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Q15642

- CIP4_HUMAN

UniProt

Q15642 - CIP4_HUMAN

Protein

Cdc42-interacting protein 4

Gene

TRIP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    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.By similarity3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei166 – 1661Mediates end-to-end attachment of dimers

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. lipid binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. cell communication Source: UniProtKB
    3. endocytosis Source: UniProtKB-KW
    4. regulation of small GTPase mediated signal transduction Source: Reactome
    5. signal transduction Source: ProtInc
    6. small GTPase mediated signal transduction Source: Reactome

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    SignaLinkiQ15642.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:TRIP10
    Synonyms:CIP4, STOT, STP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:12304. TRIP10.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB-SubCell
    2. cell projection Source: UniProtKB-KW
    3. cytoplasm Source: UniProtKB
    4. cytoskeleton Source: UniProtKB-SubCell
    5. cytosol Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. Golgi apparatus Source: UniProtKB-SubCell
    8. intracellular membrane-bounded organelle Source: HPA
    9. lysosome Source: UniProtKB-SubCell
    10. nucleus Source: HPA
    11. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    12. phagocytic cup Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Lysosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi454 – 4541I → S: Abrogates interaction with CDC42. 1 Publication
    Mutagenesisi468 – 4681L → S: Impairs interaction with CDC42. 1 Publication

    Organism-specific databases

    PharmGKBiPA36983.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 601601Cdc42-interacting protein 4PRO_0000089766Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei296 – 2961Phosphoserine3 Publications
    Modified residuei299 – 2991Phosphoserine1 Publication
    Modified residuei335 – 3351Phosphoserine2 Publications
    Modified residuei351 – 3511Phosphoserine2 Publications
    Modified residuei482 – 4821Phosphoserine1 Publication

    Post-translational modificationi

    Tyrosine phosphorylated. Also phosphorylated by PKA.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15642.
    PaxDbiQ15642.
    PRIDEiQ15642.

    PTM databases

    PhosphoSiteiQ15642.

    Expressioni

    Tissue specificityi

    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.5 Publications

    Inductioni

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

    Gene expression databases

    ArrayExpressiQ15642.
    BgeeiQ15642.
    GenevestigatoriQ15642.

    Organism-specific databases

    HPAiHPA041934.

    Interactioni

    Subunit structurei

    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.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-739936,EBI-739936
    DAAM1Q9Y4D12EBI-6550597,EBI-2817289
    FASLGP480234EBI-739936,EBI-495538

    Protein-protein interaction databases

    BioGridi114733. 27 interactions.
    IntActiQ15642. 10 interactions.
    MINTiMINT-124352.

    Structurei

    Secondary structure

    1
    601
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 5344
    Helixi68 – 9730
    Helixi99 – 16062
    Helixi166 – 20641
    Helixi208 – 25851
    Helixi261 – 27111
    Helixi273 – 2753
    Beta strandi391 – 3944
    Helixi396 – 42126
    Helixi423 – 43311
    Helixi435 – 4373
    Helixi440 – 4423
    Helixi444 – 47734
    Beta strandi544 – 5496
    Beta strandi566 – 5716
    Beta strandi574 – 5763
    Beta strandi578 – 5825
    Beta strandi584 – 5863
    Beta strandi588 – 5925
    Helixi593 – 5953
    Beta strandi596 – 5983

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CT4NMR-A543-599[»]
    2EFKX-ray2.30A10-303[»]
    2KE4NMR-A388-481[»]
    ProteinModelPortaliQ15642.
    SMRiQ15642. Positions 10-288, 384-481, 544-599.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15642.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 6565FCHPROSITE-ProRule annotationAdd
    BLAST
    Repeati405 – 48177REMAdd
    BLAST
    Domaini540 – 60162SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 288288F-BAR domainAdd
    BLAST
    Regioni1 – 117117Required for podosome formation and interaction with AKAP9 and microtubulesAdd
    BLAST
    Regioni1 – 117117Required for translocation to the plasma membrane in response to insulinBy similarityAdd
    BLAST
    Regioni293 – 601309Interaction with PDE6GBy similarityAdd
    BLAST
    Regioni293 – 537245Interaction with CDC42Add
    BLAST
    Regioni471 – 601131Required for interaction with FASLG and localization to lysosomesAdd
    BLAST
    Regioni487 – 54155Interaction with DNM2 and WASLBy similarityAdd
    BLAST
    Regioni529 – 60173Interaction with DNM1 and WASLAdd
    BLAST
    Regioni538 – 60164Required for podosome formationAdd
    BLAST
    Regioni544 – 60158Interaction with WASAdd
    BLAST
    Regioni546 – 60156Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili67 – 259193Add
    BLAST
    Coiled coili388 – 48194Add
    BLAST

    Domaini

    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.1 Publication

    Sequence similaritiesi

    Belongs to the FNBP1 family.Curated
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 REM (Hr1) repeat.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG323796.
    HOVERGENiHBG002489.
    InParanoidiQ15642.
    KOiK07196.
    OMAiAWLEDIQ.
    OrthoDBiEOG780RQK.
    PhylomeDBiQ15642.
    TreeFamiTF351162.

    Family and domain databases

    InterProiIPR028498. CIP4.
    IPR001060. FCH_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR12602:SF7. PTHR12602:SF7. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    SMARTiSM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15642-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV    50
    KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL 100
    ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK 150
    AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD 200
    QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE 250
    GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL 300
    GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP 350
    SPRSGRDPLA ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR 400
    KRLQQQLEER SRELQKEVDQ REALKKMKDV YEKTPQMGDP ASLEPQIAET 450
    LSNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPASAPPDS 500
    SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS PIGHCVAIYH 550
    FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL 600
    N 601
    Length:601
    Mass (Da):68,352
    Last modified:November 28, 2006 - v3
    Checksum:iA9BFE85520C7ABC5
    GO
    Isoform 2 (identifier: Q15642-2) [UniParc]FASTAAdd to Basket

    Also known as: A, W

    The sequence of this isoform differs from the canonical sequence as follows:
         329-384: Missing.

    Show »
    Length:545
    Mass (Da):62,592
    Checksum:i9C9D72EA734BC6E2
    GO
    Isoform 3 (identifier: Q15642-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:593
    Mass (Da):67,603
    Checksum:i888A0FE78B42428B
    GO
    Isoform 4 (identifier: Q15642-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:456
    Mass (Da):52,700
    Checksum:iDBB2D486BC96832A
    GO
    Isoform 5 (identifier: Q15642-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:341
    Mass (Da):39,583
    Checksum:iA9568C38795E2E1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti158 – 1581L → P in AAK77492. (PubMed:12054674)Curated
    Sequence conflicti310 – 3101L → P in AAK77492. (PubMed:12054674)Curated
    Sequence conflicti419 – 4191D → G in BAD96829. 1 PublicationCurated
    Sequence conflicti440 – 4401P → S in BAD96829. 1 PublicationCurated
    Sequence conflicti473 – 4731S → R in AAK77492. (PubMed:12054674)Curated
    Sequence conflicti487 – 49913ARPPD…SAPPD → KHPIICRLIHFSN in AAC41729. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti553 – 5531G → W in CAG38751. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei329 – 38456Missing in isoform 2, isoform 3 and isoform 4. 7 PublicationsVSP_021716Add
    BLAST
    Alternative sequencei330 – 34112RPPPL…LGGPV → SRQPWDSGDRGF in isoform 5. 1 PublicationVSP_021717Add
    BLAST
    Alternative sequencei342 – 601260Missing in isoform 5. 1 PublicationVSP_021718Add
    BLAST
    Alternative sequencei512 – 5121S → R in isoform 4. 1 PublicationVSP_021719
    Alternative sequencei513 – 60189Missing in isoform 4. 1 PublicationVSP_021720Add
    BLAST
    Alternative sequencei553 – 60149GSSEG…RVTLN → DLGPPPPPSQGPARALSLWP RVKTSVLWKKTKGTAGPGSG GKREARATCPPPTSESRSIE PCQRREEGGCRLLLLGHGGS QDLGTLFLTPWLRLRPV in isoform 3. 1 PublicationVSP_021721Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS12172.1. [Q15642-2]
    RefSeqiNP_001275891.1. NM_001288962.1. [Q15642-1]
    NP_001275892.1. NM_001288963.1.
    NP_004231.1. NM_004240.3. [Q15642-2]
    UniGeneiHs.515094.

    Genome annotation databases

    EnsembliENST00000313244; ENSP00000320117; ENSG00000125733. [Q15642-1]
    ENST00000313285; ENSP00000320493; ENSG00000125733. [Q15642-2]
    GeneIDi9322.
    KEGGihsa:9322.
    UCSCiuc002mfr.3. human. [Q15642-2]
    uc002mfs.3. human. [Q15642-1]

    Polymorphism databases

    DMDMi118572632.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS12172.1. [Q15642-2 ]
    RefSeqi NP_001275891.1. NM_001288962.1. [Q15642-1 ]
    NP_001275892.1. NM_001288963.1.
    NP_004231.1. NM_004240.3. [Q15642-2 ]
    UniGenei Hs.515094.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CT4 NMR - A 543-599 [» ]
    2EFK X-ray 2.30 A 10-303 [» ]
    2KE4 NMR - A 388-481 [» ]
    ProteinModelPortali Q15642.
    SMRi Q15642. Positions 10-288, 384-481, 544-599.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114733. 27 interactions.
    IntActi Q15642. 10 interactions.
    MINTi MINT-124352.

    PTM databases

    PhosphoSitei Q15642.

    Polymorphism databases

    DMDMi 118572632.

    Proteomic databases

    MaxQBi Q15642.
    PaxDbi Q15642.
    PRIDEi Q15642.

    Protocols and materials databases

    DNASUi 9322.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313244 ; ENSP00000320117 ; ENSG00000125733 . [Q15642-1 ]
    ENST00000313285 ; ENSP00000320493 ; ENSG00000125733 . [Q15642-2 ]
    GeneIDi 9322.
    KEGGi hsa:9322.
    UCSCi uc002mfr.3. human. [Q15642-2 ]
    uc002mfs.3. human. [Q15642-1 ]

    Organism-specific databases

    CTDi 9322.
    GeneCardsi GC19P006737.
    H-InvDB HIX0014704.
    HGNCi HGNC:12304. TRIP10.
    HPAi HPA041934.
    MIMi 604504. gene.
    neXtProti NX_Q15642.
    PharmGKBi PA36983.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323796.
    HOVERGENi HBG002489.
    InParanoidi Q15642.
    KOi K07196.
    OMAi AWLEDIQ.
    OrthoDBi EOG780RQK.
    PhylomeDBi Q15642.
    TreeFami TF351162.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    SignaLinki Q15642.

    Miscellaneous databases

    ChiTaRSi TRIP10. human.
    EvolutionaryTracei Q15642.
    GeneWikii TRIP10.
    GenomeRNAii 9322.
    NextBioi 34921.
    PROi Q15642.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15642.
    Bgeei Q15642.
    Genevestigatori Q15642.

    Family and domain databases

    InterProi IPR028498. CIP4.
    IPR001060. FCH_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR12602:SF7. PTHR12602:SF7. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    SMARTi SM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    26. 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. 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. 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.

    Entry informationi

    Entry nameiCIP4_HUMAN
    AccessioniPrimary (citable) accession number: Q15642
    Secondary accession number(s): B2R8A6
    , B7WP22, D6W645, O15184, Q53G22, Q5TZN1, Q6FI24, Q8NFL1, Q8TCY1, Q8TDX3, Q96RJ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3