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Q15642

- CIP4_HUMAN

UniProt

Q15642 - CIP4_HUMAN

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Protein

Cdc42-interacting protein 4

Gene

TRIP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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 projection Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. Golgi apparatus Source: UniProtKB-KW
  7. intracellular membrane-bounded organelle Source: HPA
  8. lysosome Source: UniProtKB-KW
  9. nucleus Source: HPA
  10. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ15642.
ExpressionAtlasiQ15642. baseline and differential.
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.
GeneTreeiENSGT00510000046403.
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

        10         20         30         40         50
MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV
60 70 80 90 100
KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL
110 120 130 140 150
ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK
160 170 180 190 200
AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD
210 220 230 240 250
QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE
260 270 280 290 300
GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL
310 320 330 340 350
GTPSDGRPEL RGPGRSRTKR WPFGKKNKPR PPPLSPLGGP VPSALPNGPP
360 370 380 390 400
SPRSGRDPLA ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR
410 420 430 440 450
KRLQQQLEER SRELQKEVDQ REALKKMKDV YEKTPQMGDP ASLEPQIAET
460 470 480 490 500
LSNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPASAPPDS
510 520 530 540 550
SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS PIGHCVAIYH
560 570 580 590 600
FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL

N
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]
CCDS74271.1. [Q15642-1]
CCDS74272.1. [Q15642-3]
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 ]
CCDS74271.1. [Q15642-1 ]
CCDS74272.1. [Q15642-3 ]
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.
GeneTreei ENSGT00510000046403.
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

Bgeei Q15642.
ExpressionAtlasi Q15642. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 144 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