GA2L1_HUMAN
ID GA2L1_HUMAN Reviewed; 681 AA.
AC Q99501; B5MCR7; Q53EN7; Q92640; Q9BUY9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=GAS2-like protein 1;
DE AltName: Full=GAS2-related protein on chromosome 22;
DE AltName: Full=Growth arrest-specific protein 2-like 1;
GN Name=GAS2L1; Synonyms=GAR22;
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 [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3).
RX PubMed=8975699; DOI=10.1006/geno.1996.0625;
RA Zucman-Rossi J., Legoix P., Thomas G.;
RT "Identification of new members of the Gas2 and Ras families in the 22q12
RT chromosome region.";
RL Genomics 38:247-254(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 [5]
RP FUNCTION, AND ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=12584248; DOI=10.1242/jcs.00272;
RA Goriounov D., Leung C.L., Liem R.K.;
RT "Protein products of human Gas2-related genes on chromosomes 17 and 22
RT (hGAR17 and hGAR22) associate with both microfilaments and microtubules.";
RL J. Cell Sci. 116:1045-1058(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193; SER-306; THR-391;
RP SER-394; SER-492 AND THR-498, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-316; THR-334;
RP SER-352; SER-355; SER-394; SER-436; SER-438; SER-479; SER-486 AND SER-492,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 647-ILE-PRO-648.
RX PubMed=24706950; DOI=10.1242/jcs.140558;
RA Stroud M.J., Nazgiewicz A., McKenzie E.A., Wang Y., Kammerer R.A.,
RA Ballestrem C.;
RT "GAS2-like proteins mediate communication between microtubules and actin
RT through interactions with end-binding proteins.";
RL J. Cell Sci. 127:2672-2682(2014).
CC -!- FUNCTION: Involved in the cross-linking of microtubules and
CC microfilaments (PubMed:12584248, PubMed:24706950). Regulates
CC microtubule dynamics and stability by interacting with microtubule
CC plus-end tracking proteins, such as MAPRE1, to regulate microtubule
CC growth along actin stress fibers (PubMed:24706950).
CC {ECO:0000269|PubMed:12584248, ECO:0000269|PubMed:24706950}.
CC -!- SUBUNIT: Interacts with MAPRE1. {ECO:0000269|PubMed:24706950}.
CC -!- INTERACTION:
CC Q99501; P81274: GPSM2; NbExp=3; IntAct=EBI-10981762, EBI-618655;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:24706950}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:24706950}. Note=Colocalizes with the tips of
CC microtubule plus ends. {ECO:0000269|PubMed:24706950}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Beta;
CC IsoId=Q99501-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q99501-2; Sequence=VSP_015493;
CC Name=3;
CC IsoId=Q99501-3; Sequence=VSP_015494, VSP_015495;
CC Name=4;
CC IsoId=Q99501-4; Sequence=VSP_055754;
CC -!- SIMILARITY: Belongs to the GAS2 family. {ECO:0000305}.
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DR EMBL; Y07848; CAA69176.1; -; Genomic_DNA.
DR EMBL; Y07846; CAA69174.1; -; mRNA.
DR EMBL; AK223602; BAD97322.1; -; mRNA.
DR EMBL; AC002059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001782; AAH01782.1; -; mRNA.
DR EMBL; BC007624; AAH07624.1; -; mRNA.
DR EMBL; BC011047; AAH11047.1; -; mRNA.
DR CCDS; CCDS63438.1; -. [Q99501-4]
DR CCDS; CCDS74840.1; -. [Q99501-1]
DR RefSeq; NP_001265659.1; NM_001278730.1. [Q99501-4]
DR RefSeq; NP_006469.2; NM_006478.4.
DR RefSeq; NP_689422.1; NM_152236.2.
DR RefSeq; XP_011528126.1; XM_011529824.1.
DR RefSeq; XP_011528127.1; XM_011529825.1.
DR RefSeq; XP_016884022.1; XM_017028533.1.
DR AlphaFoldDB; Q99501; -.
DR SMR; Q99501; -.
DR BioGRID; 115878; 45.
DR IntAct; Q99501; 31.
DR STRING; 9606.ENSP00000481012; -.
DR iPTMnet; Q99501; -.
DR PhosphoSitePlus; Q99501; -.
DR BioMuta; GAS2L1; -.
DR DMDM; 73915341; -.
DR EPD; Q99501; -.
DR jPOST; Q99501; -.
DR MassIVE; Q99501; -.
DR MaxQB; Q99501; -.
DR PaxDb; Q99501; -.
DR PeptideAtlas; Q99501; -.
DR PRIDE; Q99501; -.
DR ProteomicsDB; 6091; -.
DR ProteomicsDB; 78300; -. [Q99501-1]
DR ProteomicsDB; 78301; -. [Q99501-2]
DR ProteomicsDB; 78302; -. [Q99501-3]
DR Antibodypedia; 10326; 209 antibodies from 24 providers.
DR DNASU; 10634; -.
DR Ensembl; ENST00000406549.7; ENSP00000383995.3; ENSG00000185340.15. [Q99501-4]
DR Ensembl; ENST00000610653.4; ENSP00000484130.1; ENSG00000185340.15. [Q99501-2]
DR GeneID; 10634; -.
DR KEGG; hsa:10634; -.
DR UCSC; uc010gvm.3; human. [Q99501-1]
DR CTD; 10634; -.
DR DisGeNET; 10634; -.
DR GeneCards; GAS2L1; -.
DR HGNC; HGNC:16955; GAS2L1.
DR HPA; ENSG00000185340; Low tissue specificity.
DR MIM; 602128; gene.
DR neXtProt; NX_Q99501; -.
DR OpenTargets; ENSG00000185340; -.
DR PharmGKB; PA38195; -.
DR VEuPathDB; HostDB:ENSG00000185340; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000154849; -.
DR HOGENOM; CLU_015447_2_0_1; -.
DR InParanoid; Q99501; -.
DR OMA; ACKPASV; -.
DR OrthoDB; 1343422at2759; -.
DR PhylomeDB; Q99501; -.
DR TreeFam; TF323754; -.
DR PathwayCommons; Q99501; -.
DR SignaLink; Q99501; -.
DR BioGRID-ORCS; 10634; 5 hits in 966 CRISPR screens.
DR ChiTaRS; GAS2L1; human.
DR GeneWiki; GAS2L1; -.
DR GenomeRNAi; 10634; -.
DR Pharos; Q99501; Tbio.
DR PRO; PR:Q99501; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q99501; protein.
DR Bgee; ENSG00000185340; Expressed in cervix squamous epithelium and 194 other tissues.
DR ExpressionAtlas; Q99501; baseline and differential.
DR Genevisible; Q99501; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.30.920.20; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR029931; GAS2L1.
DR PANTHER; PTHR46756:SF16; PTHR46756:SF16; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF02187; GAS2; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00243; GAS2; 1.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51460; GAR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Methylation;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..681
FT /note="GAS2-like protein 1"
FT /id="PRO_0000190442"
FT DOMAIN 27..148
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 203..275
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 168..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 487
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP9"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP9"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 504
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP9"
FT MOD_RES 633
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP9"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZP9"
FT VAR_SEQ 280..329
FT /note="AHRPPQPRVCTFSPQRVSPTTSPRPASPVPGSERRGSRPEMTPVSLRSTK
FT -> GPGISCPPIPAPAATPGTVTPQPPPPRAAPLVPAVMTQALAPGGSDPAGG (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:8975699"
FT /id="VSP_015494"
FT VAR_SEQ 330..681
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8975699"
FT /id="VSP_015495"
FT VAR_SEQ 337..563
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055754"
FT VAR_SEQ 338..681
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8975699"
FT /id="VSP_015493"
FT VARIANT 490
FT /note="S -> G (in dbSNP:rs34124440)"
FT /id="VAR_059974"
FT MUTAGEN 647..648
FT /note="IP->NN: Loss of microtubule-end localization and
FT microtubule plus-end tracking. Decreases MAPRE1 binding."
FT /evidence="ECO:0000269|PubMed:24706950"
FT CONFLICT 544
FT /note="V -> A (in Ref. 2; BAD97322 and 4; AAH11047)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="P -> S (in Ref. 2; BAD97322)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="H -> R (in Ref. 2; BAD97322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 72717 MW; A23A10748535D900 CRC64;
MADPVAGIAG SAAKSVRPFR SSEAYVEAMK EDLAEWLNAL YGLGLPGGGD GFLTGLATGT
TLCQHANAVT EAARALAAAR PARGVAFQAH SVVPGSFMAR DNVATFIGWC RVELGVPEVL
MFETEDLVLR KNEKSVVLCL LEVARRGARL GLLAPRLVQF EQEIERELRA APPAPNAPAA
GEDTTETAPA PGTPARGPRM TPSDLRNLDE LVREILGRCT CPDQFPMIKV SEGKYRVGDS
SLLIFVRVLR SHVMVRVGGG WDTLEHYLDK HDPCRCSSTA HRPPQPRVCT FSPQRVSPTT
SPRPASPVPG SERRGSRPEM TPVSLRSTKE GPETPPRPRD QLPPHPRSRR YSGDSDSSAS
SAQSGPLGTR SDDTGTGPRR ERPSRRLTTG TPASPRRPPA LRSQSRDRLD RGRPRGAPGG
RGAQLSVPSP ARRARSQSRE EQAVLLVRRD RDGQHSWVPR GRGSGGSGRS TPQTPRARSP
AAPRLSRVSS PSPELGTTPA SIFRTPLQLD PQQEQQLFRR LEEEFLANAR ALEAVASVTP
TGPVPDPARA PDPPAPDSAY CSSSSSSSSL SVLGGKCGQP GDSGRTANGL PGPRSQALSS
SSDEGSPCPG MGGPLDAPGS PLACTEPSRT WARGRMDTQP DRKPSRIPTP RGPRRPSGPA
ELGTWHALHS VTPRAEPDSW M
