KHDR2_HUMAN
ID KHDR2_HUMAN Reviewed; 349 AA.
AC Q5VWX1; A8K7M8; Q8N4I4; Q8TCZ4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 2;
DE AltName: Full=Sam68-like mammalian protein 1;
DE Short=SLM-1;
DE Short=hSLM-1;
GN Name=KHDRBS2; Synonyms=SLM1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12549823; DOI=10.1023/a:1021246109101;
RA Wang L., Xu J., Zeng L., Ye X., Wu Q., Dai J., Ji C., Gu S., Zhao C.,
RA Xie Y., Mao Y.;
RT "Cloning and characterization of a novel human STAR domain containing cDNA
RT KHDRBS2.";
RL Mol. Biol. Rep. 29:369-375(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP METHYLATION.
RX PubMed=12529443; DOI=10.1091/mbc.e02-08-0484;
RA Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.;
RT "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-
RT methyltransferase 1.";
RL Mol. Biol. Cell 14:274-287(2003).
RN [7]
RP INTERACTION WITH RBMX.
RX PubMed=19282290; DOI=10.1074/jbc.m901026200;
RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M.,
RA Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R.,
RA Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection
RT by binding to CC(A/C)-rich regions in pre-mRNA.";
RL J. Biol. Chem. 284:14303-14315(2009).
CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of
CC alternative splicing and influences mRNA splice site selection and exon
CC inclusion. Binds both poly(A) and poly(U) homopolymers. Phosphorylation
CC by PTK6 inhibits its RNA-binding ability (By similarity). Induces an
CC increased concentration-dependent incorporation of exon in CD44 pre-
CC mRNA by direct binding to purine-rich exonic enhancer. Can regulate
CC alternative splicing of NRXN1 in the laminin G-like domain 6 containing
CC the evolutionary conserved neurexin alternative spliced segment 4 (AS4)
CC involved in neurexin selective targeting to postsynaptic partners.
CC Regulates cell-type specific alternative splicing of NRXN1 at AS4 and
CC acts synergystically with SAM68 in exon skipping. In contrast acts
CC antagonistically with SAM68 in NRXN3 exon skipping at AS4. Its
CC phosphorylation by FYN inhibits its ability to regulate splice site
CC selection. May function as an adapter protein for Src kinases during
CC mitosis. {ECO:0000250|UniProtKB:Q920F3, ECO:0000250|UniProtKB:Q9WU01}.
CC -!- SUBUNIT: Self-associates to form homooligomers (By similarity).
CC Interacts with KHDRBS1/SAM68; heterooligomer formation of KHDRBS family
CC proteins may modulate RNA substrate specificity (By similarity).
CC Interacts with RBMX (PubMed:19282290). Interacts with SAFB, SFRS9 and
CC YTHDC1. Interacts with FYN and PLCG1 (via SH3 domain). Interacts
CC (phosphorylated) with FYN, GRB2, PLCG1 and RASA1 (via SH2 domain) (By
CC similarity). {ECO:0000250|UniProtKB:Q920F3,
CC ECO:0000250|UniProtKB:Q9WU01, ECO:0000269|PubMed:19282290}.
CC -!- INTERACTION:
CC Q5VWX1; Q8WTP8: AEN; NbExp=3; IntAct=EBI-742808, EBI-8637627;
CC Q5VWX1; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-742808, EBI-742750;
CC Q5VWX1; P18075: BMP7; NbExp=3; IntAct=EBI-742808, EBI-1035195;
CC Q5VWX1; Q8NEC5: CATSPER1; NbExp=6; IntAct=EBI-742808, EBI-744545;
CC Q5VWX1; Q9Y3Y2: CHTOP; NbExp=3; IntAct=EBI-742808, EBI-347794;
CC Q5VWX1; Q9Y3Y2-3: CHTOP; NbExp=3; IntAct=EBI-742808, EBI-11984237;
CC Q5VWX1; Q14011: CIRBP; NbExp=4; IntAct=EBI-742808, EBI-538850;
CC Q5VWX1; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-742808, EBI-741032;
CC Q5VWX1; Q5D0E6-2: DALRD3; NbExp=3; IntAct=EBI-742808, EBI-9090939;
CC Q5VWX1; Q92608: DOCK2; NbExp=6; IntAct=EBI-742808, EBI-448771;
CC Q5VWX1; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-742808, EBI-11961494;
CC Q5VWX1; P02008: HBZ; NbExp=4; IntAct=EBI-742808, EBI-719843;
CC Q5VWX1; Q03014: HHEX; NbExp=3; IntAct=EBI-742808, EBI-747421;
CC Q5VWX1; P61978-2: HNRNPK; NbExp=4; IntAct=EBI-742808, EBI-7060731;
CC Q5VWX1; O43390: HNRNPR; NbExp=3; IntAct=EBI-742808, EBI-713419;
CC Q5VWX1; O75525: KHDRBS3; NbExp=4; IntAct=EBI-742808, EBI-722504;
CC Q5VWX1; Q8IXW0: LMNTD2; NbExp=3; IntAct=EBI-742808, EBI-12028858;
CC Q5VWX1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-742808, EBI-739832;
CC Q5VWX1; Q13330: MTA1; NbExp=3; IntAct=EBI-742808, EBI-714236;
CC Q5VWX1; Q96AH0: NABP1; NbExp=3; IntAct=EBI-742808, EBI-2889252;
CC Q5VWX1; Q9NQX5: NPDC1; NbExp=6; IntAct=EBI-742808, EBI-748927;
CC Q5VWX1; Q8WWY3: PRPF31; NbExp=8; IntAct=EBI-742808, EBI-1567797;
CC Q5VWX1; P79522: PRR3; NbExp=6; IntAct=EBI-742808, EBI-2803328;
CC Q5VWX1; Q13882: PTK6; NbExp=4; IntAct=EBI-742808, EBI-1383632;
CC Q5VWX1; P98175: RBM10; NbExp=3; IntAct=EBI-742808, EBI-721525;
CC Q5VWX1; Q96PK6: RBM14; NbExp=3; IntAct=EBI-742808, EBI-954272;
CC Q5VWX1; P98179: RBM3; NbExp=8; IntAct=EBI-742808, EBI-2949699;
CC Q5VWX1; P38159: RBMX; NbExp=10; IntAct=EBI-742808, EBI-743526;
CC Q5VWX1; P40938: RFC3; NbExp=3; IntAct=EBI-742808, EBI-1055010;
CC Q5VWX1; O00560: SDCBP; NbExp=6; IntAct=EBI-742808, EBI-727004;
CC Q5VWX1; Q9UQ90: SPG7; NbExp=3; IntAct=EBI-742808, EBI-717201;
CC Q5VWX1; P0DMM9: SULT1A3; NbExp=3; IntAct=EBI-742808, EBI-10196922;
CC Q5VWX1; P29597: TYK2; NbExp=7; IntAct=EBI-742808, EBI-1383454;
CC Q5VWX1; Q8TAI1: TYMSOS; NbExp=3; IntAct=EBI-742808, EBI-742060;
CC Q5VWX1; Q96MU7: YTHDC1; NbExp=6; IntAct=EBI-742808, EBI-2849854;
CC Q5VWX1; G3V1X1: ZFC3H1; NbExp=3; IntAct=EBI-742808, EBI-6448783;
CC Q5VWX1; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-742808, EBI-10486136;
CC Q5VWX1; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-742808, EBI-745520;
CC Q5VWX1; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-742808, EBI-16429014;
CC Q5VWX1; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-742808, EBI-11962574;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9WU01}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney and small
CC intestine. Weakly expressed in placenta, liver, spleen, thymus, ovary
CC and colon. {ECO:0000269|PubMed:12549823}.
CC -!- PTM: Methylated. {ECO:0000269|PubMed:12529443}.
CC -!- PTM: Tyrosine phosphorylated by FYN, PTK6 and SRC. Tyrosine
CC phosphorylated by SRC during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9WU01}.
CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000305}.
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DR EMBL; AY077838; AAL77219.1; -; mRNA.
DR EMBL; AK292043; BAF84732.1; -; mRNA.
DR EMBL; AL360220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z93021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471143; EAW88490.1; -; Genomic_DNA.
DR EMBL; BC034043; AAH34043.1; -; mRNA.
DR CCDS; CCDS4963.1; -.
DR RefSeq; NP_689901.2; NM_152688.3.
DR AlphaFoldDB; Q5VWX1; -.
DR SMR; Q5VWX1; -.
DR BioGRID; 128436; 136.
DR IntAct; Q5VWX1; 73.
DR MINT; Q5VWX1; -.
DR STRING; 9606.ENSP00000281156; -.
DR GlyGen; Q5VWX1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VWX1; -.
DR PhosphoSitePlus; Q5VWX1; -.
DR BioMuta; KHDRBS2; -.
DR DMDM; 74762274; -.
DR EPD; Q5VWX1; -.
DR jPOST; Q5VWX1; -.
DR MassIVE; Q5VWX1; -.
DR MaxQB; Q5VWX1; -.
DR PaxDb; Q5VWX1; -.
DR PeptideAtlas; Q5VWX1; -.
DR PRIDE; Q5VWX1; -.
DR ProteomicsDB; 65566; -.
DR Antibodypedia; 17553; 145 antibodies from 20 providers.
DR DNASU; 202559; -.
DR Ensembl; ENST00000281156.5; ENSP00000281156.3; ENSG00000112232.10.
DR GeneID; 202559; -.
DR KEGG; hsa:202559; -.
DR MANE-Select; ENST00000281156.5; ENSP00000281156.3; NM_152688.4; NP_689901.2.
DR UCSC; uc003peg.3; human.
DR CTD; 202559; -.
DR DisGeNET; 202559; -.
DR GeneCards; KHDRBS2; -.
DR HGNC; HGNC:18114; KHDRBS2.
DR HPA; ENSG00000112232; Tissue enhanced (brain, retina, thyroid gland).
DR MIM; 610487; gene.
DR neXtProt; NX_Q5VWX1; -.
DR OpenTargets; ENSG00000112232; -.
DR PharmGKB; PA30093; -.
DR VEuPathDB; HostDB:ENSG00000112232; -.
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000157134; -.
DR HOGENOM; CLU_034976_0_1_1; -.
DR InParanoid; Q5VWX1; -.
DR OMA; HETYEEY; -.
DR PhylomeDB; Q5VWX1; -.
DR TreeFam; TF314878; -.
DR PathwayCommons; Q5VWX1; -.
DR Reactome; R-HSA-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR SignaLink; Q5VWX1; -.
DR BioGRID-ORCS; 202559; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; KHDRBS2; human.
DR GenomeRNAi; 202559; -.
DR Pharos; Q5VWX1; Tbio.
DR PRO; PR:Q5VWX1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5VWX1; protein.
DR Bgee; ENSG00000112232; Expressed in cortical plate and 81 other tissues.
DR ExpressionAtlas; Q5VWX1; baseline and differential.
DR Genevisible; Q5VWX1; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IEA:Ensembl.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032571; Qua1_dom.
DR InterPro; IPR032335; Sam68-YY.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16274; Qua1; 1.
DR Pfam; PF16568; Sam68-YY; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Methylation; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; SH3-binding; Transcription; Transcription regulation.
FT CHAIN 1..349
FT /note="KH domain-containing, RNA-binding, signal
FT transduction-associated protein 2"
FT /id="PRO_0000308953"
FT DOMAIN 65..135
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 182..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU01"
FT MOD_RES 240
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU01"
FT VARIANT 308
FT /note="G -> A (in dbSNP:rs7449840)"
FT /id="VAR_036885"
FT CONFLICT 65
FT /note="L -> P (in Ref. 1; AAL77219)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="A -> V (in Ref. 1; AAL77219)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="R -> S (in Ref. 5; AAH34043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38927 MW; EF16E301D8A12164 CRC64;
MEEEKYLPEL MAEKDSLDPS FVHASRLLAE EIEKFQGSDG KKEDEEKKYL DVISNKNIKL
SERVLIPVKQ YPKFNFVGKL LGPRGNSLKR LQEETGAKMS ILGKGSMRDK AKEEELRKSG
EAKYAHLSDE LHVLIEVFAP PGEAYSRMSH ALEEIKKFLV PDYNDEIRQE QLRELSYLNG
SEDSGRGRGI RGRGIRIAPT APSRGRGGAI PPPPPPGRGV LTPRGSTVTR GALPVPPVAR
GVPTPRARGA PTVPGYRAPP PPAHEAYEEY GYDDGYGGEY DDQTYETYDN SYATQTQSVP
EYYDYGHGVS EDAYDSYAPE EWATTRSSLK APPQRSARGG YREHPYGRY
