SLAI2_MOUSE
ID SLAI2_MOUSE Reviewed; 581 AA.
AC Q8CI08; Q05DK1; Q3UJI9; Q6ZPQ5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=SLAIN motif-containing protein 2;
GN Name=Slain2; Synonyms=Kiaa1458;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=DBA/2J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-406 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 182-581 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
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-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-88; SER-147; SER-248;
RP SER-316 AND SER-324, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, INTERACTION WITH CLIP1 AND MAPRE1, AND IDENTIFICATION BY MASS
RP 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).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-538 AND ARG-551, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
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).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Colocalizes with microtubules. Detected at the plus end of growing
CC microtubules (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CI08-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CI08-2; Sequence=VSP_030834;
CC -!- DOMAIN: The N-terminus forms a two-stranded coiled coil. {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLAIN motif-containing family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10836.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH10836.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential vector sequence.; Evidence={ECO:0000305};
CC Sequence=AAH38019.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98175.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE27166.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129365; BAC98175.1; ALT_INIT; mRNA.
DR EMBL; AK146432; BAE27166.1; ALT_INIT; mRNA.
DR EMBL; BC010836; AAH10836.1; ALT_SEQ; mRNA.
DR EMBL; BC038019; AAH38019.1; ALT_SEQ; mRNA.
DR CCDS; CCDS19335.2; -. [Q8CI08-2]
DR CCDS; CCDS51517.1; -. [Q8CI08-1]
DR RefSeq; NP_001106894.1; NM_001113423.2. [Q8CI08-1]
DR RefSeq; NP_705795.2; NM_153567.3. [Q8CI08-2]
DR AlphaFoldDB; Q8CI08; -.
DR SMR; Q8CI08; -.
DR BioGRID; 217891; 12.
DR IntAct; Q8CI08; 7.
DR MINT; Q8CI08; -.
DR STRING; 10090.ENSMUSP00000115871; -.
DR iPTMnet; Q8CI08; -.
DR PhosphoSitePlus; Q8CI08; -.
DR EPD; Q8CI08; -.
DR jPOST; Q8CI08; -.
DR MaxQB; Q8CI08; -.
DR PaxDb; Q8CI08; -.
DR PeptideAtlas; Q8CI08; -.
DR PRIDE; Q8CI08; -.
DR ProteomicsDB; 261417; -. [Q8CI08-1]
DR ProteomicsDB; 261418; -. [Q8CI08-2]
DR Antibodypedia; 23807; 110 antibodies from 26 providers.
DR DNASU; 75991; -.
DR Ensembl; ENSMUST00000143829; ENSMUSP00000115871; ENSMUSG00000036087. [Q8CI08-2]
DR Ensembl; ENSMUST00000144843; ENSMUSP00000116528; ENSMUSG00000036087. [Q8CI08-1]
DR GeneID; 75991; -.
DR KEGG; mmu:75991; -.
DR UCSC; uc008xsh.3; mouse. [Q8CI08-1]
DR UCSC; uc008xsi.1; mouse. [Q8CI08-2]
DR CTD; 57606; -.
DR MGI; MGI:1923241; Slain2.
DR VEuPathDB; HostDB:ENSMUSG00000036087; -.
DR eggNOG; ENOG502QSZP; Eukaryota.
DR GeneTree; ENSGT00390000017860; -.
DR HOGENOM; CLU_027278_2_0_1; -.
DR InParanoid; Q8CI08; -.
DR OMA; PTDLQTN; -.
DR OrthoDB; 616171at2759; -.
DR PhylomeDB; Q8CI08; -.
DR TreeFam; TF331616; -.
DR BioGRID-ORCS; 75991; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slain2; mouse.
DR PRO; PR:Q8CI08; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CI08; protein.
DR Bgee; ENSMUSG00000036087; Expressed in interventricular septum and 244 other tissues.
DR ExpressionAtlas; Q8CI08; baseline and differential.
DR Genevisible; Q8CI08; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISO:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IMP:UniProtKB.
DR InterPro; IPR026179; Slain.
DR PANTHER; PTHR22406; PTHR22406; 1.
DR Pfam; PF15301; SLAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..581
FT /note="SLAIN motif-containing protein 2"
FT /id="PRO_0000316967"
FT REGION 27..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..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:0000255"
FT COMPBIAS 199..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 581
FT /note="Important for interaction with CLIP1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P270"
FT MOD_RES 538
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 551
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 454..455
FT /note="AI -> ATSQRLKSLPRTSLKAKQLLPTSSTKRV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030834"
FT CONFLICT 462
FT /note="R -> H (in Ref. 2; BAE27166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 62378 MW; 1C412715B6E313DC CRC64;
MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGLLGPGSPA RVGVSTPSSG
AASPRGFPLG LGAKASGGAG SGPRRTSSED LRDATSLLAA GEGGLLDEVE PLRPDELERL
SGWEEEEESW LYSSPKKKLT PMQKSVSPLV WCRQVLDYPS PDVECAKKSL IHKLDQTMSA
LKRQNLYNNP FNSVSYSNSY SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNFKSS
SDRNPPLSPQ SSIDSELSAS ELDEDSIGSN YKLNDVTDVQ ILARMQEESL RQEYAASTSR
RSSGSSCNST RRGTFSDQEL DAQSLDDEDD SLQHAVHPAL NRFSPSPRNS PRPSPKQSPR
NSPRSRSPAR GIEYSRASPQ PMISRLQQPR LSLQGHPTDL QTSNVKNEEK LRRSLPNLSR
TSSTQVDSVK SSRSDSNFQV PNGGIPRMQP QASAIPSPGK FRSPAAPSPL ALRQPVKAFS
NHGSGSGSQE TTQFTQTTSS PGPPVVQNSA PANPSSNINS ATLTRPAGTT AMRSGLPRPS
APSAGGIPVP RSKLVQPVRR SLPAPKSYGS MKDDSWKDGC Y
