KHDR3_HUMAN
ID KHDR3_HUMAN Reviewed; 346 AA.
AC O75525; Q6NUL8; Q9UPA8;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 3;
DE AltName: Full=RNA-binding protein T-Star;
DE AltName: Full=Sam68-like mammalian protein 2;
DE Short=SLM-2;
DE AltName: Full=Sam68-like phosphotyrosine protein;
GN Name=KHDRBS3; Synonyms=SALP, SLM2;
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 1), NUCLEOTIDE SEQUENCE [MRNA] OF 8-346
RP (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH P85 SUBUNIT OF
RP PI3-KINASE, AND PHOSPHORYLATION.
RC TISSUE=Retina;
RX PubMed=10564820; DOI=10.1016/s0378-1119(99)00421-7;
RA Lee J.-S., Burr J.G.;
RT "Salpalpha and Salpbeta, growth-arresting homologs of Sam68.";
RL Gene 240:133-147(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH KHDRBS1 AND RBMX,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=10332027; DOI=10.1093/hmg/8.6.959;
RA Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J.,
RA Cooke H.J., Artzt K., Eperon I.C.;
RT "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
RT binding protein implicated in spermatogenesis.";
RL Hum. Mol. Genet. 8:959-969(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Skin;
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 [4]
RP PROTEIN SEQUENCE OF 45-52 AND 154-164, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10077576; DOI=10.1073/pnas.96.6.2710;
RA Di Fruscio M., Chen T., Richard S.;
RT "Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1
RT is a Src substrate during mitosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2710-2715(1999).
RN [6]
RP INTERACTION WITH RBMY1A1.
RC TISSUE=Testis;
RX PubMed=10749975; DOI=10.1093/hmg/9.5.685;
RA Venables J.P., Elliott D.J., Makarova O.V., Makarov E.M., Cooke H.J.,
RA Eperon E.C.;
RT "RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins
RT interact with Tra2beta and affect splicing.";
RL Hum. Mol. Genet. 9:685-694(2000).
RN [7]
RP INDUCTION, AND MUTAGENESIS OF 327-LYS--TYR-346.
RX PubMed=11714634;
RA Kool J., van Zaane W., van der Eb A.J., Terleth C.;
RT "Down-regulation of T-STAR, a growth inhibitory protein, after SV40-
RT mediated immortalization.";
RL Cell Growth Differ. 12:535-541(2001).
RN [8]
RP FUNCTION.
RX PubMed=11741900; DOI=10.1074/jbc.m106836200;
RA Reddy T.R., Suhasini M., Xu W., Yeh L.-Y., Yang J.-P., Wu J., Artzt K.,
RA Wong-Staal F.;
RT "A role for KH domain proteins (Sam68-like mammalian proteins and quaking
RT proteins) in the post-transcriptional regulation of HIV replication.";
RL J. Biol. Chem. 277:5778-5784(2002).
RN [9]
RP INTERACTION WITH SIAH1, DOMAIN, AND MUTAGENESIS OF 212-ARG--PRO-251.
RX PubMed=15163637; DOI=10.1093/hmg/ddh165;
RA Venables J.P., Dalgliesh C., Paronetto M.P., Skitt L., Thornton J.K.,
RA Saunders P.T., Sette C., Jones K.T., Elliott D.J.;
RT "SIAH1 targets the alternative splicing factor T-STAR for degradation by
RT the proteasome.";
RL Hum. Mol. Genet. 13:1525-1534(2004).
RN [10]
RP SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
RX PubMed=15901763; DOI=10.1681/asn.2005020204;
RA Cohen C.D., Doran P.P., Blattner S.M., Merkle M., Wang G.Q., Schmid H.,
RA Mathieson P.W., Saleem M.A., Henger A., Rastaldi M.P., Kretzler M.;
RT "Sam68-like mammalian protein 2, identified by digital differential display
RT as expressed by podocytes, is induced in proteinuria and involved in splice
RT site selection of vascular endothelial growth factor.";
RL J. Am. Soc. Nephrol. 16:1958-1965(2005).
RN [11]
RP RNA-BINDING.
RX PubMed=19561594; DOI=10.1038/nbt.1550;
RA Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S.,
RA Blencowe B.J., Morris Q., Hughes T.R.;
RT "Rapid and systematic analysis of the RNA recognition specificities of RNA-
RT binding proteins.";
RL Nat. Biotechnol. 27:667-670(2009).
RN [12]
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 [13]
RP INTERACTION WITH SERPINB5.
RX PubMed=21725612; DOI=10.3892/or.2011.1369;
RA Lei K.F., Liu B.Y., Wang Y.F., Chen X.H., Yu B.Q., Guo Y., Zhu Z.G.;
RT "SerpinB5 interacts with KHDRBS3 and FBXO32 in gastric cancer cells.";
RL Oncol. Rep. 26:1115-1120(2011).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP 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 [15]
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 1-183 IN COMPLEX WITH RNA
RP SUBSTRATES, FUNCTION, MUTAGENESIS OF TYR-141, AND SELF-ASSOCIATION.
RX PubMed=26758068; DOI=10.1038/ncomms10355;
RA Feracci M., Foot J.N., Grellscheid S.N., Danilenko M., Stehle R.,
RA Gonchar O., Kang H.S., Dalgliesh C., Meyer N.H., Liu Y., Lahat A.,
RA Sattler M., Eperon I.C., Elliott D.J., Dominguez C.;
RT "Structural basis of RNA recognition and dimerization by the STAR proteins
RT T-STAR and Sam68.";
RL Nat. Commun. 7:10355-10355(2016).
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 preferentially to the 5'-[AU]UAAA-3' motif in vitro.
CC Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif
CC spaced by more than 15 nucleotides. Binds poly(A). RNA-binding
CC abilities are down-regulated by tyrosine kinase PTK6 (PubMed:10564820,
CC PubMed:19561594, PubMed:26758068). Involved in splice site selection of
CC vascular endothelial growth factor (PubMed:15901763). In vitro
CC regulates CD44 alternative splicing by direct binding to purine-rich
CC exonic enhancer (By similarity). Can regulate alternative splicing of
CC neurexins NRXN1-3 in the laminin G-like domain 6 containing the
CC evolutionary conserved neurexin alternative spliced segment 4 (AS4)
CC involved in neurexin selective targeting to postsynaptic partners such
CC as neuroligins and LRRTM family members (PubMed:26758068). Targeted,
CC cell-type specific splicing regulation of NRXN1 at AS4 is involved in
CC neuronal glutamatergic synapse function and plasticity (By similarity).
CC May regulate expression of KHDRBS2/SLIM-1 in defined brain neuron
CC populations by modifying its alternative splicing (By similarity). Can
CC bind FABP9 mRNA (By similarity). May play a role as a negative
CC regulator of cell growth. Inhibits cell proliferation.
CC {ECO:0000250|UniProtKB:Q9JLP1, ECO:0000250|UniProtKB:Q9R226,
CC ECO:0000269|PubMed:10564820, ECO:0000269|PubMed:15901763,
CC ECO:0000269|PubMed:19561594, ECO:0000269|PubMed:26758068}.
CC -!- FUNCTION: (Microbial infection) Involved in post-transcriptional
CC regulation of HIV-1 gene expression. {ECO:0000269|PubMed:11741900}.
CC -!- SUBUNIT: Self-associates to form homooligomers; dimerization increases
CC RNA affinity (PubMed:26758068). Interacts with KHDRBS2/SLM-1 (By
CC similarity). Interacts with KHDRBS1/SAM68; heterooligomer formation of
CC KHDRBS family proteins may modulate RNA substrate specificity
CC (PubMed:10332027). Interacts with the splicing regulatory proteins
CC SFRS9, SAFB and YTHDC1. Interacts with HNRPL (By similarity). Interacts
CC with RBMX, RBMY1A1, p85 subunit of PI3-kinase, SERPINB5
CC (PubMed:10564820, PubMed:10332027, PubMed:10749975, PubMed:21725612).
CC Interacts with SIAH1 which promotes targeting for degradation
CC (PubMed:15163637). {ECO:0000250|UniProtKB:Q9JLP1,
CC ECO:0000250|UniProtKB:Q9R226, ECO:0000269|PubMed:10332027,
CC ECO:0000269|PubMed:10564820, ECO:0000269|PubMed:10749975,
CC ECO:0000269|PubMed:15163637, ECO:0000269|PubMed:21725612}.
CC -!- INTERACTION:
CC O75525; P29972: AQP1; NbExp=3; IntAct=EBI-722504, EBI-745213;
CC O75525; Q8TBE0: BAHD1; NbExp=4; IntAct=EBI-722504, EBI-742750;
CC O75525; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-722504, EBI-741032;
CC O75525; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-722504, EBI-9679045;
CC O75525; Q92608: DOCK2; NbExp=3; IntAct=EBI-722504, EBI-448771;
CC O75525; P02008: HBZ; NbExp=3; IntAct=EBI-722504, EBI-719843;
CC O75525; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-722504, EBI-7060731;
CC O75525; Q92835: INPP5D; NbExp=3; IntAct=EBI-722504, EBI-1380477;
CC O75525; Q92835-2: INPP5D; NbExp=3; IntAct=EBI-722504, EBI-9092209;
CC O75525; Q5VWX1: KHDRBS2; NbExp=4; IntAct=EBI-722504, EBI-742808;
CC O75525; Q8IXW0: LMNTD2; NbExp=3; IntAct=EBI-722504, EBI-12028858;
CC O75525; Q6IPE9: MARK4; NbExp=3; IntAct=EBI-722504, EBI-10250211;
CC O75525; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-722504, EBI-14086479;
CC O75525; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-722504, EBI-2858213;
CC O75525; Q8WX92: NELFB; NbExp=2; IntAct=EBI-722504, EBI-347721;
CC O75525; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-722504, EBI-10329013;
CC O75525; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-722504, EBI-1567797;
CC O75525; P79522: PRR3; NbExp=3; IntAct=EBI-722504, EBI-2803328;
CC O75525; P25786: PSMA1; NbExp=3; IntAct=EBI-722504, EBI-359352;
CC O75525; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-722504, EBI-3437896;
CC O75525; Q9Y272: RASD1; NbExp=3; IntAct=EBI-722504, EBI-740818;
CC O75525; P98179: RBM3; NbExp=3; IntAct=EBI-722504, EBI-2949699;
CC O75525; P38159: RBMX; NbExp=4; IntAct=EBI-722504, EBI-743526;
CC O75525; P40938: RFC3; NbExp=3; IntAct=EBI-722504, EBI-1055010;
CC O75525; Q9UNE2: RPH3AL; NbExp=3; IntAct=EBI-722504, EBI-2855824;
CC O75525; Q9BYB0: SHANK3; NbExp=3; IntAct=EBI-722504, EBI-1752330;
CC O75525; Q96RF0: SNX18; NbExp=3; IntAct=EBI-722504, EBI-298169;
CC O75525; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-722504, EBI-10241197;
CC O75525; P29597: TYK2; NbExp=3; IntAct=EBI-722504, EBI-1383454;
CC O75525; Q96MU7: YTHDC1; NbExp=6; IntAct=EBI-722504, EBI-2849854;
CC O75525; Q5BKZ1: ZNF326; NbExp=3; IntAct=EBI-722504, EBI-2560158;
CC O75525; Q9H9D4: ZNF408; NbExp=4; IntAct=EBI-722504, EBI-347633;
CC O75525; Q86XF7: ZNF575; NbExp=3; IntAct=EBI-722504, EBI-14069183;
CC O75525; Q9UK33: ZNF580; NbExp=3; IntAct=EBI-722504, EBI-746277;
CC O75525; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-722504, EBI-16429014;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10332027,
CC ECO:0000269|PubMed:15901763}. Note=Localized in a compartment adjacent
CC to the nucleolus, but distinct from the peri-nucleolar one.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SALP-alpha;
CC IsoId=O75525-1; Sequence=Displayed;
CC Name=2; Synonyms=SALP-beta;
CC IsoId=O75525-2; Sequence=VSP_017905, VSP_017906;
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in testis,
CC skeletal muscle and brain. Expressed in the kidney only in podocytes,
CC the glomerular epithelial cells of the kidney. Strongly expressed after
CC meiosis. {ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:10332027,
CC ECO:0000269|PubMed:10564820}.
CC -!- INDUCTION: Induced in proteinuric diseases. Down-regulated in
CC immortalized fibroblasts isolated after a proliferative crisis
CC accompanied with massive cell death. {ECO:0000269|PubMed:11714634,
CC ECO:0000269|PubMed:15901763}.
CC -!- DOMAIN: The proline-rich site binds the SH3 domain of the p85 subunit
CC of PI3-kinase. {ECO:0000269|PubMed:10564820}.
CC -!- PTM: Phosphorylated on tyrosine residues. Isoform 1 C-terminal region
CC is tyrosine-rich, but isoform 2 lacking this C-terminal region is also
CC tyrosine-phosphorylated. {ECO:0000269|PubMed:10564820}.
CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000305}.
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DR EMBL; AF051321; AAC99294.1; -; mRNA.
DR EMBL; AF051322; AAC99295.1; -; mRNA.
DR EMBL; AF069681; AAC24857.1; -; mRNA.
DR EMBL; BC032606; AAH32606.1; -; mRNA.
DR EMBL; BC068536; AAH68536.1; -; mRNA.
DR CCDS; CCDS6374.1; -. [O75525-1]
DR RefSeq; NP_006549.1; NM_006558.2. [O75525-1]
DR PDB; 5EL3; X-ray; 1.59 A; A/B/C/D=50-160.
DR PDB; 5ELR; X-ray; 2.30 A; C/D=50-183.
DR PDB; 5ELS; X-ray; 2.87 A; A/B/C/D/E/F=50-160.
DR PDB; 5ELT; X-ray; 2.13 A; A/B=1-160.
DR PDB; 5EMO; X-ray; 3.03 A; A/B=1-183.
DR PDBsum; 5EL3; -.
DR PDBsum; 5ELR; -.
DR PDBsum; 5ELS; -.
DR PDBsum; 5ELT; -.
DR PDBsum; 5EMO; -.
DR AlphaFoldDB; O75525; -.
DR SMR; O75525; -.
DR BioGRID; 115899; 87.
DR IntAct; O75525; 67.
DR MINT; O75525; -.
DR STRING; 9606.ENSP00000348108; -.
DR GlyGen; O75525; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75525; -.
DR PhosphoSitePlus; O75525; -.
DR BioMuta; KHDRBS3; -.
DR EPD; O75525; -.
DR jPOST; O75525; -.
DR MassIVE; O75525; -.
DR MaxQB; O75525; -.
DR PaxDb; O75525; -.
DR PeptideAtlas; O75525; -.
DR PRIDE; O75525; -.
DR ProteomicsDB; 50061; -. [O75525-1]
DR ProteomicsDB; 50062; -. [O75525-2]
DR TopDownProteomics; O75525-2; -. [O75525-2]
DR Antibodypedia; 612; 201 antibodies from 28 providers.
DR DNASU; 10656; -.
DR Ensembl; ENST00000355849.10; ENSP00000348108.5; ENSG00000131773.14. [O75525-1]
DR GeneID; 10656; -.
DR KEGG; hsa:10656; -.
DR MANE-Select; ENST00000355849.10; ENSP00000348108.5; NM_006558.3; NP_006549.1.
DR UCSC; uc003yuv.4; human. [O75525-1]
DR CTD; 10656; -.
DR DisGeNET; 10656; -.
DR GeneCards; KHDRBS3; -.
DR HGNC; HGNC:18117; KHDRBS3.
DR HPA; ENSG00000131773; Tissue enhanced (testis).
DR MIM; 610421; gene.
DR neXtProt; NX_O75525; -.
DR OpenTargets; ENSG00000131773; -.
DR PharmGKB; PA30094; -.
DR VEuPathDB; HostDB:ENSG00000131773; -.
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000157280; -.
DR HOGENOM; CLU_034976_0_0_1; -.
DR InParanoid; O75525; -.
DR OMA; PPIVQET; -.
DR OrthoDB; 1012406at2759; -.
DR PhylomeDB; O75525; -.
DR TreeFam; TF314878; -.
DR PathwayCommons; O75525; -.
DR Reactome; R-HSA-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR SignaLink; O75525; -.
DR BioGRID-ORCS; 10656; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; KHDRBS3; human.
DR GeneWiki; KHDRBS3; -.
DR GenomeRNAi; 10656; -.
DR Pharos; O75525; Tbio.
DR PRO; PR:O75525; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O75525; protein.
DR Bgee; ENSG00000131773; Expressed in cortical plate and 188 other tissues.
DR ExpressionAtlas; O75525; baseline and differential.
DR Genevisible; O75525; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Host-virus interaction; Isopeptide bond; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; SH3-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..346
FT /note="KH domain-containing, RNA-binding, signal
FT transduction-associated protein 3"
FT /id="PRO_0000232522"
FT DOMAIN 61..127
FT /note="KH"
FT REGION 1..160
FT /note="Involved in homodimerization"
FT /evidence="ECO:0000269|PubMed:26758068"
FT REGION 212..251
FT /note="Interaction with SIAH1"
FT /evidence="ECO:0000269|PubMed:15163637"
FT REGION 213..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 270..271
FT /note="DY -> WC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10564820"
FT /id="VSP_017905"
FT VAR_SEQ 272..346
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10564820"
FT /id="VSP_017906"
FT MUTAGEN 141
FT /note="Y->E: Fails to influence alternative splicing of
FT CD44, NRXN2 and NRXN3."
FT /evidence="ECO:0000269|PubMed:26758068"
FT MUTAGEN 212..251
FT /note="Missing: Complete loss of SIAH1-mediated
FT degradation."
FT /evidence="ECO:0000269|PubMed:15163637"
FT MUTAGEN 327..346
FT /note="Missing: Complete loss of nuclear sublocalization."
FT /evidence="ECO:0000269|PubMed:11714634"
FT CONFLICT 41
FT /note="Missing (in Ref. 3; AAH68536)"
FT /evidence="ECO:0000305"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:5ELT"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:5ELT"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5ELT"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:5EL3"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5EL3"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:5EL3"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5ELT"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:5EL3"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5EL3"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5ELS"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:5EL3"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:5EL3"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:5EL3"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:5EL3"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5EL3"
SQ SEQUENCE 346 AA; 38800 MW; CA37968A4DF6D573 CRC64;
MEEKYLPELM AEKDSLDPSF THALRLVNQE IEKFQKGEGK DEEKYIDVVI NKNMKLGQKV
LIPVKQFPKF NFVGKLLGPR GNSLKRLQEE TLTKMSILGK GSMRDKAKEE ELRKSGEAKY
FHLNDDLHVL IEVFAPPAEA YARMGHALEE IKKFLIPDYN DEIRQAQLQE LTYLNGGSEN
ADVPVVRGKP TLRTRGVPAP AITRGRGGVT ARPVGVVVPR GTPTPRGVLS TRGPVSRGRG
LLTPRARGVP PTGYRPPPPP PTQETYGEYD YDDGYGTAYD EQSYDSYDNS YSTPAQSGAD
YYDYGHGLSE ETYDSYGQEE WTNSRHKAPS ARTAKGVYRD QPYGRY
