ID E9PEK4_HUMAN Unreviewed; 671 AA.
AC E9PEK4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 28-JAN-2026, entry version 95.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=CSF1R {ECO:0000313|Ensembl:ENSP00000422212.1};
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:ENSP00000422212.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000422212.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11237011; DOI=10.1038/35057062;
RG International Human Genome Sequencing Consortium;
RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA Shizuya H., Choi S., Chen Y.J.;
RT "Initial sequencing and analysis of the human genome.";
RL Nature 409:860-921(2001).
RN [2] {ECO:0000313|Ensembl:ENSP00000422212.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3] {ECO:0000313|Ensembl:ENSP00000422212.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496913; DOI=10.1038/nature03001;
RG International Human Genome Sequencing Consortium;
RT "Finishing the euchromatic sequence of the human genome.";
RL Nature 431:931-945(2004).
RN [4] {ECO:0000313|Ensembl:ENSP00000422212.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [5] {ECO:0000313|Ensembl:ENSP00000422212.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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DR EMBL; AC011382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E9PEK4; -.
DR SMR; E9PEK4; -.
DR MassIVE; E9PEK4; -.
DR ProteomicsDB; 19911; -.
DR Ensembl; ENST00000504875.5; ENSP00000422212.1; ENSG00000182578.15.
DR Ensembl; ENST00000504875.5; ENSP00000422212.1; ENSG00000182578.14.
DR UCSC; uc063ipr.1; human.
DR HGNC; HGNC:2433; CSF1R.
DR OpenTargets; ENSG00000182578; -.
DR VEuPathDB; HostDB:ENSG00000182578; -.
DR GeneTree; ENSGT00940000155506; -.
DR OrthoDB; 6077854at2759; -.
DR ChiTaRS; CSF1R; human.
DR Proteomes; UP000005640; Chromosome 5.
DR Bgee; ENSG00000182578; Expressed in granulocyte and 166 other cell types or tissues.
DR ExpressionAtlas; E9PEK4; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0030097; P:hemopoiesis; IEA:UniProtKB-ARBA.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR GO; GO:0050793; P:regulation of developmental process; IEA:UniProtKB-ARBA.
DR GO; GO:0002682; P:regulation of immune system process; IEA:UniProtKB-ARBA.
DR CDD; cd00096; Ig; 1.
DR CDD; cd20936; IgI_3_CSF-1R; 1.
DR CDD; cd04975; IgI_4_SCFR_like; 1.
DR FunFam; 2.60.40.10:FF:001029; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001088; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001101; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001160; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 2.60.40.10:FF:001169; Macrophage colony-stimulating factor 1 receptor; 1.
DR FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR InterPro; IPR030658; CSF-1_receptor.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR050122; RTK.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR PANTHER; PTHR24416:SF47; MACROPHAGE COLONY-STIMULATING FACTOR 1 RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500947; CSF-1_receptor; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW 2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR500947-52};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000615-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|PeptideAtlas:E9PEK4,
KW ECO:0007829|ProteomicsDB:E9PEK4}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..671
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003244041"
FT TRANSMEM 514..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..85
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 203..290
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 402..502
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 582..671
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 561
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 588..596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-51"
FT BINDING 589..596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 42..84
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 127..177
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 224..278
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
FT DISULFID 419..485
FT /evidence="ECO:0000256|PIRSR:PIRSR500947-52"
SQ SEQUENCE 671 AA; 74269 MW; 205F93FFECC8D891 CRC64;
MGPGVLLLLL VATAWHGQGI PVIEPSVPEL VVKPGATVTL RCVGNGSVEW DGPPSPHWTL
YSDGSSSILS TNNATFQNTG TYRCTEPGDP LGGSAAIHLY VKDPARPWNV LAQEVVVFED
QDALLPCLLT DPVLEAGVSL VRVRGRPLMR HTNYSFSPWH GFTIHRAKFI QSQDYQCSAL
MGGRKVMSIS IRLKVQKVIP GPPALTLVPA ELVRIRGEAA QIVCSASSVD VNFDVFLQHN
NTKLAIPQQS DFHNNRYQKV LTLNLDQVDF QHAGNYSCVA SNVQGKHSTS MFFRVVESAY
LNLSSEQNLI QEVTVGEGLN LKVMVEAYPG LQGFNWTYLG PFSDHQPEPK LANATTKDTY
RHTFTLSLPR LKPSEAGRYS FLARNPGGWR ALTFELTLRY PPEVSVIWTF INGSGTLLCA
ASGYPQPNVT WLQCSGHTDR CDEAQVLQVW DDPYPEVLSQ EPFHKVTVQS LLTVETLEHN
QTYECRAHNS VGSGSWAFIP ISAGAHTHPP DEFLFTPVVV ACMSIMALLL LLLLLLLYKY
KQKPKYQVRW KIIESYEGNS YTFIDPTQLP YNEKWEFPRN NLQFGKTLGA GAFGKVVEAT
AFGLGKEDAV LKVAVKMLKS TAHADEKEAL MSELKIMSHL GQHENIVNLL GACTHGGTVA
SPARVWTPMW R
//
