GAS2_HUMAN
ID GAS2_HUMAN Reviewed; 313 AA.
AC O43903; B2R9C8; D3DQZ0; Q6ICV8; Q7Z3X8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Growth arrest-specific protein 2;
DE Short=GAS-2;
GN Name=GAS2;
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 1).
RC TISSUE=Kidney;
RX PubMed=9521882; DOI=10.1006/geno.1997.5172;
RA Collavin L., Buzzai M., Saccone S., Bernard L., Federico C.,
RA della Valle G., Brancolini C., Schneider C.;
RT "cDNA characterization and chromosome mapping of the human GAS2 gene.";
RL Genomics 48:265-269(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pericardium;
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Skeletal muscle;
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 [7]
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 [8]
RP SUBCELLULAR LOCATION.
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: May play a role in apoptosis by acting as a cell death
CC substrate for caspases. Is cleaved during apoptosis and the cleaved
CC form induces dramatic rearrangements of the actin cytoskeleton and
CC potent changes in the shape of the affected cells. May be involved in
CC the membrane ruffling process (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O43903-2; Q8IYX1: TBC1D21; NbExp=5; IntAct=EBI-12952691, EBI-12018146;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:24706950}. Membrane {ECO:0000250|UniProtKB:P11862};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P11862}.
CC Note=Component of the microfilament system. Colocalizes with actin
CC fibers at the cell border and along the stress fibers in growth-
CC arrested fibroblasts. Mainly membrane-associated. When
CC hyperphosphorylated, accumulates at membrane ruffles.
CC {ECO:0000250|UniProtKB:P11862}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43903-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43903-2; Sequence=VSP_055080, VSP_055081;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC liver, lung, and kidney. Not found in spleen.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed at growth arrest.
CC -!- PTM: Cleaved, during apoptosis, on a specific aspartic residue by
CC caspases.
CC -!- PTM: Phosphorylated on serine residues during the G0-G1 transition
CC phase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAS2 family. {ECO:0000305}.
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DR EMBL; U95032; AAC52058.1; -; mRNA.
DR EMBL; CR450285; CAG29281.1; -; mRNA.
DR EMBL; AK313734; BAG36475.1; -; mRNA.
DR EMBL; AC006299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68317.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68318.1; -; Genomic_DNA.
DR EMBL; BC013326; AAH13326.1; -; mRNA.
DR EMBL; BC040470; AAH40470.1; -; mRNA.
DR CCDS; CCDS7858.1; -. [O43903-1]
DR RefSeq; NP_001137302.1; NM_001143830.1. [O43903-1]
DR RefSeq; NP_005247.1; NM_005256.3. [O43903-1]
DR RefSeq; NP_808221.1; NM_177553.2. [O43903-1]
DR RefSeq; XP_016873017.1; XM_017017528.1.
DR RefSeq; XP_016873018.1; XM_017017529.1.
DR RefSeq; XP_016873019.1; XM_017017530.1.
DR RefSeq; XP_016873020.1; XM_017017531.1.
DR AlphaFoldDB; O43903; -.
DR BMRB; O43903; -.
DR SMR; O43903; -.
DR BioGRID; 108890; 13.
DR IntAct; O43903; 2.
DR STRING; 9606.ENSP00000401145; -.
DR iPTMnet; O43903; -.
DR PhosphoSitePlus; O43903; -.
DR BioMuta; GAS2; -.
DR jPOST; O43903; -.
DR MassIVE; O43903; -.
DR MaxQB; O43903; -.
DR PaxDb; O43903; -.
DR PeptideAtlas; O43903; -.
DR PRIDE; O43903; -.
DR ProteomicsDB; 49224; -. [O43903-1]
DR ProteomicsDB; 69093; -.
DR Antibodypedia; 12653; 336 antibodies from 32 providers.
DR DNASU; 2620; -.
DR Ensembl; ENST00000278187.7; ENSP00000278187.3; ENSG00000148935.12. [O43903-1]
DR Ensembl; ENST00000454584.7; ENSP00000401145.2; ENSG00000148935.12. [O43903-1]
DR Ensembl; ENST00000524701.5; ENSP00000432026.1; ENSG00000148935.12. [O43903-2]
DR Ensembl; ENST00000630668.2; ENSP00000485708.1; ENSG00000148935.12. [O43903-2]
DR GeneID; 2620; -.
DR KEGG; hsa:2620; -.
DR MANE-Select; ENST00000454584.7; ENSP00000401145.2; NM_001143830.3; NP_001137302.1.
DR UCSC; uc001mqm.4; human. [O43903-1]
DR CTD; 2620; -.
DR DisGeNET; 2620; -.
DR GeneCards; GAS2; -.
DR HGNC; HGNC:4167; GAS2.
DR HPA; ENSG00000148935; Tissue enriched (liver).
DR MIM; 602835; gene.
DR neXtProt; NX_O43903; -.
DR OpenTargets; ENSG00000148935; -.
DR PharmGKB; PA28580; -.
DR VEuPathDB; HostDB:ENSG00000148935; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000155755; -.
DR HOGENOM; CLU_025484_1_0_1; -.
DR InParanoid; O43903; -.
DR OMA; KFKESME; -.
DR OrthoDB; 1343422at2759; -.
DR PhylomeDB; O43903; -.
DR TreeFam; TF323754; -.
DR PathwayCommons; O43903; -.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR SignaLink; O43903; -.
DR SIGNOR; O43903; -.
DR BioGRID-ORCS; 2620; 19 hits in 1075 CRISPR screens.
DR ChiTaRS; GAS2; human.
DR GeneWiki; GAS2; -.
DR GenomeRNAi; 2620; -.
DR Pharos; O43903; Tbio.
DR PRO; PR:O43903; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O43903; protein.
DR Bgee; ENSG00000148935; Expressed in trigeminal ganglion and 142 other tissues.
DR ExpressionAtlas; O43903; baseline and differential.
DR Genevisible; O43903; HS.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0001547; P:antral ovarian follicle growth; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0001544; P:initiation of primordial ovarian follicle growth; IEA:Ensembl.
DR GO; GO:0030728; P:ovulation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
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; IPR029929; GAS2.
DR PANTHER; PTHR46756:SF9; PTHR46756:SF9; 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 Alternative splicing; Apoptosis; Cell cycle; Cell shape; Cytoplasm;
KW Cytoskeleton; Growth arrest; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..313
FT /note="Growth arrest-specific protein 2"
FT /id="PRO_0000190440"
FT DOMAIN 34..156
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 197..270
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 175..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 278..279
FT /note="Cleavage; by a caspase during apoptosis"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11862"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 137..141
FT /note="VLHKQ -> GFGGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055080"
FT VAR_SEQ 142..313
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055081"
SQ SEQUENCE 313 AA; 34945 MW; A5FBA611A0C8B36F CRC64;
MCTALSPKVR SGPGLSDMHQ YSQWLASRHE ANLLPMKEDL ALWLTNLLGK EITAETFMEK
LDNGALLCQL AETMQEKFKE SMDANKPTKN LPLKKIPCKT SAPSGSFFAR DNTANFLSWC
RDLGVDETCL FESEGLVLHK QPREVCLCLL ELGRIAARYG VEPPGLIKLE KEIEQEETLS
APSPSPSPSS KSSGKKSTGN LLDDAVKRIS EDPPCKCPNK FCVERLSQGR YRVGEKILFI
RMLHNKHVMV RVGGGWETFA GYLLKHDPCR MLQISRVDGK TSPIQSKSPT LKDMNPDNYL
VVSASYKAKK EIK
