ID   SLAI2_HUMAN             Reviewed;         581 AA.
AC   Q9P270; A8K4P1; Q8N5R3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=SLAIN motif-containing protein 2;
GN   Name=SLAIN2; Synonyms=KIAA1458;
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 [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA] OF 180-581.
RC   TISSUE=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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-48 AND SER-160, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-48; SER-63; SER-147;
RP   SER-179; SER-247; SER-250; SER-251; SER-254; SER-323; SER-377; SER-413;
RP   SER-456; SER-462 AND SER-467, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-462 AND SER-467, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-63; SER-134; SER-147;
RP   SER-179; SER-247; SER-315; SER-323; SER-377; SER-391; SER-433; SER-456;
RP   SER-462 AND SER-467, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-63 AND SER-391, AND
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   [13]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-551, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 574-581 IN COMPLEX WITH CLIP1,
RP   FUNCTION, CIRCULAR DICHROISM, COILED-COIL DOMAIN, INTERACTION WITH CLIP1;
RP   CLIP2; CLASP1; CKAP5; MAPRE1 AND MAPRE3, PHOSPHORYLATION, MUTAGENESIS OF
RP   TYR-581, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21646404; DOI=10.1083/jcb.201012179;
RA   van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M.,
RA   Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O.,
RA   Akhmanova A.;
RT   "SLAIN2 links microtubule plus end-tracking proteins and controls
RT   microtubule growth in interphase.";
RL   J. Cell Biol. 193:1083-1099(2011).
CC   -!- FUNCTION: Binds to the plus end of microtubules and regulates
CC       microtubule dynamics and microtubule organization. Promotes cytoplasmic
CC       microtubule nucleation and elongation. Required for normal structure of
CC       the microtubule cytoskeleton during interphase.
CC       {ECO:0000269|PubMed:21646404}.
CC   -!- SUBUNIT: Interacts with CLIP1, CLIP2, CKAP5, CLASP1, MAPRE1 and MAPRE3.
CC       {ECO:0000269|PubMed:21646404}.
CC   -!- INTERACTION:
CC       Q9P270; Q14008: CKAP5; NbExp=4; IntAct=EBI-3959887, EBI-310585;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes with
CC       microtubules. Detected at the plus end of growing microtubules.
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in adult
CC       liver, testis and ovary, and lowest levels in adult pancreas and spleen
CC       and in fetal brain. {ECO:0000269|PubMed:10819331}.
CC   -!- DOMAIN: The N-terminus forms a two-stranded coiled coil.
CC   -!- PTM: Is highly phosphorylated during mitosis, but not during
CC       interphase. The highly phosphorylated form does not localize at
CC       microtubule plus ends and does not interact with MAPRE1 or CKAP5.
CC       {ECO:0000269|PubMed:21646404}.
CC   -!- SIMILARITY: Belongs to the SLAIN motif-containing family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31691.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA95982.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB040891; BAA95982.1; ALT_INIT; mRNA.
DR   EMBL; AK291006; BAF83695.1; -; mRNA.
DR   EMBL; BC031691; AAH31691.2; ALT_INIT; mRNA.
DR   CCDS; CCDS47051.1; -.
DR   RefSeq; NP_065897.1; NM_020846.1.
DR   PDB; 3RDV; X-ray; 1.75 A; E/F/G/H=574-581.
DR   PDBsum; 3RDV; -.
DR   AlphaFoldDB; Q9P270; -.
DR   SMR; Q9P270; -.
DR   BioGRID; 121654; 131.
DR   ELM; Q9P270; -.
DR   IntAct; Q9P270; 64.
DR   MINT; Q9P270; -.
DR   STRING; 9606.ENSP00000264313; -.
DR   GlyGen; Q9P270; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9P270; -.
DR   PhosphoSitePlus; Q9P270; -.
DR   BioMuta; SLAIN2; -.
DR   DMDM; 166977679; -.
DR   EPD; Q9P270; -.
DR   jPOST; Q9P270; -.
DR   MassIVE; Q9P270; -.
DR   MaxQB; Q9P270; -.
DR   PaxDb; 9606-ENSP00000264313; -.
DR   PeptideAtlas; Q9P270; -.
DR   ProteomicsDB; 83740; -.
DR   Pumba; Q9P270; -.
DR   Antibodypedia; 23807; 128 antibodies from 26 providers.
DR   DNASU; 57606; -.
DR   Ensembl; ENST00000264313.11; ENSP00000264313.5; ENSG00000109171.15.
DR   GeneID; 57606; -.
DR   KEGG; hsa:57606; -.
DR   MANE-Select; ENST00000264313.11; ENSP00000264313.5; NM_020846.2; NP_065897.1.
DR   UCSC; uc003gya.5; human.
DR   AGR; HGNC:29282; -.
DR   CTD; 57606; -.
DR   DisGeNET; 57606; -.
DR   GeneCards; SLAIN2; -.
DR   HGNC; HGNC:29282; SLAIN2.
DR   HPA; ENSG00000109171; Low tissue specificity.
DR   MIM; 610492; gene.
DR   neXtProt; NX_Q9P270; -.
DR   OpenTargets; ENSG00000109171; -.
DR   PharmGKB; PA162403457; -.
DR   VEuPathDB; HostDB:ENSG00000109171; -.
DR   eggNOG; ENOG502QSZP; Eukaryota.
DR   GeneTree; ENSGT00390000017860; -.
DR   HOGENOM; CLU_027278_2_0_1; -.
DR   InParanoid; Q9P270; -.
DR   OMA; PLKAMAN; -.
DR   OrthoDB; 5260916at2759; -.
DR   PhylomeDB; Q9P270; -.
DR   TreeFam; TF331616; -.
DR   PathwayCommons; Q9P270; -.
DR   SignaLink; Q9P270; -.
DR   SIGNOR; Q9P270; -.
DR   BioGRID-ORCS; 57606; 29 hits in 1153 CRISPR screens.
DR   ChiTaRS; SLAIN2; human.
DR   GenomeRNAi; 57606; -.
DR   Pharos; Q9P270; Tbio.
DR   PRO; PR:Q9P270; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9P270; Protein.
DR   Bgee; ENSG00000109171; Expressed in tibialis anterior and 192 other cell types or tissues.
DR   ExpressionAtlas; Q9P270; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR   GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR   InterPro; IPR026179; Slain.
DR   PANTHER; PTHR22406:SF4; SLAIN MOTIF-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR22406; UNCHARACTERIZED; 1.
DR   Pfam; PF15301; SLAIN; 1.
DR   Genevisible; Q9P270; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Methylation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..581
FT                   /note="SLAIN motif-containing protein 2"
FT                   /id="PRO_0000316965"
FT   REGION          26..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          4..39
FT                   /evidence="ECO:0000269|PubMed:21646404"
FT   COMPBIAS        108..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            581
FT                   /note="Important for interaction with CLIP1"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CI08"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         462
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         538
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CI08"
FT   MOD_RES         551
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MUTAGEN         581
FT                   /note="Missing: Abolishes interaction with CLIP1."
FT                   /evidence="ECO:0000269|PubMed:21646404"
FT   CONFLICT        233
FT                   /note="N -> D (in Ref. 2; BAF83695)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        558
FT                   /note="V -> A (in Ref. 2; BAF83695)"
FT                   /evidence="ECO:0000305"
FT   HELIX           575..577
FT                   /evidence="ECO:0007829|PDB:3RDV"
SQ   SEQUENCE   581 AA;  62543 MW;  44B10B1BBD555B26 CRC64;
     MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGSLGPGSPV RAGASIPSSG
     AASPRGFPLG LSAKSGGGPG SGPRRTSSEE LRDATSLLAA GEGGLLDEVE PLRPDELERL
     SGWEEEEESW LYSSPKKKLT PMQKSVSPLV WCRQVLDYPS PDVECAKKSL IHKLDQTMSA
     LKRQNLYNNP FNSMSYTSPY SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNLKSS
     DRNPPLSPQS SIDSELSASE LDEDSIGSNY KLNDVTDVQI LARMQEESLR QEYAATTSRR
     SSGSSCNSTR RGTFSDQELD AQSLDDEDDN MHHAVYPAVN RFSPSPRNSP RPSPKQSPRN
     SPRSRSPARG IEYSRVSPQP MISRLQQPRL SLQGHPTDLQ TSNVKNEEKL RRSLPNLSRT
     SNTQVDSVKS SRSDSNFQVP NGGIPRMQPQ ASAIPSPGKF RSPAAPSPLA LRQPVKAFSN
     HGSGSPGSQE ITQLTQTTSS PGPPMVQSTV SANPPSNINS ATLTRPAGTT AMRSGLPRPS
     APSAGGIPVP RSKLAQPVRR SLPAPKTYGS MKDDSWKDGC Y
//