AMOL1_HUMAN
ID AMOL1_HUMAN Reviewed; 956 AA.
AC Q8IY63; Q63HK7; Q8NDN0; Q8TEN8; Q8WXD1; Q96CM5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Angiomotin-like protein 1;
GN Name=AMOTL1;
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=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-557 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12406577; DOI=10.1016/s0378-1119(02)00928-9;
RA Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA Holmgren L.;
RT "Angiomotin belongs to a novel protein family with conserved coiled-coil
RT and PDZ binding domains.";
RL Gene 298:69-77(2002).
RN [6]
RP ERRATUM OF PUBMED:12406577.
RA Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA Holmgren L.;
RL Gene 310:231-231(2003).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-295; SER-720 AND
RP SER-906, AND 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 [10]
RP UBIQUITINATION BY NEDD4.
RX PubMed=22385262; DOI=10.1042/bj20111983;
RA Wang C., An J., Zhang P., Xu C., Gao K., Wu D., Wang D., Yu H., Liu J.O.,
RA Yu L.;
RT "The Nedd4-like ubiquitin E3 ligases target angiomotin/p130 to ubiquitin-
RT dependent degradation.";
RL Biochem. J. 444:279-289(2012).
RN [11]
RP FUNCTION.
RX PubMed=22362771; DOI=10.1074/jbc.m112.347419;
RA Li Z., Wang Y., Zhang M., Xu P., Huang H., Wu D., Meng A.;
RT "The Amotl2 gene inhibits Wnt/beta-catenin signaling and regulates
RT embryonic development in zebrafish.";
RL J. Biol. Chem. 287:13005-13015(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-295; SER-793;
RP SER-805; SER-828; SER-900; THR-902 AND SER-906, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805; SER-828 AND SER-906, AND
RP IDENTIFICATION BY 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: Inhibits the Wnt/beta-catenin signaling pathway, probably by
CC recruiting CTNNB1 to recycling endosomes and hence preventing its
CC translocation to the nucleus. {ECO:0000269|PubMed:22362771}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IY63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IY63-2; Sequence=VSP_015710;
CC -!- PTM: Polyubiquitinated by NEDD4, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:22385262}.
CC -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84910.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84910.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK074084; BAB84910.1; ALT_SEQ; mRNA.
DR EMBL; AL833833; CAD38693.1; -; mRNA.
DR EMBL; AP001152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX648729; CAH56180.1; -; mRNA.
DR EMBL; BC014126; AAH14126.1; -; mRNA.
DR EMBL; BC037539; AAH37539.1; -; mRNA.
DR EMBL; AF453742; AAL49764.1; -; mRNA.
DR CCDS; CCDS44712.1; -. [Q8IY63-1]
DR CCDS; CCDS73368.1; -. [Q8IY63-2]
DR RefSeq; NP_001287936.1; NM_001301007.1. [Q8IY63-2]
DR RefSeq; NP_570899.1; NM_130847.2. [Q8IY63-1]
DR AlphaFoldDB; Q8IY63; -.
DR SMR; Q8IY63; -.
DR BioGRID; 127559; 83.
DR CORUM; Q8IY63; -.
DR DIP; DIP-50682N; -.
DR IntAct; Q8IY63; 26.
DR MINT; Q8IY63; -.
DR STRING; 9606.ENSP00000387739; -.
DR iPTMnet; Q8IY63; -.
DR PhosphoSitePlus; Q8IY63; -.
DR BioMuta; AMOTL1; -.
DR DMDM; 74728292; -.
DR EPD; Q8IY63; -.
DR jPOST; Q8IY63; -.
DR MassIVE; Q8IY63; -.
DR MaxQB; Q8IY63; -.
DR PaxDb; Q8IY63; -.
DR PeptideAtlas; Q8IY63; -.
DR PRIDE; Q8IY63; -.
DR ProteomicsDB; 71115; -. [Q8IY63-1]
DR ProteomicsDB; 71116; -. [Q8IY63-2]
DR Antibodypedia; 654; 132 antibodies from 25 providers.
DR DNASU; 154810; -.
DR Ensembl; ENST00000317829.12; ENSP00000320968.8; ENSG00000166025.18. [Q8IY63-2]
DR Ensembl; ENST00000433060.3; ENSP00000387739.2; ENSG00000166025.18. [Q8IY63-1]
DR GeneID; 154810; -.
DR KEGG; hsa:154810; -.
DR MANE-Select; ENST00000433060.3; ENSP00000387739.2; NM_130847.3; NP_570899.1.
DR UCSC; uc001pfb.4; human. [Q8IY63-1]
DR CTD; 154810; -.
DR DisGeNET; 154810; -.
DR GeneCards; AMOTL1; -.
DR HGNC; HGNC:17811; AMOTL1.
DR HPA; ENSG00000166025; Tissue enhanced (skeletal).
DR MIM; 614657; gene.
DR neXtProt; NX_Q8IY63; -.
DR OpenTargets; ENSG00000166025; -.
DR PharmGKB; PA24774; -.
DR VEuPathDB; HostDB:ENSG00000166025; -.
DR eggNOG; ENOG502QVI5; Eukaryota.
DR GeneTree; ENSGT00940000160158; -.
DR HOGENOM; CLU_009937_1_0_1; -.
DR InParanoid; Q8IY63; -.
DR OMA; GMPEYNA; -.
DR OrthoDB; 369983at2759; -.
DR PhylomeDB; Q8IY63; -.
DR TreeFam; TF333368; -.
DR PathwayCommons; Q8IY63; -.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR SignaLink; Q8IY63; -.
DR SIGNOR; Q8IY63; -.
DR BioGRID-ORCS; 154810; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; AMOTL1; human.
DR GeneWiki; AMOTL1; -.
DR GenomeRNAi; 154810; -.
DR Pharos; Q8IY63; Tbio.
DR PRO; PR:Q8IY63; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8IY63; protein.
DR Bgee; ENSG00000166025; Expressed in tibialis anterior and 188 other tissues.
DR ExpressionAtlas; Q8IY63; baseline and differential.
DR Genevisible; Q8IY63; HS.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR009114; Angiomotin.
DR InterPro; IPR024646; Angiomotin_C.
DR Pfam; PF12240; Angiomotin_C; 1.
DR PRINTS; PR01807; ANGIOMOTIN.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Phosphoprotein;
KW Reference proteome; Tight junction; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..956
FT /note="Angiomotin-like protein 1"
FT /id="PRO_0000190670"
FT REGION 197..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..279
FT /evidence="ECO:0000255"
FT COILED 438..639
FT /evidence="ECO:0000255"
FT COILED 665..694
FT /evidence="ECO:0000255"
FT COILED 729..762
FT /evidence="ECO:0000255"
FT MOTIF 953..956
FT /note="PDZ-binding"
FT COMPBIAS 197..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 902
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 17..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_015710"
FT VARIANT 847
FT /note="P -> L (in dbSNP:rs11020968)"
FT /id="VAR_033498"
FT CONFLICT 459..460
FT /note="LQ -> HE (in Ref. 4; AAH14126)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="K -> E (in Ref. 2; CAH56180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 106574 MW; 6F47AE3A13816E95 CRC64;
MWRAKLRRGT CEPAVKGSPS ACYSPSSPVQ VLEDSTYFSP DFQLYSGRHE TSALTVEATS
SIREKVVEDP LCNFHSPNFL RISEVEMRGS EDAAAGTVLQ RLIQEQLRYG TPTENMNLLA
IQHQATGSAG PAHPTNNFSS TENLTQEDPQ MVYQSARQEP QGQEHQVDNT VMEKQVRSTQ
PQQNNEELPT YEEAKAQSQF FRGQQQQQQQ QGAVGHGYYM AGGTSQKSRT EGRPTVNRAN
SGQAHKDEAL KELKQGHVRS LSERIMQLSL ERNGAKQHLP GSGNGKGFKV GGGPSPAQPA
GKVLDPRGPP PEYPFKTKQM MSPVSKTQEH GLFYGDQHPG MLHEMVKPYP APQPVRTDVA
VLRYQPPPEY GVTSRPCQLP FPSTMQQHSP MSSQTSSASG PLHSVSLPLP LPMALGAPQP
PPAASPSQQL GPDAFAIVER AQQMVEILTE ENRVLHQELQ GYYDNADKLH KFEKELQRIS
EAYESLVKST TKRESLDKAM RNKLEGEIRR LHDFNRDLRD RLETANRQLS SREYEGHEDK
AAEGHYASQN KEFLKEKEKL EMELAAVRTA SEDHRRHIEI LDQALSNAQA RVIKLEEELR
EKQAYVEKVE KLQQALTQLQ SACEKREQME RRLRTWLERE LDALRTQQKH GNGQPANMPE
YNAPALLELV REKEERILAL EADMTKWEQK YLEESTIRHF AMNAAATAAA ERDTTIINHS
RNGSYGESSL EAHIWQEEEE VVQANRRCQD MEYTIKNLHA KIIEKDAMIK VLQQRSRKDA
GKTDSSSLRP ARSVPSIAAA TGTHSRQTSL TSSQLAEEKK EEKTWKGSIG LLLGKEHHEH
ASAPLLPPPP TSALSSIAST TAASSAHAKT GSKDSSTQTD KSAELFWPSM ASLPSRGRLS
TTPAHSPVLK HPAAKGTAEK LENSPGHGKS PDHRGRVSSL LHKPEFPDGE MMEVLI
