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Database: UniProt
Entry: C9JME2_HUMAN
LinkDB: C9JME2_HUMAN
Original site: C9JME2_HUMAN 
ID   C9JME2_HUMAN            Unreviewed;      1076 AA.
AC   C9JME2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=FERM, ARHGEF and pleckstrin domain-containing protein 1 {ECO:0000256|ARBA:ARBA00040395};
DE   AltName: Full=FERM, RhoGEF and pleckstrin domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042170};
GN   Name=FARP1 {ECO:0000313|Ensembl:ENSP00000471242.1};
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 {ECO:0000313|Ensembl:ENSP00000471242.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000471242.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [2] {ECO:0007829|PubMed:17081983}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [3] {ECO:0007829|PubMed:17924679}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [4] {ECO:0007829|PubMed:18220336}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [5] {ECO:0007829|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [6] {ECO:0007829|PubMed:18318008}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [7] {ECO:0007829|PubMed:19413330}
RP   IDENTIFICATION BY MASS 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   [8] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [9] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10] {ECO:0007829|PubMed:21406692}
RP   IDENTIFICATION BY MASS SPECTROMETRY [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   [11] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
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   [12] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [13] {ECO:0000313|Ensembl:ENSP00000471242.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC       {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic spine
CC       {ECO:0000256|ARBA:ARBA00004552}. Cell projection, filopodium
CC       {ECO:0000256|ARBA:ARBA00004486}. Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Synapse, synaptosome
CC       {ECO:0000256|ARBA:ARBA00034102}.
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DR   EMBL; AL136300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF455815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001273768.1; NM_001286839.1.
DR   RefSeq; XP_011519348.1; XM_011521046.2.
DR   ProteomicsDB; 10830; -.
DR   Antibodypedia; 619; 255 antibodies from 20 providers.
DR   DNASU; 10160; -.
DR   Ensembl; ENST00000595437.5; ENSP00000471242.1; ENSG00000152767.17.
DR   Ensembl; ENST00000627049.2; ENSP00000486285.1; ENSG00000152767.17.
DR   GeneID; 10160; -.
DR   UCSC; uc001vnh.4; human.
DR   CTD; 10160; -.
DR   HGNC; HGNC:3591; FARP1.
DR   VEuPathDB; HostDB:ENSG00000152767; -.
DR   GeneTree; ENSGT00940000155318; -.
DR   OMA; LAMQPTE; -.
DR   OrthoDB; 2876516at2759; -.
DR   BioGRID-ORCS; 10160; 15 hits in 1145 CRISPR screens.
DR   ChiTaRS; FARP1; human.
DR   GenomeRNAi; 10160; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000152767; Expressed in renal medulla and 204 other cell types or tissues.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13193; FERM_C_FARP1-like; 1.
DR   CDD; cd01220; PH1_FARP1-like; 1.
DR   CDD; cd13235; PH2_FARP1-like; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
DR   InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45858; FERM DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45858:SF2; FERM, ARHGEF AND PLECKSTRIN DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 3.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Proteomics identification {ECO:0007829|EPD:C9JME2,
KW   ECO:0007829|MaxQB:C9JME2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599}.
FT   DOMAIN          40..320
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          540..730
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          790..887
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          963..1060
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..401
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1076 AA;  122095 MW;  34B31A3B5AA0A043 CRC64;
     MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA
     PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF
     PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL
     AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI
     NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD
     FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ
     FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG
     EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL
     SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK
     AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK
     EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR
     LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI
     TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGRPG SFSLIRTPHL GQARRIPCAP
     ERRPLLLVKE FIRLGSLSKL SGKGLQQRMF FLFNDVLLYT SRGLTASNQF KVHGQLPLYG
     MTIEESEDEW GVPHCLTLRG QRQSIIVAAS SRSEMEKWVE DIQMAIDLAE KSSSPAPEFL
     ASSPPDNKSP DEATAADQES EDDLSASRTS LERQAPHRGN TMVHVCWHRN TSVSMVDFSI
     AVENQLSGNL LRKFKNSNGW QKLWVVFTNF CLFFYKSHQD NHPLASLPLL GYSLTIPSES
     ENIQKDYVFK LHFKSHVYYF RAESEYTFER WMEVIRSATS SASRPHVLSH KESLVY
//
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