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Q15642 (CIP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cdc42-interacting protein 4
Alternative name(s):
Protein Felic
Salt tolerant protein
Short name=hSTP
Thyroid receptor-interacting protein 10
Short name=TR-interacting protein 10
Short name=TRIP-10
Gene names
Name:TRIP10
Synonyms:CIP4, STOT, STP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling By similarity. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL. Ref.15 Ref.21 Ref.23

Subunit structure

Interacts specifically with GTP-bound RHOQ. Interacts with DNM2 and PDE6G By similarity. Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts specifically with GTP-bound CDC42. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, SRC, WAS/WASP and WASL/N-WASP. Interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone. May interact with CTNNB1 and HD/HTT. Ref.1 Ref.3 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.31

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projectionphagocytic cup. Note: Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ By similarity. Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9. Ref.1 Ref.3 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24

Isoform 5: Cytoplasmperinuclear region Ref.1 Ref.3 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24.

Tissue specificity

Expressed in brain, colon, heart, kidney, liver, lung, megakaryocyte, ovary, pancreas, peripheral blood lymphocytes, placenta, prostate, skeletal muscle, small intestine, spleen, testis, thymus and trachea. Ref.1 Ref.2 Ref.13 Ref.18 Ref.19

Induction

Induced by adriamycin treatment and this effect is counteracted by HGF/SF. Expression is reduced during differentiation. Ref.2 Ref.16

Domain

The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation. Ref.31 Ref.32

Post-translational modification

Tyrosine phosphorylated. Also phosphorylated by PKA. Ref.3 Ref.18 Ref.20

Sequence similarities

Belongs to the FNBP1 family.

Contains 1 FCH domain.

Contains 1 REM (Hr1) repeat.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Golgi apparatus
Lysosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
SH3 domain
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Non-traceable author statement Ref.1. Source: UniProtKB

cell communication

Non-traceable author statement Ref.1. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.1. Source: ProtInc

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Non-traceable author statement Ref.1. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

phagocytic cup

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.31PubMed 18329367. Source: IntAct

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.23Ref.24. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15642-1)

Also known as: L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15642-2)

Also known as: A; W;

The sequence of this isoform differs from the canonical sequence as follows:
     329-384: Missing.
Isoform 3 (identifier: Q15642-3)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     329-384: Missing.
     553-601: GSSEGTISMA...PTSYLRVTLN → DLGPPPPPSQ...LTPWLRLRPV
Note: No experimental confirmation available.
Isoform 4 (identifier: Q15642-4)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     329-384: Missing.
     512-512: S → R
     513-601: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q15642-5)

Also known as: V;

The sequence of this isoform differs from the canonical sequence as follows:
     330-341: RPPPLSPLGGPV → SRQPWDSGDRGF
     342-601: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Cdc42-interacting protein 4
PRO_0000089766

Regions

Domain1 – 6565FCH
Repeat405 – 48177REM
Domain540 – 60162SH3
Region1 – 288288F-BAR domain
Region1 – 117117Required for podosome formation and interaction with AKAP9 and microtubules
Region1 – 117117Required for translocation to the plasma membrane in response to insulin By similarity
Region293 – 601309Interaction with PDE6G By similarity
Region293 – 537245Interaction with CDC42
Region471 – 601131Required for interaction with FASLG and localization to lysosomes
Region487 – 54155Interaction with DNM2 and WASL By similarity
Region529 – 60173Interaction with DNM1 and WASL
Region538 – 60164Required for podosome formation
Region544 – 60158Interaction with WAS
Region546 – 60156Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2
Coiled coil67 – 259193 Ref.31 Ref.32
Coiled coil388 – 48194 Ref.31 Ref.32

Sites

Site1661Mediates end-to-end attachment of dimers

Amino acid modifications

Modified residue2961Phosphoserine Ref.3 Ref.18 Ref.26 Ref.27 Ref.29
Modified residue2991Phosphoserine Ref.3 Ref.18 Ref.26
Modified residue3351Phosphoserine Ref.3 Ref.18 Ref.26 Ref.27
Modified residue3511Phosphoserine Ref.3 Ref.18 Ref.26 Ref.27
Modified residue4821Phosphoserine Ref.3 Ref.18 Ref.27

Natural variations

Alternative sequence329 – 38456Missing in isoform 2, isoform 3 and isoform 4.
VSP_021716
Alternative sequence330 – 34112RPPPL…LGGPV → SRQPWDSGDRGF in isoform 5.
VSP_021717
Alternative sequence342 – 601260Missing in isoform 5.
VSP_021718
Alternative sequence5121S → R in isoform 4.
VSP_021719
Alternative sequence513 – 60189Missing in isoform 4.
VSP_021720
Alternative sequence553 – 60149GSSEG…RVTLN → DLGPPPPPSQGPARALSLWP RVKTSVLWKKTKGTAGPGSG GKREARATCPPPTSESRSIE PCQRREEGGCRLLLLGHGGS QDLGTLFLTPWLRLRPV in isoform 3.
VSP_021721

Experimental info

Mutagenesis4541I → S: Abrogates interaction with CDC42. Ref.14
Mutagenesis4681L → S: Impairs interaction with CDC42. Ref.14
Sequence conflict1581L → P in AAK77492. Ref.2
Sequence conflict3101L → P in AAK77492. Ref.2
Sequence conflict4191D → G in BAD96829. Ref.8
Sequence conflict4401P → S in BAD96829. Ref.8
Sequence conflict4731S → R in AAK77492. Ref.2
Sequence conflict487 – 49913ARPPD…SAPPD → KHPIICRLIHFSN in AAC41729. Ref.10
Sequence conflict5531G → W in CAG38751. Ref.5

Secondary structure

......................................... 601
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (L) [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: A9BFE85520C7ABC5

FASTA60168,352
        10         20         30         40         50         60 
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV KKYLPKRPAK 

        70         80         90        100        110        120 
DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL ELTKYSQEMK QERKMHFQEG 

       130        140        150        160        170        180 
RRAQQQLENG FKQLENSKRK FERDCREAEK AAQTAERLDQ DINATKADVE KAKQQAHLRS 

       190        200        210        220        230        240 
HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE 

       250        260        270        280        290        300 
VVPIIAKCLE GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL 

       310        320        330        340        350        360 
GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP SPRSGRDPLA 

       370        380        390        400        410        420 
ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR KRLQQQLEER SRELQKEVDQ 

       430        440        450        460        470        480 
REALKKMKDV YEKTPQMGDP ASLEPQIAET LSNIERLKLE VQKYEAWLAE AESRVLSNRG 

       490        500        510        520        530        540 
DSLSRHARPP DPPASAPPDS SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS 

       550        560        570        580        590        600 
PIGHCVAIYH FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL 


N 

« Hide

Isoform 2 (A) (W) [UniParc].

Checksum: 9C9D72EA734BC6E2
Show »

FASTA54562,592
Isoform 3 (B) [UniParc].

Checksum: 888A0FE78B42428B
Show »

FASTA59367,603
Isoform 4 (C) [UniParc].

Checksum: DBB2D486BC96832A
Show »

FASTA45652,700
Isoform 5 (V) [UniParc].

Checksum: A9568C38795E2E1E
Show »

FASTA34139,583

References

« Hide 'large scale' references
[1]"A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton."
Aspenstroem P.
Curr. Biol. 7:479-487(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CDC42, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms."
Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., Deng X., Whitcomb D., Corey S.J.
Biochem. Biophys. Res. Commun. 293:1426-1430(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, INDUCTION.
[3]"Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell-cell adhesion: expression and function in renal cell carcinoma."
Tsuji E., Tsuji Y., Fujiwara T., Ogata S., Tsukamoto K., Saku K.
Biochem. Biophys. Res. Commun. 339:1083-1088(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYROSINE RESIDUES.
Tissue: Renal cell carcinoma.
[4]"Identification of a Cdc42-interacting protein 4 longer variant (Cip4L) which is differentially expressed in human tissues."
Wang L., Rudert W.A., Sullivan K., Deng X., Corey S.J.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lung.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Small intestine.
[8]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[9]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Muscle.
[12]"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 487-601 (ISOFORMS 1/2).
[13]"Molecular cloning and chromosomal localization of human salt-tolerant protein."
Tsuji E., Tsuji Y.
Genetica 108:259-262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[14]"Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules."
Tian L., Nelson D.L., Stewart D.M.
J. Biol. Chem. 275:7854-7861(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC42; MICROTUBULES AND WAS, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-454 AND LEU-468.
[15]"Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages."
Linder S., Huefner K., Wintergerst U., Aepfelbacher M.
J. Cell Sci. 113:4165-4176(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Altered gene expression pattern in cultured human breast cancer cells treated with hepatocyte growth factor/scatter factor in the setting of DNA damage."
Yuan R.-Q., Fan S., Achary M., Stewart D.M., Goldberg I.D., Rosen E.M.
Cancer Res. 61:8022-8031(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[17]"Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1."
Richnau N., Aspenstroem P.
J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGAP17, SUBCELLULAR LOCATION.
[18]"Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup."
Dombrosky-Ferlan P., Grishin A., Botelho R.J., Sampson M., Wang L., Rudert W.A., Grinstein S., Corey S.J.
Blood 101:2804-2809(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC42; LYN AND SRC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYROSINE RESIDUES.
[19]"Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease."
Holbert S., Dedeoglu A., Humbert S., Saudou F., Ferrante R.J., Neri C.
Proc. Natl. Acad. Sci. U.S.A. 100:2712-2717(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[20]"AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus."
Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., Goldenring J.R.
Mol. Biol. Cell 15:2771-2781(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKAP9, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[21]"Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins."
Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.
Dev. Cell 9:791-804(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM1 AND WASL, SUBCELLULAR LOCATION.
[22]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL."
Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., Janssen O.
Cell. Signal. 18:1327-1337(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FASLG, SUBCELLULAR LOCATION.
[24]"The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics."
Aspenstroem P., Richnau N., Johansson A.-S.
Exp. Cell Res. 312:2180-2194(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2, SUBCELLULAR LOCATION.
[25]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[26]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-335 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-335; SER-351 AND SER-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Solution structure of the SH3 domain of the CDC42-interacting protein 4."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 543-599.
[31]"Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis."
Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., Akasaka R., Nishino Y., Toyama M., Chen L., Liu Z.-J., Wang B.C., Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M. expand/collapse author list , Nagayama K., Takenawa T., Yokoyama S.
Cell 129:761-772(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 10-303, DOMAIN F-BAR, COILED-COIL DOMAIN, SUBUNIT.
[32]"The NMR structure of the TC10- and Cdc42-interacting domain of CIP4."
Kobashigawa Y., Kumeta H., Kanoh D., Inagaki F.
J. Biomol. NMR 44:113-118(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 388-481, COILED-COIL DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000414 mRNA. Translation: CAA04062.1.
AF380114 mRNA. Translation: AAK77492.1.
AY081141 mRNA. Translation: AAL89588.1.
AB072596 mRNA. Translation: BAB88853.1.
AF502289 mRNA. Translation: AAM46851.1.
CR536513 mRNA. Translation: CAG38751.1.
BT006698 mRNA. Translation: AAP35344.1.
BT020167 mRNA. Translation: AAV38969.1.
BT020171 mRNA. Translation: AAV43773.1.
AK223109 mRNA. Translation: BAD96829.1.
AK313296 mRNA. Translation: BAG36103.1.
AC008760 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69065.1.
CH471139 Genomic DNA. Translation: EAW69062.1.
CH471139 Genomic DNA. Translation: EAW69063.1.
BC013002 mRNA. Translation: AAH13002.1.
L40379 mRNA. Translation: AAC41729.1.
CCDSCCDS12172.1. [Q15642-2]
RefSeqNP_001275891.1. NM_001288962.1. [Q15642-1]
NP_001275892.1. NM_001288963.1.
NP_004231.1. NM_004240.3. [Q15642-2]
UniGeneHs.515094.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CT4NMR-A543-599[»]
2EFKX-ray2.30A10-303[»]
2KE4NMR-A388-481[»]
ProteinModelPortalQ15642.
SMRQ15642. Positions 10-288, 384-481, 544-599.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114733. 27 interactions.
IntActQ15642. 10 interactions.
MINTMINT-124352.

PTM databases

PhosphoSiteQ15642.

Polymorphism databases

DMDM118572632.

Proteomic databases

MaxQBQ15642.
PaxDbQ15642.
PRIDEQ15642.

Protocols and materials databases

DNASU9322.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313244; ENSP00000320117; ENSG00000125733. [Q15642-1]
ENST00000313285; ENSP00000320493; ENSG00000125733. [Q15642-2]
GeneID9322.
KEGGhsa:9322.
UCSCuc002mfr.3. human. [Q15642-2]
uc002mfs.3. human. [Q15642-1]

Organism-specific databases

CTD9322.
GeneCardsGC19P006737.
H-InvDBHIX0014704.
HGNCHGNC:12304. TRIP10.
HPAHPA041934.
MIM604504. gene.
neXtProtNX_Q15642.
PharmGKBPA36983.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG323796.
HOVERGENHBG002489.
InParanoidQ15642.
KOK07196.
OMAAWLEDIQ.
OrthoDBEOG780RQK.
PhylomeDBQ15642.
TreeFamTF351162.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ15642.

Gene expression databases

ArrayExpressQ15642.
BgeeQ15642.
GenevestigatorQ15642.

Family and domain databases

InterProIPR028498. CIP4.
IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR12602:SF7. PTHR12602:SF7. 1 hit.
PfamPF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRIP10. human.
EvolutionaryTraceQ15642.
GeneWikiTRIP10.
GenomeRNAi9322.
NextBio34921.
PROQ15642.
SOURCESearch...

Entry information

Entry nameCIP4_HUMAN
AccessionPrimary (citable) accession number: Q15642
Secondary accession number(s): B2R8A6 expand/collapse secondary AC list , B7WP22, D6W645, O15184, Q53G22, Q5TZN1, Q6FI24, Q8NFL1, Q8TCY1, Q8TDX3, Q96RJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM