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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) (pp68)

 HNRPQ_MOUSE             Reviewed;         623 AA.
Q7TMK9; O88991; Q2YDV8; Q68ED6; Q80YV6; Q8BGP1; Q8C5K6; Q8CGC2;
Q91ZR0; Q99KU9; Q9QYF4;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
10-OCT-2018, entry version 143.
RecName: Full=Heterogeneous nuclear ribonucleoprotein Q;
Short=hnRNP Q;
AltName: Full=Glycine- and tyrosine-rich RNA-binding protein;
Short=GRY-RBP;
AltName: Full=NS1-associated protein 1;
AltName: Full=Synaptotagmin-binding, cytoplasmic RNA-interacting protein;
AltName: Full=pp68;
Name=Syncrip; Synonyms=Hnrpq, Nsap1, Nsap1l;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Du G., Pan M., Zhou Y., Chen J., Yao H., Yuan J., Qiang B.;
"Cloning of human and mouse GRY-RBP cDNA.";
Chin. Sci. Bull. 45:343-349(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 257-282,
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION
WITH SYT7; SYT8 AND SYT9.
STRAIN=ddY; TISSUE=Brain, and Cerebellum;
PubMed=10734137; DOI=10.1074/jbc.275.13.9823;
Mizutani A., Fukuda M., Ibata K., Shiraishi Y., Mikoshiba K.;
"SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
ribonucleoprotein R, interacts with ubiquitous synaptotagmin
isoforms.";
J. Biol. Chem. 275:9823-9831(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo, and Medulla oblongata;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, Czech II, and FVB/N;
TISSUE=Embryo, Embryonic brain, Kidney, Mammary tumor, and Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 66-561 (ISOFORM 2).
Zhou M., Raschke W.C.;
"Mus musculus RRM RNA binding protein, NSAP1.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT TYROSINE RESIDUES, AND ASSOCIATION WITH POLYSOMES.
TISSUE=Adipocyte;
PubMed=11994298; DOI=10.1074/jbc.M202556200;
Hresko R.C., Mueckler M.;
"Identification of pp68 as the tyrosine-phosphorylated form of
SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein.";
J. Biol. Chem. 277:25233-25238(2002).
[7]
TISSUE SPECIFICITY.
PubMed=9847309;
Harris C.E., Boden R.A., Astell C.R.;
"A novel heterogeneous nuclear ribonucleoprotein-like protein
interacts with NS1 of the minute virus of mice.";
J. Virol. 73:72-80(1999).
[8]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH SMN.
PubMed=11773003; DOI=10.1093/hmg/11.1.93;
Rossoll W., Kroening A.-K., Ohndorf U.-M., Steegborn C., Jablonka S.,
Sendtner M.;
"Specific interaction of Smn, the spinal muscular atrophy determining
gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA
processing in motor axons?";
Hum. Mol. Genet. 11:93-105(2002).
[9]
IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=19470752; DOI=10.1128/MCB.00296-09;
Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
"Three proteins of the U7-specific Sm ring function as the molecular
ruler to determine the site of 3'-end processing in mammalian histone
pre-mRNA.";
Mol. Cell. Biol. 29:4045-4056(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)
implicated in mRNA processing mechanisms. Component of the CRD-
mediated complex that promotes MYC mRNA stability. Isoform 1 and
isoform 2 are associated in vitro with pre-mRNA, splicing
intermediates and mature mRNA protein complexes. Isoform 1 binds
to apoB mRNA AU-rich sequences (By similarity). 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 (By similarity). 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 (By similarity).
Interacts in vitro preferentially with poly(A) and poly(U) RNA
sequences. Isoform 2 may be involved in cytoplasmic vesicle-based
mRNA transport through interaction with synaptotagmins.
{ECO:0000250}.
-!- SUBUNIT: Identified in the spliceosome C complex. Component of the
coding region determinant (CRD)-mediated complex, composed of
DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a mRNP
complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU,
IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
YBX1. Identified in a mRNP granule complex, at least composed of
ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with
GTPBP1 (By similarity). Isoform 1 is a component of the APOB mRNA
editosome complex. Isoform 1 interacts with APOBEC1 and A1CF. Part
of a complex associated with the FOS mCRD domain and consisting of
PABPC1, PAIP1, CSDE1/UNR, HNRPD and SYNCRIP. Isoform 2 interacts
with HNRPR. Interacts with POLR2A hyperphosphorylated C-terminal
domain. Interacts with HABP4 (By similarity). Identified in a
histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
SNRPB, SYNCRIP and YBX1. Isoform 1 and isoform 2 interact with
SMN. Isoform 2 interacts through its C-terminal domain with SYT7,
SYT8 and SYT9. The non-phosphorylated and phosphorylated forms are
colocalized with PAIP1 in polysomes.
{ECO:0000250|UniProtKB:O60506, ECO:0000269|PubMed:10734137,
ECO:0000269|PubMed:11773003, ECO:0000269|PubMed:19470752}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10734137,
ECO:0000269|PubMed:11994298}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:O43390}. Microsome
{ECO:0000269|PubMed:11994298}. Cytoplasm
{ECO:0000269|PubMed:10734137}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs (By similarity). Isoforms 1
and 2 are expressed predominantly in the nucleoplasm. According to
PubMed:10734137, isoform 2 is predominantly found in cytoplasm.
The tyrosine phosphorylated form bound to RNA is found in
microsomes. {ECO:0000250|UniProtKB:O43390,
ECO:0000269|PubMed:10734137}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7TMK9-1; Sequence=Displayed;
Name=2;
IsoId=Q7TMK9-2; Sequence=VSP_009585, VSP_009586;
Note=May be due to a competing donor splice site and to an exon
inclusion. Ref.2 (BAA88342) and Ref.4 (AAH41148) sequences are
in conflict in positions: 549:GQ->G. {ECO:0000305};
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, spleen,
lung, liver, skeletal muscle, adipocytes, kidney and testis.
{ECO:0000269|PubMed:10734137, ECO:0000269|PubMed:11773003,
ECO:0000269|PubMed:9847309}.
-!- DEVELOPMENTAL STAGE: Expressed in spinal cord at 14 dpc and
onwards. {ECO:0000269|PubMed:11773003}.
-!- DOMAIN: The domain containing eight Arg-Gly-Gly repeats (RGG/RXR-
box) may be involved in RNA-binding and protein-protein
interactions. It is methylated by PRMT1, and essential for nuclear
localization (By similarity). {ECO:0000250}.
-!- PTM: 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.
{ECO:0000269|PubMed:11994298}.
-!- SEQUENCE CAUTION:
Sequence=AAH55863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH58807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF093821; AAC62511.1; -; mRNA.
EMBL; AB035725; BAA88342.1; -; mRNA.
EMBL; AK034845; BAC28852.1; -; mRNA.
EMBL; AK077588; BAC36880.1; -; mRNA.
EMBL; AK078158; BAC37152.1; -; mRNA.
EMBL; BC004001; AAH04001.1; ALT_SEQ; mRNA.
EMBL; BC041148; AAH41148.2; -; mRNA.
EMBL; BC050079; AAH50079.2; -; mRNA.
EMBL; BC055863; AAH55863.1; ALT_INIT; mRNA.
EMBL; BC058807; AAH58807.1; ALT_INIT; mRNA.
EMBL; BC080309; AAH80309.1; -; mRNA.
EMBL; BC108363; AAI08364.2; -; mRNA.
EMBL; AF408434; AAL11726.1; -; mRNA.
CCDS; CCDS23388.1; -. [Q7TMK9-2]
CCDS; CCDS57686.1; -. [Q7TMK9-1]
RefSeq; NP_001271257.1; NM_001284328.1.
RefSeq; NP_001298042.1; NM_001311113.1.
RefSeq; NP_062640.2; NM_019666.2. [Q7TMK9-1]
RefSeq; NP_062770.1; NM_019796.5. [Q7TMK9-2]
UniGene; Mm.260545; -.
ProteinModelPortal; Q7TMK9; -.
SMR; Q7TMK9; -.
BioGrid; 207955; 7.
ComplexPortal; CPX-1078; mCRD-poly(A)-bridging complex.
ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
ComplexPortal; CPX-1098; C-to-U editosome complex. [Q7TMK9-1]
IntAct; Q7TMK9; 3.
MINT; Q7TMK9; -.
STRING; 10090.ENSMUSP00000133649; -.
iPTMnet; Q7TMK9; -.
PhosphoSitePlus; Q7TMK9; -.
SwissPalm; Q7TMK9; -.
REPRODUCTION-2DPAGE; IPI00406117; -.
EPD; Q7TMK9; -.
PaxDb; Q7TMK9; -.
PeptideAtlas; Q7TMK9; -.
PRIDE; Q7TMK9; -.
Ensembl; ENSMUST00000069221; ENSMUSP00000063744; ENSMUSG00000032423. [Q7TMK9-2]
Ensembl; ENSMUST00000173801; ENSMUSP00000133649; ENSMUSG00000032423. [Q7TMK9-1]
GeneID; 56403; -.
KEGG; mmu:56403; -.
UCSC; uc009qyo.2; mouse. [Q7TMK9-2]
UCSC; uc009qyq.2; mouse. [Q7TMK9-1]
CTD; 10492; -.
MGI; MGI:1891690; Syncrip.
eggNOG; KOG0117; Eukaryota.
eggNOG; ENOG410XTJ5; LUCA.
GeneTree; ENSGT00550000074366; -.
HOVERGEN; HBG051917; -.
InParanoid; Q7TMK9; -.
KO; K13160; -.
OMA; WYQDSYG; -.
OrthoDB; EOG091G0EUB; -.
PhylomeDB; Q7TMK9; -.
TreeFam; TF314932; -.
PRO; PR:Q7TMK9; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032423; Expressed in 318 organ(s), highest expression level in ureter smooth muscle.
ExpressionAtlas; Q7TMK9; baseline and differential.
Genevisible; Q7TMK9; MM.
GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0097452; C:GAIT complex; ISO:MGI.
GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0008143; F:poly(A) binding; IDA:MGI.
GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
CDD; cd12483; RRM1_hnRNPQ; 1.
CDD; cd12489; RRM2_hnRNPQ; 1.
Gene3D; 3.30.70.330; -; 3.
InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
InterPro; IPR034544; hnRNPQ_RRM1.
InterPro; IPR034548; hnRNPQ_RRM2.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 3.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Endoplasmic reticulum; Isopeptide bond;
Methylation; Microsome; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
RNA-binding; Spliceosome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O60506}.
CHAIN 2 623 Heterogeneous nuclear ribonucleoprotein
Q.
/FTId=PRO_0000081868.
DOMAIN 162 241 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 243 325 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 338 408 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REPEAT 448 450 1-1.
REPEAT 451 453 1-2.
REPEAT 460 464 2-1.
REPEAT 469 472 2-2.
REPEAT 478 480 1-3.
REPEAT 485 488 2-3.
REPEAT 498 500 1-4.
REPEAT 526 528 1-5.
REPEAT 539 541 1-6.
REPEAT 554 556 1-7.
REPEAT 557 559 1-8.
REGION 400 561 Interaction with APOBEC1. {ECO:0000250}.
REGION 448 559 8 X 3 AA repeats of R-G-G.
REGION 460 488 3 X 4 AA repeats of Y-Y-G-Y.
REGION 518 549 Interaction with SMN. {ECO:0000250}.
MOTIF 564 578 Bipartite nuclear localization signal.
{ECO:0000255}.
COMPBIAS 431 434 Poly-Tyr.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 221 221 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 363 363 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 373 373 Phosphotyrosine.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 444 444 Asymmetric dimethylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 444 444 Omega-N-methylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 496 496 Omega-N-methylarginine; by PRMT1.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 510 510 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 518 518 Asymmetric dimethylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 518 518 Omega-N-methylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 526 526 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 526 526 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 536 536 Asymmetric dimethylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 536 536 Omega-N-methylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 539 539 Asymmetric dimethylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 539 539 Omega-N-methylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:O60506}.
MOD_RES 587 587 Phosphoserine.
{ECO:0000250|UniProtKB:O60506}.
CROSSLNK 168 168 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60506}.
CROSSLNK 607 607 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O60506}.
VAR_SEQ 550 562 VRGARGGRGGNVG -> QGKGVEAGPDLLQ (in
isoform 2). {ECO:0000303|PubMed:10734137,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.5}.
/FTId=VSP_009585.
VAR_SEQ 563 623 Missing (in isoform 2).
{ECO:0000303|PubMed:10734137,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.5}.
/FTId=VSP_009586.
CONFLICT 143 143 K -> E (in Ref. 4; AAH58807).
{ECO:0000305}.
CONFLICT 194 194 M -> T (in Ref. 4; AAH50079).
{ECO:0000305}.
CONFLICT 201 201 L -> LTGL (in Ref. 1; AAC62511).
{ECO:0000305}.
CONFLICT 220 220 V -> A (in Ref. 1; AAC62511).
{ECO:0000305}.
CONFLICT 291 291 L -> Q (in Ref. 1; AAC62511).
{ECO:0000305}.
CONFLICT 298 298 T -> A (in Ref. 1; AAC62511).
{ECO:0000305}.
CONFLICT 407 407 K -> N (in Ref. 3; BAC37152).
{ECO:0000305}.
CONFLICT 411 411 Q -> K (in Ref. 3; BAC37152).
{ECO:0000305}.
CONFLICT 421 421 Q -> H (in Ref. 3; BAC37152).
{ECO:0000305}.
CONFLICT 528 528 G -> A (in Ref. 1; AAC62511).
{ECO:0000305}.
CONFLICT 543 543 Missing (in Ref. 1; AAC62511).
{ECO:0000305}.
CONFLICT 582 582 N -> H (in Ref. 1; AAC62511).
{ECO:0000305}.
SEQUENCE 623 AA; 69633 MW; 8139FF9E2C8FB304 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 EEILEKSFSQ
FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR
QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG
YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG
GAQQQRGRGV RGARGGRGGN VGGKRKADGY NQPDTKRRQT NNQNWGSQPI AQQPLQGGDH
SGNYGYKSEN QEFYQDTFGQ QWK


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