HNRPQ_HUMAN
ID HNRPQ_HUMAN Reviewed; 623 AA.
AC O60506; E1P501; E1P502; Q53H05; Q5TCG2; Q5TCG3; Q8IW78; Q8N599; Q96LC1;
AC Q96LC2; Q9Y583;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 209.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH MINUTE VIRUS
RP OF MICE NS1 (MICROBIAL INFECTION).
RC TISSUE=Cervix carcinoma;
RX PubMed=9847309; DOI=10.1128/jvi.73.1.72-80.1999;
RA Harris C.E., Boden R.A., Astell C.R.;
RT "A novel heterogeneous nuclear ribonucleoprotein-like protein interacts
RT 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, AND
RP 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 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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 43-60 AND 370-381, AND IDENTIFICATION BY MASS
RP 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, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT 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 IN A
RP 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 between
RT the poly(A) tail and a c-fos RNA coding determinant via a protein
RT 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 AND
RP APOBEC1.
RX PubMed=11134005; DOI=10.1074/jbc.m006435200;
RA Blanc V., Navaratnam N., Henderson J.O., Anant S., Kennedy S., Jarmuz A.,
RA Scott J., Davidson N.O.;
RT "Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that
RT interacts with both apobec-1 and apobec-1 complementation factor to
RT 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 of
RT 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 the
RT nuclear proteome link transcription to DNA/chromatin modification and RNA
RT processing.";
RL Mol. Cell. Proteomics 1:598-610(2002).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP 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., Kinter M.,
RA Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
RT "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific
RT 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 important
RT 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP INTERACTION WITH HABP4.
RX PubMed=19523114; DOI=10.1111/j.1742-4658.2009.07092.x;
RA Bressan G.C., Quaresma A.J., Moraes E.C., Manfiolli A.O., Passos D.O.,
RA Gomes M.D., Kobarg J.;
RT "Functional association of human Ki-1/57 with pre-mRNA splicing events.";
RL FEBS J. 276:3770-3783(2009).
RN [22]
RP INTERACTION WITH EPRS1.
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 IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-363, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Buerckstuemmer T.,
RA 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-binding
RT 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
RP METHYLATION AT ARG-444; ARG-496; ARG-510; ARG-518; ARG-526; ARG-536 AND
RP ARG-539 BY PRMT1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23455924; DOI=10.1038/nmeth.2397;
RA Weimann M., Grossmann A., Woodsmith J., Ozkan Z., Birth P., Meierhofer D.,
RA Benlasfer N., Valovka T., Timmermann B., Wanker E.E., Sauer S., Stelzl U.;
RT "A Y2H-seq approach defines the human protein methyltransferase
RT interactome.";
RL Nat. Methods 10:339-342(2013).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-168 AND LYS-607, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [33]
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) implicated in
CC mRNA processing mechanisms. Component of the CRD-mediated complex that
CC promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are
CC associated in vitro with pre-mRNA, splicing intermediates and mature
CC mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences.
CC Isoform 1 is part of the APOB mRNA editosome complex and may modulate
CC the postranscriptional C to U RNA-editing of the APOB mRNA through
CC either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1
CC or to RNA itself. May be involved in translationally coupled mRNA
CC turnover. Implicated with other RNA-binding proteins in the cytoplasmic
CC deadenylation/translational and decay interplay of the FOS mRNA
CC mediated by the major coding-region determinant of instability (mCRD)
CC domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA
CC sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA
CC transport through interaction with synaptotagmins. Component of the
CC GAIT (gamma interferon-activated inhibitor of translation) complex
CC which mediates interferon-gamma-induced transcript-selective
CC translation inhibition in inflammation processes. Upon interferon-gamma
CC activation assembles into the GAIT complex which binds to stem loop-
CC containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs
CC (such as ceruplasmin) and suppresses their translation; seems not to be
CC essential for GAIT complex function. {ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11352648,
CC ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:23071094}.
CC -!- SUBUNIT: Isoform 1 is a component of the APOB mRNA editosome complex
CC and interacts with APOBEC1 and A1CF (APOBEC1 complementation factor).
CC Part of a complex associated with the FOS mCRD domain and consisting of
CC PABPC1, PAIP1, CSDE1/UNR, HNRPD and SYNCRIP. Isoform 3 interacts with
CC HNRPR. Interacts with POLR2A hyperphosphorylated C-terminal domain.
CC Isoform 1, isoform 2 and isoform 3 interact with SMN. Isoform 3
CC interacts through its C-terminal domain with SYT7, SYT8 and SYT9 (By
CC similarity). The non-phosphorylated and phosphorylated forms are
CC colocalized with PAIP1 in polysomes (By similarity). Interacts with
CC HABP4 (PubMed:19523114). Identified in a histone pre-mRNA complex, at
CC least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By
CC similarity). Identified in the spliceosome C complex. Component of the
CC coding region determinant (CRD)-mediated complex, composed of DHX9,
CC HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP complex, at
CC least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1,
CC PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP
CC granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1,
CC HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8,
CC IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3,
CC RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, YBX1 and untranslated mRNAs.
CC Interacts with GTPBP1. Component of the GAIT complex; in humans the
CC complex assembly seems to be a two-step process in which EPRS1 first
CC associates with SYNCRIP to form a pre-GAIT complex which is deficient
CC in GAIT element binding. {ECO:0000250, ECO:0000269|PubMed:11051545,
CC ECO:0000269|PubMed:11134005, ECO:0000269|PubMed:11352648,
CC ECO:0000269|PubMed:11574476, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12376575, ECO:0000269|PubMed:15479637,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:19647514,
CC ECO:0000269|PubMed:21515746, ECO:0000269|PubMed:9731529}.
CC -!- SUBUNIT: (Microbial infection) Interacts with minute virus of mice
CC (MVM) NS1 protein. {ECO:0000269|PubMed:9847309}.
CC -!- INTERACTION:
CC O60506; P07814: EPRS1; NbExp=3; IntAct=EBI-1024357, EBI-355315;
CC O60506; Q5JVS0: HABP4; NbExp=2; IntAct=EBI-1024357, EBI-523625;
CC O60506; Q14103-4: HNRNPD; NbExp=3; IntAct=EBI-1024357, EBI-432545;
CC O60506; Q99873: PRMT1; NbExp=2; IntAct=EBI-1024357, EBI-78738;
CC O60506; Q9NR22: PRMT8; NbExp=4; IntAct=EBI-1024357, EBI-745545;
CC O60506; Q9NR22-2: PRMT8; NbExp=3; IntAct=EBI-1024357, EBI-10186886;
CC O60506-4; Q86V38: ATN1; NbExp=3; IntAct=EBI-11123832, EBI-11954292;
CC O60506-4; P55212: CASP6; NbExp=3; IntAct=EBI-11123832, EBI-718729;
CC O60506-4; P02489: CRYAA; NbExp=3; IntAct=EBI-11123832, EBI-6875961;
CC O60506-4; Q01658: DR1; NbExp=3; IntAct=EBI-11123832, EBI-750300;
CC O60506-4; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-11123832, EBI-356015;
CC O60506-4; P41091: EIF2S3; NbExp=3; IntAct=EBI-11123832, EBI-1054228;
CC O60506-4; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-11123832, EBI-10226858;
CC O60506-4; Q00403: GTF2B; NbExp=3; IntAct=EBI-11123832, EBI-389564;
CC O60506-4; O00291: HIP1; NbExp=3; IntAct=EBI-11123832, EBI-473886;
CC O60506-4; P54652: HSPA2; NbExp=3; IntAct=EBI-11123832, EBI-356991;
CC O60506-4; Q92876: KLK6; NbExp=3; IntAct=EBI-11123832, EBI-2432309;
CC O60506-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-11123832, EBI-21591415;
CC O60506-4; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-11123832, EBI-2858213;
CC O60506-4; Q13153: PAK1; NbExp=3; IntAct=EBI-11123832, EBI-1307;
CC O60506-4; P16284: PECAM1; NbExp=3; IntAct=EBI-11123832, EBI-716404;
CC O60506-4; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-11123832, EBI-473160;
CC O60506-4; Q99873-3: PRMT1; NbExp=4; IntAct=EBI-11123832, EBI-17165527;
CC O60506-4; Q9NR22: PRMT8; NbExp=3; IntAct=EBI-11123832, EBI-745545;
CC O60506-4; P20339: RAB5A; NbExp=3; IntAct=EBI-11123832, EBI-399437;
CC O60506-4; P62826: RAN; NbExp=3; IntAct=EBI-11123832, EBI-286642;
CC O60506-4; Q6NXR8: RPS3A; NbExp=3; IntAct=EBI-11123832, EBI-11602692;
CC O60506-4; P34741: SDC2; NbExp=3; IntAct=EBI-11123832, EBI-1172957;
CC O60506-4; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-11123832, EBI-2623095;
CC O60506-4; Q13148: TARDBP; NbExp=6; IntAct=EBI-11123832, EBI-372899;
CC O60506-4; P61086: UBE2K; NbExp=3; IntAct=EBI-11123832, EBI-473850;
CC O60506-4; P08670: VIM; NbExp=3; IntAct=EBI-11123832, EBI-353844;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11574476,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19029303}. Microsome
CC {ECO:0000250|UniProtKB:Q7TMK9}. Endoplasmic reticulum {ECO:0000250}.
CC Nucleus {ECO:0000250|UniProtKB:Q7TMK9}. Note=The tyrosine
CC phosphorylated form bound to RNA is found in microsomes (By
CC similarity). Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs (By similarity). {ECO:0000250|UniProtKB:O43390,
CC ECO:0000250|UniProtKB:Q7TMK9}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q7TMK9}. Note=Expressed predominantly in the
CC nucleoplasm. {ECO:0000250|UniProtKB:Q7TMK9}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q7TMK9}. Note=Expressed predominantly in the
CC nucleoplasm. {ECO:0000250|UniProtKB:Q7TMK9}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q7TMK9}. Note=Expressed predominantly in the
CC nucleoplasm. {ECO:0000250|UniProtKB:Q7TMK9}.
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 Name=3; Synonyms=hnRNP Q1;
CC IsoId=O60506-3; Sequence=VSP_009584;
CC Name=4;
CC IsoId=O60506-4; Sequence=VSP_009583, VSP_009584;
CC Name=5;
CC IsoId=O60506-5; Sequence=VSP_009581, VSP_009582, VSP_009584;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Detected in heart, brain,
CC pancreas, placenta, spleen, lung, liver, skeletal muscle, kidney,
CC thymus, prostate, uterus, small intestine, colon, peripheral blood and
CC testis. {ECO:0000269|PubMed:11352648}.
CC -!- DOMAIN: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-box)
CC may be involved in RNA-binding and protein-protein interactions. It is
CC methylated by PRMT1, and essential for nuclear 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 similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice site
CC and to an exon inclusion. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to a competing donor splice site
CC and to an exon inclusion. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to a competing donor splice site
CC and to an exon inclusion. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15575.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 413.; Evidence={ECO:0000305};
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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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS5005.1; -. [O60506-1]
DR CCDS; CCDS55041.1; -. [O60506-3]
DR RefSeq; NP_001153145.1; NM_001159673.1.
DR RefSeq; NP_001153146.1; NM_001159674.1. [O60506-4]
DR RefSeq; NP_001153147.1; NM_001159675.1. [O60506-2]
DR RefSeq; NP_001153148.1; NM_001159676.1.
DR RefSeq; NP_001153149.1; NM_001159677.1. [O60506-3]
DR RefSeq; NP_001240700.1; NM_001253771.1. [O60506-5]
DR RefSeq; NP_006363.4; NM_006372.4. [O60506-1]
DR RefSeq; XP_005248694.1; XM_005248637.2. [O60506-1]
DR RefSeq; XP_016865667.1; XM_017010178.1. [O60506-3]
DR PDB; 2DGU; NMR; -; A=334-423.
DR PDB; 2MXT; NMR; -; A=24-107.
DR PDB; 2NBB; NMR; -; A=24-140.
DR PDB; 6KOR; X-ray; 2.60 A; A=242-428.
DR PDBsum; 2DGU; -.
DR PDBsum; 2MXT; -.
DR PDBsum; 2NBB; -.
DR PDBsum; 6KOR; -.
DR AlphaFoldDB; O60506; -.
DR SMR; O60506; -.
DR BioGRID; 115755; 596.
DR ComplexPortal; CPX-1076; mCRD-poly(A)-bridging complex.
DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex.
DR ComplexPortal; CPX-1097; C-to-U editosome complex. [O60506-1]
DR CORUM; O60506; -.
DR DIP; DIP-35540N; -.
DR IntAct; O60506; 254.
DR MINT; O60506; -.
DR STRING; 9606.ENSP00000358635; -.
DR ChEMBL; CHEMBL4295997; -.
DR GlyGen; O60506; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60506; -.
DR MetOSite; O60506; -.
DR PhosphoSitePlus; O60506; -.
DR SwissPalm; O60506; -.
DR BioMuta; SYNCRIP; -.
DR EPD; O60506; -.
DR jPOST; O60506; -.
DR MassIVE; O60506; -.
DR MaxQB; O60506; -.
DR PaxDb; O60506; -.
DR PeptideAtlas; O60506; -.
DR PRIDE; O60506; -.
DR ProteomicsDB; 49444; -. [O60506-1]
DR ProteomicsDB; 49445; -. [O60506-2]
DR ProteomicsDB; 49446; -. [O60506-3]
DR ProteomicsDB; 49447; -. [O60506-4]
DR ProteomicsDB; 49448; -. [O60506-5]
DR Antibodypedia; 18610; 298 antibodies from 37 providers.
DR DNASU; 10492; -.
DR Ensembl; ENST00000355238.11; ENSP00000347380.6; ENSG00000135316.19. [O60506-3]
DR Ensembl; ENST00000369622.8; ENSP00000358635.3; ENSG00000135316.19. [O60506-1]
DR Ensembl; ENST00000444272.2; ENSP00000397782.2; ENSG00000135316.19. [O60506-3]
DR Ensembl; ENST00000676637.1; ENSP00000502974.1; ENSG00000135316.19. [O60506-3]
DR Ensembl; ENST00000676688.1; ENSP00000504706.1; ENSG00000135316.19. [O60506-1]
DR Ensembl; ENST00000678355.1; ENSP00000503783.1; ENSG00000135316.19. [O60506-1]
DR Ensembl; ENST00000678528.1; ENSP00000503246.1; ENSG00000135316.19. [O60506-3]
DR Ensembl; ENST00000678930.1; ENSP00000504120.1; ENSG00000135316.19. [O60506-2]
DR GeneID; 10492; -.
DR KEGG; hsa:10492; -.
DR MANE-Select; ENST00000369622.8; ENSP00000358635.3; NM_006372.5; NP_006363.4.
DR UCSC; uc003pkv.4; human. [O60506-1]
DR CTD; 10492; -.
DR DisGeNET; 10492; -.
DR GeneCards; SYNCRIP; -.
DR HGNC; HGNC:16918; SYNCRIP.
DR HPA; ENSG00000135316; Low tissue specificity.
DR neXtProt; NX_O60506; -.
DR OpenTargets; ENSG00000135316; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA134985065; -.
DR VEuPathDB; HostDB:ENSG00000135316; -.
DR eggNOG; KOG0117; Eukaryota.
DR GeneTree; ENSGT00940000153511; -.
DR InParanoid; O60506; -.
DR OMA; KAMEGMN; -.
DR OrthoDB; 1384330at2759; -.
DR PhylomeDB; O60506; -.
DR TreeFam; TF314932; -.
DR PathwayCommons; O60506; -.
DR SignaLink; O60506; -.
DR SIGNOR; O60506; -.
DR BioGRID-ORCS; 10492; 122 hits in 1089 CRISPR screens.
DR ChiTaRS; SYNCRIP; human.
DR EvolutionaryTrace; O60506; -.
DR GeneWiki; SYNCRIP; -.
DR GenomeRNAi; 10492; -.
DR Pharos; O60506; Tbio.
DR PRO; PR:O60506; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60506; protein.
DR Bgee; ENSG00000135316; Expressed in ventricular zone and 204 other tissues.
DR ExpressionAtlas; O60506; baseline and differential.
DR Genevisible; O60506; HS.
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:0005829; C:cytosol; IDA:ComplexPortal.
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:0106002; C:mCRD-mediated mRNA stability complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045293; C:mRNA editing complex; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal.
DR GO; GO:0016556; P:mRNA modification; IDA:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:ComplexPortal.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IC:ComplexPortal.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR CDD; cd12483; RRM1_hnRNPQ; 1.
DR CDD; cd12489; RRM2_hnRNPQ; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR041337; hnRNP_Q_AcD.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR034544; hnRNPQ_RRM1.
DR InterPro; IPR034548; hnRNPQ_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF18360; hnRNP_Q_AcD; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 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; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Host-virus interaction;
KW Isopeptide bond; Methylation; Microsome; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..623
FT /note="Heterogeneous nuclear ribonucleoprotein Q"
FT /id="PRO_0000081867"
FT DOMAIN 162..241
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 243..325
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 338..408
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 448..450
FT /note="1-1"
FT REPEAT 451..453
FT /note="1-2"
FT REPEAT 460..464
FT /note="2-1"
FT REPEAT 469..472
FT /note="2-2"
FT REPEAT 478..480
FT /note="1-3"
FT REPEAT 485..488
FT /note="2-3"
FT REPEAT 498..500
FT /note="1-4"
FT REPEAT 526..528
FT /note="1-5"
FT REPEAT 539..541
FT /note="1-6"
FT REPEAT 554..556
FT /note="1-7"
FT REPEAT 557..559
FT /note="1-8"
FT REGION 400..561
FT /note="Interaction with APOBEC1"
FT REGION 448..559
FT /note="8 X 3 AA repeats of R-G-G"
FT REGION 460..488
FT /note="3 X 4 AA repeats of Y-Y-G-Y"
FT REGION 497..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..549
FT /note="Interaction with SMN"
FT /evidence="ECO:0000269|PubMed:11574476"
FT MOTIF 564..578
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 574..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 221
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 363
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 373
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12601080"
FT MOD_RES 444
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 444
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 496
FT /note="Omega-N-methylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 510
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 518
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 518
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 526
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 526
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 536
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 536
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 539
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 539
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:23455924"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009581"
FT VAR_SEQ 153..163
FT /note="YSGQQPSVGTE -> MEDHLQIPFIQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009582"
FT VAR_SEQ 302..336
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11574476,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_009583"
FT VAR_SEQ 550..623
FT /note="VRGARGGRGGNVGGKRKADGYNQPDSKRRQTNNQNWGSQPIAQQPLQGGDHS
FT GNYGYKSENQEFYQDTFGQQWK -> QGKGVEAGPDLLQ (in isoform 3,
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11574476,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9847309"
FT /id="VSP_009584"
FT CONFLICT 265
FT /note="K -> Q (in Ref. 1; AAD38198)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="G -> S (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="F -> S (in Ref. 7; AAH40844)"
FT /evidence="ECO:0000305"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:2MXT"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:2MXT"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2MXT"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:2MXT"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:2MXT"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:6KOR"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:6KOR"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:6KOR"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:6KOR"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:6KOR"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:6KOR"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:6KOR"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:6KOR"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:6KOR"
FT HELIX 351..359
FT /evidence="ECO:0007829|PDB:6KOR"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6KOR"
FT STRAND 371..380
FT /evidence="ECO:0007829|PDB:6KOR"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:6KOR"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:2DGU"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:6KOR"
FT CONFLICT O60506-3:550..551
FT /note="QG -> V (in Ref. 5; AAK59705)"
FT /evidence="ECO:0000305"
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
