
RT binding protein 1 (GTPBP1) with its target mRNAs.";
RL FASEB J. 25:2757-2769(2011).
RN [27]
RP FUNCTION, AND RECONSTITUTION OF THE GAIT COMPLEX.
RX PubMed=23071094; DOI=10.1128/MCB.01168-12;
RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT "Heterotrimeric GAIT complex drives transcript-selective translation
RT inhibition in murine macrophages.";
RL Mol. Cell. Biol. 32:5046-5055(2012).
RN [28]
RP METHYLATION AT ARG-444; ARG-496; ARG-510; ARG-518; ARG-526; ARG-536
RP AND ARG-539 BY PRMT1, AND MASS SPECTROMETRY.
RX PubMed=23455924; DOI=10.1038/nmeth.2397;
RA Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P.,
RA Meierhofer D., Benlasfer N., Valovka T., Timmermann B., Wanker E.E.,
RA Sauer S., Stelzl U.;
RT "A Y2H-seq approach defines the human protein methyltransferase
RT interactome.";
RL Nat. Methods 10:339-342(2013).
RN [29]
RP STRUCTURE BY NMR OF 334-423.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain in heterogeneous nuclear
RT ribonucleoprotein Q.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Heterogenous nuclear ribonucleoprotein (hnRNP)
CC implicated in mRNA processing mechanisms. Component of the CRD-
CC mediated complex that promotes MYC mRNA stability. Isoform 1,
CC isoform 2 and isoform 3 are associated in vitro with pre-mRNA,
CC splicing intermediates and mature mRNA protein complexes. Isoform
CC 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the
CC APOB mRNA editosome complex and may modulate the
CC postranscriptional C to U RNA-editing of the APOB mRNA through
CC either by binding to A1CF (APOBEC1 complementation factor), to
CC APOBEC1 or to RNA itself. May be involved in translationally
CC coupled mRNA turnover. Implicated with other RNA-binding proteins
CC in the cytoplasmic deadenylation/translational and decay interplay
CC of the FOS mRNA mediated by the major coding-region determinant of
CC instability (mCRD) domain. Interacts in vitro preferentially with
CC poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in
CC cytoplasmic vesicle-based mRNA transport through interaction with
CC synaptotagmins. Component of the GAIT (gamma interferon-activated
CC inhibitor of translation) complex which mediates interferon-gamma-
CC induced transcript-selective translation inhibition in
CC inflammation processes. Upon interferon-gamma activation assembles
CC into the GAIT complex which binds to stem loop-containing GAIT
CC elements in the 3'-UTR of diverse inflammatory mRNAs (such as
CC ceruplasmin) and suppresses their translation; seems not to be
CC essential for GAIT complex function.
CC -!- SUBUNIT: Isoform 1 is a component of the APOB mRNA editosome
CC complex and interacts with APOBEC1 and A1CF (APOBEC1
CC complementation factor). Part of a complex associated with the FOS
CC mCRD domain and consisting of PABPC1, PAIP1, CSDE1/UNR, HNRPD and
CC SYNCRIP. Isoform 3 interacts with HNRPR. Interacts with POLR2A
CC hyperphosphorylated C-terminal domain. Interacts with minute virus
CC of mice (MVM) NS1 protein. Isoform 1, isoform 2 and isoform 3
CC interact with SMN. Isoform 3 interacts through its C-terminal
CC domain with SYT7, SYT8 and SYT9 (By similarity). The non-
CC phosphorylated and phosphorylated forms are colocalized with PAIP1
CC in polysomes (By similarity). Identified in a histone pre-mRNA
CC complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP
CC and YBX1 (By similarity). Identified in the spliceosome C complex.
CC Component of the coding region determinant (CRD)-mediated complex,
CC composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in
CC a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU,
CC IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Identified in a mRNP granule complex, at least composed of
CC ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with
CC GTPBP1. Component of the GAIT complex; in humans the complex
CC assembly seems to be a two-step process in which EPRS first
CC associates with SYNCRIP to form a pre-GAIT complex which is
CC deficient in GAIT element binding.
CC -!- INTERACTION:
CC Q5JVS0:HABP4; NbExp=2; IntAct=EBI-1024357, EBI-523625;
CC Q14103-4:HNRNPD; NbExp=3; IntAct=EBI-1024357, EBI-432545;
CC Q99873:PRMT1; NbExp=2; IntAct=EBI-1024357, EBI-78738;
CC Q9NR22:PRMT8; NbExp=3; IntAct=EBI-1024357, EBI-745545;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Microsome (By similarity).
CC Endoplasmic reticulum (By similarity). Nucleus (By similarity).
CC Note=The tyrosine phosphorylated form bound to RNA is found in
CC microsomes (By similarity). Localized in cytoplasmic mRNP granules
CC containing untranslated mRNAs.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleoplasm (By
CC similarity). Note=Expressed predominantly in the nucleoplasm (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleoplasm (By
CC similarity). Note=Expressed predominantly in the nucleoplasm (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleoplasm (By
CC similarity). Note=Expressed predominantly in the nucleoplasm (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=hnRNP Q3;
CC IsoId=O60506-1; Sequence=Displayed;
CC Name=2; Synonyms=hnRNP Q2;
CC IsoId=O60506-2; Sequence=VSP_009583;
CC Note=May be due to a competing donor splice site;
CC Name=3; Synonyms=hnRNP Q1;
CC IsoId=O60506-3; Sequence=VSP_009584;
CC Note=May be due to a competing donor splice site and to an exon
CC inclusion. Ref.5 (AAK59705) sequence is in conflict in
CC positions: 550:QG->V;
CC Name=4;
CC IsoId=O60506-4; Sequence=VSP_009583, VSP_009584;
CC Note=May be due to a competing donor splice site and to an exon
CC inclusion. No experimental confirmation available;
CC Name=5;
CC IsoId=O60506-5; Sequence=VSP_009581, VSP_009582, VSP_009584;
CC Note=May be due to a competing donor splice site and to an exon
CC inclusion;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Detected in heart,
CC brain, pancreas, placenta, spleen, lung, liver, skeletal muscle,
CC kidney, thymus, prostate, uterus, small intestine, colon,
CC peripheral blood and testis.
CC -!- DOMAIN: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-
CC box) may be involved in RNA-binding and protein-protein
CC interactions. It is methylated by PRMT1, and essential for nuclear
CC localization.
CC -!- PTM: Phosphorylated on tyrosine. The membrane-bound form found in
CC microsomes is phosphorylated in vitro by insulin receptor tyrosine
CC kinase (INSR). Phosphorylation is inhibited upon binding to RNA,
CC whereas the cytoplasmic form is poorly phosphorylated (By
CC similarity).
CC -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15575.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 413;
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DR EMBL; AF155568; AAD38198.1; -; mRNA.
DR EMBL; AF037448; AAC12926.1; -; mRNA.
DR EMBL; AY034481; AAK59703.1; -; mRNA.
DR EMBL; AY034482; AAK59704.1; -; mRNA.
DR EMBL; AY034483; AAK59705.1; -; mRNA.
DR EMBL; AK222776; BAD96496.1; -; mRNA.
DR EMBL; AL136082; CAI20446.1; -; Genomic_DNA.
DR EMBL; AL136082; CAI20447.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48625.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48626.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48629.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48630.1; -; Genomic_DNA.
DR EMBL; BC015575; AAH15575.1; ALT_SEQ; mRNA.
DR EMBL; BC032643; AAH32643.1; -; mRNA.
DR EMBL; BC040844; AAH40844.1; -; mRNA.
DR RefSeq; NP_001153145.1; NM_001159673.1.
DR RefSeq; NP_001153146.1; NM_001159674.1.
DR RefSeq; NP_001153147.1; NM_001159675.1.
DR RefSeq; NP_001153148.1; NM_001159676.1.
DR RefSeq; NP_001153149.1; NM_001159677.1.
DR RefSeq; NP_001240700.1; NM_001253771.1.
DR RefSeq; NP_006363.4; NM_006372.4.
DR RefSeq; XP_005248694.1; XM_005248637.1.
DR RefSeq; XP_005248695.1; XM_005248638.1.
DR RefSeq; XP_005248696.1; XM_005248639.1.
DR UniGene; Hs.571177; -.
DR PDB; 2DGU; NMR; -; A=334-423.
DR PDBsum; 2DGU; -.
DR ProteinModelPortal; O60506; -.
DR SMR; O60506; 96-423.
DR DIP; DIP-35540N; -.
DR IntAct; O60506; 36.
DR MINT; MINT-2796763; -.
DR PhosphoSite; O60506; -.
DR PaxDb; O60506; -.
DR PRIDE; O60506; -.
DR DNASU; 10492; -.
DR Ensembl; ENST00000355238; ENSP00000347380; ENSG00000135316.
DR Ensembl; ENST00000369622; ENSP00000358635; ENSG00000135316.
DR GeneID; 10492; -.
DR KEGG; hsa:10492; -.
DR UCSC; uc003pku.3; human.
DR CTD; 10492; -.
DR GeneCards; GC06M086317; -.
DR HGNC; HGNC:16918; SYNCRIP.
DR HPA; CAB010895; -.
DR neXtProt; NX_O60506; -.
DR PharmGKB; PA134985065; -.
DR eggNOG; NOG258596; -.
DR HOVERGEN; HBG051917; -.
DR InParanoid; O60506; -.
DR KO; K13160; -.
DR OMA; KSDNQEF; -.
DR OrthoDB; EOG73JKW2; -.
DR PhylomeDB; O60506; -.
DR ChiTaRS; SYNCRIP; human.
DR EvolutionaryTrace; O60506; -.
DR GeneWiki; SYNCRIP; -.
DR GenomeRNAi; 10492; -.
DR NextBio; 39814; -.
DR PRO; PR:O60506; -.
DR ArrayExpress; O60506; -.
DR Bgee; O60506; -.
DR CleanEx; HS_SYNCRIP; -.
DR Genevestigator; O60506; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008143; F:poly(A) RNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW Host-virus interaction; Isopeptide bond; Methylation; Microsome;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Translation regulation; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 623 Heterogeneous nuclear ribonucleoprotein
FT Q.
FT /FTId=PRO_0000081867.
FT DOMAIN 162 241 RRM 1.
FT DOMAIN 243 325 RRM 2.
FT DOMAIN 338 408 RRM 3.
FT REPEAT 448 450 1-1.
FT REPEAT 451 453 1-2.
FT REPEAT 460 464 2-1.
FT REPEAT 469 472 2-2.
FT REPEAT 478 480 1-3.
FT REPEAT 485 488 2-3.
FT REPEAT 498 500 1-4.
FT REPEAT 526 528 1-5.
FT REPEAT 539 541 1-6.
FT REPEAT 554 556 1-7.
FT REPEAT 557 559 1-8.
FT REGION 400 561 Interaction with APOBEC1.
FT REGION 448 559 8 X 3 AA repeats of R-G-G.
FT REGION 460 488 3 X 4 AA repeats of Y-Y-G-Y.
FT REGION 518 549 Interaction with SMN.
FT MOTIF 564 578 Bipartite nuclear localization signal
FT (Potential).
FT COMPBIAS 431 434 Poly-Tyr.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 221 221 N6-acetyllysine.
FT MOD_RES 363 363 N6-acetyllysine.
FT MOD_RES 373 373 Phosphotyrosine.
FT MOD_RES 444 444 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 444 444 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 496 496 Omega-N-methylarginine; by PRMT1.
FT MOD_RES 510 510 Asymmetric dimethylarginine; by PRMT1.
FT MOD_RES 518 518 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 518 518 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 536 536 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 536 536 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 539 539 Asymmetric dimethylarginine; by PRMT1;
FT alternate.
FT MOD_RES 539 539 Omega-N-methylarginine; by PRMT1;
FT alternate.
FT MOD_RES 587 587 Phosphoserine.
FT CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VAR_SEQ 1 152 Missing (in isoform 5).
FT /FTId=VSP_009581.
FT VAR_SEQ 153 163 YSGQQPSVGTE -> MEDHLQIPFIQ (in isoform
FT 5).
FT /FTId=VSP_009582.
FT VAR_SEQ 302 336 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_009583.
FT VAR_SEQ 550 623 VRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPI
FT AQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK -> QGKG
FT VEAGPDLLQ (in isoform 3, isoform 4 and
FT isoform 5).
FT /FTId=VSP_009584.
FT CONFLICT 265 265 K -> Q (in Ref. 1; AAD38198).
FT CONFLICT 287 287 G -> S (in Ref. 2 and 3).
FT CONFLICT 288 288 F -> S (in Ref. 7; AAH40844).
FT STRAND 340 343
FT HELIX 351 361
FT STRAND 364 369
FT STRAND 374 380
FT HELIX 381 391
FT STRAND 394 396
FT STRAND 399 405
SQ SEQUENCE 623 AA; 69603 MW; 0669FA604E8FBBDF CRC64;
MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER
AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD
EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP
LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV
ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA
QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKAFSQ
FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR
QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG
YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG
GAQQQRGRGV RGARGGRGGN VGGKRKADGY NQPDSKRRQT NNQNWGSQPI AQQPLQGGDH
SGNYGYKSEN QEFYQDTFGQ QWK
//