SPDLY_HUMAN
ID SPDLY_HUMAN Reviewed; 605 AA.
AC Q96EA4; B4E393; C9JS47; Q8TEC8; Q9HD44; Q9NX97;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein Spindly {ECO:0000255|HAMAP-Rule:MF_03041};
DE Short=hSpindly;
DE AltName: Full=Arsenite-related gene 1 protein;
DE AltName: Full=Coiled-coil domain-containing protein 99 {ECO:0000255|HAMAP-Rule:MF_03041};
DE AltName: Full=Rhabdomyosarcoma antigen MU-RMS-40.4A;
DE AltName: Full=Spindle apparatus coiled-coil domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03041};
GN Name=SPDL1 {ECO:0000255|HAMAP-Rule:MF_03041};
GN Synonyms=CCDC99 {ECO:0000255|HAMAP-Rule:MF_03041};
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 2), AND VARIANTS HIS-508 AND SER-586.
RA Gu Y.Q., Yang L., Yang Q.S., Wu H., Pang Z.M., Xia F., Ying K., Mao Y.M.,
RA Xie Y.;
RT "Cloning a novel human cDNA having elevated expression when induced with
RT arsenite.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HIS-508 AND SER-586.
RC TISSUE=Embryonic rhabdomyosarcoma;
RA Behrends U., Gotz C., Mautner J.;
RT "SEREX-defined rhabdomyosarcoma antigens.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP HIS-508 AND SER-586.
RC TISSUE=Colon, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-508
RP AND SER-586.
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17576797; DOI=10.1083/jcb.200702062;
RA Griffis E.R., Stuurman N., Vale R.D.;
RT "Spindly, a novel protein essential for silencing the spindle assembly
RT checkpoint, recruits dynein to the kinetochore.";
RL J. Cell Biol. 177:1005-1015(2007).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP FUNCTION, INTERACTION WITH KNTC1 AND ZW10, AND SUBCELLULAR LOCATION.
RX PubMed=19468067; DOI=10.1083/jcb.200812167;
RA Chan Y.W., Fava L.L., Uldschmid A., Schmitz M.H.A., Gerlich D.W.,
RA Nigg E.A., Santamaria A.;
RT "Mitotic control of kinetochore-associated dynein and spindle orientation
RT by human Spindly.";
RL J. Cell Biol. 185:859-874(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-515, VARIANT
RP [LARGE SCALE ANALYSIS] HIS-508, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [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-513 AND SER-515, VARIANT
RP [LARGE SCALE ANALYSIS] HIS-508, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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 FUNCTION, AND INTERACTION WITH DYNEIN INTERMEDIATE CHAIN AND DCTN1.
RX PubMed=25035494; DOI=10.1126/science.1254198;
RA McKenney R.J., Huynh W., Tanenbaum M.E., Bhabha G., Vale R.D.;
RT "Activation of cytoplasmic dynein motility by dynactin-cargo adapter
RT complexes.";
RL Science 345:337-341(2014).
RN [13]
RP FUNCTION, INTERACTION WITH USP45, UBIQUITINATION, AND DEUBIQUITINATION BY
RP USP45.
RX PubMed=30258100; DOI=10.1038/s41598-018-32685-8;
RA Conte C., Griffis E.R., Hickson I., Perez-Oliva A.B.;
RT "USP45 and Spindly are part of the same complex implicated in cell
RT migration.";
RL Sci. Rep. 8:14375-14375(2018).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-508, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-508, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-508, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Required for the localization of dynein and dynactin to the
CC mitotic kintochore. Dynein is believed to control the initial lateral
CC interaction between the kinetochore and spindle microtubules and to
CC facilitate the subsequent formation of end-on kinetochore-microtubule
CC attachments mediated by the NDC80 complex. Also required for correct
CC spindle orientation. Does not appear to be required for the removal of
CC spindle assembly checkpoint (SAC) proteins from the kinetochore upon
CC bipolar spindle attachment (PubMed:17576797, PubMed:19468067). Acts as
CC an adapter protein linking the dynein motor complex to various cargos
CC and converts dynein from a non-processive to a highly processive motor
CC in the presence of dynactin. Facilitates the interaction between dynein
CC and dynactin and activates dynein processivity (the ability to move
CC along a microtubule for a long distance without falling off the track)
CC (PubMed:25035494). Plays a role in cell migration (PubMed:30258100).
CC {ECO:0000255|HAMAP-Rule:MF_03041, ECO:0000269|PubMed:17576797,
CC ECO:0000269|PubMed:19468067, ECO:0000269|PubMed:25035494,
CC ECO:0000269|PubMed:30258100}.
CC -!- SUBUNIT: Interacts with KNTC1 and ZW10. These interactions appear weak
CC and may be transient or indirect (PubMed:19468067). Interacts with
CC dynein intermediate chain and dynactin (DCTN1) (PubMed:25035494).
CC Interacts with the catalytically active form of USP45
CC (PubMed:30258100). {ECO:0000255|HAMAP-Rule:MF_03041,
CC ECO:0000269|PubMed:19468067, ECO:0000269|PubMed:25035494,
CC ECO:0000269|PubMed:30258100}.
CC -!- INTERACTION:
CC Q96EA4; P35219: CA8; NbExp=6; IntAct=EBI-715381, EBI-718700;
CC Q96EA4; Q8WXU2: DNAAF4; NbExp=3; IntAct=EBI-715381, EBI-2946907;
CC Q96EA4; Q8WXU2-2: DNAAF4; NbExp=3; IntAct=EBI-715381, EBI-9381887;
CC Q96EA4; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-715381, EBI-2557469;
CC Q96EA4; Q14D33: RTP5; NbExp=3; IntAct=EBI-715381, EBI-10217913;
CC Q96EA4; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-715381, EBI-3650647;
CC Q96EA4; Q9Y4E8: USP15; NbExp=3; IntAct=EBI-715381, EBI-1043104;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Chromosome, centromere, kinetochore. Nucleus.
CC Cytoplasm, cytoskeleton, spindle pole. Note=Localizes to the nucleus in
CC interphase and to the kinetochore in early prometaphase. Relocalizes to
CC the mitotic spindle pole before metaphase and is subsequently lost from
CC the spindle poles after chromosome congression is completed. Removal of
CC this protein from the kinetochore requires the dynein/dynactin complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96EA4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96EA4-2; Sequence=VSP_022777;
CC Name=3;
CC IsoId=Q96EA4-3; Sequence=VSP_054244;
CC -!- PTM: Monoubiquitinated with'Lys-48' linkage (PubMed:30258100).
CC Deubiquitinated by USP45 (PubMed:30258100).
CC {ECO:0000269|PubMed:30258100}.
CC -!- SIMILARITY: Belongs to the Spindly family. {ECO:0000255|HAMAP-
CC Rule:MF_03041}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01408.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91119.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB85022.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF269167; AAG01408.1; ALT_FRAME; mRNA.
DR EMBL; AY517557; AAT44530.1; -; mRNA.
DR EMBL; AK074227; BAB85022.1; ALT_INIT; mRNA.
DR EMBL; AK000371; BAA91119.1; ALT_FRAME; mRNA.
DR EMBL; AK304623; BAG65405.1; -; mRNA.
DR EMBL; AC008680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012568; AAH12568.1; -; mRNA.
DR CCDS; CCDS4370.1; -. [Q96EA4-1]
DR RefSeq; NP_001316570.1; NM_001329641.1. [Q96EA4-1]
DR RefSeq; NP_060255.3; NM_017785.4. [Q96EA4-1]
DR AlphaFoldDB; Q96EA4; -.
DR SMR; Q96EA4; -.
DR BioGRID; 120253; 293.
DR DIP; DIP-47296N; -.
DR IntAct; Q96EA4; 26.
DR MINT; Q96EA4; -.
DR STRING; 9606.ENSP00000265295; -.
DR iPTMnet; Q96EA4; -.
DR PhosphoSitePlus; Q96EA4; -.
DR BioMuta; SPDL1; -.
DR DMDM; 296452913; -.
DR EPD; Q96EA4; -.
DR jPOST; Q96EA4; -.
DR MassIVE; Q96EA4; -.
DR MaxQB; Q96EA4; -.
DR PaxDb; Q96EA4; -.
DR PeptideAtlas; Q96EA4; -.
DR PRIDE; Q96EA4; -.
DR ProteomicsDB; 5884; -.
DR ProteomicsDB; 76388; -. [Q96EA4-1]
DR ProteomicsDB; 76389; -. [Q96EA4-2]
DR Antibodypedia; 28760; 246 antibodies from 30 providers.
DR DNASU; 54908; -.
DR Ensembl; ENST00000265295.9; ENSP00000265295.4; ENSG00000040275.17. [Q96EA4-1]
DR GeneID; 54908; -.
DR KEGG; hsa:54908; -.
DR MANE-Select; ENST00000265295.9; ENSP00000265295.4; NM_017785.5; NP_060255.3.
DR UCSC; uc003mae.5; human. [Q96EA4-1]
DR CTD; 54908; -.
DR DisGeNET; 54908; -.
DR GeneCards; SPDL1; -.
DR HGNC; HGNC:26010; SPDL1.
DR HPA; ENSG00000040275; Tissue enhanced (testis).
DR MIM; 616401; gene.
DR neXtProt; NX_Q96EA4; -.
DR OpenTargets; ENSG00000040275; -.
DR PharmGKB; PA144596466; -.
DR VEuPathDB; HostDB:ENSG00000040275; -.
DR eggNOG; ENOG502S27G; Eukaryota.
DR GeneTree; ENSGT00510000047951; -.
DR HOGENOM; CLU_031713_0_0_1; -.
DR InParanoid; Q96EA4; -.
DR OMA; SCPNNLE; -.
DR OrthoDB; 1595638at2759; -.
DR PhylomeDB; Q96EA4; -.
DR TreeFam; TF332470; -.
DR PathwayCommons; Q96EA4; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q96EA4; -.
DR SIGNOR; Q96EA4; -.
DR BioGRID-ORCS; 54908; 755 hits in 1090 CRISPR screens.
DR ChiTaRS; SPDL1; human.
DR GenomeRNAi; 54908; -.
DR Pharos; Q96EA4; Tbio.
DR PRO; PR:Q96EA4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96EA4; protein.
DR Bgee; ENSG00000040275; Expressed in secondary oocyte and 145 other tissues.
DR ExpressionAtlas; Q96EA4; baseline and differential.
DR Genevisible; Q96EA4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0043515; F:kinetochore binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
DR HAMAP; MF_03041; SPDLY; 1.
DR InterPro; IPR028593; SPDLY_chordates.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..605
FT /note="Protein Spindly"
FT /id="PRO_0000274516"
FT REGION 544..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..442
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03041"
FT COMPBIAS 547..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923A2"
FT VAR_SEQ 105..182
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054244"
FT VAR_SEQ 178..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022777"
FT VARIANT 508
FT /note="Y -> H (in dbSNP:rs3797713)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.2, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT /id="VAR_030307"
FT VARIANT 586
FT /note="L -> S (in dbSNP:rs3777084)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.2"
FT /id="VAR_030308"
FT CONFLICT 89
FT /note="M -> I (in Ref. 1; AAG01408)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> H (in Ref. 3; BAB85022)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="E -> G (in Ref. 3; BAB85022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 605 AA; 70172 MW; 1F8D38C9261D6605 CRC64;
MEADIITNLR CRLKEAEEER LKAAQYGLQL VESQNELQNQ LDKCRNEMMT MTESYEQEKY
TLQREVELKS RMLESLSCEC EAIKQQQKMH LEKLEEQLSR SHGQEVNELK TKIEKLKVEL
DEARLSEKQL KHQVDHQKEL LSCKSEELRV MSERVQESMS SEMLALQIEL TEMESMKTTL
KEEVNELQYR QEQLELLITN LMRQVDRLKE EKEEREKEAV SYYNALEKAR VANQDLQVQL
DQALQQALDP NSKGNSLFAE VEDRRAAMER QLISMKVKYQ SLKKQNVFNR EQMQRMKLQI
ATLLQMKGSQ TEFEQQERLL AMLEQKNGEI KHLLGEIRNL EKFKNLYDSM ESKPSVDSGT
LEDNTYYTDL LQMKLDNLNK EIESTKGELS IQRMKALFES QRALDIERKL FANERCLQLS
ESENMKLRAK LDELKLKYEP EETVEVPVLK KRREVLPVDI TTAKDACVNN SALGGEVYRL
PPQKEETQSC PNSLEDNNLQ LEKSVSIYTP VVSLSPHKNL PVDMQLKKEK KCVKLIGVPA
DAEALSERSG NTPNSPRLAA ESKLQTEVKE GKETSSKLEK ETCKKLHPIL YVSSKSTPET
QCPQQ
