Q15642 (CIP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TRIP10
Synonyms:	CIP4, STOT, STP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	601 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cytoplasm › cell cortex. Lysosome. Golgi apparatus. Cell membrane. Cell projection › phagocytic 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: Cytoplasm › perinuclear 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 process	Endocytosis
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Golgi apparatus Lysosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization 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 small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	Golgi 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 cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic cup Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-739936,EBI-739936
DAAM1	Q9Y4D1	2	EBI-6550597,EBI-2817289

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 601

601

Cdc42-interacting protein 4

PRO_0000089766

Regions

Domain

1 – 65

65

FCH

Repeat

405 – 481

77

REM

Domain

540 – 601

62

SH3

Region

1 – 288

288

F-BAR domain

Region

1 – 117

117

Required for podosome formation and interaction with AKAP9 and microtubules

Region

1 – 117

117

Required for translocation to the plasma membrane in response to insulin By similarity

Region

293 – 601

309

Interaction with PDE6G By similarity

Region

293 – 537

245

Interaction with CDC42

Region

471 – 601

131

Required for interaction with FASLG and localization to lysosomes

Region

487 – 541

55

Interaction with DNM2 and WASL By similarity

Region

529 – 601

73

Interaction with DNM1 and WASL

Region

538 – 601

64

Required for podosome formation

Region

544 – 601

58

Interaction with WAS

Region

546 – 601

56

Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2

Coiled coil

67 – 259

193

Ref.31 Ref.32

Coiled coil

388 – 481

94

Ref.31 Ref.32

Sites

Site

166

1

Mediates end-to-end attachment of dimers

Amino acid modifications

Modified residue

296

1

Phosphoserine Ref.3 Ref.18 Ref.26 Ref.27 Ref.29

Modified residue

299

1

Phosphoserine Ref.3 Ref.18 Ref.26

Modified residue

335

1

Phosphoserine Ref.3 Ref.18 Ref.26 Ref.27

Modified residue

351

1

Phosphoserine Ref.3 Ref.18 Ref.26 Ref.27

Modified residue

482

1

Phosphoserine Ref.3 Ref.18 Ref.27

Natural variations

Alternative sequence

329 – 384

56

Missing in isoform 2, isoform 3 and isoform 4.

VSP_021716

Alternative sequence

330 – 341

12

RPPPL…LGGPV → SRQPWDSGDRGF in isoform 5.

VSP_021717

Alternative sequence

342 – 601

260

Missing in isoform 5.

VSP_021718

Alternative sequence

512

1

S → R in isoform 4.

VSP_021719

Alternative sequence

513 – 601

89

Missing in isoform 4.

VSP_021720

Alternative sequence

553 – 601

49

GSSEG…RVTLN → DLGPPPPPSQGPARALSLWP RVKTSVLWKKTKGTAGPGSG GKREARATCPPPTSESRSIE PCQRREEGGCRLLLLGHGGS QDLGTLFLTPWLRLRPV in isoform 3.

VSP_021721

Experimental info

Mutagenesis

454

1

I → S: Abrogates interaction with CDC42. Ref.14

Mutagenesis

468

1

L → S: Impairs interaction with CDC42. Ref.14

Sequence conflict

158

1

L → P in AAK77492. Ref.2

Sequence conflict

310

1

L → P in AAK77492. Ref.2

Sequence conflict

419

1

D → G in BAD96829. Ref.8

Sequence conflict

440

1

P → S in BAD96829. Ref.8

Sequence conflict

473

1

S → R in AAK77492. Ref.2

Sequence conflict

487 – 499

13

ARPPD…SAPPD → KHPIICRLIHFSN in AAC41729. Ref.10

Sequence conflict

553

1

G → W in CAG38751. Ref.5

Secondary structure

1

.

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601

Helix Strand Turn

Details...

Helix

10 – 53

44

Helix

68 – 97

30

Helix

99 – 160

62

Helix

166 – 206

41

Helix

208 – 258

51

Helix

261 – 271

11

Helix

273 – 275

3

Beta strand

391 – 394

4

Helix

396 – 421

26

Helix

423 – 433

11

Helix

435 – 437

3

Helix

440 – 442

3

Helix

444 – 477

34

Beta strand

544 – 549

6

Beta strand

566 – 571

6

Beta strand

574 – 576

3

Beta strand

578 – 582

5

Beta strand

584 – 586

3

Beta strand

588 – 592

5

Helix

593 – 595

3

Beta strand

596 – 598

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (L) [UniParc]. Last modified November 28, 2006. Version 3. Checksum: A9BFE85520C7ABC5	FASTA	601	68,352
	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
	Isoform 2 (A) (W) [UniParc]. Checksum: 9C9D72EA734BC6E2	FASTA	545	62,592
	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 WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ LEERSRELQK 370 380 390 400 410 420 EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER LKLEVQKYEA WLAEAESRVL 430 440 450 460 470 480 SNRGDSLSRH ARPPDPPASA PPDSSSNSAS QDTKESSEEP PSEESQDTPI YTEFDEDFEE 490 500 510 520 530 540 EPTSPIGHCV AIYHFEGSSE GTISMAEGED LSLMEEDKGD GWTRVRRKEG GEGYVPTSYL RVTLN
	Isoform 3 (B) [UniParc]. Checksum: 888A0FE78B42428B	FASTA	593	67,603
	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 WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ LEERSRELQK 370 380 390 400 410 420 EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER LKLEVQKYEA WLAEAESRVL 430 440 450 460 470 480 SNRGDSLSRH ARPPDPPASA PPDSSSNSAS QDTKESSEEP PSEESQDTPI YTEFDEDFEE 490 500 510 520 530 540 EPTSPIGHCV AIYHFEDLGP PPPPSQGPAR ALSLWPRVKT SVLWKKTKGT AGPGSGGKRE 550 560 570 580 590 ARATCPPPTS ESRSIEPCQR REEGGCRLLL LGHGGSQDLG TLFLTPWLRL RPV
	Isoform 4 (C) [UniParc]. Checksum: DBB2D486BC96832A	FASTA	456	52,700
	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 WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ LEERSRELQK 370 380 390 400 410 420 EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER LKLEVQKYEA WLAEAESRVL 430 440 450 SNRGDSLSRH ARPPDPPASA PPDSSSNSAS QDTKER
	Isoform 5 (V) [UniParc]. Checksum: A9568C38795E2E1E	FASTA	341	39,583
	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 GTPSDGRPEL RGPGRSRTKR WPFGKKNKPS RQPWDSGDRG F

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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.

IPI

IPI00018804.
IPI00168849.
IPI00395401.
IPI00645818.
IPI00807460.

RefSeq

NP_004231.1. NM_004240.2.

UniGene

Hs.515094.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q15642.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15642. 8 interactions.

MINT

MINT-124352.

PTM databases

PhosphoSite

Q15642.

Polymorphism databases

DMDM

118572632.

Proteomic databases

PaxDb

Q15642.

PRIDE

Q15642.

Protocols and materials databases

DNASU

9322.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313244; ENSP00000320117; ENSG00000125733.
ENST00000313285; ENSP00000320493; ENSG00000125733.

GeneID

9322.

KEGG

hsa:9322.

UCSC

uc002mfr.3. human.
uc002mfs.3. human.
uc010dux.2. human.

Organism-specific databases

CTD

9322.

GeneCards

GC19P006690.

H-InvDB

HIX0014704.

HGNC

HGNC:12304. TRIP10.

MIM

604504. gene.

neXtProt

NX_Q15642.

PharmGKB

PA36983.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG323796.

HOVERGEN

HBG002489.

InParanoid

Q15642.

KO

K07196.

OMA

LWDQFEV.

PhylomeDB

Q15642.

Enzyme and pathway databases

Pathway_Interaction_DB

insulin_pathway. Insulin Pathway.
insulin_glucose_pathway. Insulin-mediated glucose transport.

Reactome

REACT_111102. Signal Transduction.

SignaLink

Q15642.

Gene expression databases

Bgee

Q15642.

Genevestigator

Q15642.

GermOnline

ENSG00000125733. Homo sapiens.

Family and domain databases

InterPro

IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

SMART

SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TRIP10. human.

EvolutionaryTrace

Q15642.

GenomeRNAi

9322.

NextBio

34921.

SOURCE

Search...

Entry information

Entry name

CIP4_HUMAN

Accession

Primary (citable) accession number: Q15642
Secondary accession number(s): B2R8A6 , 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:	May 29, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.