ID CIP4_HUMAN Reviewed; 601 AA. AC Q15642; B2R8A6; B7WP22; D6W645; O15184; Q53G22; Q5TZN1; Q6FI24; AC Q8NFL1; Q8TCY1; Q8TDX3; Q96RJ1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 3. DT 14-MAY-2014, entry version 139. DE RecName: Full=Cdc42-interacting protein 4; DE AltName: Full=Protein Felic; DE AltName: Full=Salt tolerant protein; DE Short=hSTP; DE AltName: Full=Thyroid receptor-interacting protein 10; DE Short=TR-interacting protein 10; DE Short=TRIP-10; GN Name=TRIP10; Synonyms=CIP4, STOT, STP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CDC42, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9210375; DOI=10.1016/S0960-9822(06)00219-3; RA Aspenstroem P.; RT "A Cdc42 target protein with homology to the non-kinase domain of FER RT has a potential role in regulating the actin cytoskeleton."; RL Curr. Biol. 7:479-487(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND RP INDUCTION. RX PubMed=12054674; DOI=10.1016/S0006-291X(02)00398-4; RA Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., RA Deng X., Whitcomb D., Corey S.J.; RT "Identification and genetic analysis of human and mouse activated RT Cdc42 interacting protein-4 isoforms."; RL Biochem. Biophys. Res. Commun. 293:1426-1430(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH CTNNB1, RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYROSINE RESIDUES. RC TISSUE=Renal cell carcinoma; RX PubMed=16343437; DOI=10.1016/j.bbrc.2005.11.117; RA Tsuji E., Tsuji Y., Fujiwara T., Ogata S., Tsukamoto K., Saku K.; RT "Splicing variant of Cdc42 interacting protein-4 disrupts beta- RT catenin-mediated cell-cell adhesion: expression and function in renal RT cell carcinoma."; RL Biochem. Biophys. Res. Commun. 339:1083-1088(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lung; RA Wang L., Rudert W.A., Sullivan K., Deng X., Corey S.J.; RT "Identification of a Cdc42-interacting protein 4 longer variant RT (Cip4L) which is differentially expressed in human tissues."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Small intestine; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 487-601 (ISOFORMS 1/2). RX PubMed=7776974; DOI=10.1210/me.9.2.243; RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.; RT "Two classes of proteins dependent on either the presence or absence RT of thyroid hormone for interaction with the thyroid hormone RT receptor."; RL Mol. Endocrinol. 9:243-254(1995). RN [13] RP TISSUE SPECIFICITY. RX PubMed=11294612; DOI=10.1023/A:1004132919896; RA Tsuji E., Tsuji Y.; RT "Molecular cloning and chromosomal localization of human salt-tolerant RT protein."; RL Genetica 108:259-262(2000). RN [14] RP INTERACTION WITH CDC42; MICROTUBULES AND WAS, SUBCELLULAR LOCATION, RP AND MUTAGENESIS OF ILE-454 AND LEU-468. RX PubMed=10713100; DOI=10.1074/jbc.275.11.7854; RA Tian L., Nelson D.L., Stewart D.M.; RT "Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich RT syndrome protein to microtubules."; RL J. Biol. Chem. 275:7854-7861(2000). RN [15] RP FUNCTION. RX PubMed=11069762; RA Linder S., Huefner K., Wintergerst U., Aepfelbacher M.; RT "Microtubule-dependent formation of podosomal adhesion structures in RT primary human macrophages."; RL J. Cell Sci. 113:4165-4176(2000). RN [16] RP INDUCTION. RX PubMed=11691828; RA Yuan R.-Q., Fan S., Achary M., Stewart D.M., Goldberg I.D., RA Rosen E.M.; RT "Altered gene expression pattern in cultured human breast cancer cells RT treated with hepatocyte growth factor/scatter factor in the setting of RT DNA damage."; RL Cancer Res. 61:8022-8031(2001). RN [17] RP INTERACTION WITH ARHGAP17, AND SUBCELLULAR LOCATION. RX PubMed=11431473; DOI=10.1074/jbc.M103540200; RA Richnau N., Aspenstroem P.; RT "Rich, a rho GTPase-activating protein domain-containing protein RT involved in signaling by Cdc42 and Rac1."; RL J. Biol. Chem. 276:35060-35070(2001). RN [18] RP INTERACTION WITH CDC42; LYN AND SRC, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND PHOSPHORYLATION AT TYROSINE RESIDUES. RX PubMed=12456510; DOI=10.1182/blood-2002-03-0851; RA Dombrosky-Ferlan P., Grishin A., Botelho R.J., Sampson M., Wang L., RA Rudert W.A., Grinstein S., Corey S.J.; RT "Felic (CIP4b), a novel binding partner with the Src kinase Lyn and RT Cdc42, localizes to the phagocytic cup."; RL Blood 101:2804-2809(2003). RN [19] RP INTERACTION WITH HD, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12604778; DOI=10.1073/pnas.0437967100; RA Holbert S., Dedeoglu A., Humbert S., Saudou F., Ferrante R.J., RA Neri C.; RT "Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and RT biological evidence for a role in Huntington's disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2712-2717(2003). RN [20] RP INTERACTION WITH AKAP9, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=15047863; DOI=10.1091/mbc.E03-10-0757; RA Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., RA Goldenring J.R.; RT "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi RT apparatus."; RL Mol. Biol. Cell 15:2771-2781(2004). RN [21] RP FUNCTION, INTERACTION WITH DNM1 AND WASL, AND SUBCELLULAR LOCATION. RX PubMed=16326391; DOI=10.1016/j.devcel.2005.11.005; RA Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., RA De Camilli P.; RT "Dynamin and the actin cytoskeleton cooperatively regulate plasma RT membrane invagination by BAR and F-BAR proteins."; RL Dev. Cell 9:791-804(2005). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [23] RP FUNCTION, INTERACTION WITH FASLG, AND SUBCELLULAR LOCATION. RX PubMed=16318909; DOI=10.1016/j.cellsig.2005.10.015; RA Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., RA Janssen O.; RT "Regulation of FasL expression: a SH3 domain containing protein family RT involved in the lysosomal association of FasL."; RL Cell. Signal. 18:1327-1337(2006). RN [24] RP INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2, AND SUBCELLULAR LOCATION. RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013; RA Aspenstroem P., Richnau N., Johansson A.-S.; RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RT RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and RT actin dynamics."; RL Exp. Cell Res. 312:2180-2194(2006). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-335 RP AND SER-351, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-335; SER-351 RP AND SER-482, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [28] 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., RA Buerckstuemmer T., 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 [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION RP 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [30] RP STRUCTURE BY NMR OF 543-599. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of the CDC42-interacting protein RT 4."; RL Submitted (NOV-2005) to the PDB data bank. RN [31] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 10-303, DOMAIN F-BAR, RP COILED-COIL DOMAIN, AND SUBUNIT. RX PubMed=17512409; DOI=10.1016/j.cell.2007.03.040; RA Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., RA Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., RA Liu Z.-J., Wang B.C., Yamamoto M., Terada T., Miyazawa A., Tanaka A., RA Sugano S., Shirouzu M., Nagayama K., Takenawa T., Yokoyama S.; RT "Curved EFC/F-BAR-domain dimers are joined end to end into a filament RT for membrane invagination in endocytosis."; RL Cell 129:761-772(2007). RN [32] RP STRUCTURE BY NMR OF 388-481, AND COILED-COIL DOMAIN. RX PubMed=19387844; DOI=10.1007/s10858-009-9317-z; RA Kobashigawa Y., Kumeta H., Kanoh D., Inagaki F.; RT "The NMR structure of the TC10- and Cdc42-interacting domain of RT CIP4."; RL J. Biomol. NMR 44:113-118(2009). CC -!- FUNCTION: Required for translocation of GLUT4 to the plasma CC membrane in response to insulin signaling (By similarity). CC Required to coordinate membrane tubulation with reorganization of CC the actin cytoskeleton during endocytosis. Binds to lipids such as CC phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and CC promotes membrane invagination and the formation of tubules. Also CC promotes CDC42-induced actin polymerization by recruiting WASL/N- CC WASP which in turn activates the Arp2/3 complex. Actin CC polymerization may promote the fission of membrane tubules to form CC endocytic vesicles. Required for the formation of podosomes, CC actin-rich adhesion structures specific to monocyte-derived cells. CC May be required for the lysosomal retention of FASLG/FASL. CC -!- SUBUNIT: Interacts specifically with GTP-bound RHOQ. Interacts CC with DNM2 and PDE6G (By similarity). Homodimerizes, the dimers can CC polymerize end-to-end to form filamentous structures. Interacts CC specifically with GTP-bound CDC42. Interacts with AKAP9, ARHGAP17, CC DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, CC microtubules, SRC, WAS/WASP and WASL/N-WASP. Interacts with the CC ligand binding domain of the thyroid receptor (TR) in the presence CC of thyroid hormone. May interact with CTNNB1 and HD/HTT. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-739936, EBI-739936; CC Q9Y4D1:DAAM1; NbExp=2; IntAct=EBI-6550597, EBI-2817289; CC P48023:FASLG; NbExp=4; IntAct=EBI-739936, EBI-495538; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell CC cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection, CC phagocytic cup. Note=Translocates to the plasma membrane in CC response to insulin stimulation, and this may require active RHOQ CC (By similarity). Localizes to cortical regions coincident with F- CC actin, to lysosomes and to sites of phagocytosis in macrophages. CC Also localizes to the Golgi, and this requires AKAP9. CC -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, perinuclear region. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=L; CC IsoId=Q15642-1; Sequence=Displayed; CC Name=2; Synonyms=A, W; CC IsoId=Q15642-2; Sequence=VSP_021716; CC Name=3; Synonyms=B; CC IsoId=Q15642-3; Sequence=VSP_021716, VSP_021721; CC Note=No experimental confirmation available; CC Name=4; Synonyms=C; CC IsoId=Q15642-4; Sequence=VSP_021716, VSP_021719, VSP_021720; CC Note=No experimental confirmation available; CC Name=5; Synonyms=V; CC IsoId=Q15642-5; Sequence=VSP_021717, VSP_021718; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, CC liver, lung, megakaryocyte, ovary, pancreas, peripheral blood CC lymphocytes, placenta, prostate, skeletal muscle, small intestine, CC spleen, testis, thymus and trachea. CC -!- INDUCTION: Induced by adriamycin treatment and this effect is CC counteracted by HGF/SF. Expression is reduced during CC differentiation. CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its CC concave surface. The end-to-end polymerization of dimers of these CC domains provides a curved surface that fits best membranes with CC around 600 A diameter, and may drive tubulation. CC -!- PTM: Tyrosine phosphorylated. Also phosphorylated by PKA. CC -!- SIMILARITY: Belongs to the FNBP1 family. CC -!- SIMILARITY: Contains 1 FCH domain. CC -!- SIMILARITY: Contains 1 REM (Hr1) repeat. CC -!- SIMILARITY: Contains 1 SH3 domain. 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; AJ000414; CAA04062.1; -; mRNA. DR EMBL; AF380114; AAK77492.1; -; mRNA. DR EMBL; AY081141; AAL89588.1; -; mRNA. DR EMBL; AB072596; BAB88853.1; -; mRNA. DR EMBL; AF502289; AAM46851.1; -; mRNA. DR EMBL; CR536513; CAG38751.1; -; mRNA. DR EMBL; BT006698; AAP35344.1; -; mRNA. DR EMBL; BT020167; AAV38969.1; -; mRNA. DR EMBL; BT020171; AAV43773.1; -; mRNA. DR EMBL; AK223109; BAD96829.1; -; mRNA. DR EMBL; AK313296; BAG36103.1; -; mRNA. DR EMBL; AC008760; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW69065.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69062.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69063.1; -; Genomic_DNA. DR EMBL; BC013002; AAH13002.1; -; mRNA. DR EMBL; L40379; AAC41729.1; -; mRNA. DR RefSeq; NP_001275891.1; NM_001288962.1. [Q15642-1] DR RefSeq; NP_001275892.1; NM_001288963.1. DR RefSeq; NP_004231.1; NM_004240.3. [Q15642-2] DR UniGene; Hs.515094; -. DR PDB; 2CT4; NMR; -; A=543-599. DR PDB; 2EFK; X-ray; 2.30 A; A=10-303. DR PDB; 2KE4; NMR; -; A=388-481. DR PDBsum; 2CT4; -. DR PDBsum; 2EFK; -. DR PDBsum; 2KE4; -. DR ProteinModelPortal; Q15642; -. DR SMR; Q15642; 10-288, 384-481, 544-599. DR BioGrid; 114733; 27. DR IntAct; Q15642; 9. DR MINT; MINT-124352; -. DR PhosphoSite; Q15642; -. DR DMDM; 118572632; -. DR MaxQB; Q15642; -. DR PaxDb; Q15642; -. DR PRIDE; Q15642; -. DR DNASU; 9322; -. DR Ensembl; ENST00000313244; ENSP00000320117; ENSG00000125733. [Q15642-1] DR Ensembl; ENST00000313285; ENSP00000320493; ENSG00000125733. [Q15642-2] DR GeneID; 9322; -. DR KEGG; hsa:9322; -. DR UCSC; uc002mfr.3; human. [Q15642-2] DR UCSC; uc002mfs.3; human. [Q15642-1] DR CTD; 9322; -. DR GeneCards; GC19P006737; -. DR H-InvDB; HIX0014704; -. DR HGNC; HGNC:12304; TRIP10. DR HPA; HPA041934; -. DR MIM; 604504; gene. DR neXtProt; NX_Q15642; -. DR PharmGKB; PA36983; -. DR eggNOG; NOG323796; -. DR HOVERGEN; HBG002489; -. DR InParanoid; Q15642; -. DR KO; K07196; -. DR OMA; AWLEDIQ; -. DR OrthoDB; EOG780RQK; -. DR PhylomeDB; Q15642; -. DR TreeFam; TF351162; -. DR Reactome; REACT_111102; Signal Transduction. DR SignaLink; Q15642; -. DR ChiTaRS; TRIP10; human. DR EvolutionaryTrace; Q15642; -. DR GeneWiki; TRIP10; -. DR GenomeRNAi; 9322; -. DR NextBio; 34921; -. DR PRO; PR:Q15642; -. DR ArrayExpress; Q15642; -. DR Bgee; Q15642; -. DR Genevestigator; Q15642; -. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0007154; P:cell communication; NAS:UniProtKB. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR InterPro; IPR028498; CIP4. DR InterPro; IPR001060; FCH_dom. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR12602:SF7; PTHR12602:SF7; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00055; FCH; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR PROSITE; PS50133; FCH; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; KW Golgi apparatus; Lipid-binding; Lysosome; Membrane; Phosphoprotein; KW Reference proteome; SH3 domain. FT CHAIN 1 601 Cdc42-interacting protein 4. FT /FTId=PRO_0000089766. FT DOMAIN 1 65 FCH. FT REPEAT 405 481 REM. FT DOMAIN 540 601 SH3. FT REGION 1 288 F-BAR domain. FT REGION 1 117 Required for podosome formation and FT interaction with AKAP9 and microtubules. FT REGION 1 117 Required for translocation to the plasma FT membrane in response to insulin (By FT similarity). FT REGION 293 601 Interaction with PDE6G (By similarity). FT REGION 293 537 Interaction with CDC42. FT REGION 471 601 Required for interaction with FASLG and FT localization to lysosomes. FT REGION 487 541 Interaction with DNM2 and WASL (By FT similarity). FT REGION 529 601 Interaction with DNM1 and WASL. FT REGION 538 601 Required for podosome formation. FT REGION 544 601 Interaction with WAS. FT REGION 546 601 Interaction with ARHGAP17, DAAM1, DIAPH1 FT and DIAPH2. FT COILED 67 259 FT COILED 388 481 FT SITE 166 166 Mediates end-to-end attachment of dimers. FT MOD_RES 296 296 Phosphoserine. FT MOD_RES 299 299 Phosphoserine. FT MOD_RES 335 335 Phosphoserine. FT MOD_RES 351 351 Phosphoserine. FT MOD_RES 482 482 Phosphoserine. FT VAR_SEQ 329 384 Missing (in isoform 2, isoform 3 and FT isoform 4). FT /FTId=VSP_021716. FT VAR_SEQ 330 341 RPPPLSPLGGPV -> SRQPWDSGDRGF (in isoform FT 5). FT /FTId=VSP_021717. FT VAR_SEQ 342 601 Missing (in isoform 5). FT /FTId=VSP_021718. FT VAR_SEQ 512 512 S -> R (in isoform 4). FT /FTId=VSP_021719. FT VAR_SEQ 513 601 Missing (in isoform 4). FT /FTId=VSP_021720. FT VAR_SEQ 553 601 GSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPT FT SYLRVTLN -> DLGPPPPPSQGPARALSLWPRVKTSVLWK FT KTKGTAGPGSGGKREARATCPPPTSESRSIEPCQRREEGGC FT RLLLLGHGGSQDLGTLFLTPWLRLRPV (in isoform FT 3). FT /FTId=VSP_021721. FT MUTAGEN 454 454 I->S: Abrogates interaction with CDC42. FT MUTAGEN 468 468 L->S: Impairs interaction with CDC42. FT CONFLICT 158 158 L -> P (in Ref. 2; AAK77492). FT CONFLICT 310 310 L -> P (in Ref. 2; AAK77492). FT CONFLICT 419 419 D -> G (in Ref. 8; BAD96829). FT CONFLICT 440 440 P -> S (in Ref. 8; BAD96829). FT CONFLICT 473 473 S -> R (in Ref. 2; AAK77492). FT CONFLICT 487 499 ARPPDPPASAPPD -> KHPIICRLIHFSN (in Ref. FT 10; AAC41729). FT CONFLICT 553 553 G -> W (in Ref. 5; CAG38751). FT HELIX 10 53 FT HELIX 68 97 FT HELIX 99 160 FT HELIX 166 206 FT HELIX 208 258 FT HELIX 261 271 FT HELIX 273 275 FT STRAND 391 394 FT HELIX 396 421 FT HELIX 423 433 FT HELIX 435 437 FT HELIX 440 442 FT HELIX 444 477 FT STRAND 544 549 FT STRAND 566 571 FT STRAND 574 576 FT STRAND 578 582 FT STRAND 584 586 FT STRAND 588 592 FT HELIX 593 595 FT STRAND 596 598 SQ SEQUENCE 601 AA; 68352 MW; A9BFE85520C7ABC5 CRC64; MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP SPRSGRDPLA ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR KRLQQQLEER SRELQKEVDQ REALKKMKDV YEKTPQMGDP ASLEPQIAET LSNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPASAPPDS SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS PIGHCVAIYH FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL N //