GA2L3_HUMAN
ID GA2L3_HUMAN Reviewed; 694 AA.
AC Q86XJ1; B2RCN2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=GAS2-like protein 3;
DE AltName: Full=Growth arrest-specific protein 2-like 3;
GN Name=GAS2L3;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 THR-441 AND SER-570, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [5]
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 [6]
RP FUNCTION, INTERACTION WITH ACTIN AND MICROTUBULES, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=21561867; DOI=10.1074/jbc.m111.242263;
RA Stroud M.J., Kammerer R.A., Ballestrem C.;
RT "Characterization of G2L3 (GAS2-like 3), a new microtubule- and actin-
RT binding protein related to spectraplakins.";
RL J. Biol. Chem. 286:24987-24995(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION BY
RP 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 [8]
RP INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 373-ILE-PRO-374 AND 461-ILE-PRO-462.
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: Cytoskeletal linker protein. May promote and stabilize the
CC formation of the actin and microtubule network.
CC {ECO:0000269|PubMed:21561867}.
CC -!- SUBUNIT: Interacts (via CH domain) with F-actin (PubMed:21561867).
CC Interacts (via C terminus) with microtubules (PubMed:21561867).
CC Interacts with MAPRE1 (PubMed:24706950). {ECO:0000269|PubMed:21561867,
CC ECO:0000269|PubMed:24706950}.
CC -!- INTERACTION:
CC Q86XJ1; Q96GD4: AURKB; NbExp=4; IntAct=EBI-9248152, EBI-624291;
CC Q86XJ1; O15392: BIRC5; NbExp=4; IntAct=EBI-9248152, EBI-518823;
CC Q86XJ1; Q53HL2: CDCA8; NbExp=2; IntAct=EBI-9248152, EBI-979174;
CC Q86XJ1; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-9248152, EBI-10242151;
CC Q86XJ1; P60660: MYL6; NbExp=3; IntAct=EBI-9248152, EBI-300817;
CC Q86XJ1; Q969E8: TSR2; NbExp=3; IntAct=EBI-9248152, EBI-746981;
CC Q86XJ1; Q15915: ZIC1; NbExp=3; IntAct=EBI-9248152, EBI-11963196;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21561867}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21561867,
CC ECO:0000269|PubMed:24706950}. Note=Localizes to microtubule and actin
CC cytoskeletons. {ECO:0000269|PubMed:21561867,
CC ECO:0000269|PubMed:24706950}.
CC -!- TISSUE SPECIFICITY: Expressed in the pancreas, heart, liver, placenta,
CC brain, skeletal muscle, kidney and lung. {ECO:0000269|PubMed:21561867}.
CC -!- DOMAIN: The GAR domain modulates the binding strength to each
CC cytoskeletal network. {ECO:0000269|PubMed:21561867}.
CC -!- SIMILARITY: Belongs to the GAS2 family. {ECO:0000305}.
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DR EMBL; AK315189; BAG37629.1; -; mRNA.
DR EMBL; CH471054; EAW97641.1; -; Genomic_DNA.
DR EMBL; BC043366; AAH43366.1; -; mRNA.
DR CCDS; CCDS9079.1; -.
DR RefSeq; NP_001290059.1; NM_001303130.1.
DR RefSeq; NP_777602.1; NM_174942.2.
DR RefSeq; XP_005268861.1; XM_005268804.3.
DR RefSeq; XP_011536521.1; XM_011538219.2.
DR RefSeq; XP_011536522.1; XM_011538220.2.
DR RefSeq; XP_011536523.1; XM_011538221.2.
DR RefSeq; XP_016874695.1; XM_017019206.1.
DR AlphaFoldDB; Q86XJ1; -.
DR SMR; Q86XJ1; -.
DR BioGRID; 129559; 29.
DR IntAct; Q86XJ1; 12.
DR MINT; Q86XJ1; -.
DR STRING; 9606.ENSP00000448955; -.
DR GlyGen; Q86XJ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86XJ1; -.
DR PhosphoSitePlus; Q86XJ1; -.
DR BioMuta; GAS2L3; -.
DR DMDM; 73919616; -.
DR EPD; Q86XJ1; -.
DR jPOST; Q86XJ1; -.
DR MassIVE; Q86XJ1; -.
DR MaxQB; Q86XJ1; -.
DR PaxDb; Q86XJ1; -.
DR PeptideAtlas; Q86XJ1; -.
DR PRIDE; Q86XJ1; -.
DR ProteomicsDB; 70285; -.
DR Antibodypedia; 30346; 104 antibodies from 16 providers.
DR DNASU; 283431; -.
DR Ensembl; ENST00000266754.9; ENSP00000266754.5; ENSG00000139354.11.
DR Ensembl; ENST00000539410.2; ENSP00000439672.1; ENSG00000139354.11.
DR Ensembl; ENST00000547754.6; ENSP00000448955.1; ENSG00000139354.11.
DR GeneID; 283431; -.
DR KEGG; hsa:283431; -.
DR MANE-Select; ENST00000547754.6; ENSP00000448955.1; NM_174942.3; NP_777602.1.
DR UCSC; uc001thu.4; human.
DR CTD; 283431; -.
DR GeneCards; GAS2L3; -.
DR HGNC; HGNC:27475; GAS2L3.
DR HPA; ENSG00000139354; Low tissue specificity.
DR neXtProt; NX_Q86XJ1; -.
DR OpenTargets; ENSG00000139354; -.
DR PharmGKB; PA134979032; -.
DR VEuPathDB; HostDB:ENSG00000139354; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000159389; -.
DR HOGENOM; CLU_025484_3_0_1; -.
DR InParanoid; Q86XJ1; -.
DR OMA; MDPMSAV; -.
DR OrthoDB; 1343422at2759; -.
DR PhylomeDB; Q86XJ1; -.
DR TreeFam; TF323754; -.
DR PathwayCommons; Q86XJ1; -.
DR SignaLink; Q86XJ1; -.
DR BioGRID-ORCS; 283431; 7 hits in 1084 CRISPR screens.
DR ChiTaRS; GAS2L3; human.
DR GenomeRNAi; 283431; -.
DR Pharos; Q86XJ1; Tbio.
DR PRO; PR:Q86XJ1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86XJ1; protein.
DR Bgee; ENSG00000139354; Expressed in trigeminal ganglion and 160 other tissues.
DR ExpressionAtlas; Q86XJ1; baseline and differential.
DR Genevisible; Q86XJ1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA: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; IPR029932; GAS2L3.
DR PANTHER; PTHR46756:SF7; PTHR46756:SF7; 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 Actin-binding; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..694
FT /note="GAS2-like protein 3"
FT /id="PRO_0000190446"
FT DOMAIN 48..168
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 208..281
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 299..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 461
FT /note="L -> S (in dbSNP:rs11834625)"
FT /id="VAR_033944"
FT VARIANT 500
FT /note="P -> T (in dbSNP:rs17030365)"
FT /id="VAR_033945"
FT MUTAGEN 373..374
FT /note="LP->NN: No effect on microtubule localization and
FT MAPRE1 binding; when associated with 461-N-N-462."
FT /evidence="ECO:0000269|PubMed:24706950"
FT MUTAGEN 461..462
FT /note="LP->NN: No effect on microtubule localization and
FT MAPRE1 binding; when associated with 373-N-N-374."
FT /evidence="ECO:0000269|PubMed:24706950"
SQ SEQUENCE 694 AA; 75214 MW; FF20533B5A0D4844 CRC64;
MQPAIQVWFG EDLPLSPRSP LTPRHGPGLA NVCQYDEWIA VRHEATLLPM QEDLSIWLSG
LLGIKVKAEK LLEELDNGVL LCQLIDVLQN MVKTCNSEES GNFPMRKVPC KKDAASGSFF
ARDNTANFLH WCRDIGVDET YLFESEGLVL HKDPRQVYLC LLEIGRIVSR YGVEPPVLVK
LEKEIELEET LLNTSGPEDS ISIPKSCCRH EELHEAVKHI AEDPPCSCSH RFSIEYLSEG
RYRLGDKILF IRMLHGKHVM VRVGGGWDTL QGFLLKYDPC RILQFATLEQ KILAFQKGVS
NESVPDSPAR TPQPPEMNPL SAVNMFQKQN SKPSVPVSIP KSKEKQGRPP GALVPASSLK
GGNLGSMSVR SKLPNSPAAS SHPKLKSSKG ITKKPQAPSN NASSSLASLN PVGKNTSSPA
LPRTAPCISE SPRKCISSPN TPKAKVIPAQ NSADLPESTL LPNKCSGKTQ PKYLKHNHIS
SRDNAVSHLA AHSNSSSKCP KLPKANIPVR PKPSFQSSAK MTKTSSKTIA TGLGTQSQPS
DGAPQAKPVP AQKLKSALNL NQPVSVSSVS PVKATQKSKD KNIVSATKKQ PQNKSAFQKT
GPSSLKSPGR TPLSIVSLPQ SSTKTQTAPK SAQTVAKSQH STKGPPRSGK TPASIRKPPS
SVKDADSGDK KPTAKKKEDD DHYFVMTGSK KPRK
