RAPH1_HUMAN
ID RAPH1_HUMAN Reviewed; 1250 AA.
AC Q70E73; Q96Q37; Q9C0I2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ras-associated and pleckstrin homology domains-containing protein 1;
DE Short=RAPH1;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 18 protein;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 9 protein;
DE AltName: Full=Lamellipodin;
DE AltName: Full=Proline-rich EVH1 ligand 2;
DE Short=PREL-2;
DE AltName: Full=Protein RMO1;
GN Name=RAPH1; Synonyms=ALS2CR18, ALS2CR9, KIAA1681, LPD, PREL2, RMO1;
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 RMO1AB).
RC TISSUE=Lymphocyte;
RX PubMed=11586298; DOI=10.1038/ng1001-166;
RA Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S.,
RA Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R., Figlewicz D.A.,
RA Kwiatkowski T., Hosler B.A., Sagie T., Skaug J., Nasir J., Brown R.H. Jr.,
RA Scherer S.W., Rouleau G.A., Hayden M.R., Ikeda J.-E.;
RT "A gene encoding a putative GTPase regulator is mutated in familial
RT amyotrophic lateral sclerosis 2.";
RL Nat. Genet. 29:166-173(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RMO1-RAPH1), INTERACTION WITH EVL AND
RP VASP, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15469845; DOI=10.1016/j.devcel.2004.07.024;
RA Krause M., Leslie J.D., Stewart M., Lafuente E.M., Valderrama F.,
RA Jagannathan R., Strasser G.A., Rubinson D.A., Liu H., Way M., Yaffe M.B.,
RA Boussiotis V.A., Gertler F.B.;
RT "Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of
RT lamellipodial dynamics.";
RL Dev. Cell 7:571-583(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RMO1AB AND RMO1ABC), ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Osteosarcoma;
RX PubMed=15609301; DOI=10.1002/ijc.20786;
RA Eppert K., Wunder J.S., Aneliunas V., Tsui L.-C., Scherer S.W.,
RA Andrulis I.L.;
RT "Altered expression and deletion of RMO1 in osteosarcoma.";
RL Int. J. Cancer 114:738-746(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RMO1-RAPH1).
RX PubMed=15586368; DOI=10.1002/path.1687;
RA Dahl E., Sadr-Nabavi A., Klopocki E., Betz B., Grube S., Kreutzfeld R.,
RA Himmelfarb M., An H.-X., Gelling S., Klaman I., Hinzmann B.,
RA Kristiansen G., Gruetzmann R., Kuner R., Petschke B., Rhiem K., Wiechen K.,
RA Sers C., Wiestler O., Schneider A., Hoefler H., Naehrig J., Dietel M.,
RA Schaefer R., Rosenthal A., Schmutzler R., Duerst M., Meindl A.,
RA Niederacher D.;
RT "Systematic identification and molecular characterization of genes
RT differentially expressed in breast and ovarian cancer.";
RL J. Pathol. 205:21-28(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1250 (ISOFORM RMO1-RAPH1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-610; SER-827;
RP THR-830; SER-853; SER-894; SER-965 AND THR-974, AND IDENTIFICATION BY MASS
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION AT TYR-426; TYR-456 AND TYR-1226.
RX PubMed=20417104; DOI=10.1016/j.cub.2010.03.048;
RA Michael M., Vehlow A., Navarro C., Krause M.;
RT "c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal ruffling of
RT fibroblasts and axonal morphogenesis.";
RL Curr. Biol. 20:783-791(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5; SER-17; SER-827; THR-830 AND SER-894, AND
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5 AND SER-17, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-1012, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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-17; SER-150; SER-192;
RP SER-203; SER-205; SER-845; SER-894; SER-996 AND SER-1183, 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).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-891 AND ALA-1228.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP INTERACTION WITH RAC1.
RX PubMed=18499456; DOI=10.1016/j.cub.2008.04.050;
RA Quinn C.C., Pfeil D.S., Wadsworth W.G.;
RT "CED-10/Rac1 mediates axon guidance by regulating the asymmetric
RT distribution of MIG-10/lamellipodin.";
RL Curr. Biol. 18:808-813(2008).
CC -!- FUNCTION: Mediator of localized membrane signals. Implicated in the
CC regulation of lamellipodial dynamics. Negatively regulates cell
CC adhesion.
CC -!- SUBUNIT: Interacts with EVL and VASP and targets them to the leading
CC edge (PubMed:15469845). Interacts (via Ras associating and PH domains)
CC with RAC1 (PubMed:18499456). {ECO:0000269|PubMed:15469845,
CC ECO:0000269|PubMed:18499456}.
CC -!- INTERACTION:
CC Q70E73; P00533: EGFR; NbExp=2; IntAct=EBI-3940924, EBI-297353;
CC Q70E73; Q99962: SH3GL2; NbExp=5; IntAct=EBI-3940924, EBI-77938;
CC Q70E73; Q99963: SH3GL3; NbExp=4; IntAct=EBI-3940924, EBI-473910;
CC Q70E73; O35964: Sh3gl1; Xeno; NbExp=13; IntAct=EBI-3940924, EBI-1149235;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15469845};
CC Peripheral membrane protein {ECO:0000269|PubMed:15469845}; Cytoplasmic
CC side {ECO:0000269|PubMed:15469845}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:15469845}. Cell projection, filopodium
CC {ECO:0000269|PubMed:15469845}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15469845}. Note=Recruited to the membrane, via the
CC PH domain, by the phosphoinositide, PI(3,4)P2. Colocalizes with
CC ENAH/VASP at the tips of lamellipodia and filopodia. Also colocalizes
CC with the pathogens, Vaccinia and Enteropathogenic E.coli (EPEC) at the
CC interface between the pathogen and their actin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=RMO1-RAPH1; Synonyms=Lamellipodin, RAPH1;
CC IsoId=Q70E73-10; Sequence=Displayed;
CC Name=RMO1;
CC IsoId=Q70E73-2; Sequence=VSP_035788, VSP_035789;
CC Name=RMO1a;
CC IsoId=Q70E73-3; Sequence=VSP_035784, VSP_035788, VSP_035789;
CC Name=RMO1b;
CC IsoId=Q70E73-4; Sequence=VSP_035786, VSP_035788, VSP_035789;
CC Name=RMO1c;
CC IsoId=Q70E73-5; Sequence=VSP_035787;
CC Name=RMO1ab; Synonyms=Lamellipodin-S, Lpd-S;
CC IsoId=Q70E73-6; Sequence=VSP_035785, VSP_035788, VSP_035789;
CC Name=RMO1ac;
CC IsoId=Q70E73-7; Sequence=VSP_035784, VSP_035787;
CC Name=RMO1bc;
CC IsoId=Q70E73-8; Sequence=VSP_035786, VSP_035787;
CC Name=RMO1abc;
CC IsoId=Q70E73-9; Sequence=VSP_035785, VSP_035787;
CC -!- TISSUE SPECIFICITY: Isoform RMO1-RAPH1 is ubiquitously expressed with
CC highest levels in brain, heart, ovary and developing embryo. Isoform
CC RMO1 is widely expressed with highest levels in liver. Low expression
CC in B-cells. {ECO:0000269|PubMed:15469845, ECO:0000269|PubMed:15609301}.
CC -!- INDUCTION: Reduced expression in metastatic osteosarcomas compared to
CC primary osteosarcoma tumors. Down-regulated in both breast (43% of
CC tissue samples) and ovarian (25% of tissue samples) cancers.
CC -!- SIMILARITY: Belongs to the MRL family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB053311; BAB69020.1; -; mRNA.
DR EMBL; AY494951; AAS82582.1; -; mRNA.
DR EMBL; AY523977; AAS16935.1; -; mRNA.
DR EMBL; AY523978; AAS16936.1; -; mRNA.
DR EMBL; AJ584699; CAE48361.1; -; mRNA.
DR EMBL; AC018891; AAY14676.1; -; Genomic_DNA.
DR EMBL; AB051468; BAB21772.1; -; mRNA.
DR CCDS; CCDS2359.1; -. [Q70E73-10]
DR CCDS; CCDS2360.1; -. [Q70E73-9]
DR RefSeq; NP_976241.1; NM_203365.3. [Q70E73-9]
DR RefSeq; NP_998754.1; NM_213589.2. [Q70E73-10]
DR PDB; 4GMV; X-ray; 2.40 A; A/B=240-520.
DR PDB; 4GN1; X-ray; 2.40 A; A/B/C/D=266-520.
DR PDBsum; 4GMV; -.
DR PDBsum; 4GN1; -.
DR AlphaFoldDB; Q70E73; -.
DR SMR; Q70E73; -.
DR BioGRID; 122380; 40.
DR DIP; DIP-61336N; -.
DR IntAct; Q70E73; 20.
DR MINT; Q70E73; -.
DR STRING; 9606.ENSP00000316543; -.
DR GlyConnect; 2905; 1 O-Linked glycan (1 site).
DR GlyGen; Q70E73; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q70E73; -.
DR PhosphoSitePlus; Q70E73; -.
DR BioMuta; RAPH1; -.
DR DMDM; 215274220; -.
DR EPD; Q70E73; -.
DR jPOST; Q70E73; -.
DR MassIVE; Q70E73; -.
DR MaxQB; Q70E73; -.
DR PaxDb; Q70E73; -.
DR PeptideAtlas; Q70E73; -.
DR PRIDE; Q70E73; -.
DR ProteomicsDB; 68527; -. [Q70E73-10]
DR ProteomicsDB; 68528; -. [Q70E73-2]
DR ProteomicsDB; 68529; -. [Q70E73-3]
DR ProteomicsDB; 68530; -. [Q70E73-4]
DR ProteomicsDB; 68531; -. [Q70E73-5]
DR ProteomicsDB; 68532; -. [Q70E73-6]
DR ProteomicsDB; 68533; -. [Q70E73-7]
DR ProteomicsDB; 68534; -. [Q70E73-8]
DR ProteomicsDB; 68535; -. [Q70E73-9]
DR Antibodypedia; 19956; 81 antibodies from 25 providers.
DR DNASU; 65059; -.
DR Ensembl; ENST00000308091.8; ENSP00000311293.4; ENSG00000173166.18. [Q70E73-9]
DR Ensembl; ENST00000319170.10; ENSP00000316543.5; ENSG00000173166.18. [Q70E73-10]
DR Ensembl; ENST00000418114.5; ENSP00000396711.1; ENSG00000173166.18. [Q70E73-2]
DR Ensembl; ENST00000419464.5; ENSP00000390578.1; ENSG00000173166.18. [Q70E73-5]
DR Ensembl; ENST00000423104.5; ENSP00000397751.1; ENSG00000173166.18. [Q70E73-7]
DR Ensembl; ENST00000439222.5; ENSP00000411138.1; ENSG00000173166.18. [Q70E73-8]
DR Ensembl; ENST00000453034.5; ENSP00000406662.1; ENSG00000173166.18. [Q70E73-6]
DR GeneID; 65059; -.
DR KEGG; hsa:65059; -.
DR MANE-Select; ENST00000319170.10; ENSP00000316543.5; NM_213589.3; NP_998754.1.
DR UCSC; uc002vad.5; human. [Q70E73-10]
DR CTD; 65059; -.
DR DisGeNET; 65059; -.
DR GeneCards; RAPH1; -.
DR HGNC; HGNC:14436; RAPH1.
DR HPA; ENSG00000173166; Tissue enhanced (liver).
DR MIM; 609035; gene.
DR neXtProt; NX_Q70E73; -.
DR OpenTargets; ENSG00000173166; -.
DR PharmGKB; PA24749; -.
DR VEuPathDB; HostDB:ENSG00000173166; -.
DR eggNOG; KOG3751; Eukaryota.
DR GeneTree; ENSGT00940000156552; -.
DR HOGENOM; CLU_022700_0_0_1; -.
DR InParanoid; Q70E73; -.
DR OMA; NKHSYLD; -.
DR PhylomeDB; Q70E73; -.
DR TreeFam; TF317511; -.
DR PathwayCommons; Q70E73; -.
DR SignaLink; Q70E73; -.
DR SIGNOR; Q70E73; -.
DR BioGRID-ORCS; 65059; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; RAPH1; human.
DR GeneWiki; RAPH1; -.
DR GenomeRNAi; 65059; -.
DR Pharos; Q70E73; Tbio.
DR PRO; PR:Q70E73; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q70E73; protein.
DR Bgee; ENSG00000173166; Expressed in epithelial cell of pancreas and 193 other tissues.
DR ExpressionAtlas; Q70E73; baseline and differential.
DR Genevisible; Q70E73; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd01259; PH_APBB1IP; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039664; GRB/APBB1IP.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR039665; PH_APBB1IP.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11243; PTHR11243; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1250
FT /note="Ras-associated and pleckstrin homology domains-
FT containing protein 1"
FT /id="PRO_0000181352"
FT DOMAIN 269..355
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 396..505
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..725
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..892
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 426
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:20417104"
FT MOD_RES 456
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:20417104"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 830
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 974
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1012
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1226
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:20417104"
FT VAR_SEQ 244
FT /note="E -> EHAISLRCSSKQAKRHIDFTEEQAELTP (in isoform RMO1a
FT and isoform RMO1ac)"
FT /evidence="ECO:0000305"
FT /id="VSP_035784"
FT VAR_SEQ 244
FT /note="E -> EHAISLRCSSKQAKRHIDFTEEQAELTPHSYLDRETSLLLRNIAGKP
FT SHLLTK (in isoform RMO1ab and isoform RMO1abc)"
FT /evidence="ECO:0000303|PubMed:11586298,
FT ECO:0000303|PubMed:15609301"
FT /id="VSP_035785"
FT VAR_SEQ 244
FT /note="E -> EHSYLDRETSLLLRNIAGKPSHLLTK (in isoform RMO1b
FT and isoform RMO1bc)"
FT /evidence="ECO:0000305"
FT /id="VSP_035786"
FT VAR_SEQ 593..1250
FT /note="Missing (in isoform RMO1c, isoform RMO1ac, isoform
FT RMO1bc and isoform RMO1abc)"
FT /evidence="ECO:0000303|PubMed:15609301"
FT /id="VSP_035787"
FT VAR_SEQ 593..597
FT /note="ARMES -> VTASF (in isoform RMO1, isoform RMO1a,
FT isoform RMO1b and isoform RMO1ab)"
FT /evidence="ECO:0000303|PubMed:11586298,
FT ECO:0000303|PubMed:15609301"
FT /id="VSP_035788"
FT VAR_SEQ 598..1250
FT /note="Missing (in isoform RMO1, isoform RMO1a, isoform
FT RMO1b and isoform RMO1ab)"
FT /evidence="ECO:0000303|PubMed:11586298,
FT ECO:0000303|PubMed:15609301"
FT /id="VSP_035789"
FT VARIANT 891
FT /note="A -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036009"
FT VARIANT 1228
FT /note="T -> A (in a breast cancer sample; somatic mutation;
FT dbSNP:rs774304253)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036010"
FT CONFLICT 1081
FT /note="E -> D (in Ref. 2; AAS82582, 4; CAE48361 and 6;
FT BAB21772)"
FT /evidence="ECO:0000305"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:4GMV"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:4GMV"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:4GN1"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:4GN1"
FT HELIX 507..516
FT /evidence="ECO:0007829|PDB:4GN1"
SQ SEQUENCE 1250 AA; 135256 MW; 1DFB651F945DA3DC CRC64;
MEQLSDEEID HGAEEDSDKE DQDLDKMFGA WLGELDKLTQ SLDSDKPMEP VKRSPLRQET
NMANFSYRFS IYNLNEALNQ GETVDLDALM ADLCSIEQEL SSIGSGNSKR QITETKATQK
LPVSRHTLKH GTLKGLSSSS NRIAKPSHAS YSLDDVTAQL EQASLSMDEA AQQSVLEDTK
PLVTNQHRRT ASAGTVSDAE VHSISNSSHS SITSAASSMD SLDIDKVTRP QELDLTHQGQ
PITEEEQAAK LKAEKIRVAL EKIKEAQVKK LVIRVHMSDD SSKTMMVDER QTVRQVLDNL
MDKSHCGYSL DWSLVETVSE LQMERIFEDH ENLVENLLNW TRDSQNKLIF MERIEKYALF
KNPQNYLLGK KETAEMADRN KEVLLEECFC GSSVTVPEIE GVLWLKDDGK KSWKKRYFLL
RASGIYYVPK GKAKVSRDLV CFLQLDHVNV YYGQDYRNKY KAPTDYCLVL KHPQIQKKSQ
YIKYLCCDDV RTLHQWVNGI RIAKYGKQLY MNYQEALKRT ESAYDWTSLS SSSIKSGSSS
SSIPESQSNH SNQSDSGVSD TQPAGHVRSQ SIVSSVFSEA WKRGTQLEES SKARMESMNR
PYTSLVPPLS PQPKIVTPYT ASQPSPPLPP PPPPPPPPPP PPPPPPPPLP SQSAPSAGSA
APMFVKYSTI TRLQNASQHS GALFKPPTPP VMQSQSVKPQ ILVPPNGVVP PPPPPPPPPT
PGSAMAQLKP APCAPSLPQF SAPPPPLKIH QVQHITQVAP PTPPPPPPIP APLPPQAPPK
PLVTIPAPTS TKTVAPVVTQ AAPPTPTPPV PPAKKQPAFP ASYIPPSPPT PPVPVPPPTL
PKQQSFCAKP PPSPLSPVPS VVKQIASQFP PPPTPPAMES QPLKPVPANV APQSPPAVKA
KPKWQPSSIP VPSPDFPPPP PESSLVFPPP PPSPVPAPPP PPPPTASPTP DKSGSPGKKT
SKTSSPGGKK PPPTPQRNSS IKSSSGAEHP EPKRPSVDSL VSKFTPPAES GSPSKETLPP
PAAPPKPGKL NLSGVNLPGV LQQGCVSAKA PVLSGRGKDS VVEFPSPPSD SDFPPPPPET
ELPLPPIEIP AVFSGNTSPK VAVVNPQPQQ WSKMSVKKAP PPTRPKRNDS TRLTQAEISE
QPTMATVVPQ VPTSPKSSLS VQPGFLADLN RTLQRKSITR HGSLSSRMSR AEPTATMDDM
ALPPPPPELL SDQQKAGYGG SHISGYATLR RGPPPAPPKR DQNTKLSRDW
